GenomeNet

Database: PDB
Entry: 3GTT
LinkDB: 3GTT
Original site: 3GTT 
HEADER    OXIDOREDUCTASE                          28-MAR-09   3GTT              
TITLE     MOUSE SOD1                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: SOD1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PKA8H                                     
KEYWDS    OXIDOREDUCTASE, MOUSE CU, ZN SUPEROXIDE DISMUTASE, ANTIOXIDANT,       
KEYWDS   2 METAL-BINDING, AMYOTROPHIC LATERAL SCLEROSIS, DISULFIDE BOND,        
KEYWDS   3 PHOSPHOPROTEIN                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.V.SEETHARAMAN,A.B.TAYLOR,P.J.HART                                   
REVDAT   2   05-JAN-11 3GTT    1       JRNL                                     
REVDAT   1   08-SEP-10 3GTT    0                                                
JRNL        AUTH   S.V.SEETHARAMAN,A.B.TAYLOR,S.HOLLOWAY,P.J.HART               
JRNL        TITL   STRUCTURES OF MOUSE SOD1 AND HUMAN/MOUSE SOD1 CHIMERAS.      
JRNL        REF    ARCH.BIOCHEM.BIOPHYS.         V. 503   183 2010              
JRNL        REFN                   ISSN 0003-9861                               
JRNL        PMID   20727846                                                     
JRNL        DOI    10.1016/J.ABB.2010.08.014                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.76                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 64174                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.160                           
REMARK   3   R VALUE            (WORKING SET) : 0.158                           
REMARK   3   FREE R VALUE                     : 0.197                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3210                            
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  9.5874 -  5.9993    0.93     3014   214  0.1703 0.1786        
REMARK   3     2  5.9993 -  4.9736    0.97     3071   107  0.1481 0.1985        
REMARK   3     3  4.9736 -  4.4144    0.93     2921   214  0.1167 0.1751        
REMARK   3     4  4.4144 -  4.0439    0.97     3030   107  0.1127 0.1441        
REMARK   3     5  4.0439 -  3.7730    0.93     2908   214  0.1239 0.1521        
REMARK   3     6  3.7730 -  3.5627    0.97     3016   107  0.1324 0.1667        
REMARK   3     7  3.5627 -  3.3925    0.93     2880   214  0.1458 0.1797        
REMARK   3     8  3.3925 -  3.2509    0.97     3013   107  0.1452 0.1792        
REMARK   3     9  3.2509 -  3.1302    0.93     2852   214  0.1573 0.2026        
REMARK   3    10  3.1302 -  3.0257    0.97     2979   107  0.1671 0.2171        
REMARK   3    11  3.0257 -  2.9339    0.93     2896   214  0.1757 0.2178        
REMARK   3    12  2.9339 -  2.8523    0.96     2997   107  0.1954 0.2472        
REMARK   3    13  2.8523 -  2.7791    0.97     2980   107  0.1987 0.2360        
REMARK   3    14  2.7791 -  2.7128    0.93     2869   214  0.2014 0.2499        
REMARK   3    15  2.7128 -  2.6525    0.97     2992   107  0.2027 0.2573        
REMARK   3    16  2.6525 -  2.5972    0.93     2839   214  0.2061 0.2548        
REMARK   3    17  2.5972 -  2.5462    0.97     2984   107  0.2149 0.2220        
REMARK   3    18  2.5462 -  2.4990    0.93     2805   214  0.2154 0.2546        
REMARK   3    19  2.4990 -  2.4552    0.97     3011   107  0.2219 0.2374        
REMARK   3    20  2.4552 -  2.4142    0.93     2871   214  0.2275 0.2836        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 33.16                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.86810                                             
REMARK   3    B22 (A**2) : -6.88860                                             
REMARK   3    B33 (A**2) : 6.45400                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: 0.1440                                                   
REMARK   3   OPERATOR: 1/2*H+1/2*K,3/2*H-1/2*K,-L                               
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           6762                                  
REMARK   3   ANGLE     :  1.076           9114                                  
REMARK   3   CHIRALITY :  0.068            990                                  
REMARK   3   PLANARITY :  0.004           1248                                  
REMARK   3   DIHEDRAL  : 18.469           2436                                  
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 3GTT COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052298.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-NOV-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : CONFOCAL OPTICS                    
