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Database: PDB
Entry: 1ZSP
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Original site: 1ZSP 
HEADER    OXIDOREDUCTASE                          24-MAY-05   1ZSP              
TITLE     CONTRIBUTION TO STRUCTURE AND CATALYSIS OF TYROSINE 34 IN HUMAN       
TITLE    2 MANGANESE SUPEROXIDE DISMUTASE                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SOD2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: QC774I (SOD--);                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PTRC99A                                   
KEYWDS    MNSOD, MANGANESE SUPEROXIDE DISMUTASE, Y34A MUTATION, OXIDOREDUCTASE  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.S.HEARN,J.J.PERRY,D.E.CABELLI,J.A.TAINER,H.S.NICK,D.S.SILVERMAN     
REVDAT   5   13-JUL-11 1ZSP    1       VERSN                                    
REVDAT   4   26-MAY-09 1ZSP    1       JRNL                                     
REVDAT   3   07-APR-09 1ZSP    1       JRNL                                     
REVDAT   2   24-FEB-09 1ZSP    1       VERSN                                    
REVDAT   1   02-MAY-06 1ZSP    0                                                
JRNL        AUTH   J.J.PERRY,A.S.HEARN,D.E.CABELLI,H.S.NICK,J.A.TAINER,         
JRNL        AUTH 2 D.N.SILVERMAN                                                
JRNL        TITL   CONTRIBUTION OF HUMAN MANGANESE SUPEROXIDE DISMUTASE         
JRNL        TITL 2 TYROSINE 34 TO STRUCTURE AND CATALYSIS.                      
JRNL        REF    BIOCHEMISTRY                  V.  48  3417 2009              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   19265433                                                     
JRNL        DOI    10.1021/BI8023288                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.56                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 671904.810                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 31760                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.236                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1724                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5392                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2570                       
REMARK   3   BIN FREE R VALUE                    : 0.3070                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 266                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3132                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 414                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.19000                                              
REMARK   3    B22 (A**2) : 0.19000                                              
REMARK   3    B33 (A**2) : -0.38000                                             
REMARK   3    B12 (A**2) : 3.10000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.15                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.30                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.19                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.79                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.380 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.070 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.090 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.930 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 93.37                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ZSP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB033072.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.06                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI (111)            
REMARK 200  OPTICS                         : KOHZU: DOUBLE CRYSTAL SI(111)      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31760                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.560                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 48.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 11.500                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1N0J.PDB                                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5 M AMMONIUM SULFATE, 100MM            
REMARK 280  IMIDAZOLE, PH 7.50, VAPOR DIFFUSION, TEMPERATURE 293K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       80.99667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      161.99333            
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      121.49500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      202.49167            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       40.49833            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       80.99667            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      161.99333            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      202.49167            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      121.49500            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       40.49833            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER                        
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 8310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 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   BIOMT1   2  0.500000 -0.866025  0.000000       39.75750            
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000       68.86201            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      202.49167            
