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Database: PDB
Entry: 6FFK
LinkDB: 6FFK
Original site: 6FFK 
HEADER    OXIDOREDUCTASE                          08-JAN-18   6FFK              
TITLE     HUMAN APO-SOD1 BOUND TO PTCL2(1R,2R-1,4-DACH                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, D, F;                                                   
COMPND   4 SYNONYM: SUPEROXIDE DISMUTASE 1,HSOD1;                               
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: IN THE SECOND DIMER RESIDUES 68 TO 78 AND RESIDUES 125
COMPND   8 TO 140 SHOW NO DENSITY AT ALL AND SO THEY HAVE NON BEEN MODELED      
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: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.CALDERONE,C.NATIVI,F.CANTINI,L.DI CESARE MANNELLI                   
REVDAT   1   28-NOV-18 6FFK    0                                                
JRNL        AUTH   F.CANTINI,V.CALDERONE,L.DI CESARE MANNELLI,M.KORSAK,         
JRNL        AUTH 2 L.GONNELLI,O.FRANCESCONI,C.GHELARDINI,L.BANCI,C.NATIVI       
JRNL        TITL   INTERACTION OF HALF OXA-/HALFCIS-PLATIN COMPLEX WITH HUMAN   
JRNL        TITL 2 SUPEROXIDE DISMUTASE AND INDUCED REDUCTION OF NEUROTOXICITY. 
JRNL        REF    ACS MED CHEM LETT             V.   9  1094 2018              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   30429951                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.8B00199                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.94 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.3                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.94                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.46                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 43129                          
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)  : 0.227                          
REMARK   3   R VALUE            (WORKING SET)  : 0.226                          
REMARK   3   FREE R VALUE                      : 0.256                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2157                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.94                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.00                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 87.72                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2793                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2612                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2653                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2579                   
REMARK   3   BIN FREE R VALUE                        : 0.3226                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.01                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 140                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4050                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.78                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.83                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.03190                                              
REMARK   3    B22 (A**2) : -11.61590                                            
REMARK   3    B33 (A**2) : 9.58400                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.33560                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.350               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.164               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.148               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.172               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.153               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4162   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 5622   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1440   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 726    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4162   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 2      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 534    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 4289   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.12                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.92                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.93                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|1 - A|153 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   13.0627  -17.8180  -20.7048           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0919 T22:    0.6920                                    
REMARK   3     T33:    0.0400 T12:    0.0378                                    
REMARK   3     T13:   -0.0121 T23:    0.0012                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.2267 L22:    1.2070                                    
REMARK   3     L33:    5.1271 L12:   -0.2189                                    
REMARK   3     L13:   -0.0450 L23:   -0.3744                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0406 S12:   -0.2955 S13:   -0.2289                     
REMARK   3     S21:    0.1169 S22:   -0.1273 S23:    0.0333                     
REMARK   3     S31:    0.2738 S32:    0.2316 S33:    0.0868                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|1 - B|153 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):    3.8276  -11.8408  -46.3592           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0627 T22:    0.8157                                    
REMARK   3     T33:    0.0265 T12:    0.0611                                    