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS VII                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64203                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.46300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2VR7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, 30% PEG 1000, PH 8.5,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.92050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.92050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       56.22700            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       97.24750            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       56.22700            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       97.24750            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       74.92050            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       56.22700            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       97.24750            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       74.92050            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       56.22700            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       97.24750            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: 1440 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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: 1410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 1440 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 653  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO F  13   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 115     -169.66   -109.12                                   
REMARK 500    SER C  25      -39.06    -39.26                                   
REMARK 500    SER C 107      -35.13   -140.38                                   
REMARK 500    PHE D  64      108.83    -58.94                                   
REMARK 500    SER D  68       36.15     37.39                                   
REMARK 500    SER D  98       99.82   -162.41                                   
REMARK 500    ASP E  92      -50.19    -17.46                                   
REMARK 500    LYS F 136      -55.28   -127.02                                   
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 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  63   ND1                                                    
REMARK 620 2 HIS A  71   ND1 102.8                                              
REMARK 620 3 HIS A  80   ND1 110.1 122.8                                        
REMARK 620 4 ASP A  83   OD1 107.7  93.0 118.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  63   ND1                                                    
REMARK 620 2 HIS B  71   ND1  99.7                                              
REMARK 620 3 HIS B  80   ND1 108.3 125.9                                        
REMARK 620 4 ASP B  83   OD1 109.3  99.1 113.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  63   ND1                                                    
REMARK 620 2 HIS C  71   ND1 103.2                                              
REMARK 620 3 HIS C  80   ND1 114.4 127.2                                        
REMARK 620 4 ASP C  83   OD1  99.9  94.4 113.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  63   ND1                                                    
REMARK 620 2 HIS D  80   ND1 106.9                                              
REMARK 620 3 ASP D  83   OD1 110.9 118.1                                        
REMARK 620 4 HIS D  71   ND1  92.4 123.0 102.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  63   ND1                                                    
REMARK 620 2 HIS E  71   ND1 102.4                                              
REMARK 620 3 HIS E  80   ND1 115.2 118.5                                        
REMARK 620 4 ASP E  83   OD1 103.6 100.1 114.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  63   ND1                                                    
REMARK 620 2 HIS F  71   ND1 110.2                                              
REMARK 620 3 HIS F  80   ND1 103.9 127.3                                        
REMARK 620 4 ASP F  83   OD1 104.9  94.5 114.1                                  
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 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 155                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3GTV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3GTW   RELATED DB: PDB                                   
DBREF  3GTT A    1   153  UNP    P08228   SODC_MOUSE       2    154             
DBREF  3GTT B    1   153  UNP    P08228   SODC_MOUSE       2    154             
DBREF  3GTT C    1   153  UNP    P08228   SODC_MOUSE       2    154             
DBREF  3GTT D    1   153  UNP    P08228   SODC_MOUSE       2    154             
