GenomeNet

Database: PDB
Entry: 1P1V
LinkDB: 1P1V
Original site: 1P1V 
HEADER    OXIDOREDUCTASE                          14-APR-03   1P1V              
TITLE     CRYSTAL STRUCTURE OF FALS-ASSOCIATED HUMAN COPPER-ZINC                
TITLE    2 SUPEROXIDE DISMUTASE (CUZNSOD) MUTANT D125H TO 1.4A                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SOD1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: EG118;                                     
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: YEP351                                    
KEYWDS    BETA-BARREL, BOUND ANION AT COPPER SITE, CUZNSOD                      
KEYWDS   2 PEROXIDATION MECHANISM, OXIDOREDUCTASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.S.ELAM,K.MALEK,J.A.RODRIGUEZ,P.A.DOUCETTE,A.B.TAYLOR,               
AUTHOR   2 L.J.HAYWARD,D.E.CABELLI,J.S.VALENTINE,P.J.HART                       
REVDAT   2   24-FEB-09 1P1V    1       VERSN                                    
REVDAT   1   26-AUG-03 1P1V    0                                                
JRNL        AUTH   J.S.ELAM,K.MALEK,J.A.RODRIGUEZ,P.A.DOUCETTE,                 
JRNL        AUTH 2 A.B.TAYLOR,L.J.HAYWARD,D.E.CABELLI,J.S.VALENTINE,            
JRNL        AUTH 3 P.J.HART                                                     
JRNL        TITL   AN ALTERNATIVE MECHANISM OF BICARBONATE-MEDIATED             
JRNL        TITL 2 PEROXIDATION BY COPPER-ZINC SUPEROXIDE DISMUTASE:            
JRNL        TITL 3 RATES ENHANCED VIA PROPOSED ENZYME-ASSOCIATED                
JRNL        TITL 4 PEROXYCARBONATE INTERMEDIATE                                 
JRNL        REF    J.BIOL.CHEM.                  V. 278 21032 2003              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   12649272                                                     
JRNL        DOI    10.1074/JBC.M300484200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.9                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.147                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.146                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.212                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2899                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 94875                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.133                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 78424                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 3180                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 21                                            
REMARK   3   SOLVENT ATOMS      : 736                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 3936.00                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 0                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 35428                   
REMARK   3   NUMBER OF RESTRAINTS                     : 41292                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.011                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.028                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.030                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.055                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.071                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.015                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.004                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.053                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.083                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REDUCED FREE       
REMARK   3  R (NO CUTOFF) BY 4.1%                                               
REMARK   4                                                                      
REMARK   4 1P1V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB018909.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-JUN-01; 07-JUN-01               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : NSLS; NSLS                         
REMARK 200  BEAMLINE                       : X12B; X8C                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000; 1.2811                     
REMARK 200  MONOCHROMATOR                  : MIRRORS; MIRRORS                   
REMARK 200  OPTICS                         : MIRRORS; MIRRORS                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4; ADSC QUANTUM 4     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 95234                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY                : 6.910                              
REMARK 200  R MERGE                    (I) : 0.04800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 30.1600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.620                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: ZINC SULFATE, PEG MME 550, MES, PH       
REMARK 280  6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 278K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       71.54000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       71.54000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       35.22450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.57000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       35.22450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.57000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       71.54000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       35.22450            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       50.57000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       71.54000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       35.22450            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       50.57000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HOMODIMER. IN THE               
REMARK 300 ASYMMETRIC UNIT WE HAVE ONE HOMODIMER AND ONE MONOMER. THE           
REMARK 300 MONOMER'S DIMERIC PARTNER IS GENERATED THROUGH A                     
REMARK 300 CRYSTALLOGRAPHIC TWO FOLD AXIS AT THE DIMER INTERFACE.               
