GenomeNet

Database: PDB
Entry: 2WYT
LinkDB: 2WYT
Original site: 2WYT 
HEADER    OXIDOREDUCTASE                          20-NOV-09   2WYT              
TITLE     1.0 A RESOLUTION STRUCTURE OF L38V SOD1 MUTANT                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, F;                                                         
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 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 4932                                        
KEYWDS    OXIDOREDUCTASE, DISEASE MUTATION, AMYOTROPHIC LATERAL SCLEROSIS,      
KEYWDS   2 ANTIOXIDANT                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.V.ANTONYUK,R.W.STRANGE,S.S.HASNAIN                                  
REVDAT   1   27-OCT-10 2WYT    0                                                
JRNL        AUTH   S.V.ANTONYUK,R.W.STRANGE,S.S.HASNAIN                         
JRNL        TITL   STRUCTURAL DISCOVERY OF SMALL MOLECULE BINDING SITES IN      
JRNL        TITL 2 CU-ZN HUMAN SUPEROXIDE DISMUTASE FAMILIAL AMYOTROPHIC        
JRNL        TITL 3 LATERAL SCLEROSIS MUTANTS PROVIDES INSIGHTS FOR LEAD         
JRNL        TITL 4 OPTIMIZATION.                                                
JRNL        REF    J.MED.CHEM.                   V.  53  1402 2010              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   20067275                                                     
JRNL        DOI    10.1021/JM9017948                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0106                                      
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) : 1.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.08                          
REMARK   3   NUMBER OF REFLECTIONS             : 129879                         
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) : 0.12501                         
REMARK   3   R VALUE            (WORKING SET) : 0.12388                         
REMARK   3   FREE R VALUE                     : 0.14677                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) :  5.0                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 6887                            
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) : 0.999                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.025                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7650                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.285                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 404                          
REMARK   3   BIN FREE R VALUE                    : 0.283                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4721                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 62                                      
REMARK   3   SOLVENT ATOMS            : 624                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 6.5                            
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.343                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.18                                                
REMARK   3    B22 (A**2) : -0.35                                                
REMARK   3    B33 (A**2) : -0.01                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -0.95                                                
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.022         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.023         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.017         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.700         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.982                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.975                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2600 ; 0.018 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2245 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3569 ; 1.838 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5271 ; 1.533 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   381 ; 6.980 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   119 ;38.841 ;26.218       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   451 ;11.703 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;10.806 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   384 ; 0.123 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3060 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   520 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1652 ; 1.652 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   716 ; 0.545 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2671 ; 2.381 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   948 ; 3.178 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   862 ; 4.485 ; 4.500       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  4845 ; 1.351 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS. U VALUES  REFINED INDIVIDUALLY.                  
REMARK   4                                                                      
REMARK   4 2WYT COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-NOV-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-41776.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-FEB-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.75                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX10.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : SI111                              
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 136867                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.00                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 5.4                                
REMARK 200  R MERGE                    (I) : 0.12                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.00                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.9                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.36                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.20                               
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 2C9V                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 150 MM NACL, 2-3M AMMONIUM               
REMARK 280  SULPHATE, 100 MM NA ACETATE BUFFER PH 4.75                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       33.67250            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -222.8 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, LEU  39 TO VAL                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, LEU  39 TO VAL                        
