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Database: PDB
Entry: 1PZS
LinkDB: 1PZS
Original site: 1PZS 
HEADER    OXIDOREDUCTASE, METAL BINDING PROTEIN   14-JUL-03   1PZS              
TITLE     CRYSTAL STRUCTURE OF A CU-ZN SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM  
TITLE    2 TUBERCULOSIS AT 1.63 RESOLUTION                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: SEQUENCE DATABASE RESIDUES 33-240;                         
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 GENE: SODC OR RV0432 OR MT0447 OR MTCY22G10.29;                      
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: QC871;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PUC19                                     
KEYWDS    CU-PROTEIN, BETA CORE, ANTIOXIDANT, METAL BINDING, GREEK KEY BETA     
KEYWDS   2 BARREL, OXIDOREDUCTASE, METAL BINDING PROTEIN                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.DJINOVIC-CARUGO,L.SPAGNOLO,I.TORO                                   
REVDAT   4   13-JUL-11 1PZS    1       VERSN                                    
REVDAT   3   24-FEB-09 1PZS    1       VERSN                                    
REVDAT   2   17-AUG-04 1PZS    1       JRNL                                     
REVDAT   1   27-JUL-04 1PZS    0                                                
JRNL        AUTH   L.SPAGNOLO,I.TORO,M.D'ORAZIO,P.O'NEILL,J.Z.PEDERSEN,         
JRNL        AUTH 2 O.CARUGO,G.ROTILIO,A.BATTISTONI,K.DJINOVIC-CARUGO            
JRNL        TITL   UNIQUE FEATURES OF THE SODC-ENCODED SUPEROXIDE DISMUTASE     
JRNL        TITL 2 FROM MYCOBACTERIUM TUBERCULOSIS, A FULLY FUNCTIONAL          
JRNL        TITL 3 COPPER-CONTAINING ENZYME LACKING ZINC IN THE ACTIVE SITE.    
JRNL        REF    J.BIOL.CHEM.                  V. 279 33447 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15155722                                                     
JRNL        DOI    10.1074/JBC.M404699200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.63 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 1.63                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 19233                          
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) : 0.152                           
REMARK   3   R VALUE            (WORKING SET) : 0.150                           
REMARK   3   FREE R VALUE                     : 0.190                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1013                            
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) : 1.63                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.68                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1146                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3390                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 61                           
REMARK   3   BIN FREE R VALUE                    : 0.3070                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1204                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 252                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.84                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.82000                                              
REMARK   3    B22 (A**2) : -0.52000                                             
REMARK   3    B33 (A**2) : 1.14000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.19000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.083         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.087         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.054         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.561         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1248 ; 0.010 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1108 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1695 ; 1.356 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2593 ; 1.858 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   170 ; 6.233 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   198 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1420 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   227 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   208 ; 0.192 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1242 ; 0.253 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):   648 ; 0.084 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   158 ; 0.154 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    12 ; 0.132 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    69 ; 0.328 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    25 ; 0.119 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   841 ; 0.831 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1348 ; 1.484 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   407 ; 2.123 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   347 ; 3.475 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1PZS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019736.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-NOV-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID13                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9755                             
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20248                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.634                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.950                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 3.620                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.5400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.27                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.170                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1JCV.PDB                                   
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, AMMONIUM SULFATE, ZINC         
REMARK 280  CHLORIDE, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 20K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       35.02000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.21000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       35.02000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       29.21000            
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: THE BIOLOGICAL ASSEMBLY IS A DIMER GENERATED BY THE TWO      
REMARK 300 FOLD AXIS: -X, Y, -Z                                                 
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,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 3270 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 215  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     CYS A   -36                                                      
REMARK 465     SER A   -35                                                      
REMARK 465     SER A   -34                                                      
REMARK 465     PRO A   -33                                                      
REMARK 465     GLN A   -32                                                      
REMARK 465     HIS A   -31                                                      
REMARK 465     ALA A   -30                                                      
REMARK 465     SER A   -29                                                      
REMARK 465     THR A   -28                                                      
REMARK 465     VAL A   -27                                                      
