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Database: PDB
Entry: 5U9M
LinkDB: 5U9M
Original site: 5U9M 
HEADER    OXIDOREDUCTASE/CHAPERONE                16-DEC-16   5U9M              
TITLE     COPPER-ZINC SUPEROXIDE DISMUTASE IS ACTIVATED THROUGH A SULFENIC ACID 
TITLE    2 INTERMEDIATE AT A COPPER-ION ENTRY SITE                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: SUPEROXIDE DISMUTASE 1,HSOD1;                               
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: SUPEROXIDE DISMUTASE 1 COPPER CHAPERONE;                   
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SOD1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: EG118;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: YEP351;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  13 S288C);                                                              
SOURCE  14 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  15 ORGANISM_TAXID: 559292;                                              
SOURCE  16 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  17 GENE: CCS1, LYS7, YMR038C, YM9532.03C;                               
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PKA6H                                     
KEYWDS    OXIDOREDUCTASE-CHAPERONE COMPLEX, CU-ZN SUPEROXIDE DISMUTASE,         
KEYWDS   2 METALLOCHAPERONE                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.B.TAYLOR,P.J.HART,D.D.WINKLER                                       
REVDAT   3   02-AUG-17 5U9M    1       JRNL                                     
REVDAT   2   07-JUN-17 5U9M    1       JRNL                                     
REVDAT   1   31-MAY-17 5U9M    0                                                
JRNL        AUTH   M.M.FETHEROLF,S.D.BOYD,A.B.TAYLOR,H.J.KIM,J.A.WOHLSCHLEGEL,  
JRNL        AUTH 2 N.J.BLACKBURN,P.J.HART,D.R.WINGE,D.D.WINKLER                 
JRNL        TITL   COPPER-ZINC SUPEROXIDE DISMUTASE IS ACTIVATED THROUGH A      
JRNL        TITL 2 SULFENIC ACID INTERMEDIATE AT A COPPER ION ENTRY SITE.       
JRNL        REF    J. BIOL. CHEM.                V. 292 12025 2017              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   28533431                                                     
JRNL        DOI    10.1074/JBC.M117.775981                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.92                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.390                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 37948                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.270                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 46.9260 -  5.6608    0.99     2769   155  0.1646 0.1940        
REMARK   3     2  5.6608 -  4.4943    1.00     2625   146  0.1464 0.1797        
REMARK   3     3  4.4943 -  3.9265    1.00     2595   143  0.1452 0.2098        
REMARK   3     4  3.9265 -  3.5677    1.00     2583   145  0.1713 0.2228        
REMARK   3     5  3.5677 -  3.3120    1.00     2554   141  0.1931 0.2544        
REMARK   3     6  3.3120 -  3.1168    1.00     2563   144  0.2027 0.2542        
REMARK   3     7  3.1168 -  2.9607    1.00     2556   141  0.2274 0.2889        
REMARK   3     8  2.9607 -  2.8319    1.00     2513   140  0.2343 0.2758        
REMARK   3     9  2.8319 -  2.7229    1.00     2546   141  0.2145 0.3005        
REMARK   3    10  2.7229 -  2.6289    1.00     2543   142  0.2342 0.2772        
REMARK   3    11  2.6289 -  2.5467    1.00     2512   139  0.2396 0.2813        
REMARK   3    12  2.5467 -  2.4739    1.00     2549   143  0.2489 0.3174        
REMARK   3    13  2.4739 -  2.4088    1.00     2531   140  0.2644 0.2971        
REMARK   3    14  2.4088 -  2.3500    1.00     2509   140  0.2665 0.3276        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.180           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.51                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           5832                                  
REMARK   3   ANGLE     :  1.142           7886                                  
REMARK   3   CHIRALITY :  0.046            890                                  
REMARK   3   PLANARITY :  0.005           1037                                  
REMARK   3   DIHEDRAL  : 13.126           2116                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5U9M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000225539.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-FEB-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38015                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.510                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.11200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.12500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: 1OZU,1JK9                                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25 % PEG 3350, 0.2 M AMMONIUM SULFATE,   