REMARK   3     T13:   -0.0121 T23:   -0.0176                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.7525 L22:    1.1106                                    
REMARK   3     L33:    3.9817 L12:    0.1855                                    
REMARK   3     L13:    0.2617 L23:    0.1228                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0216 S12:    0.6566 S13:    0.1347                     
REMARK   3     S21:   -0.0513 S22:    0.1000 S23:    0.0233                     
REMARK   3     S31:   -0.0891 S32:   -0.2653 S33:   -0.1216                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { D|1 - D|153 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):  -22.0225  -12.1999   -7.4932           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0822 T22:    0.6381                                    
REMARK   3     T33:    0.0066 T12:    0.0666                                    
REMARK   3     T13:   -0.0236 T23:    0.0383                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.0608 L22:    2.7983                                    
REMARK   3     L33:    6.2547 L12:   -0.4219                                    
REMARK   3     L13:    1.1927 L23:   -0.6083                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0542 S12:   -0.5658 S13:   -0.2135                     
REMARK   3     S21:    0.2002 S22:    0.0407 S23:   -0.0682                     
REMARK   3     S31:    0.2926 S32:   -0.0782 S33:    0.0135                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { F|1 - F|153 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):  -29.1056   -0.8913  -31.9538           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1013 T22:    0.7743                                    
REMARK   3     T33:    0.0504 T12:    0.1558                                    
REMARK   3     T13:   -0.0103 T23:    0.0415                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.5938 L22:    1.6898                                    
REMARK   3     L33:    6.5246 L12:   -0.5294                                    
REMARK   3     L13:   -0.3074 L23:   -0.5840                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1125 S12:    0.6495 S13:    0.3213                     
REMARK   3     S21:   -0.0592 S22:   -0.0762 S23:   -0.0709                     
REMARK   3     S31:   -0.4511 S32:   -0.4979 S33:   -0.0363                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6FFK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JAN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200008233.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-SEP-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID30B                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.972                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 82609                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.940                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: 3RE0                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 20% PEG 3350, PH 7.0,       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       78.42500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       17.68500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       78.42500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       17.68500            
REMARK 290   SMTRY3   4  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 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: 1640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 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     SER D    68                                                      
REMARK 465     ARG D    69                                                      
REMARK 465     LYS D    70                                                      
REMARK 465     HIS D    71                                                      
REMARK 465     GLY D    72                                                      
REMARK 465     GLY D    73                                                      
REMARK 465     PRO D    74                                                      
REMARK 465     LYS D    75                                                      
REMARK 465     ASP D    76                                                      
REMARK 465     GLU D    77                                                      
REMARK 465     GLU D    78                                                      
REMARK 465     ASP D   125                                                      
REMARK 465     LEU D   126                                                      
REMARK 465     GLY D   127                                                      
REMARK 465     LYS D   128                                                      
REMARK 465     GLY D   129                                                      
REMARK 465     GLY D   130                                                      
REMARK 465     ASN D   131                                                      
REMARK 465     GLU D   132                                                      
REMARK 465     GLU D   133                                                      
REMARK 465     SER D   134                                                      
REMARK 465     THR D   135                                                      
REMARK 465     LYS D   136                                                      
REMARK 465     THR D   137                                                      
REMARK 465     GLY D   138                                                      