DBREF  3GTT E    1   153  UNP    P08228   SODC_MOUSE       2    154             
DBREF  3GTT F    1   153  UNP    P08228   SODC_MOUSE       2    154             
SEQRES   1 A  153  ALA MET LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 A  153  VAL GLN GLY THR ILE HIS PHE GLU GLN LYS ALA SER GLY          
SEQRES   3 A  153  GLU PRO VAL VAL LEU SER GLY GLN ILE THR GLY LEU THR          
SEQRES   4 A  153  GLU GLY GLN HIS GLY PHE HIS VAL HIS GLN TYR GLY ASP          
SEQRES   5 A  153  ASN THR GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 A  153  PRO HIS SER LYS LYS HIS GLY GLY PRO ALA ASP GLU GLU          
SEQRES   7 A  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA GLY LYS          
SEQRES   8 A  153  ASP GLY VAL ALA ASN VAL SER ILE GLU ASP ARG VAL ILE          
SEQRES   9 A  153  SER LEU SER GLY GLU HIS SER ILE ILE GLY ARG THR MET          
SEQRES  10 A  153  VAL VAL HIS GLU LYS GLN 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 MET LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 B  153  VAL GLN GLY THR ILE HIS PHE GLU GLN LYS ALA SER GLY          
SEQRES   3 B  153  GLU PRO VAL VAL LEU SER GLY GLN ILE THR GLY LEU THR          
SEQRES   4 B  153  GLU GLY GLN HIS GLY PHE HIS VAL HIS GLN TYR GLY ASP          
SEQRES   5 B  153  ASN THR GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 B  153  PRO HIS SER LYS LYS HIS GLY GLY PRO ALA ASP GLU GLU          
SEQRES   7 B  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA GLY LYS          
SEQRES   8 B  153  ASP GLY VAL ALA ASN VAL SER ILE GLU ASP ARG VAL ILE          
SEQRES   9 B  153  SER LEU SER GLY GLU HIS SER ILE ILE GLY ARG THR MET          
SEQRES  10 B  153  VAL VAL HIS GLU LYS GLN 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 C  153  ALA MET LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 C  153  VAL GLN GLY THR ILE HIS PHE GLU GLN LYS ALA SER GLY          
SEQRES   3 C  153  GLU PRO VAL VAL LEU SER GLY GLN ILE THR GLY LEU THR          
SEQRES   4 C  153  GLU GLY GLN HIS GLY PHE HIS VAL HIS GLN TYR GLY ASP          
SEQRES   5 C  153  ASN THR GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 C  153  PRO HIS SER LYS LYS HIS GLY GLY PRO ALA ASP GLU GLU          
SEQRES   7 C  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA GLY LYS          
SEQRES   8 C  153  ASP GLY VAL ALA ASN VAL SER ILE GLU ASP ARG VAL ILE          
SEQRES   9 C  153  SER LEU SER GLY GLU HIS SER ILE ILE GLY ARG THR MET          
SEQRES  10 C  153  VAL VAL HIS GLU LYS GLN 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  153  ALA MET LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 D  153  VAL GLN GLY THR ILE HIS PHE GLU GLN LYS ALA SER GLY          
SEQRES   3 D  153  GLU PRO VAL VAL LEU SER GLY GLN ILE THR GLY LEU THR          
SEQRES   4 D  153  GLU GLY GLN HIS GLY PHE HIS VAL HIS GLN TYR GLY ASP          
SEQRES   5 D  153  ASN THR GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 D  153  PRO HIS SER LYS LYS HIS GLY GLY PRO ALA ASP GLU GLU          
SEQRES   7 D  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA GLY LYS          
SEQRES   8 D  153  ASP GLY VAL ALA ASN VAL SER ILE GLU ASP ARG VAL ILE          
SEQRES   9 D  153  SER LEU SER GLY GLU HIS SER ILE ILE GLY ARG THR MET          
SEQRES  10 D  153  VAL VAL HIS GLU LYS GLN 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 E  153  ALA MET LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 E  153  VAL GLN GLY THR ILE HIS PHE GLU GLN LYS ALA SER GLY          
SEQRES   3 E  153  GLU PRO VAL VAL LEU SER GLY GLN ILE THR GLY LEU THR          
SEQRES   4 E  153  GLU GLY GLN HIS GLY PHE HIS VAL HIS GLN TYR GLY ASP          
SEQRES   5 E  153  ASN THR GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 E  153  PRO HIS SER LYS LYS HIS GLY GLY PRO ALA ASP GLU GLU          
SEQRES   7 E  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA GLY LYS          
SEQRES   8 E  153  ASP GLY VAL ALA ASN VAL SER ILE GLU ASP ARG VAL ILE          
SEQRES   9 E  153  SER LEU SER GLY GLU HIS SER ILE ILE GLY ARG THR MET          
SEQRES  10 E  153  VAL VAL HIS GLU LYS GLN ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 E  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 E  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 F  153  ALA MET LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 F  153  VAL GLN GLY THR ILE HIS PHE GLU GLN LYS ALA SER GLY          
SEQRES   3 F  153  GLU PRO VAL VAL LEU SER GLY GLN ILE THR GLY LEU THR          
SEQRES   4 F  153  GLU GLY GLN HIS GLY PHE HIS VAL HIS GLN TYR GLY ASP          
SEQRES   5 F  153  ASN THR GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 F  153  PRO HIS SER LYS LYS HIS GLY GLY PRO ALA ASP GLU GLU          
