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Entry: 1DSW
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HEADER    OXIDOREDUCTASE                          10-JAN-00   1DSW              
TITLE     THE SOLUTION STRUCTURE OF A MONOMERIC, REDUCED FORM OF                
TITLE    2 HUMAN COPPER, ZINC SUPEROXIDE DISMUTASE BEARING THE SAME             
TITLE    3 CHARGE AS THE NATIVE PROTEIN                                         
CAVEAT     1DSW    ONE RESIDUE HAS INCORRECT CHIRALITY                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE (CU-ZN);                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: M4SOD IS A MONOMERIC VARIANT OF HUMAN SOD. THE             
COMPND   5 MUTANT IS STUDIED IN THE REDUCED FORM, EACH MOLECULE                 
COMPND   6 CONTAINS A CU(I) AND A ZN(II) IONS.;                                 
COMPND   7 EC: 1.15.1.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 OTHER_DETAILS: COPPER, ZINC SUPEROXIDE DISMUTASE (SOD) IS            
COMPND  11 AN ENZYME WHICH CATALYZES THE DISMUTATION OF SUPEROXIDE              
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: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PBR322                                    
KEYWDS    REDUCED COPPER-ZINC-PROTEIN, BETA BARREL, SINGLE ALPHA                
KEYWDS   2 HELIX, OXIDOREDUCTASE                                                
EXPDTA    SOLUTION NMR                                                          
AUTHOR    L.BANCI,I.BERTINI,R.DEL CONTE,R.FADIN,S.MANGANI,M.S.VIEZZOLI          
REVDAT   2   24-FEB-09 1DSW    1       VERSN                                    
REVDAT   1   22-MAR-00 1DSW    0                                                
JRNL        AUTH   L.BANCI,I.BERTINI,R.DEL CONTE,R.FADIN,S.MANGANI,             
JRNL        AUTH 2 M.S.VIEZZOLI                                                 
JRNL        TITL   THE SOLUTION STRUCTURE OF A MONOMERIC, REDUCED               
JRNL        TITL 2 FORM OF HUMAN COPPER,ZINC SUPEROXIDE DISMUTASE               
JRNL        TITL 3 BEARING THE SAME CHARGE AS THE NATIVE PROTEIN.               
JRNL        REF    J.BIOL.INORG.CHEM.            V.   4   795 1999              
JRNL        REFN                   ISSN 0949-8257                               
JRNL        PMID   10631612                                                     
JRNL        DOI    10.1007/S007750050353                                        
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : AMBER 4.0                                            
REMARK   3   AUTHORS     : PEALRMAN, DA, ET AL. (1991)                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: INTENSITIES OF DIPOLAR                    
REMARK   3  CONNECTIVITIES IN 3D NOESY-HSQC, 3D HNHA AND 2D NOESY WERE          
REMARK   3  MEASURED WITH THE INTEGRATION ROUTINES OF THE PROGRAM XEASY.        
REMARK   3  PEAK VOLUMES WERE CONVERTED INTO UPPER DISTANCE LIMITS BY           
REMARK   3  FOLLOWING THE METHODOLOGY OF THE PROGRAM CALIBA. 3JHNHA             
REMARK   3  COUPLING CONSTANTS WERE OBTAINED FROM THE RATIO BETWEEN THE         
REMARK   3  INTENSITY OF THE DIAGONAL PEAK AND THAT OF THE CROSS PEAK OF        
REMARK   3  THE 3D HNHA EXPERIMENT. THE 3D STRUCTURE WAS CALCULATED WITH        
REMARK   3  THE PROGRAM DYANA; THE FINAL DYANA FAMILY WAS FORMED BY THE 36      
REMARK   3  CONFORMERS WITH THE LOWEST TARGET FUNCTION. REFINEMENT WAS          
REMARK   3  PERFORMED THROUGH RESTRAINED ENERGY MINIMIZATION WITH THE           
REMARK   3  SANDER MODULE OF THE PROGRAM AMBER. NOESY CROSS PEAKS WERE          
REMARK   3  BACK -CALCULATED ON THE FINAL STRUCTURE WITH THE PROGRAM CORMA.     
REMARK   4                                                                      
REMARK   4 1DSW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB010336.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298.00                             
REMARK 210  PH                             : 5.00                               
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : ATMOSPHERIC ATM                    
REMARK 210  SAMPLE CONTENTS                : 2MM M4SOD FULLY ENRICHED IN        
REMARK 210                                   15N; 20MM PHOSPHATE BUFFER PH      
REMARK 210                                   5.0; 90% H2O, 10% D2O. THE         
REMARK 210                                   PROTEIN WAS REDUCED WITH           
REMARK 210                                   SODIUM ISOASCORBATE UNDER          
REMARK 210                                   UNAEROBIC CONDITIONS.              