REMARK 280  0.1 M BIS-TRIS PH 6.5, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       49.54850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       92.17650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.54850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       92.17650            
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: 1840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17830 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: 1860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     THR B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     ASN B     4                                                      
REMARK 465     ASP B     5                                                      
REMARK 465     THR B     6                                                      
REMARK 465     TYR B     7                                                      
REMARK 465     PRO B    14                                                      
REMARK 465     MET B    15                                                      
REMARK 465     HIS B    16                                                      
REMARK 465     ARG B    62                                                      
REMARK 465     ASN B    63                                                      
REMARK 465     CYS B    64                                                      
REMARK 465     GLY B    65                                                      
REMARK 465     LYS B    66                                                      
REMARK 465     ASP B   242                                                      
REMARK 465     ALA B   243                                                      
REMARK 465     LEU B   244                                                      
REMARK 465     ALA B   245                                                      
REMARK 465     ASN B   246                                                      
REMARK 465     ASN B   247                                                      
REMARK 465     ILE B   248                                                      
REMARK 465     LYS B   249                                                      
REMARK 465     THR D     2                                                      
REMARK 465     THR D     3                                                      
REMARK 465     ASN D     4                                                      
REMARK 465     ASP D     5                                                      
REMARK 465     MET D    15                                                      
REMARK 465     HIS D    16                                                      
REMARK 465     ASP D   242                                                      
REMARK 465     ALA D   243                                                      
REMARK 465     LEU D   244                                                      
REMARK 465     ALA D   245                                                      
REMARK 465     ASN D   246                                                      
REMARK 465     ASN D   247                                                      
REMARK 465     ILE D   248                                                      
REMARK 465     LYS D   249                                                      
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   OD2  ASP D    93     OH   TYR D   209              2.07            
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    CYS B 159       79.31   -106.64                                   
REMARK 500    PRO B 179       49.31    -82.28                                   
REMARK 500    SER B 204        0.43    -63.88                                   
REMARK 500    ASN C  65       59.73   -145.52                                   
REMARK 500    CYS D 159       79.43   -105.48                                   
REMARK 500    PRO D 179       49.00    -82.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  63   ND1                                                    
REMARK 620 2 HIS A  71   ND1 101.2                                              
REMARK 620 3 HIS A  80   ND1 112.8 127.4                                        
REMARK 620 4 ASP A  83   OD1  89.9  99.6 118.6                                  