SEQRES   7 F  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA GLY LYS          
SEQRES   8 F  153  ASP GLY VAL ALA ASN VAL SER ILE GLU ASP ARG VAL ILE          
SEQRES   9 F  153  SER LEU SER GLY GLU HIS SER ILE ILE GLY ARG THR MET          
SEQRES  10 F  153  VAL VAL HIS GLU LYS GLN 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 155       1                                                       
HET     ZN  B 155       1                                                       
HET     ZN  C 155       1                                                       
HET     ZN  D 155       1                                                       
HET     ZN  E 155       1                                                       
HET     ZN  F 155       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   7   ZN    6(ZN 2+)                                                     
FORMUL  13  HOH   *722(H2 O)                                                    
HELIX    1   1 CYS A   57  GLY A   61  5                                   5    
HELIX    2   2 ASN A  131  GLY A  138  1                                   8    
HELIX    3   3 CYS B   57  GLY B   61  5                                   5    
HELIX    4   4 GLU B  133  GLY B  138  1                                   6    
HELIX    5   5 CYS C   57  GLY C   61  5                                   5    
HELIX    6   6 GLU C  133  GLY C  138  1                                   6    
HELIX    7   7 CYS D   57  GLY D   61  5                                   5    
HELIX    8   8 CYS E   57  GLY E   61  5                                   5    
HELIX    9   9 ASN E  131  GLY E  138  1                                   8    
HELIX   10  10 CYS F   57  GLY F   61  5                                   5    
HELIX   11  11 SER F  107  SER F  111  5                                   5    
HELIX   12  12 GLU F  133  GLY F  138  1                                   6    
SHEET    1   A 5 ALA A  95  ASP A 101  0                                        
SHEET    2   A 5 VAL A  29  THR A  36 -1  N  ILE A  35   O  ALA A  95           
SHEET    3   A 5 GLN A  15  GLN A  22 -1  N  HIS A  19   O  SER A  32           
SHEET    4   A 5 MET A   2  LYS A   9 -1  N  MET A   2   O  GLN A  22           
SHEET    5   A 5 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5           
SHEET    1   B 4 ASP A  83  ALA A  89  0                                        
SHEET    2   B 4 GLY A  41  HIS A  48 -1  N  GLY A  41   O  ALA A  89           
SHEET    3   B 4 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    4   B 4 ARG A 143  VAL A 148 -1  O  GLY A 147   N  MET A 117           
SHEET    1   C 5 ALA B  95  ASP B 101  0                                        
SHEET    2   C 5 VAL B  29  THR B  36 -1  N  LEU B  31   O  ILE B  99           
SHEET    3   C 5 GLN B  15  GLN B  22 -1  N  HIS B  19   O  SER B  32           
SHEET    4   C 5 MET B   2  LYS B   9 -1  N  LEU B   8   O  GLY B  16           
SHEET    5   C 5 GLY B 150  ILE B 151 -1  O  GLY B 150   N  VAL B   5           
SHEET    1   D 4 ASP B  83  ALA B  89  0                                        
SHEET    2   D 4 GLY B  41  HIS B  48 -1  N  GLY B  41   O  ALA B  89           
SHEET    3   D 4 THR B 116  HIS B 120 -1  O  THR B 116   N  HIS B  48           
SHEET    4   D 4 ARG B 143  VAL B 148 -1  O  LEU B 144   N  VAL B 119           
SHEET    1   E 5 ALA C  95  ASP C 101  0                                        
SHEET    2   E 5 VAL C  29  THR C  36 -1  N  LEU C  31   O  ILE C  99           
SHEET    3   E 5 GLN C  15  GLN C  22 -1  N  HIS C  19   O  SER C  32           
SHEET    4   E 5 MET C   2  LEU C   8 -1  N  LEU C   8   O  GLY C  16           
SHEET    5   E 5 GLY C 150  ILE C 151 -1  O  GLY C 150   N  VAL C   5           
SHEET    1   F 4 ASP C  83  ALA C  89  0                                        
SHEET    2   F 4 GLY C  41  HIS C  48 -1  N  GLY C  41   O  ALA C  89           
SHEET    3   F 4 THR C 116  HIS C 120 -1  O  THR C 116   N  HIS C  48           
SHEET    4   F 4 ARG C 143  VAL C 148 -1  O  ALA C 145   N  VAL C 119           
SHEET    1   G 5 ALA D  95  ASP D 101  0                                        
SHEET    2   G 5 VAL D  29  THR D  36 -1  N  LEU D  31   O  ILE D  99           
SHEET    3   G 5 GLN D  15  GLN D  22 -1  N  HIS D  19   O  SER D  32           
SHEET    4   G 5 MET D   2  LEU D   8 -1  N  ALA D   4   O  PHE D  20           
SHEET    5   G 5 GLY D 150  ILE D 151 -1  O  GLY D 150   N  VAL D   5           
SHEET    1   H 4 ASP D  83  ALA D  89  0                                        
SHEET    2   H 4 GLY D  41  HIS D  48 -1  N  GLY D  41   O  ALA D  89           
SHEET    3   H 4 THR D 116  HIS D 120 -1  O  THR D 116   N  HIS D  48           
