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Database: PDB
Entry: 5O40
LinkDB: 5O40
Original site: 5O40 
HEADER    OXIDOREDUCTASE                          25-MAY-17   5O40              
TITLE     SOD1 BOUND TO EBSELEN                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, F;                                                         
COMPND   4 SYNONYM: SUPEROXIDE DISMUTASE 1,HSOD1;                               
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SOD1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    OXIDOREDUCTASE, COMPLEX, INHIBITOR                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.J.CAPPER,G.S.A.WRIGHT,S.V.ANTONYUK,S.S.HASNAIN                      
REVDAT   2   27-JUN-18 5O40    1       JRNL                                     
REVDAT   1   13-JUN-18 5O40    0                                                
JRNL        AUTH   M.J.CAPPER,G.S.A.WRIGHT,L.BARBIERI,E.LUCHINAT,E.MERCATELLI,  
JRNL        AUTH 2 L.MCALARY,J.J.YERBURY,P.M.O'NEILL,S.V.ANTONYUK,L.BANCI,      
JRNL        AUTH 3 S.S.HASNAIN                                                  
JRNL        TITL   THE CYSTEINE-REACTIVE SMALL MOLECULE EBSELEN FACILITATES     
JRNL        TITL 2 EFFECTIVE SOD1 MATURATION.                                   
JRNL        REF    NAT COMMUN                    V.   9  1693 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   29703933                                                     
JRNL        DOI    10.1038/S41467-018-04114-X                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 37783                          
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) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2081                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2748                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.63                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 181                          
REMARK   3   BIN FREE R VALUE                    : 0.3020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2220                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 46                                      
REMARK   3   SOLVENT ATOMS            : 309                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.52000                                             
REMARK   3    B22 (A**2) : 0.63000                                              
REMARK   3    B33 (A**2) : 0.19000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.56000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.109         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.086         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.077         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.995         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2338 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2059 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3179 ; 1.363 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4784 ; 1.220 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   318 ; 6.627 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    95 ;39.102 ;25.474       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   349 ; 9.902 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ; 9.304 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   346 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2732 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   452 ; 0.002 ; 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):  1251 ; 1.275 ; 1.073       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1250 ; 1.276 ; 1.073       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1570 ; 1.738 ; 1.618       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1571 ; 1.739 ; 1.618       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1087 ; 1.673 ; 1.246       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1084 ; 1.674 ; 1.247       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1602 ; 2.207 ; 1.790       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  2561 ; 4.279 ;15.289       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  2468 ; 3.486 ;14.227       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  4385 ; 4.575 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   152 ;32.449 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  4483 ;11.472 ; 5.000       
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 : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5O40 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200005144.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUL-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.987                              
REMARK 200  MONOCHROMATOR                  : CRYOGENICALLY COOLED CRYSTAL       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39891                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.010                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
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: 2V0A                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NAACT PH 4, 2.4 M AMSO4, 150 MM   
REMARK 280  NACL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K               
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       33.92000            
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: 2260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -135.0 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 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A    9   CD   CE   NZ                                        
REMARK 480     LYS A   23   CD   CE   NZ                                        
REMARK 480     GLU A   24   CD   OE1  OE2                                       
REMARK 480     LYS A   30   CD   CE   NZ                                        
REMARK 480     LYS A   70   CE   NZ                                             
REMARK 480     LYS A   75   CD   CE   NZ                                        
REMARK 480     GLU A  132   CD   OE1  OE2                                       
REMARK 480     LYS A  136   CD   CE   NZ                                        
REMARK 480     LYS F   23   CD   CE   NZ                                        
REMARK 480     ASN F   26   CG   OD1  ND2                                       
REMARK 480     LYS F   36   CE   NZ                                             
REMARK 480     LYS F   70   CE   NZ                                             
REMARK 480     LYS F   75   CD   CE   NZ                                        
REMARK 480     GLU F   77   CD   OE1  OE2                                       
REMARK 480     GLU F  132   CG   CD   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   SG   CYS A   111    SE1   9JT A   503              1.87            
REMARK 500   SG   CYS F   111    SE1   9JT F   503              1.87            
REMARK 500   OD1  ASN F    26     O    HOH F   601              1.89            
REMARK 500   CG   ASN F    26     O    HOH F   601              1.94            
REMARK 500   OD1  ASN F    26     O    HOH F   602              1.95            
REMARK 500   ND2  ASN F    26     O    HOH F   601              2.04            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS A   136     O    HOH F   661     2645     0.59            
REMARK 500   CE   LYS A   136     O    HOH F   661     2645     1.69            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 132   CG    GLU A 132   CD     -0.103                       