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: 2030 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -129.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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      -70.44900            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       71.54000            
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 A1057  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C1086  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     GLY A   129                                                      
REMARK 465     GLY A   130                                                      
REMARK 465     ASN A   131                                                      
REMARK 465     GLU A   132                                                      
REMARK 465     GLU A   133                                                      
REMARK 465     SER A   134                                                      
REMARK 465     THR A   135                                                      
REMARK 465     LYS B   128                                                      
REMARK 465     GLY B   129                                                      
REMARK 465     GLY B   130                                                      
REMARK 465     ASN B   131                                                      
REMARK 465     GLU B   132                                                      
REMARK 465     GLU B   133                                                      
REMARK 465     SER B   134                                                      
REMARK 465     THR B   135                                                      
REMARK 465     LYS B   136                                                      
REMARK 465     GLY C   129                                                      
REMARK 465     GLY C   130                                                      
REMARK 465     ASN C   131                                                      
REMARK 465     GLU C   132                                                      
REMARK 465     GLU C   133                                                      
REMARK 465     SER C   134                                                      
REMARK 465     THR C   135                                                      
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    ARG B  79   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP B  83   CB  -  CG  -  OD1 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ASP B  96   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG B 115   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG C  69   CD  -  NE  -  CZ  ANGL. DEV. =   9.4 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    ASN A  65       59.98   -147.63                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SO4 A 801   O1                                                     
REMARK 620 2 HIS A  46   ND1 102.9                                              
REMARK 620 3 HIS A  48   NE2 100.4 119.8                                        
REMARK 620 4 HIS A 120   NE2 104.1 101.3 125.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 203  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SO4 B 802   O2                                                     
REMARK 620 2 HIS B  46   ND1  98.8                                              
REMARK 620 3 HIS B  48   NE2 105.6 113.9                                        
REMARK 620 4 HIS B 120   NE2 110.6  98.9 125.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 205  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SO4 C 803   O1                                                     
REMARK 620 2 HIS C  46   ND1 102.3                                              
REMARK 620 3 HIS C  48   NE2 102.0 119.3                                        
REMARK 620 4 HIS C 120   NE2 104.1 100.4 125.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  63   ND1                                                    
REMARK 620 2 HIS A  71   ND1 102.2                                              
REMARK 620 3 HIS A  80   ND1 107.9 123.2                                        
REMARK 620 4 ASP A  83   OD1 105.2  98.1 118.0                                  
REMARK 620 5 ASP A  83   OD2 157.1  79.8  89.1  52.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 204  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  63   ND1                                                    
REMARK 620 2 HIS B  71   ND1 104.1                                              
REMARK 620 3 HIS B  80   ND1  99.3 122.8                                        
REMARK 620 4 ASP B  83   OD1 109.8  97.5 122.2                                  
REMARK 620 5 ASP B  83   OD2 163.2  78.6  92.8  53.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 206  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  63   ND1                                                    
REMARK 620 2 HIS C  71   ND1 105.7                                              
REMARK 620 3 HIS C  80   ND1 107.7 122.3                                        
REMARK 620 4 ASP C  83   OD1 104.2  99.4 115.8                                  
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 SO4 A 801                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 802                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 803                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 201                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 202                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 203                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 204                  
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 205                  
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 206                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AZV   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FALS-ASSOCIATED COPPER-ZINC SUPEROXIDE          