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU F 100    OE1  OE2                                            
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   HD1  HIS F    63    ZN     ZN F   155              1.16            
REMARK 500   HD1  HIS A    71    ZN     ZN A   155              1.18            
REMARK 500   HD1  HIS A    63    ZN     ZN A   155              1.19            
REMARK 500   HD1  HIS F    71    ZN     ZN F   155              1.24            
REMARK 500   HD1  HIS A    80    ZN     ZN A   155              1.29            
REMARK 500   HD1  HIS F    80    ZN     ZN F   155              1.33            
REMARK 500   O    HOH A  2326     O    HOH F  2131              1.48            
REMARK 500  HH11  ARG F    69     O    HOH F  2158              1.58            
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  26       16.69     55.25                                   
REMARK 500    LYS F 136      -55.07   -121.40                                   
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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
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: (10X,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    THR A   2        22.7      L          L   OUTSIDE RANGE           
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 154A ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 120   NE2                                                    
REMARK 620 2 HIS A  48   NE2 117.8                                              
REMARK 620 N                    1                                               
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 105.1                                              
REMARK 620 3 HIS A  80   ND1 110.6 120.7                                        
REMARK 620 4 ASP A  83   OD1 104.6 100.1 114.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 154A ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  48   NE2                                                    
REMARK 620 2 HIS F 120   NE2 118.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  63   ND1                                                    
REMARK 620 2 ASP F  83   OD1 106.5                                              
REMARK 620 3 HIS F  80   ND1 110.5 115.5                                        
REMARK 620 4 HIS F  71   ND1 104.8  98.5 119.5                                  
REMARK 620 N                    1     2     3                                   
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 120   NE2                                                    
REMARK 620 2 HIS A  46   ND1 102.3                                              
REMARK 620 3 HIS A  48   NE2 118.5 138.7                                        
REMARK 620 N                    1     2                                         
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  63   NE2                                                    
REMARK 620 2 HIS A 120   NE2 152.8                                              
REMARK 620 3 SO4 A 161   O1   69.2  85.3                                        
REMARK 620 4 HIS A  46   ND1 105.0  90.9 146.3                                  
REMARK 620 5 HIS A  48   NE2 106.5  86.4 100.0 113.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU F 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  48   NE2                                                    
REMARK 620 2 HIS F 120   NE2 118.9                                              
REMARK 620 3 HIS F  46   ND1 139.0 101.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU F 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  48   NE2                                                    
REMARK 620 2 HIS F 120   NE2  98.8                                              
REMARK 620 3 SO4 F 156   O1  104.7  89.2                                        
REMARK 620 4 HIS F  46   ND1 120.2  96.7 133.0                                  
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 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A 154A                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 157                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 158                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 160                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 161                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 163                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU F 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN F 154A                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN F 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL F 160                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1OEZ   RELATED DB: PDB                                   
REMARK 900  ZN HIS46ARG MUTANT OF HUMAN CU, ZN                                  
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 1PTZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN CU, ZN                               
REMARK 900  SUPEROXIDE DISMUTASE,FAMILIAL AMYOTROPHIC                           
REMARK 900  LATERAL SCLEROSIS (FALS) MUTANT H43R                                
REMARK 900 RELATED ID: 1AZV   RELATED DB: PDB                                   
REMARK 900  FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)                            
REMARK 900 RELATED ID: 1HL4   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF APO TYPE HUMAN CU, ZN                              
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 1OZU   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF FAMILIAL ALS MUTANT                            
REMARK 900  S134N OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (                         
REMARK 900  CUZNSOD) TO 1.3A RESOLUTION                                         
REMARK 900 RELATED ID: 2VR6   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF G85R ALS MUTANT OF                             
REMARK 900  HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD)                          
REMARK 900  AT 1.3 A RESOLUTION                                                 
REMARK 900 RELATED ID: 2C9V   RELATED DB: PDB                                   
REMARK 900  ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN                          