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D 15N NOESY-HSQC, 3D HNHA,        
REMARK 210                                   2D NOESY                           
REMARK 210  SPECTROMETER FIELD STRENGTH    : 800 MHZ, 600 MHZ                   
REMARK 210  SPECTROMETER MODEL             : AVANCE                             
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : XWINNMR 2.1, CALIBA 1.5,           
REMARK 210                                   DYANA 1.4, CORMA                   
REMARK 210   METHOD USED                   : THE NMR STRUCTURE CALCULATION      
REMARK 210                                   PROGRAM USED DYANA THAT USES       
REMARK 210                                   SIMULATED ANNEALING COMBINED       
REMARK 210                                   WITH MOLECULAR DYNAMICS IN         
REMARK 210                                   TORSION ANGLE SPACE (TORSION       
REMARK 210                                   ANGLE DYNAMICS)                    
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : NULL                               
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 1                                  
REMARK 210 CONFORMERS, SELECTION CRITERIA  : NULL                               
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
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    GLU A  24     -169.37   -174.91                                   
REMARK 500    GLU A  50      -77.11   -163.69                                   
REMARK 500    GLU A  51      -44.96     62.20                                   
REMARK 500    ALA A  55      -50.48   -120.56                                   
REMARK 500    THR A  58      -72.16    -79.06                                   
REMARK 500    SER A  59       43.48   -100.28                                   
REMARK 500    PRO A  62     -175.24    -65.14                                   
REMARK 500    LEU A  67      -80.72   -144.16                                   
REMARK 500    LYS A  75      -53.59   -146.35                                   
REMARK 500    VAL A  81      -49.87    171.44                                   
REMARK 500    SER A  98       95.23   -166.31                                   
REMARK 500    ASP A 109      -67.48    -23.31                                   
REMARK 500    SER A 111       66.85     33.55                                   
REMARK 500    ARG A 115      142.67    -35.83                                   
REMARK 500    ARG A 143       70.72     52.99                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    HIS A  43         0.11    SIDE_CHAIN                              
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     ALA A   1       122.0                     ALPHA-CARBON           
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                              CU A 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 151.2                                              
REMARK 620 3 HIS A 120   NE2  81.4 110.4                                        
REMARK 620 N                    1     2                                         
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  71   ND1  97.6                                              
REMARK 620 3 HIS A  80   ND1 104.8 118.2                                        
REMARK 620 4 ASP A  83   OD1  85.7 121.8 116.8                                  
REMARK 620 5 ASP A  83   OD2 150.7  91.9  94.8  65.9                            
REMARK 620 N                    1     2     3     4                             
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 154                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155                  
DBREF  1DSW A    1   153  UNP    P00441   SODC_HUMAN       2    154             
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 HIS VAL HIS 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 SER ILE ILE GLY ARG THR LEU          
SEQRES  10 A  153  VAL VAL HIS 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 LYS ILE GLY LYS ALA GLN                      
HET     CU  A 154       1                                                       
HET     ZN  A 155       1                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
FORMUL   2   CU    CU 2+                                                        
FORMUL   3   ZN    ZN 2+                                                        
HELIX    1   1 ASN A  131  GLY A  138  1                                   8    
SHEET    1   A 5 VAL A  94  ASP A 101  0                                        
SHEET    2   A 5 VAL A  29  LYS A  36 -1  N  VAL A  29   O  ASP A 101           
SHEET    3   A 5 GLN A  15  GLN A  22 -1  O  GLN A  15   N  LYS A  36           
SHEET    4   A 5 LYS A   3  LYS A   9 -1  O  ALA A   4   N  PHE A  20           
SHEET    5   A 5 ILE A 149  LYS A 151 -1  N  GLY A 150   O  VAL A   5           
SHEET    1   B 4 ASP A  83  ALA A  89  0                                        
SHEET    2   B 4 GLY A  41  HIS A  48 -1  N  GLY A  41   O  ALA A  89           
SHEET    3   B 4 THR A 116  VAL A 119 -1  O  THR A 116   N  HIS A  48           
SHEET    4   B 4 ALA A 145  CYS A 146 -1  O  ALA A 145   N  VAL A 119           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.05  
LINK         ND1 HIS A  46                CU    CU A 154     1555   1555  2.13  
LINK         NE2 HIS A  48                CU    CU A 154     1555   1555  2.01  
LINK         ND1 HIS A  63                ZN    ZN A 155     1555   1555  2.10  
LINK         ND1 HIS A  71                ZN    ZN A 155     1555   1555  2.10  
LINK         ND1 HIS A  80                ZN    ZN A 155     1555   1555  2.14  
LINK         OD1 ASP A  83                ZN    ZN A 155     1555   1555  2.03  
LINK         OD2 ASP A  83                ZN    ZN A 155     1555   1555  1.99  
LINK         NE2 HIS A 120                CU    CU A 154     1555   1555  2.18  
SITE     1 AC1  5 HIS A  46  HIS A  48  HIS A  63  VAL A 118                    
SITE     2 AC1  5 HIS A 120                                                     
SITE     1 AC2  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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