REMARK 465     PRO A   -26                                                      
REMARK 465     GLY A   -25                                                      
REMARK 465     THR A   -24                                                      
REMARK 465     THR A   -23                                                      
REMARK 465     PRO A   -22                                                      
REMARK 465     SER A   -21                                                      
REMARK 465     ILE A   -20                                                      
REMARK 465     TRP A   -19                                                      
REMARK 465     THR A   -18                                                      
REMARK 465     GLY A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     PRO A   -15                                                      
REMARK 465     ALA A   -14                                                      
REMARK 465     PRO A   -13                                                      
REMARK 465     SER A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     LEU A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     ASP A    -6                                                      
REMARK 465     GLU A    -5                                                      
REMARK 465     GLU A    -4                                                      
REMARK 465     SER A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ALA A     0                                                      
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   NE2  HIS A    75     O    HOH A   448              1.98            
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    LYS A 120     -170.33     67.50                                   
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 322        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH A 338        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH A 394        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH A 411        DISTANCE =  5.41 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 172  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  47   ND1                                                    
REMARK 620 2 HIS A  49   NE2 151.0                                              
REMARK 620 3 HIS A 126   NE2  95.8 113.1                                        
REMARK 620 4 HOH A 448   O    81.8 102.1  86.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 172                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JCV   RELATED DB: PDB                                   
REMARK 900 REDUCED BRIDGE-BROKEN YEAST CU/ZN SUPEROXIDE DISMUTASE LOW           
REMARK 900 TEMPERATURE (-180C) STRUCTURE                                        
REMARK 900 RELATED ID: 1BZO   RELATED DB: PDB                                   
REMARK 900 THREE-DIMENSIONAL STRUCTURE OF PROKARYOTIC CU, ZN                    
REMARK 900 SUPEROXIDE DISMUTASE FROM P. LEIOGNATHI, SOLVED BY X-RAY             
REMARK 900 CRYSTALLOGRAPHY.                                                     
REMARK 900 RELATED ID: 1ESO   RELATED DB: PDB                                   
REMARK 900 MONOMERIC CU, ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI          
REMARK 900 RELATED ID: 1XSO   RELATED DB: PDB                                   
REMARK 900 THREE-DIMENSIONAL STRUCTURE OF XENOPUS LAEVIS CU, ZN                 
REMARK 900 SUPEROXIDE DISMUTASE B DETERMINED BY X-RAY CRYSTALLOGRAPHY           
REMARK 900 AT 1.5 ANGSTROM RESOLUTION.                                          
REMARK 900 RELATED ID: 1EQW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF SALMONELLA TYPHIMURIUM CU, ZN                   
REMARK 900 SUPEROXIDE DISMUTASE                                                 
DBREF  1PZS A  -34   171  UNP    P0A608   SODC_MYCTU      33    240             
SEQRES   1 A  208  CYS SER SER PRO GLN HIS ALA SER THR VAL PRO GLY THR          
SEQRES   2 A  208  THR PRO SER ILE TRP THR GLY SER PRO ALA PRO SER GLY          
SEQRES   3 A  208  LEU SER GLY HIS ASP GLU GLU SER PRO GLY ALA GLN SER          
SEQRES   4 A  208  LEU THR SER THR LEU THR ALA PRO ASP GLY THR LYS VAL          
SEQRES   5 A  208  ALA THR ALA LYS PHE GLU PHE ALA ASN GLY TYR ALA THR          
SEQRES   6 A  208  VAL THR ILE ALA THR THR GLY VAL GLY LYS LEU THR PRO          
SEQRES   7 A  208  GLY PHE HIS GLY LEU HIS ILE HIS GLN VAL GLY LYS CYS          
SEQRES   8 A  208  GLU PRO ASN SER VAL ALA PRO THR GLY GLY ALA PRO GLY          
SEQRES   9 A  208  ASN PHE LEU SER ALA GLY GLY HIS TYR HIS VAL PRO GLY          
SEQRES  10 A  208  HIS THR GLY THR PRO ALA SER GLY ASP LEU ALA SER LEU          
SEQRES  11 A  208  GLN VAL ARG GLY ASP GLY SER ALA MET LEU VAL THR THR          
SEQRES  12 A  208  THR ASP ALA PHE THR MET ASP ASP LEU LEU SER GLY ALA          
SEQRES  13 A  208  LYS THR ALA ILE ILE ILE HIS ALA GLY ALA ASP ASN PHE          
SEQRES  14 A  208  ALA ASN ILE PRO PRO GLU ARG TYR VAL GLN VAL ASN GLY          
SEQRES  15 A  208  THR PRO GLY PRO ASP GLU THR THR LEU THR THR GLY ASP          
SEQRES  16 A  208  ALA GLY LYS ARG VAL ALA CYS GLY VAL ILE GLY SER GLY          
HET     CU  A 172       1                                                       
HETNAM      CU COPPER (II) ION                                                  
FORMUL   2   CU    CU 2+                                                        
FORMUL   3  HOH   *252(H2 O)                                                    
HELIX    1   1 PHE A   69  GLY A   73  5                                   5    
HELIX    2   2 THR A  111  SER A  117  1                                   7    
HELIX    3   3 ASP A  150  GLY A  157  1                                   8    
SHEET    1   A 4 SER A   2  THR A   8  0                                        
SHEET    2   A 4 LYS A  14  ALA A  23 -1  O  ALA A  16   N  LEU A   7           
SHEET    3   A 4 TYR A  26  THR A  33 -1  O  THR A  28   N  GLU A  21           
SHEET    4   A 4 MET A 102  THR A 107 -1  O  THR A 107   N  ALA A  27           
SHEET    1   B 2 GLY A  42  HIS A  44  0                                        
SHEET    2   B 2 LEU A  93  VAL A  95 -1  O  VAL A  95   N  GLY A  42           
SHEET    1   C 3 LEU A  46  HIS A  49  0                                        
SHEET    2   C 3 ALA A 122  HIS A 126 -1  O  ALA A 122   N  HIS A  49           
SHEET    3   C 3 ARG A 162  VAL A 167 -1  O  GLY A 166   N  ILE A 123           
SSBOND   1 CYS A   54    CYS A  165                          1555   1555  2.06  
LINK        CU    CU A 172                 ND1 HIS A  47     1555   1555  2.07  
LINK        CU    CU A 172                 NE2 HIS A  49     1555   1555  2.05  
LINK        CU    CU A 172                 NE2 HIS A 126     1555   1555  2.04  
LINK        CU    CU A 172                 O   HOH A 448     1555   1555  1.93  
CISPEP   1 THR A   84    PRO A   85          0        -0.65                     
SITE     1 AC1  5 HIS A  47  HIS A  49  HIS A  75  HIS A 126                    
SITE     2 AC1  5 HOH A 448                                                     
CRYST1   70.040   58.420   51.390  90.00 126.99  90.00 C 1 2 1       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      0.014278  0.000000  0.010755        0.00000                         
SCALE2      0.000000  0.017117  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.024362        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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