REMARK 620 5 ASP A  83   OD2 143.2  80.9  93.1  54.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  17   SG                                                     
REMARK 620 2 CYS B  20   SG  108.2                                              
REMARK 620 3 CYS D  17   SG  130.4  42.8                                        
REMARK 620 4 CYS D  20   SG  130.6  41.3   1.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  63   ND1                                                    
REMARK 620 2 HIS C  71   ND1 105.9                                              
REMARK 620 3 HIS C  80   ND1 114.8 125.1                                        
REMARK 620 4 ASP C  83   OD1  94.0  96.7 114.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 201                  
DBREF  5U9M A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5U9M B    2   249  UNP    P40202   CCS1_YEAST       2    249             
DBREF  5U9M C    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5U9M D    2   249  UNP    P40202   CCS1_YEAST       2    249             
SEQADV 5U9M ARG A   46  UNP  P00441    HIS    47 ENGINEERED MUTATION            
SEQADV 5U9M GLN A   48  UNP  P00441    HIS    49 ENGINEERED MUTATION            
SEQADV 5U9M ALA B  238  UNP  P40202    GLU   238 ENGINEERED MUTATION            
SEQADV 5U9M ALA B  239  UNP  P40202    GLU   239 ENGINEERED MUTATION            
SEQADV 5U9M ALA B  240  UNP  P40202    ARG   240 ENGINEERED MUTATION            
SEQADV 5U9M ARG C   46  UNP  P00441    HIS    47 ENGINEERED MUTATION            
SEQADV 5U9M GLN C   48  UNP  P00441    HIS    49 ENGINEERED MUTATION            
SEQADV 5U9M ALA D  238  UNP  P40202    GLU   238 ENGINEERED MUTATION            
SEQADV 5U9M ALA D  239  UNP  P40202    GLU   239 ENGINEERED MUTATION            
SEQADV 5U9M ALA D  240  UNP  P40202    ARG   240 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 LEU THR          
SEQRES   4 A  153  GLU GLY LEU HIS GLY PHE ARG VAL GLN 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  248  THR THR ASN ASP THR TYR GLU ALA THR TYR ALA ILE PRO          
SEQRES   2 B  248  MET HIS CYS GLU ASN CYS VAL ASN ASP ILE LYS ALA CYS          
SEQRES   3 B  248  LEU LYS ASN VAL PRO GLY ILE ASN SER LEU ASN PHE ASP          
SEQRES   4 B  248  ILE GLU GLN GLN ILE MET SER VAL GLU SER SER VAL ALA          
SEQRES   5 B  248  PRO SER THR ILE ILE ASN THR LEU ARG ASN CYS GLY LYS          
SEQRES   6 B  248  ASP ALA ILE ILE ARG GLY ALA GLY LYS PRO ASN SER SER          
SEQRES   7 B  248  ALA VAL ALA ILE LEU GLU THR PHE GLN LYS TYR THR ILE          
SEQRES   8 B  248  ASP GLN LYS LYS ASP THR ALA VAL ARG GLY LEU ALA ARG          
SEQRES   9 B  248  ILE VAL GLN VAL GLY GLU ASN LYS THR LEU PHE ASP ILE          
SEQRES  10 B  248  THR VAL ASN GLY VAL PRO GLU ALA GLY ASN TYR HIS ALA          
SEQRES  11 B  248  SER ILE HIS GLU LYS GLY ASP VAL SER LYS GLY VAL GLU          
SEQRES  12 B  248  SER THR GLY LYS VAL TRP HIS LYS PHE ASP GLU PRO ILE          
SEQRES  13 B  248  GLU CYS PHE ASN GLU SER ASP LEU GLY LYS ASN LEU TYR          
SEQRES  14 B  248  SER GLY LYS THR PHE LEU SER ALA PRO LEU PRO THR TRP          
SEQRES  15 B  248  GLN LEU ILE GLY ARG SER PHE VAL ILE SER LYS SER LEU          
SEQRES  16 B  248  ASN HIS PRO GLU ASN GLU PRO SER SER VAL LYS ASP TYR          
SEQRES  17 B  248  SER PHE LEU GLY VAL ILE ALA ARG SER ALA GLY VAL TRP          
SEQRES  18 B  248  GLU ASN ASN LYS GLN VAL CYS ALA CYS THR GLY LYS THR          
SEQRES  19 B  248  VAL TRP ALA ALA ALA LYS ASP ALA LEU ALA ASN ASN ILE          
SEQRES  20 B  248  LYS                                                          
SEQRES   1 C  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 C  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 C  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 C  153  GLU GLY LEU HIS GLY PHE ARG VAL GLN GLU PHE GLY ASP          
SEQRES   5 C  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 C  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 C  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 C  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 C  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 C  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 C  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 C  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 D  248  THR THR ASN ASP THR TYR GLU ALA THR TYR ALA ILE PRO          
SEQRES   2 D  248  MET HIS CYS GLU ASN CYS VAL ASN ASP ILE LYS ALA CYS          
SEQRES   3 D  248  LEU LYS ASN VAL PRO GLY ILE ASN SER LEU ASN PHE ASP          
