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Database: PDB
Entry: 1XSO
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Original site: 1XSO 
HEADER    OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR)    14-MAR-95   1XSO              
TITLE     THREE-DIMENSIONAL STRUCTURE OF XENOPUS LAEVIS CU,ZN                   
TITLE    2 SUPEROXIDE DISMUTASE B DETERMINED BY X-RAY CRYSTALLOGRAPHY           
TITLE    3 AT 1.5 ANGSTROMS RESOLUTION                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COPPER,ZINC SUPEROXIDE DISMUTASE;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;                                 
SOURCE   3 ORGANISM_COMMON: AFRICAN CLAWED FROG;                                
SOURCE   4 ORGANISM_TAXID: 8355;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PKK233-2 TRC PROMOTER                     
KEYWDS    OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR)                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.DJINOVIC CARUGO,A.CODA,A.BATTISTONI,M.T.CARRI,                      
AUTHOR   2 F.POLTICELLI,A.DESIDERI,G.ROTILIO,K.S.WILSON,M.BOLOGNESI             
REVDAT   3   24-FEB-09 1XSO    1       VERSN                                    
REVDAT   2   03-MAY-99 1XSO    1       JRNL                                     
REVDAT   1   10-JUL-95 1XSO    0                                                
JRNL        AUTH   K.DJINOVIC CARUGO,A.BATTISTONI,M.T.CARRI,                    
JRNL        AUTH 2 F.POLTICELLI,A.DESIDERI,G.ROTILIO,A.CODA,                    
JRNL        AUTH 3 K.S.WILSON,M.BOLOGNESI                                       
JRNL        TITL   THREE-DIMENSIONAL STRUCTURE OF XENOPUS LAEVIS                
JRNL        TITL 2 CU,ZN SUPEROXIDE DISMUTASE B DETERMINED BY X-RAY             
JRNL        TITL 3 CRYSTALLOGRAPHY AT 1.5 A RESOLUTION.                         
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  52   176 1996              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   15299740                                                     
JRNL        DOI    10.1107/S0907444995007608                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   D.BORDO,K.DJINOVIC,K.M.BOLOGNESI                             
REMARK   1  TITL   CONSERVED PATTERNS IN THE CU,ZN SUPEROXIDE                   
REMARK   1  TITL 2 DISMUTASE FAMILY                                             
REMARK   1  REF    J.MOL.BIOL.                   V. 238   366 1994              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   K.DJINOVIC CARUGO,K.F.POLTICELLI,A.DESIDERI,                 
REMARK   1  AUTH 2 G.ROTILIO,K.S.WILSON,M.BOLOGNESI                             
REMARK   1  TITL   CRYSTALLOGRAPHIC STUDY OF AZIDE-INHIBITED BOVINE             
REMARK   1  TITL 2 CU,ZN SUPEROXIDE DISMUTASE                                   
REMARK   1  REF    J.MOL.BIOL.                   V. 240   179 1994              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   K.DJINOVIC CARUGO,K.A.BATTISTONI,M.T.CARRI,                  
REMARK   1  AUTH 2 F.POLTICELLI,A.DESIDERI,G.ROTILIO,A.CODA,                    
REMARK   1  AUTH 3 M.BOLOGNESI                                                  
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE CYANIDE-INHIBITED XENOPUS           
REMARK   1  TITL 2 LAEVIS CU,ZN SUPEROXIDE DISMUTASE AT 98 K                    
REMARK   1  REF    FEBS LETT.                    V. 349    93 1994              
REMARK   1  REFN                   ISSN 0014-5793                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   K.DJINOVIC CARUGO,K.C.COLLYER,A.CODA,M.T.CARRI,              
REMARK   1  AUTH 2 A.BATTISTONI,G.BOTARO,F.POLTICELLI,A.DESIDERI,               
REMARK   1  AUTH 3 M.BOLOGNESI                                                  
REMARK   1  TITL   CRYSTALLISATION AND PRELIMINARY CRYSTALLOGRAPHIC             
REMARK   1  TITL 2 ANALYSIS OF RECOMBINANT XENOPUS LAEVIS CU,ZN                 
REMARK   1  TITL 3 SUPEROXIDE DISMUTASE B                                       
REMARK   1  REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 194  1008 1993              
REMARK   1  REFN                   ISSN 0006-291X                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   K.DJINOVIC,G.GATTI,L.ANTOLINI,G.PELOSI,A.DESIDERI,           
REMARK   1  AUTH 2 M.FALCONI,F.MARMOCCHI,G.ROTILIO,M.BOLOGNESI                  
REMARK   1  TITL   CRYSTAL STRUCTURE OF YEAST CU,ZN SUPEROXIDE                  
REMARK   1  TITL 2 DISMUTASE                                                    