REMARK 900 DISMUTASE (CUZNSOD) MUTANT G37R                                      
REMARK 900 RELATED ID: 1OZU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FALS-ASSOCIATED COPPER-ZINC SUPEROXIDE          
REMARK 900 DISMUTASE (CUZNSOD) MUTANT S134N                                     
REMARK 900 RELATED ID: 1OZT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FALS-ASSOCIATED COPPER-ZINC SUPEROXIDE          
REMARK 900 DISMUTASE (CUZNSOD) MUTANT APO-H46R                                  
REMARK 900 RELATED ID: 1OEZ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FALS-ASSOCIATED COPPER-ZINC SUPEROXIDE          
REMARK 900 DISMUTASE (CUZNSOD) MUTANT ZN-LOADED H46R                            
DBREF  1P1V A    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1P1V B    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1P1V C    1   153  UNP    P00441   SODC_HUMAN       1    153             
SEQADV 1P1V CSX A  111  UNP  P00441    CYS   111 MODIFIED RESIDUE               
SEQADV 1P1V HIS A  125  UNP  P00441    ASP   125 ENGINEERED                     
SEQADV 1P1V CSX B  111  UNP  P00441    CYS   111 MODIFIED RESIDUE               
SEQADV 1P1V HIS B  125  UNP  P00441    ASP   125 ENGINEERED                     
SEQADV 1P1V CSX C  111  UNP  P00441    CYS   111 MODIFIED RESIDUE               
SEQADV 1P1V HIS C  125  UNP  P00441    ASP   125 ENGINEERED                     
SEQRES   1 A  153  ALA THR LYS ALA VAL CYS 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 PHE GLY 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 CSX ILE ILE GLY ARG THR LEU          
SEQRES  10 A  153  VAL VAL HIS GLU LYS ALA ASP HIS LEU GLY LYS GLY GLY          
SEQRES  11 A  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 A  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 B  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 B  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 B  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 B  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 B  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 B  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 B  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 B  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 B  153  SER LEU SER GLY ASP HIS CSX ILE ILE GLY ARG THR LEU          
SEQRES  10 B  153  VAL VAL HIS GLU LYS ALA ASP HIS LEU GLY LYS GLY GLY          
SEQRES  11 B  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 B  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 C  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 C  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 C  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 C  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 C  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 C  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 C  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 C  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 C  153  SER LEU SER GLY ASP HIS CSX ILE ILE GLY ARG THR LEU          
SEQRES  10 C  153  VAL VAL HIS GLU LYS ALA ASP HIS LEU GLY LYS GLY GLY          
SEQRES  11 C  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 C  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
MODRES 1P1V CSX A  111  CYS  S-OXY CYSTEINE                                     
MODRES 1P1V CSX B  111  CYS  S-OXY CYSTEINE                                     
MODRES 1P1V CSX C  111  CYS  S-OXY CYSTEINE                                     
HET    CSX  A 111       7                                                       
HET    CSX  B 111       7                                                       
HET    CSX  C 111       7                                                       
HET    SO4  A 801       5                                                       
HET    SO4  B 802       5                                                       
HET    SO4  C 803       5                                                       
HET     ZN  A 201       1                                                       
HET     ZN  A 202       1                                                       
HET     ZN  B 203       1                                                       
HET     ZN  B 204       1                                                       
HET     ZN  C 205       1                                                       
HET     ZN  C 206       1                                                       
HETNAM     CSX S-OXY CYSTEINE                                                   
HETNAM     SO4 SULFATE ION                                                      
HETNAM      ZN ZINC ION                                                         
FORMUL   1  CSX    3(C3 H7 N O3 S)                                              
FORMUL   4  SO4    3(O4 S 2-)                                                   
FORMUL   7   ZN    6(ZN 2+)                                                     
FORMUL  13  HOH   *736(H2 O)                                                    
HELIX    1   1 CYS A   57  GLY A   61  5                                   5    
HELIX    2   2 SER A  107  CSX A  111  5                                   5    
HELIX    3   3 ALA B   55  GLY B   61  5                                   7    
HELIX    4   4 CYS C   57  GLY C   61  5                                   5    
HELIX    5   5 SER C  107  CSX C  111  5                                   5    
SHEET    1   A 5 ALA A  95  ASP A 101  0                                        
SHEET    2   A 5 VAL A  29  LYS A  36 -1  N  ILE A  35   O  ALA A  95           
SHEET    3   A 5 GLN A  15  GLU A  21 -1  N  ASN A  19   O  TRP A  32           
SHEET    4   A 5 LYS A   3  LEU A   8 -1  N  ALA A   4   O  PHE A  20           
SHEET    5   A 5 GLY A 150  ILE A 151 -1  O  GLY A 150   N  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  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    4   B 4 ARG A 143  VAL A 148 -1  O  ALA A 145   N  VAL A 119           