SEQRES   4 D  248  ILE GLU GLN GLN ILE MET SER VAL GLU SER SER VAL ALA          
SEQRES   5 D  248  PRO SER THR ILE ILE ASN THR LEU ARG ASN CYS GLY LYS          
SEQRES   6 D  248  ASP ALA ILE ILE ARG GLY ALA GLY LYS PRO ASN SER SER          
SEQRES   7 D  248  ALA VAL ALA ILE LEU GLU THR PHE GLN LYS TYR THR ILE          
SEQRES   8 D  248  ASP GLN LYS LYS ASP THR ALA VAL ARG GLY LEU ALA ARG          
SEQRES   9 D  248  ILE VAL GLN VAL GLY GLU ASN LYS THR LEU PHE ASP ILE          
SEQRES  10 D  248  THR VAL ASN GLY VAL PRO GLU ALA GLY ASN TYR HIS ALA          
SEQRES  11 D  248  SER ILE HIS GLU LYS GLY ASP VAL SER LYS GLY VAL GLU          
SEQRES  12 D  248  SER THR GLY LYS VAL TRP HIS LYS PHE ASP GLU PRO ILE          
SEQRES  13 D  248  GLU CYS PHE ASN GLU SER ASP LEU GLY LYS ASN LEU TYR          
SEQRES  14 D  248  SER GLY LYS THR PHE LEU SER ALA PRO LEU PRO THR TRP          
SEQRES  15 D  248  GLN LEU ILE GLY ARG SER PHE VAL ILE SER LYS SER LEU          
SEQRES  16 D  248  ASN HIS PRO GLU ASN GLU PRO SER SER VAL LYS ASP TYR          
SEQRES  17 D  248  SER PHE LEU GLY VAL ILE ALA ARG SER ALA GLY VAL TRP          
SEQRES  18 D  248  GLU ASN ASN LYS GLN VAL CYS ALA CYS THR GLY LYS THR          
SEQRES  19 D  248  VAL TRP ALA ALA ALA LYS ASP ALA LEU ALA ASN ASN ILE          
SEQRES  20 D  248  LYS                                                          
HET     ZN  A 201       1                                                       
HET     ZN  B 301       1                                                       
HET     ZN  C 201       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   5   ZN    3(ZN 2+)                                                     
FORMUL   8  HOH   *120(H2 O)                                                    
HELIX    1 AA1 GLY A   56  GLY A   61  1                                   6    
HELIX    2 AA2 SER A  107  CYS A  111  5                                   5    
HELIX    3 AA3 GLU A  133  GLY A  138  1                                   6    
HELIX    4 AA4 GLU B   18  LYS B   29  1                                  12    
HELIX    5 AA5 ALA B   53  LEU B   61  1                                   9    
HELIX    6 AA6 LYS B  141  GLY B  147  5                                   7    
HELIX    7 AA7 PRO B  181  LEU B  185  5                                   5    
HELIX    8 AA8 GLY C   56  GLY C   61  1                                   6    
HELIX    9 AA9 SER C  107  CYS C  111  5                                   5    
HELIX   10 AB1 ASN C  131  GLY C  138  1                                   8    
HELIX   11 AB2 GLU D   18  LYS D   29  1                                  12    
HELIX   12 AB3 ALA D   53  ASN D   63  1                                  11    
HELIX   13 AB4 LYS D  141  GLY D  147  5                                   7    
HELIX   14 AB5 PRO D  181  LEU D  185  5                                   5    
HELIX   15 AB6 HIS D  198  GLU D  202  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  GLU A  21 -1  N  ASN A  19   O  TRP A  32           
SHEET    4 AA1 5 LYS A   3  LYS A   9 -1  N  ALA A   4   O  PHE A  20           
SHEET    5 AA1 5 GLY A 150  GLN A 153 -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  VAL A  47 -1  N  GLY A  41   O  ALA A  89           
SHEET    3 AA2 4 THR A 116  HIS A 120 -1  O  HIS A 120   N  GLY A  44           
SHEET    4 AA2 4 ARG A 143  VAL A 148 -1  O  GLY A 147   N  LEU A 117           
SHEET    1 AA3 4 ILE B  34  ASP B  40  0                                        
SHEET    2 AA3 4 ILE B  45  SER B  50 -1  O  SER B  47   N  ASN B  38           
SHEET    3 AA3 4 ALA B   9  ALA B  12 -1  N  TYR B  11   O  MET B  46           
SHEET    4 AA3 4 ILE B  69  ARG B  71 -1  O  ARG B  71   N  THR B  10           
SHEET    1 AA4 9 VAL B 149  CYS B 159  0                                        
SHEET    2 AA4 9 GLY B 127  HIS B 134 -1  N  TYR B 129   O  ILE B 157           
SHEET    3 AA4 9 SER B 189  SER B 195 -1  O  SER B 193   N  HIS B 130           
SHEET    4 AA4 9 ASP B 208  VAL B 214 -1  O  TYR B 209   N  LYS B 194           
SHEET    5 AA4 9 SER B  79  THR B  86 -1  N  GLU B  85   O  LEU B 212           
SHEET    6 AA4 9 VAL B 100  GLN B 108 -1  O  ILE B 106   N  ALA B  80           
SHEET    7 AA4 9 THR B 114  VAL B 123 -1  O  ASP B 117   N  ARG B 105           
SHEET    8 AA4 9 TYR B 170  ALA B 178 -1  O  GLY B 172   N  VAL B 120           
SHEET    9 AA4 9 ASN B 161  GLU B 162 -1  N  ASN B 161   O  SER B 171           
SHEET    1 AA5 6 VAL B 149  CYS B 159  0                                        
SHEET    2 AA5 6 GLY B 127  HIS B 134 -1  N  TYR B 129   O  ILE B 157           