REMARK 465     ASN D   139                                                      
REMARK 465     ALA D   140                                                      
REMARK 465     SER F    68                                                      
REMARK 465     ARG F    69                                                      
REMARK 465     LYS F    70                                                      
REMARK 465     HIS F    71                                                      
REMARK 465     GLY F    72                                                      
REMARK 465     GLY F    73                                                      
REMARK 465     PRO F    74                                                      
REMARK 465     LYS F    75                                                      
REMARK 465     ASP F    76                                                      
REMARK 465     GLU F    77                                                      
REMARK 465     GLU F    78                                                      
REMARK 465     ASP F   125                                                      
REMARK 465     LEU F   126                                                      
REMARK 465     GLY F   127                                                      
REMARK 465     LYS F   128                                                      
REMARK 465     GLY F   129                                                      
REMARK 465     GLY F   130                                                      
REMARK 465     ASN F   131                                                      
REMARK 465     GLU F   132                                                      
REMARK 465     GLU F   133                                                      
REMARK 465     SER F   134                                                      
REMARK 465     THR F   135                                                      
REMARK 465     LYS F   136                                                      
REMARK 465     THR F   137                                                      
REMARK 465     GLY F   138                                                      
REMARK 465     ASN F   139                                                      
REMARK 465     ALA F   140                                                      
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    SER A  98       85.51   -150.83                                   
REMARK 500    ASP B  90     -169.92    -74.47                                   
REMARK 500    ASN D  26       34.72    -95.88                                   
REMARK 500    ASP F  83       95.79    -68.75                                   
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                             D7Z A 201  PT8                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 111   SG                                                     
REMARK 620 2 D7Z A 201   N1   97.7                                              
REMARK 620 3 D7Z A 201   N2  119.5  87.2                                        
REMARK 620 4 D7Z A 201  CL1   84.3 177.8  91.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             D7Z B 201  PT8                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 111   SG                                                     
REMARK 620 2 D7Z B 201   N1   95.5                                              
REMARK 620 3 D7Z B 201   N2  113.4  87.0                                        
REMARK 620 4 D7Z B 201  CL1   85.7 178.6  92.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             D7Z D 201  PT8                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 111   SG                                                     
REMARK 620 2 D7Z D 201   N1   94.0                                              
REMARK 620 3 D7Z D 201   N2  117.2  87.1                                        
REMARK 620 4 D7Z D 201  CL1   88.6 177.3  92.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             D7Z F 201  PT8                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 111   SG                                                     
REMARK 620 2 D7Z F 201   N1   93.7                                              
REMARK 620 3 D7Z F 201   N2  124.2  86.8                                        
REMARK 620 4 D7Z F 201  CL1   88.0 178.3  92.3                                  
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 D7Z A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue D7Z B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue D7Z D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue D7Z F 201                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3RE0   RELATED DB: PDB                                   
DBREF  6FFK A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  6FFK B    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  6FFK D    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  6FFK F    1   153  UNP    P00441   SODC_HUMAN       2    154             
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 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 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 CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 B  153  VAL VAL HIS GLU LYS ALA ASP ASP 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 D  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 D  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 D  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 D  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 D  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 D  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 D  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 D  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 D  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 D  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 D  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 D  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 LEU 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    D7Z  A 201      10                                                       