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 B5023  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A5012  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B5152  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A5221  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B5167  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 142     -124.05     48.84                                   
REMARK 500    TYR A 165      -17.09   -151.21                                   
REMARK 500    LYS A 170     -136.56     53.09                                   
REMARK 500    ASN B 142     -123.92     46.74                                   
REMARK 500    TYR B 165      -18.62   -154.14                                   
REMARK 500    LYS B 170     -142.95     56.07                                   
REMARK 500    LYS B 197      -74.20    -81.36                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A5085        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH A5105        DISTANCE =  6.52 ANGSTROMS                       
REMARK 525    HOH A5124        DISTANCE =  5.46 ANGSTROMS                       
REMARK 525    HOH A5127        DISTANCE =  6.76 ANGSTROMS                       
REMARK 525    HOH A5130        DISTANCE =  5.75 ANGSTROMS                       
REMARK 525    HOH A5141        DISTANCE =  5.45 ANGSTROMS                       
REMARK 525    HOH A5175        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH A5182        DISTANCE =  8.28 ANGSTROMS                       
REMARK 525    HOH A5187        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH A5191        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH A5192        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH A5205        DISTANCE =  7.94 ANGSTROMS                       
REMARK 525    HOH A5208        DISTANCE =  5.38 ANGSTROMS                       
REMARK 525    HOH A5217        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH A5221        DISTANCE =  7.49 ANGSTROMS                       
REMARK 525    HOH A5231        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH A5232        DISTANCE =  9.46 ANGSTROMS                       
REMARK 525    HOH A5238        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH A5239        DISTANCE =  7.81 ANGSTROMS                       
REMARK 525    HOH B5090        DISTANCE =  5.59 ANGSTROMS                       
REMARK 525    HOH B5094        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH B5132        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH B5134        DISTANCE =  7.50 ANGSTROMS                       
REMARK 525    HOH B5145        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH B5152        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH B5159        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH B5170        DISTANCE =  7.76 ANGSTROMS                       
REMARK 525    HOH B5181        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH B5184        DISTANCE =  9.48 ANGSTROMS                       
REMARK 525    HOH B5185        DISTANCE =  6.63 ANGSTROMS                       
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                              MN A 199  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  26   NE2                                                    
REMARK 620 2 HIS A  74   NE2  93.9                                              
REMARK 620 3 ASP A 159   OD1  85.3 110.4                                        
REMARK 620 4 HIS A 163   NE2  90.8 134.1 115.4                                  
REMARK 620 5 HOH A5011   O   166.2  91.2  80.9  94.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 199  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  26   NE2                                                    
REMARK 620 2 HIS B  74   NE2  83.5                                              
REMARK 620 3 ASP B 159   OD1  85.2 113.6                                        
REMARK 620 4 HIS B 163   NE2  92.3 138.7 106.8                                  
REMARK 620 5 HOH B5022   O   165.3  93.8  82.8  99.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 199                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 199                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ZTE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1ZUQ   RELATED DB: PDB                                   
DBREF  1ZSP A    1   198  UNP    P04179   SODM_HUMAN      25    222             
DBREF  1ZSP B    1   198  UNP    P04179   SODM_HUMAN      25    222             
SEQADV 1ZSP ALA A   34  UNP  P04179    TYR    58 ENGINEERED                     
SEQADV 1ZSP ALA B   34  UNP  P04179    TYR    58 ENGINEERED                     
SEQRES   1 A  198  LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR GLY ALA          
SEQRES   2 A  198  LEU GLU PRO HIS ILE ASN ALA GLN ILE MET GLN LEU HIS          
SEQRES   3 A  198  HIS SER LYS HIS HIS ALA ALA ALA VAL ASN ASN LEU ASN          
SEQRES   4 A  198  VAL THR GLU GLU LYS TYR GLN GLU ALA LEU ALA LYS GLY          
SEQRES   5 A  198  ASP VAL THR ALA GLN ILE ALA LEU GLN PRO ALA LEU LYS          
SEQRES   6 A  198  PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE TRP          
SEQRES   7 A  198  THR ASN LEU SER PRO ASN GLY GLY GLY GLU PRO LYS GLY          
SEQRES   8 A  198  GLU LEU LEU GLU ALA ILE LYS ARG ASP PHE GLY SER PHE          
SEQRES   9 A  198  ASP LYS PHE LYS GLU LYS LEU THR ALA ALA SER VAL GLY          
SEQRES  10 A  198  VAL GLN GLY SER GLY TRP GLY TRP LEU GLY PHE ASN LYS          
SEQRES  11 A  198  GLU ARG GLY HIS LEU GLN ILE ALA ALA CYS PRO ASN GLN          
SEQRES  12 A  198  ASP PRO LEU GLN GLY THR THR GLY LEU ILE PRO LEU LEU          
SEQRES  13 A  198  GLY ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU GLN TYR          
SEQRES  14 A  198  LYS ASN VAL ARG PRO ASP TYR LEU LYS ALA ILE TRP ASN          