REMARK   1  REF    J.MOL.BIOL.                   V. 225   791 1992              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.49 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ, X-PLOR, SHELXL-93                            
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 49209                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.104                           
REMARK   3   R VALUE            (WORKING SET) : 0.104                           
REMARK   3   FREE R VALUE                     : 0.169                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2187                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 350                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 2.580 ; 3.000               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 3.530 ; 4.000               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 6.520 ; 5.000               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 8.920 ; 6.000               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RESIDUE 24 IS IN POOR ELECTRON            
REMARK   3  DENSITY.                                                            
REMARK   4                                                                      
REMARK   4 1XSO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-AUG-93                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X31                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.92                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM-MADE                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49209                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 4.980                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       36.72500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       29.38000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.47000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       29.38000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.72500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.47000            
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 300 REMARK: MTRIX                                                        
REMARK 300  THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW                
REMARK 300  DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE               
REMARK 300  VARIOUS DOMAINS IN THIS ENTRY.  APPLYING THE APPROPRIATE            
REMARK 300  MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL              
REMARK 300  YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED               
REMARK 300  SECOND.                                                             
REMARK 300                                                                      
REMARK 300            APPLIED TO           TRANSFORMED TO                       
REMARK 300  MTRIX      RESIDUES               RESIDUES         RMSD             
REMARK 300    M1   A    2  ..  A  151     B    2  ..  B  151   0.279            
REMARK 300                                                                      
REMARK 300   CALCULATED FOR C-ALPHA ATOMS                                       
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: 1590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A    3   NZ                                                  
REMARK 480     LYS A   15   CD    NZ                                            
REMARK 480     GLN A   23   OE1   NE2                                           
REMARK 480     ASP A   24   CB                                                  
REMARK 480     GLU A   25   CB    CG    CD    OE1   OE2                         
REMARK 480     GLU A   34   CD    OE1   OE2                                     
REMARK 480     MET A   56   CG                                                  
REMARK 480     GLN A   94   CG                                                  
REMARK 480     LYS A  105   CD                                                  
REMARK 480     LYS A  120   CE                                                  
REMARK 480     LYS A  126   CD    CE    NZ                                      
REMARK 480     LYS B    3   NZ                                                  
REMARK 480     ASP B   13   OD2                                                 
REMARK 480     LYS B   15   CE    NZ                                            