HET    D7Z  B 201      10                                                       
HET    D7Z  D 201      10                                                       
HET    D7Z  F 201      10                                                       
HETNAM     D7Z PTCL2(1(R),2(R)-DACH)                                            
FORMUL   5  D7Z    4(C6 H12 CL2 N2 PT)                                          
HELIX    1 AA1 ALA A   55  GLY A   61  5                                   7    
HELIX    2 AA2 ALA B   55  GLY B   61  5                                   7    
HELIX    3 AA3 ALA D   55  GLY D   61  5                                   7    
HELIX    4 AA4 SER D  107  CYS D  111  5                                   5    
HELIX    5 AA5 CYS F   57  GLY F   61  5                                   5    
SHEET    1 AA1 5 ALA A  95  ASP A 101  0                                        
SHEET    2 AA1 5 VAL A  29  LYS A  36 -1  N  VAL A  29   O  ASP A 101           
SHEET    3 AA1 5 GLN A  15  GLN A  22 -1  N  ASN A  19   O  TRP A  32           
SHEET    4 AA1 5 THR A   2  LYS A   9 -1  N  ALA A   4   O  PHE A  20           
SHEET    5 AA1 5 GLY A 150  ALA A 152 -1  O  ALA A 152   N  LYS A   3           
SHEET    1 AA2 4 ASP A  83  ALA A  89  0                                        
SHEET    2 AA2 4 GLY A  41  HIS A  48 -1  N  PHE A  45   O  GLY A  85           
SHEET    3 AA2 4 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    4 AA2 4 ARG A 143  VAL A 148 -1  O  ALA A 145   N  VAL A 119           
SHEET    1 AA3 5 ALA B  95  ASP B 101  0                                        
SHEET    2 AA3 5 VAL B  29  LYS B  36 -1  N  VAL B  31   O  ILE B  99           
SHEET    3 AA3 5 GLN B  15  GLN B  22 -1  N  ASN B  19   O  TRP B  32           
SHEET    4 AA3 5 THR B   2  LYS B   9 -1  N  CYS B   6   O  ILE B  18           
SHEET    5 AA3 5 GLY B 150  ILE B 151 -1  O  GLY B 150   N  VAL B   5           
SHEET    1 AA4 4 ASP B  83  ALA B  89  0                                        
SHEET    2 AA4 4 GLY B  41  HIS B  48 -1  N  PHE B  45   O  GLY B  85           
SHEET    3 AA4 4 THR B 116  HIS B 120 -1  O  THR B 116   N  HIS B  48           
SHEET    4 AA4 4 ARG B 143  VAL B 148 -1  O  ALA B 145   N  VAL B 119           
SHEET    1 AA5 5 ALA D  95  ASP D 101  0                                        
SHEET    2 AA5 5 VAL D  29  LYS D  36 -1  N  VAL D  31   O  ILE D  99           
SHEET    3 AA5 5 GLN D  15  GLN D  22 -1  N  ASN D  19   O  TRP D  32           
SHEET    4 AA5 5 THR D   2  LEU D   8 -1  N  CYS D   6   O  ILE D  18           
SHEET    5 AA5 5 GLY D 150  ILE D 151 -1  O  GLY D 150   N  VAL D   5           
SHEET    1 AA6 4 ASP D  83  ALA D  89  0                                        
SHEET    2 AA6 4 GLY D  41  HIS D  48 -1  N  PHE D  45   O  GLY D  85           
SHEET    3 AA6 4 THR D 116  HIS D 120 -1  O  THR D 116   N  HIS D  48           
SHEET    4 AA6 4 ARG D 143  VAL D 148 -1  O  GLY D 147   N  LEU D 117           
SHEET    1 AA7 5 ALA F  95  ASP F 101  0                                        
SHEET    2 AA7 5 VAL F  29  LYS F  36 -1  N  VAL F  31   O  ILE F  99           
SHEET    3 AA7 5 GLN F  15  GLN F  22 -1  N  ASN F  19   O  TRP F  32           
SHEET    4 AA7 5 THR F   2  LEU F   8 -1  N  LEU F   8   O  GLY F  16           
SHEET    5 AA7 5 GLY F 150  ILE F 151 -1  O  GLY F 150   N  VAL F   5           
SHEET    1 AA8 4 ASP F  83  ALA F  89  0                                        
SHEET    2 AA8 4 GLY F  41  HIS F  48 -1  N  HIS F  43   O  VAL F  87           
SHEET    3 AA8 4 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    4 AA8 4 ARG F 143  VAL F 148 -1  O  GLY F 147   N  LEU F 117           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.06  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.06  
SSBOND   3 CYS D   57    CYS D  146                          1555   1555  2.06  
SSBOND   4 CYS F   57    CYS F  146                          1555   1555  2.06  
LINK         SG  CYS A 111                PT8  D7Z A 201     1555   1555  2.34  
LINK         SG  CYS B 111                PT8  D7Z B 201     1555   1555  2.39  
LINK         SG  CYS D 111                PT8  D7Z D 201     1555   1555  2.26  
LINK         SG  CYS F 111                PT8  D7Z F 201     1555   1555  2.26  
SITE     1 AC1  4 LEU A 106  SER A 107  CYS A 111  ILE A 113                    
SITE     1 AC2  5 LEU B 106  SER B 107  GLY B 108  CYS B 111                    
SITE     2 AC2  5 ILE B 113                                                     
SITE     1 AC3  4 LEU D 106  CYS D 111  ILE D 113  ARG D 115                    
SITE     1 AC4  5 LEU F 106  SER F 107  GLY F 108  CYS F 111                    
SITE     2 AC4  5 ILE F 113                                                     
CRYST1  156.850   35.370  114.590  90.00 112.26  90.00 C 1 2 1      16          
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      0.006376  0.000000  0.002610        0.00000                         
SCALE2      0.000000  0.028273  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009430        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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