SEQRES  15 A  198  VAL ILE ASN TRP GLU ASN VAL THR GLU ARG TYR MET ALA          
SEQRES  16 A  198  CYS LYS LYS                                                  
SEQRES   1 B  198  LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR GLY ALA          
SEQRES   2 B  198  LEU GLU PRO HIS ILE ASN ALA GLN ILE MET GLN LEU HIS          
SEQRES   3 B  198  HIS SER LYS HIS HIS ALA ALA ALA VAL ASN ASN LEU ASN          
SEQRES   4 B  198  VAL THR GLU GLU LYS TYR GLN GLU ALA LEU ALA LYS GLY          
SEQRES   5 B  198  ASP VAL THR ALA GLN ILE ALA LEU GLN PRO ALA LEU LYS          
SEQRES   6 B  198  PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE TRP          
SEQRES   7 B  198  THR ASN LEU SER PRO ASN GLY GLY GLY GLU PRO LYS GLY          
SEQRES   8 B  198  GLU LEU LEU GLU ALA ILE LYS ARG ASP PHE GLY SER PHE          
SEQRES   9 B  198  ASP LYS PHE LYS GLU LYS LEU THR ALA ALA SER VAL GLY          
SEQRES  10 B  198  VAL GLN GLY SER GLY TRP GLY TRP LEU GLY PHE ASN LYS          
SEQRES  11 B  198  GLU ARG GLY HIS LEU GLN ILE ALA ALA CYS PRO ASN GLN          
SEQRES  12 B  198  ASP PRO LEU GLN GLY THR THR GLY LEU ILE PRO LEU LEU          
SEQRES  13 B  198  GLY ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU GLN TYR          
SEQRES  14 B  198  LYS ASN VAL ARG PRO ASP TYR LEU LYS ALA ILE TRP ASN          
SEQRES  15 B  198  VAL ILE ASN TRP GLU ASN VAL THR GLU ARG TYR MET ALA          
SEQRES  16 B  198  CYS LYS LYS                                                  
HET     MN  A 199       1                                                       
HET     MN  B 199       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   5  HOH   *414(H2 O)                                                    
HELIX    1   1 ASN A   19  LYS A   29  1                                  11    
HELIX    2   2 LYS A   29  GLY A   52  1                                  24    
HELIX    3   3 ASP A   53  ASN A   80  1                                  28    
HELIX    4   4 LYS A   90  GLY A  102  1                                  13    
HELIX    5   5 SER A  103  GLY A  117  1                                  15    
HELIX    6   6 PRO A  145  GLY A  151  1                                   7    
HELIX    7   7 TRP A  161  ALA A  164  5                                   4    
HELIX    8   8 TYR A  165  LYS A  170  1                                   6    
HELIX    9   9 VAL A  172  TRP A  181  1                                  10    
HELIX   10  10 ASN A  182  ILE A  184  5                                   3    
HELIX   11  11 ASN A  185  LYS A  198  1                                  14    
HELIX   12  12 ASN B   19  LYS B   29  1                                  11    
HELIX   13  13 LYS B   29  LYS B   51  1                                  23    
HELIX   14  14 ASP B   53  LEU B   60  1                                   8    
HELIX   15  15 LEU B   60  ASN B   80  1                                  21    
HELIX   16  16 GLY B   91  GLY B  102  1                                  12    
HELIX   17  17 SER B  103  GLY B  117  1                                  15    
HELIX   18  18 PRO B  145  GLY B  151  1                                   7    
HELIX   19  19 TRP B  161  ALA B  164  5                                   4    
HELIX   20  20 TYR B  165  LYS B  170  1                                   6    
HELIX   21  21 VAL B  172  TRP B  181  1                                  10    
HELIX   22  22 ASN B  182  ILE B  184  5                                   3    
HELIX   23  23 ASN B  185  CYS B  196  1                                  12    
SHEET    1   A 3 HIS A 134  PRO A 141  0                                        
SHEET    2   A 3 GLY A 122  ASN A 129 -1  N  GLY A 127   O  GLN A 136           
SHEET    3   A 3 ILE A 153  ASP A 159 -1  O  ILE A 158   N  GLY A 124           
SHEET    1   B 3 HIS B 134  PRO B 141  0                                        
SHEET    2   B 3 GLY B 122  ASN B 129 -1  N  GLY B 127   O  GLN B 136           
SHEET    3   B 3 ILE B 153  ASP B 159 -1  O  ILE B 158   N  GLY B 124           
LINK        MN    MN A 199                 NE2 HIS A  26     1555   1555  2.18  
LINK        MN    MN A 199                 NE2 HIS A  74     1555   1555  2.22  
LINK        MN    MN A 199                 OD1 ASP A 159     1555   1555  2.00  
LINK        MN    MN A 199                 NE2 HIS A 163     1555   1555  2.15  
LINK        MN    MN B 199                 NE2 HIS B  26     1555   1555  2.18  
LINK        MN    MN B 199                 NE2 HIS B  74     1555   1555  2.19  
LINK        MN    MN B 199                 OD1 ASP B 159     1555   1555  2.00  
LINK        MN    MN B 199                 NE2 HIS B 163     1555   1555  2.14  
LINK        MN    MN A 199                 O   HOH A5011     1555   1555  2.16  
LINK        MN    MN B 199                 O   HOH B5022     1555   1555  2.14  
CISPEP   1 GLU A   15    PRO A   16          0        -0.01                     
CISPEP   2 GLU B   15    PRO B   16          0         0.10                     
SITE     1 AC1  5 HIS A  26  HIS A  74  ASP A 159  HIS A 163                    
SITE     2 AC1  5 HOH A5011                                                     
SITE     1 AC2  5 HIS B  26  HIS B  74  ASP B 159  HIS B 163                    
SITE     2 AC2  5 HOH B5022                                                     
CRYST1   79.515   79.515  242.990  90.00  90.00 120.00 P 61 2 2     24          
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      0.012576  0.007261  0.000000        0.00000                         
SCALE2      0.000000  0.014522  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004115        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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