REMARK 480     GLN B   23   CG    CD    OE1   NE2                               
REMARK 480     ASP B   24   CG    OD1   OD2                                     
REMARK 480     GLU B   30   OE2                                                 
REMARK 480     LYS B   32   NZ                                                  
REMARK 480     ASN B   66   ND2                                                 
REMARK 480     LYS B   96   CD    CE    NZ                                      
REMARK 480     LYS B  105   CD    CE    NZ                                      
REMARK 480     LYS B  120   NZ                                                  
REMARK 480     LYS B  126   CE    NZ                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   167     O    HOH A   263              2.09            
REMARK 500   O    HOH B   222     O    HOH B   298              2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A   6   CB    CYS A   6   SG     -0.103                       
REMARK 500    CYS A   6   CB    CYS A   6   SG     -0.098                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A   6   N   -  CA  -  CB  ANGL. DEV. = -11.1 DEGREES          
REMARK 500    CYS A   6   N   -  CA  -  CB  ANGL. DEV. =  14.2 DEGREES          
REMARK 500    ARG A 113   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    CYS B   6   CB  -  CA  -  C   ANGL. DEV. = -13.7 DEGREES          
REMARK 500    CYS B   6   N   -  CA  -  CB  ANGL. DEV. = -19.0 DEGREES          
REMARK 500    LEU B   8   N   -  CA  -  CB  ANGL. DEV. =  12.5 DEGREES          
REMARK 500    ASN B  51   CB  -  CA  -  C   ANGL. DEV. = -16.1 DEGREES          
REMARK 500    VAL B  92   N   -  CA  -  CB  ANGL. DEV. =  16.0 DEGREES          
REMARK 500    SER B 100   N   -  CA  -  CB  ANGL. DEV. =  17.9 DEGREES          
REMARK 500    ARG B 141   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    SER B 150   N   -  CA  -  CB  ANGL. DEV. = -13.2 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  24     -138.67     56.46                                   
REMARK 500    ASN A  53       51.00   -115.30                                   
REMARK 500    ASP B  24     -136.64     50.71                                   
REMARK 500    ASN B  63       58.35   -145.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500   M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                
REMARK 500     CYS A   6        23.6      L          L   OUTSIDE RANGE          
REMARK 500     ASP A  38        23.4      L          L   OUTSIDE RANGE          
REMARK 500     ASN A  51        20.7      L          L   OUTSIDE RANGE          
REMARK 500     MET A  56        24.3      L          L   OUTSIDE RANGE          
REMARK 500     CYS B   6        45.2      L          L   OUTSIDE RANGE          
REMARK 500     LEU B   8        24.3      L          L   OUTSIDE RANGE          
REMARK 500     VAL B  92        19.9      L          L   OUTSIDE RANGE          
REMARK 500     SER B 100        19.0      L          L   OUTSIDE RANGE          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 253        DISTANCE =  7.76 ANGSTROMS                       
REMARK 525    HOH A 275        DISTANCE =  5.69 ANGSTROMS                       
REMARK 525    HOH A 286        DISTANCE =  7.11 ANGSTROMS                       
REMARK 525    HOH A 314        DISTANCE =  5.43 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A   1  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 118   NE2                                                    
REMARK 620 2 HIS A  46   NE2  99.9                                              
REMARK 620 3 HIS A  44   ND1  90.6 139.7                                        
REMARK 620 4 HIS A  61   NE2 166.3  90.5  87.1                                  
REMARK 620 5 HOH A 167   O    87.3 100.6 118.8  82.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 152  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  81   OD1                                                    
REMARK 620 2 HIS A  78   ND1 112.3                                              
REMARK 620 3 HIS A  69   ND1  96.7 121.8                                        
REMARK 620 4 HIS A  61   ND1 105.0 109.4 109.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 152  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  44   ND1                                                    
REMARK 620 2 HOH B 159   O   126.0                                              
REMARK 620 3 HOH B 154   O    89.0  38.4                                        