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 1PU0   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN CU,ZN SUPEROXIDE                                 
REMARK 900  DISMUTASE                                                           
REMARK 900 RELATED ID: 1FUN   RELATED DB: PDB                                   
REMARK 900  SUPEROXIDE DISMUTASE MUTANT WITH LYS 136                            
REMARK 900  REPLACED BY GLU, CYS 6 REPLACED BY ALA                              
REMARK 900  AND CYS 111 REPLACED BY SER (K136E, C6A,                            
REMARK 900  C111S)                                                              
REMARK 900 RELATED ID: 1SOS   RELATED DB: PDB                                   
REMARK 900  SUPEROXIDE DISMUTASE MUTANT WITH CYS 6                              
REMARK 900  REPLACED BY ALA AND CYS 111 REPLACED BY                             
REMARK 900  SER (C6A, C111S)                                                    
REMARK 900 RELATED ID: 1N19   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE HSOD A4V MUTANT                                    
REMARK 900 RELATED ID: 1P1V   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF FALS-ASSOCIATED HUMAN                          
REMARK 900  COPPER-ZINCSUPEROXIDE DISMUTASE (CUZNSOD) MUTANT                    
REMARK 900   D125H TO 1.4A                                                      
REMARK 900 RELATED ID: 1L3N   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF REDUCED DIMERIC                           
REMARK 900  COPPER ZINC SOD:THE STRUCTURAL EFFECTS OF                           
REMARK 900  DIMERIZATION                                                        
REMARK 900 RELATED ID: 2WKO   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF METAL LOADED PATHOGENIC SOD1                           
REMARK 900  MUTANT G93A.                                                        
REMARK 900 RELATED ID: 1UXL   RELATED DB: PDB                                   
REMARK 900  I113T MUTANT OF HUMAN SOD1                                          
REMARK 900 RELATED ID: 2AF2   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF DISULFIDE REDUCED AND                         
REMARK 900  COPPER DEPLETEDHUMAN SUPEROXIDE DISMUTASE                           
REMARK 900 RELATED ID: 2VR8   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF G85R ALS MUTANT OF                             
REMARK 900  HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD)                          
REMARK 900  AT 1.36 A RESOLUTION                                                
REMARK 900 RELATED ID: 1RK7   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE                          
REMARK 900  DISMUTASE: ROLEOF METAL IONS IN PROTEIN                             
REMARK 900  FOLDING                                                             
REMARK 900 RELATED ID: 2VR7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF G85R ALS MUTANT OF                             
REMARK 900  HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD)                          
REMARK 900  AT 1.58 A RESOLUTION                                                
REMARK 900 RELATED ID: 2V0A   RELATED DB: PDB                                   
REMARK 900  ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN                        
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 1MFM   RELATED DB: PDB                                   
REMARK 900  MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q                          
REMARK 900  AT ATOMIC RESOLUTION                                                
REMARK 900 RELATED ID: 4SOD   RELATED DB: PDB                                   
REMARK 900  CU,ZN SUPEROXIDE DISMUTASE MUTANT WITH CYS                          
REMARK 900  6 REPLACED BY ALA AND CYS 111 REPLACED                              
REMARK 900  BY SER (C6A,C111S) WITH AN 18-RESIDUE                               
REMARK 900  HEPARIN-BINDING PEPTIDE FUSED TO THE C-                             
REMARK 900  TERMINUS (THEORETICAL MODEL)                                        
REMARK 900 RELATED ID: 2C9S   RELATED DB: PDB                                   
REMARK 900  1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN-                          
REMARK 900  ZN HUMAN SUPEROXIDE DISMUTASE                                       
REMARK 900 RELATED ID: 1DSW   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF A MONOMERIC,                              
REMARK 900  REDUCED FORM OFHUMAN COPPER, ZINC SUPEROXIDE                        
REMARK 900  DISMUTASE BEARING THE SAMECHARGE AS THE                             
REMARK 900  NATIVE PROTEIN                                                      
REMARK 900 RELATED ID: 1KMG   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF MONOMERIC COPPER-                         
REMARK 900  FREE SUPEROXIDEDISMUTASE                                            
REMARK 900 RELATED ID: 1OZT   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF APO-H46R FAMILIAL ALS                          
REMARK 900  MUTANT HUMAN CU,ZN SUPEROXIDE DISMUTASE (                           
REMARK 900  CUZNSOD) TO 2.5A RESOLUTION                                         
REMARK 900 RELATED ID: 1N18   RELATED DB: PDB                                   
REMARK 900  THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE                             
REMARK 900  DISMUTASE, C6A,C111S                                                
REMARK 900 RELATED ID: 1BA9   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF REDUCED MONOMERIC                         
REMARK 900  SUPEROXIDE DISMUTASE, NMR, 36 STRUCTURES                            
REMARK 900 RELATED ID: 2C9U   RELATED DB: PDB                                   
REMARK 900  1.24 ANGSTROMS RESOLUTION STRUCTURE OF AS-                          
REMARK 900  ISOLATED CU-ZN HUMAN SUPEROXIDE DISMUTASE                           
REMARK 900 RELATED ID: 1HL5   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN                             
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 1UXM   RELATED DB: PDB                                   
REMARK 900  A4V MUTANT OF HUMAN SOD1                                            
REMARK 900 RELATED ID: 1SPD   RELATED DB: PDB                                   
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 2WZ0   RELATED DB: PDB                                   
REMARK 900  L38V SOD1 MUTANT COMPLEXED WITH ANILINE.                            