SHEET    1   C 5 ALA B  95  ASP B 101  0                                        
SHEET    2   C 5 VAL B  29  LYS B  36 -1  N  ILE B  35   O  ALA B  95           
SHEET    3   C 5 GLN B  15  GLN B  22 -1  N  ASN B  19   O  TRP B  32           
SHEET    4   C 5 THR B   2  LEU B   8 -1  N  THR B   2   O  GLN B  22           
SHEET    5   C 5 GLY B 150  ALA B 152 -1  O  GLY B 150   N  VAL B   5           
SHEET    1   D 4 ASP B  83  ALA B  89  0                                        
SHEET    2   D 4 GLY B  41  HIS B  48 -1  N  GLY B  41   O  ALA B  89           
SHEET    3   D 4 THR B 116  HIS B 120 -1  O  THR B 116   N  HIS B  48           
SHEET    4   D 4 ARG B 143  VAL B 148 -1  O  ALA B 145   N  VAL B 119           
SHEET    1   E 5 ALA C  95  ASP C 101  0                                        
SHEET    2   E 5 VAL C  29  LYS C  36 -1  N  ILE C  35   O  ALA C  95           
SHEET    3   E 5 GLN C  15  GLU C  21 -1  N  GLU C  21   O  LYS C  30           
SHEET    4   E 5 LYS C   3  LEU C   8 -1  N  LEU C   8   O  GLY C  16           
SHEET    5   E 5 GLY C 150  ILE C 151 -1  O  GLY C 150   N  VAL C   5           
SHEET    1   F 4 ASP C  83  ALA C  89  0                                        
SHEET    2   F 4 GLY C  41  HIS C  48 -1  N  GLY C  41   O  ALA C  89           
SHEET    3   F 4 THR C 116  HIS C 120 -1  O  THR C 116   N  HIS C  48           
SHEET    4   F 4 ARG C 143  VAL C 148 -1  O  GLY C 147   N  LEU C 117           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.10  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.06  
SSBOND   3 CYS C   57    CYS C  146                          1555   1555  2.12  
LINK        ZN    ZN A 201                 O1  SO4 A 801     1555   1555  1.95  
LINK        ZN    ZN B 203                 O2  SO4 B 802     1555   1555  1.92  
LINK        ZN    ZN C 205                 O1  SO4 C 803     1555   1555  1.95  
LINK        ZN    ZN A 201                 ND1 HIS A  46     1555   1555  2.01  
LINK        ZN    ZN A 201                 NE2 HIS A  48     1555   1555  2.02  
LINK        ZN    ZN A 201                 NE2 HIS A 120     1555   1555  2.03  
LINK        ZN    ZN A 202                 ND1 HIS A  63     1555   1555  2.02  
LINK        ZN    ZN A 202                 ND1 HIS A  71     1555   1555  2.04  
LINK        ZN    ZN A 202                 ND1 HIS A  80     1555   1555  2.03  
LINK        ZN    ZN A 202                 OD1 ASP A  83     1555   1555  1.95  
LINK        ZN    ZN B 203                 ND1 HIS B  46     1555   1555  2.04  
LINK        ZN    ZN B 203                 NE2 HIS B  48     1555   1555  2.02  
LINK        ZN    ZN B 203                 NE2 HIS B 120     1555   1555  1.92  
LINK        ZN    ZN B 204                 ND1 HIS B  63     1555   1555  2.05  
LINK        ZN    ZN B 204                 ND1 HIS B  71     1555   1555  2.07  
LINK        ZN    ZN B 204                 ND1 HIS B  80     1555   1555  2.01  
LINK        ZN    ZN B 204                 OD1 ASP B  83     1555   1555  1.76  
LINK        ZN    ZN C 205                 ND1 HIS C  46     1555   1555  2.02  
LINK        ZN    ZN C 205                 NE2 HIS C  48     1555   1555  2.02  
LINK        ZN    ZN C 205                 NE2 HIS C 120     1555   1555  2.03  
LINK        ZN    ZN C 206                 ND1 HIS C  63     1555   1555  2.03  
LINK        ZN    ZN C 206                 ND1 HIS C  71     1555   1555  2.02  
LINK        ZN    ZN C 206                 ND1 HIS C  80     1555   1555  1.98  
LINK        ZN    ZN C 206                 OD1 ASP C  83     1555   1555  1.96  
LINK         C   HIS A 110                 N   CSX A 111     1555   1555  1.33  
LINK         C   CSX A 111                 N   ILE A 112     1555   1555  1.33  
LINK        ZN    ZN A 202                 OD2 ASP A  83     1555   1555  2.75  
LINK         C   HIS B 110                 N   CSX B 111     1555   1555  1.32  
LINK         C   CSX B 111                 N   ILE B 112     1555   1555  1.35  
LINK        ZN    ZN B 204                 OD2 ASP B  83     1555   1555  2.65  
LINK         C   HIS C 110                 N   CSX C 111     1555   1555  1.33  
LINK         C   CSX C 111                 N   ILE C 112     1555   1555  1.35  
SITE     1 AC1 12 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC1 12 THR A 137  ARG A 143   ZN A 201  HOH A 823                    
SITE     3 AC1 12 HOH A 852  HOH A 868  HOH A 877  ASN C  26                    
SITE     1 AC2 10 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     2 AC2 10 THR B 137  ARG B 143   ZN B 203  HOH B 881                    
SITE     3 AC2 10 HOH B 897  HOH B 899                                          
SITE     1 AC3 12 ASN A  26  HIS C  46  HIS C  48  HIS C  63                    
SITE     2 AC3 12 HIS C 120  THR C 137  ARG C 143   ZN C 205                    
SITE     3 AC3 12 HOH C 819  HOH C 826  HOH C 838  HOH C 862                    
SITE     1 AC4  5 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC4  5 SO4 A 801                                                     
SITE     1 AC5  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC6  5 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     2 AC6  5 SO4 B 802                                                     
SITE     1 AC7  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     1 AC8  5 HIS C  46  HIS C  48  HIS C  63  HIS C 120                    
SITE     2 AC8  5 SO4 C 803                                                     
SITE     1 AC9  4 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
CRYST1   70.449  101.140  143.080  90.00  90.00  90.00 C 2 2 21     24          
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      0.014195  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009887  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006989        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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