REMARK 620 4 HIS B 118   NE2  91.8  89.2  79.5                                  
REMARK 620 5 HIS B  61   NE2  86.4  80.7  86.7 166.1                            
REMARK 620 6 HIS B  46   NE2 137.8  95.3 133.2  97.8  92.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 153  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  69   ND1                                                    
REMARK 620 2 HIS B  78   ND1 122.4                                              
REMARK 620 3 ASP B  81   OD1  97.2 111.2                                        
REMARK 620 4 HIS B  61   ND1 109.4 110.5 104.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: A                                                   
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: B                                                   
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 1                    
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 152                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 152                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 153                  
DBREF  1XSO A    2   151  UNP    P15107   SODC2_XENLA      1    150             
DBREF  1XSO B    2   151  UNP    P15107   SODC2_XENLA      1    150             
SEQADV 1XSO SER A   60  UNP  P15107    PRO    60 CONFLICT                       
SEQADV 1XSO SER B   60  UNP  P15107    PRO    60 CONFLICT                       
SEQRES   1 A  150  VAL LYS ALA VAL CYS VAL LEU ALA GLY SER GLY ASP VAL          
SEQRES   2 A  150  LYS GLY VAL VAL HIS PHE GLU GLN GLN ASP GLU GLY ALA          
SEQRES   3 A  150  VAL SER VAL GLU GLY LYS ILE GLU GLY LEU THR ASP GLY          
SEQRES   4 A  150  LEU HIS GLY PHE HIS ILE HIS VAL PHE GLY ASP ASN THR          
SEQRES   5 A  150  ASN GLY CYS MET SER ALA GLY SER HIS PHE ASN PRO GLU          
SEQRES   6 A  150  ASN LYS ASN HIS GLY ALA PRO GLY ASP THR ASP ARG HIS          
SEQRES   7 A  150  VAL GLY ASP LEU GLY ASN VAL THR ALA GLU GLY GLY VAL          
SEQRES   8 A  150  ALA GLN PHE LYS ILE THR ASP SER LEU ILE SER LEU LYS          
SEQRES   9 A  150  GLY PRO ASN SER ILE ILE GLY ARG THR ALA VAL VAL HIS          
SEQRES  10 A  150  GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY ASN ASP GLU          
SEQRES  11 A  150  SER LEU LYS THR GLY ASN ALA GLY GLY ARG LEU ALA CYS          
SEQRES  12 A  150  GLY VAL ILE GLY TYR SER PRO                                  
SEQRES   1 B  150  VAL LYS ALA VAL CYS VAL LEU ALA GLY SER GLY ASP VAL          
SEQRES   2 B  150  LYS GLY VAL VAL HIS PHE GLU GLN GLN ASP GLU GLY ALA          
SEQRES   3 B  150  VAL SER VAL GLU GLY LYS ILE GLU GLY LEU THR ASP GLY          
SEQRES   4 B  150  LEU HIS GLY PHE HIS ILE HIS VAL PHE GLY ASP ASN THR          
SEQRES   5 B  150  ASN GLY CYS MET SER ALA GLY SER HIS PHE ASN PRO GLU          
SEQRES   6 B  150  ASN LYS ASN HIS GLY ALA PRO GLY ASP THR ASP ARG HIS          
SEQRES   7 B  150  VAL GLY ASP LEU GLY ASN VAL THR ALA GLU GLY GLY VAL          
SEQRES   8 B  150  ALA GLN PHE LYS ILE THR ASP SER LEU ILE SER LEU LYS          
SEQRES   9 B  150  GLY PRO ASN SER ILE ILE GLY ARG THR ALA VAL VAL HIS          
SEQRES  10 B  150  GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY ASN ASP GLU          
SEQRES  11 B  150  SER LEU LYS THR GLY ASN ALA GLY GLY ARG LEU ALA CYS          
SEQRES  12 B  150  GLY VAL ILE GLY TYR SER PRO                                  
HET     CU  A   1       1                                                       
HET     ZN  A 152       1                                                       
HET     CU  B 152       1                                                       
HET     ZN  B 153       1                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
FORMUL   3   CU    2(CU 2+)                                                     
FORMUL   4   ZN    2(ZN 2+)                                                     
FORMUL   7  HOH   *350(H2 O)                                                    
HELIX    1   1 GLY A   54  ALA A   58  5                                   5    
HELIX    2   2 GLU A  131  THR A  135  5                                   5    
HELIX    3   3 GLY B   54  SER B   57  5                                   4    
HELIX    4   4 SER B  132  THR B  135  1                                   4    
SHEET    1   A 4 LYS A   3  LEU A   8  0                                        
SHEET    2   A 4 LYS A  15  GLN A  22 -1  N  PHE A  20   O  ALA A   4           
SHEET    3   A 4 VAL A  27  GLU A  34 -1  N  GLU A  34   O  LYS A  15           