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 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 122.8                                              
REMARK 620 3 HIS A 120   NE2  96.8 126.5                                        
REMARK 620 4 SO4 A 504   O4  100.7 105.2 100.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  63   ND1                                                    
REMARK 620 2 HIS A  71   ND1 101.8                                              
REMARK 620 3 HIS A  80   ND1 107.9 124.5                                        
REMARK 620 4 ASP A  83   OD1 105.7  95.8 118.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  46   ND1                                                    
REMARK 620 2 HIS F  48   NE2 121.0                                              
REMARK 620 3 HIS F 120   NE2  99.4 127.0                                        
REMARK 620 4 SO4 F 504   O1   99.7 104.4 100.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  63   ND1                                                    
REMARK 620 2 HIS F  71   ND1 100.5                                              
REMARK 620 3 HIS F  80   ND1 109.4 125.0                                        
REMARK 620 4 ASP F  83   OD1 105.1  96.6 117.5                                  
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 ZN A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9JT A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9JT F 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 504                 
DBREF  5O40 A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5O40 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 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     ZN  A 501       1                                                       
HET     ZN  A 502       1                                                       
HET    9JT  A 503      16                                                       
HET    SO4  A 504       5                                                       
HET     ZN  F 501       1                                                       
HET     ZN  F 502       1                                                       
HET    9JT  F 503      16                                                       
HET    SO4  F 504       5                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     9JT ~{N}-PHENYL-2-SELANYL-BENZAMIDE                                  
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3   ZN    4(ZN 2+)                                                     
FORMUL   5  9JT    2(C13 H11 N O SE)                                            
FORMUL   6  SO4    2(O4 S 2-)                                                   
FORMUL  11  HOH   *309(H2 O)                                                    
HELIX    1 AA1 ALA A   55  GLY A   61  5                                   7    
HELIX    2 AA2 GLU A  132  LYS A  136  5                                   5    
HELIX    3 AA3 ALA F   55  GLY F   61  5                                   7    
HELIX    4 AA4 SER F  107  CYS F  111  5                                   5    
HELIX    5 AA5 GLU F  132  LYS F  136  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  ILE A  35   O  ALA A  95           
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  LEU A   8 -1  N  ALA A   4   O  PHE A  20           
SHEET    5 AA1 5 GLY A 150  ALA A 152 -1  O  GLY A 150   N  VAL A   5           
SHEET    1 AA2 4 ASP A  83  ALA A  89  0                                        
SHEET    2 AA2 4 GLY A  41  HIS A  48 -1  N  GLY A  41   O  ALA A  89           
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 F  95  ASP F 101  0                                        
SHEET    2 AA3 5 VAL F  29  LYS F  36 -1  N  ILE F  35   O  ALA F  95           
SHEET    3 AA3 5 VAL F  14  GLN F  22 -1  N  ASN F  19   O  TRP F  32           
SHEET    4 AA3 5 THR F   2  GLY F  10 -1  N  THR F   2   O  GLN F  22           
SHEET    5 AA3 5 GLY F 150  ILE F 151 -1  O  GLY F 150   N  VAL F   5           
SHEET    1 AA4 4 ASP F  83  ALA F  89  0                                        
SHEET    2 AA4 4 GLY F  41  HIS F  48 -1  N  GLY F  41   O  ALA F  89           
SHEET    3 AA4 4 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    4 AA4 4 ARG F 143  VAL F 148 -1  O  ALA F 145   N  VAL F 119           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.05  
SSBOND   2 CYS F   57    CYS F  146                          1555   1555  2.05  
LINK         ND1 HIS A  46                ZN    ZN A 502     1555   1555  2.08  
LINK         NE2 HIS A  48                ZN    ZN A 502     1555   1555  2.07  
LINK         ND1 HIS A  63                ZN    ZN A 501     1555   1555  2.05  
LINK         ND1 HIS A  71                ZN    ZN A 501     1555   1555  2.06  
LINK         ND1 HIS A  80                ZN    ZN A 501     1555   1555  2.02  
LINK         OD1 ASP A  83                ZN    ZN A 501     1555   1555  1.97  
LINK         NE2 HIS A 120                ZN    ZN A 502     1555   1555  1.98  
LINK         ND1 HIS F  46                ZN    ZN F 502     1555   1555  2.08  
LINK         NE2 HIS F  48                ZN    ZN F 502     1555   1555  2.11  
LINK         ND1 HIS F  63                ZN    ZN F 501     1555   1555  2.04  
LINK         ND1 HIS F  71                ZN    ZN F 501     1555   1555  2.09  
LINK         ND1 HIS F  80                ZN    ZN F 501     1555   1555  2.04  
LINK         OD1 ASP F  83                ZN    ZN F 501     1555   1555  1.98  
LINK         NE2 HIS F 120                ZN    ZN F 502     1555   1555  1.97  
LINK        ZN    ZN A 502                 O4  SO4 A 504     1555   1555  2.01  
LINK        ZN    ZN F 502                 O1  SO4 F 504     1555   1555  1.97  
CISPEP   1 GLY F   12    PRO F   13          0        -1.48                     
SITE     1 AC1  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC2  5 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC2  5 SO4 A 504                                                     
SITE     1 AC3  9 GLN A  15  LYS A  36  LEU A 106  SER A 107                    
SITE     2 AC3  9 GLY A 108  CYS A 111  ILE A 113  HOH A 613                    
SITE     3 AC3  9 9JT F 503                                                     
SITE     1 AC4 10 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC4 10 THR A 137  ARG A 143   ZN A 502  HOH A 602                    
SITE     3 AC4 10 HOH A 629  HOH A 646                                          
SITE     1 AC5  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 AC6  5 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 AC6  5 SO4 F 504                                                     
SITE     1 AC7  8 9JT A 503  LEU F 106  GLY F 108  ASP F 109                    
SITE     2 AC7  8 CYS F 111  ILE F 113  HOH F 609  HOH F 685                    
SITE     1 AC8 10 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 AC8 10 THR F 137  ARG F 143   ZN F 502  HOH F 618                    
SITE     3 AC8 10 HOH F 626  HOH F 646                                          
CRYST1   38.100   67.840   51.040  90.00 106.35  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      0.026247  0.000000  0.007700        0.00000                         
SCALE2      0.000000  0.014741  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020418        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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