SHEET    3 AA5 6 SER B 189  SER B 195 -1  O  SER B 193   N  HIS B 130           
SHEET    4 AA5 6 ASP B 208  VAL B 214 -1  O  TYR B 209   N  LYS B 194           
SHEET    5 AA5 6 SER B  79  THR B  86 -1  N  GLU B  85   O  LEU B 212           
SHEET    6 AA5 6 ALA B 216  ARG B 217 -1  O  ALA B 216   N  VAL B  81           
SHEET    1 AA6 2 GLN B 227  CYS B 229  0                                        
SHEET    2 AA6 2 THR B 235  ALA B 238 -1  O  TRP B 237   N  VAL B 228           
SHEET    1 AA7 9 LYS C   3  LYS C   9  0                                        
SHEET    2 AA7 9 GLN C  15  GLU C  21 -1  O  ILE C  18   N  CYS C   6           
SHEET    3 AA7 9 VAL C  29  LYS C  36 -1  O  LYS C  30   N  GLU C  21           
SHEET    4 AA7 9 ALA C  95  ASP C 101 -1  O  ALA C  95   N  ILE C  35           
SHEET    5 AA7 9 ASP C  83  ALA C  89 -1  N  THR C  88   O  ASP C  96           
SHEET    6 AA7 9 GLY C  41  VAL C  47 -1  N  GLY C  41   O  ALA C  89           
SHEET    7 AA7 9 THR C 116  HIS C 120 -1  O  VAL C 118   N  ARG C  46           
SHEET    8 AA7 9 ARG C 143  GLN C 153 -1  O  GLY C 147   N  LEU C 117           
SHEET    9 AA7 9 LYS C   3  LYS C   9 -1  N  VAL C   5   O  GLY C 150           
SHEET    1 AA8 4 ILE D  34  ASP D  40  0                                        
SHEET    2 AA8 4 ILE D  45  SER D  50 -1  O  GLU D  49   N  ASN D  35           
SHEET    3 AA8 4 TYR D   7  ALA D  12 -1  N  ALA D   9   O  VAL D  48           
SHEET    4 AA8 4 ILE D  69  ARG D  71 -1  O  ILE D  69   N  ALA D  12           
SHEET    1 AA9 9 VAL D 149  CYS D 159  0                                        
SHEET    2 AA9 9 GLY D 127  HIS D 134 -1  N  ILE D 133   O  TRP D 150           
SHEET    3 AA9 9 SER D 189  SER D 195 -1  O  VAL D 191   N  SER D 132           
SHEET    4 AA9 9 ASP D 208  VAL D 214 -1  O  TYR D 209   N  LYS D 194           
SHEET    5 AA9 9 SER D  79  THR D  86 -1  N  GLU D  85   O  LEU D 212           
SHEET    6 AA9 9 VAL D 100  GLN D 108 -1  O  ILE D 106   N  ALA D  80           
SHEET    7 AA9 9 THR D 114  VAL D 123 -1  O  ASP D 117   N  ARG D 105           
SHEET    8 AA9 9 GLY D 166  ALA D 178 -1  O  GLY D 172   N  VAL D 120           
SHEET    9 AA9 9 ASN D 161  SER D 163 -1  N  ASN D 161   O  SER D 171           
SHEET    1 AB1 6 VAL D 149  CYS D 159  0                                        
SHEET    2 AB1 6 GLY D 127  HIS D 134 -1  N  ILE D 133   O  TRP D 150           
SHEET    3 AB1 6 SER D 189  SER D 195 -1  O  VAL D 191   N  SER D 132           
SHEET    4 AB1 6 ASP D 208  VAL D 214 -1  O  TYR D 209   N  LYS D 194           
SHEET    5 AB1 6 SER D  79  THR D  86 -1  N  GLU D  85   O  LEU D 212           
SHEET    6 AB1 6 ALA D 216  SER D 218 -1  O  ALA D 216   N  VAL D  81           
SHEET    1 AB2 2 GLN D 227  CYS D 229  0                                        
SHEET    2 AB2 2 THR D 235  ALA D 238 -1  O  TRP D 237   N  VAL D 228           
SSBOND   1 CYS D   27    CYS D   64                          1555   1555  2.03  
LINK         ND1 HIS A  63                ZN    ZN A 201     1555   1555  1.96  
LINK         ND1 HIS A  71                ZN    ZN A 201     1555   1555  2.13  
LINK         ND1 HIS A  80                ZN    ZN A 201     1555   1555  1.99  
LINK         OD1 ASP A  83                ZN    ZN A 201     1555   1555  2.07  
LINK         OD2 ASP A  83                ZN    ZN A 201     1555   1555  2.69  
LINK         SG  CYS B  17                ZN    ZN B 301     1555   1555  2.28  
LINK         SG  CYS B  20                ZN    ZN B 301     1555   1555  2.36  
LINK         ND1 HIS C  63                ZN    ZN C 201     1555   1555  2.08  
LINK         ND1 HIS C  71                ZN    ZN C 201     1555   1555  2.06  
LINK         ND1 HIS C  80                ZN    ZN C 201     1555   1555  2.01  
LINK         OD1 ASP C  83                ZN    ZN C 201     1555   1555  1.90  
LINK         SG  CYS D  17                ZN    ZN B 301     1555   1656  2.65  
LINK         SG  CYS D  20                ZN    ZN B 301     1555   1656  2.92  
SITE     1 AC1  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC2  4 CYS B  17  CYS B  20  CYS D  17  CYS D  20                    
SITE     1 AC3  4 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
CRYST1   99.097  184.353   48.514  90.00  90.00  90.00 P 21 21 2     8          
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      0.010091  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005424  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020613        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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