SHEET    4   A 4 VAL A  92  ASP A  99 -1  N  ASP A  99   O  VAL A  27           
SHEET    1   B 2 GLY A  39  GLY A  42  0                                        
SHEET    2   B 2 ASN A  84  ALA A  87 -1  N  ALA A  87   O  GLY A  39           
SHEET    1   C 3 PHE A  43  HIS A  46  0                                        
SHEET    2   C 3 THR A 114  HIS A 118 -1  N  VAL A 116   O  HIS A  44           
SHEET    3   C 3 ARG A 141  VAL A 146 -1  N  GLY A 145   O  ALA A 115           
SHEET    1   D 4 LYS B   3  LEU B   8  0                                        
SHEET    2   D 4 LYS B  15  GLU B  21 -1  N  PHE B  20   O  ALA B   4           
SHEET    3   D 4 VAL B  27  GLU B  34 -1  N  GLU B  34   O  LYS B  15           
SHEET    4   D 4 VAL B  92  ASP B  99 -1  N  ASP B  99   O  VAL B  27           
SHEET    1   E 2 GLY B  39  GLY B  42  0                                        
SHEET    2   E 2 ASN B  84  ALA B  87 -1  N  ALA B  87   O  GLY B  39           
SHEET    1   F 3 PHE B  43  HIS B  46  0                                        
SHEET    2   F 3 THR B 114  HIS B 118 -1  N  VAL B 116   O  HIS B  44           
SHEET    3   F 3 ARG B 141  VAL B 146 -1  N  GLY B 145   O  ALA B 115           
SSBOND   1 CYS A   55    CYS A  144                          1555   1555  2.02  
SSBOND   2 CYS B   55    CYS B  144                          1555   1555  2.04  
LINK        CU    CU A   1                 NE2 HIS A 118     1555   1555  2.11  
LINK        CU    CU A   1                 NE2 HIS A  46     1555   1555  2.21  
LINK        CU    CU A   1                 ND1 HIS A  44     1555   1555  2.00  
LINK        CU    CU A   1                 NE2 HIS A  61     1555   1555  2.08  
LINK        CU    CU A   1                 O   HOH A 167     1555   1555  2.26  
LINK        ZN    ZN A 152                 OD1 ASP A  81     1555   1555  2.00  
LINK        ZN    ZN A 152                 ND1 HIS A  78     1555   1555  2.06  
LINK        ZN    ZN A 152                 ND1 HIS A  69     1555   1555  2.07  
LINK        ZN    ZN A 152                 ND1 HIS A  61     1555   1555  2.04  
LINK        CU    CU B 152                 ND1 HIS B  44     1555   1555  2.02  
LINK        CU    CU B 152                 O   HOH B 159     1555   1555  2.40  
LINK        CU    CU B 152                 O   HOH B 154     1555   1555  2.49  
LINK        CU    CU B 152                 NE2 HIS B 118     1555   1555  2.07  
LINK        CU    CU B 152                 NE2 HIS B  61     1555   1555  2.08  
LINK        CU    CU B 152                 NE2 HIS B  46     1555   1555  2.20  
LINK        ZN    ZN B 153                 ND1 HIS B  69     1555   1555  2.04  
LINK        ZN    ZN B 153                 ND1 HIS B  78     1555   1555  2.00  
LINK        ZN    ZN B 153                 OD1 ASP B  81     1555   1555  1.97  
LINK        ZN    ZN B 153                 ND1 HIS B  61     1555   1555  2.02  
SITE     1   A  9 HIS A  44  HIS A  46  HIS A  61  HIS A 118                    
SITE     2   A  9 HIS A  69  HIS A  78  ASP A  81   CU A   1                    
SITE     3   A  9  ZN A 152                                                     
SITE     1   B  9 HIS B  44  HIS B  46  HIS B  61  HIS B 118                    
SITE     2   B  9 HIS B  69  HIS B  78  ASP B  81   CU B 152                    
SITE     3   B  9  ZN B 153                                                     
SITE     1 AC1  5 HIS A  44  HIS A  46  HIS A  61  HIS A 118                    
SITE     2 AC1  5 HOH A 167                                                     
SITE     1 AC2  4 HIS A  61  HIS A  69  HIS A  78  ASP A  81                    
SITE     1 AC3  6 HIS B  44  HIS B  46  HIS B  61  HIS B 118                    
SITE     2 AC3  6 HOH B 154  HOH B 159                                          
SITE     1 AC4  4 HIS B  61  HIS B  69  HIS B  78  ASP B  81                    
CRYST1   73.450   68.940   58.760  90.00  90.00  90.00 P 21 21 21    8          
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      0.013615  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014505  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017018        0.00000                         
MTRIX1   1  0.987830 -0.010290 -0.155220        1.43777    1                    
MTRIX2   1 -0.008360 -0.999880  0.013070       33.15571    1                    
MTRIX3   1 -0.155330 -0.011610 -0.987790       17.07902    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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