REMARK 900 RELATED ID: 2WYZ   RELATED DB: PDB                                   
REMARK 900  L38V SOD1 MUTANT COMPLEXED WITH UMP                                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 MUTATION LEU38 TO VAL                                                
DBREF  2WYT A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  2WYT F    1   153  UNP    P00441   SODC_HUMAN       2    154             
SEQADV 2WYT VAL A   38  UNP  P00441    LEU    39 ENGINEERED MUTATION            
SEQADV 2WYT VAL F   38  UNP  P00441    LEU    39 ENGINEERED MUTATION            
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 VAL 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 CYS 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 VAL ILE GLY ILE ALA GLN                      
SEQRES   1 F  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 F  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 F  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY VAL THR          
SEQRES   4 F  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 F  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 F  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 F  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 F  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 F  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 F  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 F  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 F  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
HET     CU  A 154       2                                                       
HET     ZN  A 154A      1                                                       
HET     ZN  A 155       1                                                       
HET    SO4  A 156       5                                                       
HET    SO4  A 157      10                                                       
HET    SO4  A 158      10                                                       
HET    ACT  A 160       7                                                       
HET    SO4  A 161       5                                                       
HET     CL  A 162       1                                                       
HET    SO4  A 163      10                                                       
HET     CU  F 154       2                                                       
HET     ZN  F 154A      1                                                       
HET     ZN  F 155       1                                                       
HET    SO4  F 156       5                                                       
HET     CL  F 160       1                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ACT ACETATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3   CU    2(CU 2+)                                                     
FORMUL   4   ZN    4(ZN 2+)                                                     
FORMUL   5  SO4    6(O4 S 2-)                                                   
FORMUL   6  ACT    C2 H3 O2 1-                                                  
FORMUL   7   CL    2(CL 1-)                                                     
FORMUL   8  HOH   *624(H2 O)                                                    
HELIX    1   1 ALA A   55  GLY A   61  5                                   7    
HELIX    2   2 SER A  107  HIS A  110  5                                   4    
HELIX    3   3 ASN A  131  LYS A  136  5                                   6    
HELIX    4   4 ALA F   55  GLY F   61  5                                   7    
HELIX    5   5 GLU F  133  GLY F  138  1                                   6    
SHEET    1  AA 5 ALA A  95  ASP A 101  0                                        
SHEET    2  AA 5 VAL A  29  LYS A  36 -1  O  VAL A  29   N  ASP A 101           
SHEET    3  AA 5 GLN A  15  GLN A  22 -1  O  GLN A  15   N  LYS A  36           
SHEET    4  AA 5 THR A   2  LEU A   8 -1  O  THR A   2   N  GLN A  22           
SHEET    5  AA 5 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5           
SHEET    1  AB 4 ASP A  83  ALA A  89  0                                        
SHEET    2  AB 4 GLY A  41  HIS A  48 -1  O  GLY A  41   N  ALA A  89           
SHEET    3  AB 4 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    4  AB 4 ARG A 143  VAL A 148 -1  N  LEU A 144   O  VAL A 119           
SHEET    1  FA 5 VAL F  94  ASP F 101  0                                        
SHEET    2  FA 5 VAL F  29  LYS F  36 -1  O  VAL F  29   N  ASP F 101           
SHEET    3  FA 5 VAL F  14  GLN F  22 -1  O  GLN F  15   N  LYS F  36           
SHEET    4  FA 5 LYS F   3  GLY F  10 -1  O  ALA F   4   N  PHE F  20           
SHEET    5  FA 5 GLY F 150  ILE F 151 -1  O  GLY F 150   N  VAL F   5           
SHEET    1  FB 4 ASP F  83  ALA F  89  0                                        
SHEET    2  FB 4 GLY F  41  HIS F  48 -1  O  GLY F  41   N  ALA F  89           
SHEET    3  FB 4 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    4  FB 4 ARG F 143  VAL F 148 -1  N  LEU F 144   O  VAL F 119           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.26  