SHEET    4   H 4 ARG D 143  VAL D 148 -1  O  GLY D 147   N  MET D 117           
SHEET    1   I 5 ALA E  95  ASP E 101  0                                        
SHEET    2   I 5 VAL E  29  THR E  36 -1  N  ILE E  35   O  ALA E  95           
SHEET    3   I 5 GLN E  15  GLN E  22 -1  N  GLN E  15   O  THR E  36           
SHEET    4   I 5 MET E   2  LEU E   8 -1  N  CYS E   6   O  ILE E  18           
SHEET    5   I 5 GLY E 150  ILE E 151 -1  O  GLY E 150   N  VAL E   5           
SHEET    1   J 4 ASP E  83  ALA E  89  0                                        
SHEET    2   J 4 GLY E  41  HIS E  48 -1  N  GLY E  41   O  ALA E  89           
SHEET    3   J 4 THR E 116  HIS E 120 -1  O  THR E 116   N  HIS E  48           
SHEET    4   J 4 ARG E 143  VAL E 148 -1  O  GLY E 147   N  MET E 117           
SHEET    1   K 5 ALA F  95  ASP F 101  0                                        
SHEET    2   K 5 VAL F  29  THR F  36 -1  N  LEU F  31   O  ILE F  99           
SHEET    3   K 5 GLN F  15  GLN F  22 -1  N  GLU F  21   O  VAL F  30           
SHEET    4   K 5 MET F   2  LEU F   8 -1  N  CYS F   6   O  ILE F  18           
SHEET    5   K 5 GLY F 150  ILE F 151 -1  O  GLY F 150   N  VAL F   5           
SHEET    1   L 4 ASP F  83  ALA F  89  0                                        
SHEET    2   L 4 GLY F  41  HIS F  48 -1  N  PHE F  45   O  GLY F  85           
SHEET    3   L 4 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    4   L 4 ARG F 143  VAL F 148 -1  O  LEU F 144   N  VAL F 119           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.64  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.90  
SSBOND   3 CYS C   57    CYS C  146                          1555   1555  2.84  
SSBOND   4 CYS D   57    CYS D  146                          1555   1555  2.83  
SSBOND   5 CYS E   57    CYS E  146                          1555   1555  2.79  
SSBOND   6 CYS F   57    CYS F  146                          1555   1555  2.75  
LINK         ND1 HIS A  63                ZN    ZN A 155     1555   1555  2.17  
LINK         ND1 HIS A  71                ZN    ZN A 155     1555   1555  2.28  
LINK         ND1 HIS A  80                ZN    ZN A 155     1555   1555  2.13  
LINK         OD1 ASP A  83                ZN    ZN A 155     1555   1555  2.00  
LINK         ND1 HIS B  63                ZN    ZN B 155     1555   1555  2.14  
LINK         ND1 HIS B  71                ZN    ZN B 155     1555   1555  2.28  
LINK         ND1 HIS B  80                ZN    ZN B 155     1555   1555  2.20  
LINK         OD1 ASP B  83                ZN    ZN B 155     1555   1555  1.94  
LINK         ND1 HIS C  63                ZN    ZN C 155     1555   1555  2.24  
LINK         ND1 HIS C  71                ZN    ZN C 155     1555   1555  2.25  
LINK         ND1 HIS C  80                ZN    ZN C 155     1555   1555  2.33  
LINK         OD1 ASP C  83                ZN    ZN C 155     1555   1555  1.99  
LINK         ND1 HIS D  63                ZN    ZN D 155     1555   1555  2.15  
LINK         ND1 HIS D  80                ZN    ZN D 155     1555   1555  2.21  
LINK         OD1 ASP D  83                ZN    ZN D 155     1555   1555  1.99  
LINK         ND1 HIS E  63                ZN    ZN E 155     1555   1555  2.20  
LINK         ND1 HIS E  71                ZN    ZN E 155     1555   1555  2.34  
LINK         ND1 HIS E  80                ZN    ZN E 155     1555   1555  2.10  
LINK         OD1 ASP E  83                ZN    ZN E 155     1555   1555  1.91  
LINK         ND1 HIS F  63                ZN    ZN F 155     1555   1555  2.25  
LINK         ND1 HIS F  71                ZN    ZN F 155     1555   1555  2.12  
LINK         ND1 HIS F  80                ZN    ZN F 155     1555   1555  2.27  
LINK         OD1 ASP F  83                ZN    ZN F 155     1555   1555  1.97  
LINK         ND1 HIS D  71                ZN    ZN D 155     1555   1555  2.43  
SITE     1 AC1  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC2  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     1 AC3  5 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
SITE     2 AC3  5 LYS C 136                                                     
SITE     1 AC4  4 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     1 AC5  4 HIS E  63  HIS E  71  HIS E  80  ASP E  83                    
SITE     1 AC6  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
CRYST1  112.454  194.495  149.841  90.00  90.00  90.00 C 2 2 21     48          
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      0.008893  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005142  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006674        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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