SSBOND   2 CYS F   57    CYS F  146                          1555   1555  2.21  
LINK        ZN  B ZN A 154A                NE2 HIS A 120     1555   1555  1.81  
LINK        ZN  B ZN A 154A                NE2 HIS A  48     1555   1555  2.19  
LINK        CU  A CU A 154                 NE2 HIS A 120     1555   1555  2.05  
LINK        CU  A CU A 154                 ND1 HIS A  46     1555   1555  1.98  
LINK        CU  A CU A 154                 NE2 HIS A  48     1555   1555  1.95  
LINK        CU  C CU A 154                 NE2 HIS A  63     1555   1555  2.36  
LINK        CU  C CU A 154                 NE2 HIS A 120     1555   1555  2.50  
LINK        CU  C CU A 154                 O1 CSO4 A 161     1555   1555  2.24  
LINK        CU  C CU A 154                 NE2 HIS A  48     1555   1555  2.52  
LINK        CU  C CU A 154                 ND1 HIS A  46     1555   1555  1.86  
LINK        ZN    ZN A 155                 ND1 HIS A  63     1555   1555  2.03  
LINK        ZN    ZN A 155                 ND1 HIS A  71     1555   1555  2.00  
LINK        ZN    ZN A 155                 OD1 ASP A  83     1555   1555  1.98  
LINK        ZN    ZN A 155                 ND1 HIS A  80     1555   1555  2.00  
LINK        CU  A CU F 154                 NE2 HIS F  48     1555   1555  1.93  
LINK        CU  C CU F 154                 NE2 HIS F  48     1555   1555  2.28  
LINK        CU  C CU F 154                 NE2 HIS F 120     1555   1555  2.22  
LINK        CU  C CU F 154                 O1 CSO4 F 156     1555   1555  2.36  
LINK        CU  C CU F 154                 ND1 HIS F  46     1555   1555  2.01  
LINK        ZN  B ZN F 154A                NE2 HIS F 120     1555   1555  1.78  
LINK        CU  A CU F 154                 NE2 HIS F 120     1555   1555  2.04  
LINK        CU  A CU F 154                 ND1 HIS F  46     1555   1555  2.05  
LINK        ZN  B ZN F 154A                NE2 HIS F  48     1555   1555  2.19  
LINK        ZN    ZN F 155                 ND1 HIS F  71     1555   1555  2.05  
LINK        ZN    ZN F 155                 ND1 HIS F  80     1555   1555  2.02  
LINK        ZN    ZN F 155                 OD1 ASP F  83     1555   1555  1.94  
LINK        ZN    ZN F 155                 ND1 HIS F  63     1555   1555  2.00  
CISPEP   1 GLY F   12    PRO F   13          0        -0.42                     
SITE     1 AC1  6 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC1  6 SO4 A 161  HOH A2319                                          
SITE     1 AC2  6 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC2  6 SO4 A 161  HOH A2319                                          
SITE     1 AC3  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC4  9 THR A  58  SER A 142  ARG A 143  HOH A2143                    
SITE     2 AC4  9 HOH A2299  HOH A2300  HOH A2301  HOH A2302                    
SITE     3 AC4  9 HOH A2303                                                     
SITE     1 AC5 11 HOH A2304  HOH A2305  HOH A2306  HOH A2307                    
SITE     2 AC5 11 HOH A2308  THR F 137  ASN F 139  ALA F 140                    
SITE     3 AC5 11 GLY F 141  SO4 F 156  HOH F2290                               
SITE     1 AC6 11 THR A 137  ASN A 139  ALA A 140  GLY A 141                    
SITE     2 AC6 11 SO4 A 161  HOH A2309  HOH A2310  HOH A2311                    
SITE     3 AC6 11 HOH A2312  HOH A2313  HOH A2317                               
SITE     1 AC7  5 GLU A  49  PHE A  64  ASN A  65  PRO A  66                    
SITE     2 AC7  5 HOH A2314                                                     
SITE     1 AC8 14 HIS A  48  HIS A  63  HIS A 120  THR A 137                    
SITE     2 AC8 14 ARG A 143   CU A 154   ZN A 154A SO4 A 158                    
SITE     3 AC8 14 HOH A2276  HOH A2315  HOH A2316  HOH A2317                    
SITE     4 AC8 14 HOH A2319  HOH A2320                                          
SITE     1 AC9 11 HOH A2321  HOH A2322  HOH A2323  HOH A2324                    
SITE     2 AC9 11 HOH A2325  HOH A2326  THR F  58  SER F 142                    
SITE     3 AC9 11 ARG F 143  HOH F2131  HOH F2293                               
SITE     1 BC1  7 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 BC1  7 SO4 F 156  HOH F2294  HOH F2297                               
SITE     1 BC2  7 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 BC2  7 SO4 F 156  HOH F2294  HOH F2297                               
SITE     1 BC3  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 BC4 15 SO4 A 157  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 BC4 15 THR F 137  ARG F 143   CU F 154   ZN F 154A                   
SITE     3 BC4 15 HOH F2290  HOH F2292  HOH F2293  HOH F2294                    
SITE     4 BC4 15 HOH F2295  HOH F2296  HOH F2297                               
SITE     1 BC5  1 HOH F2063                                                     
CRYST1   38.690   67.345   52.577  90.00 106.57  90.00 P 1 21 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      0.025846  0.000000  0.007690        0.00000                         
SCALE2      0.000000  0.014849  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019844        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system