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Database: PDB
Entry: 1PL4
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Original site: 1PL4 
HEADER    OXIDOREDUCTASE                          06-JUN-03   1PL4              
TITLE     CRYSTAL STRUCTURE OF HUMAN MNSOD Y166F MUTANT                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL;                  
COMPND   3 CHAIN: A, B, C, D;                                                   
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 ORGANELLE: MITOCHONDRIA;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: QC774;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PTRC99A                                   
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.FAN,J.A.TAINER                                                      
REVDAT   4   11-OCT-17 1PL4    1       REMARK                                   
REVDAT   3   24-FEB-09 1PL4    1       VERSN                                    
REVDAT   2   30-MAR-04 1PL4    1       JRNL                                     
REVDAT   1   16-DEC-03 1PL4    0                                                
JRNL        AUTH   A.S.HEARN,L.FAN,J.R.LEPOCK,J.P.LUBA,W.B.GREENLEAF,           
JRNL        AUTH 2 D.E.CABELLI,J.A.TAINER,H.S.NICK,D.N.SILVERMAN                
JRNL        TITL   AMINO ACID SUBSTITUTION AT THE DIMERIC INTERFACE OF HUMAN    
JRNL        TITL 2 MANGANESE SUPEROXIDE DISMUTASE                               
JRNL        REF    J.BIOL.CHEM.                  V. 279  5861 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   14638684                                                     
JRNL        DOI    10.1074/JBC.M311310200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.47 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL                                               
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.47                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 4.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.0                           
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.201                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.200                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.237                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 5218                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 123830                 
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.186                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 104006                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 6249                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 4                                             
REMARK   3   SOLVENT ATOMS      : 680                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 6934.0                  
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 6052.0                  
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 0                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 27839                   
REMARK   3   NUMBER OF RESTRAINTS                     : 25962                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.005                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.024                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : NULL                    
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : NULL                    
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : NULL                    
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : NULL                    
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL                    
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL                    
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL                    
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REDUCED FREE R     
REMARK   3  (NO CUTOFF)                                                         
REMARK   4                                                                      
REMARK   4 1PL4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000019405.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-DEC-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 123885                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : 0.04900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.47                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.38600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
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: PDB ENTRY 1ABM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, POTASSIUM PHOSPHATE, PH 7.6,   
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 298.0K                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       36.84450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.89750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.85550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.89750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.84450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.85550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE FOUR MOLECULES IN THE ASYMMETRIC UNIT REVEAL THE         
REMARK 300 BIOLOGICAL TETRAMERIC ASSEMBLY.                                      
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                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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     LYS B   197                                                      
REMARK 465     LYS B   198                                                      
REMARK 465     LYS C   198                                                      
REMARK 465     LYS D   198                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS D  31   ND1   HIS D  31   CE1    -0.098                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    HIS A  31   CB  -  CG  -  CD2 ANGL. DEV. =   9.6 DEGREES          
REMARK 500    HIS A  31   CG  -  ND1 -  CE1 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    TYR A  45   CB  -  CG  -  CD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    TYR A  45   CB  -  CG  -  CD1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    TRP A  78   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    TRP A  78   CD1 -  NE1 -  CE2 ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ARG A 192   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    HIS B  31   CB  -  CG  -  CD2 ANGL. DEV. =  14.3 DEGREES          
REMARK 500    HIS B  31   CB  -  CG  -  ND1 ANGL. DEV. = -10.0 DEGREES          
REMARK 500    TRP B  78   CD1 -  NE1 -  CE2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ARG B  99   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ASP B 144   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    HIS C  31   CB  -  CG  -  CD2 ANGL. DEV. =  12.7 DEGREES          
REMARK 500    HIS C  31   CG  -  ND1 -  CE1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    TYR C  34   CG  -  CD1 -  CE1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    TYR C  34   CG  -  CD2 -  CE2 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    TYR C  34   CD1 -  CE1 -  CZ  ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    TYR C  34   CZ  -  CE2 -  CD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    TYR C  45   CB  -  CG  -  CD2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    TRP C  78   CB  -  CG  -  CD1 ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    TRP C  78   CD1 -  NE1 -  CE2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    HIS D  31   CB  -  CG  -  CD2 ANGL. DEV. =  15.9 DEGREES          
REMARK 500    HIS D  31   ND1 -  CG  -  CD2 ANGL. DEV. =  -8.9 DEGREES          
REMARK 500    HIS D  31   CG  -  ND1 -  CE1 ANGL. DEV. =  12.1 DEGREES          
REMARK 500    TYR D 176   CB  -  CG  -  CD1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG D 192   CD  -  NE  -  CZ  ANGL. DEV. =  27.3 DEGREES          
REMARK 500    ARG D 192   NE  -  CZ  -  NH1 ANGL. DEV. =  -8.1 DEGREES          
REMARK 500    ARG D 192   NE  -  CZ  -  NH2 ANGL. DEV. =   4.1 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    LYS A  29      -62.36   -109.05                                   
REMARK 500    ASN A 142     -126.52     58.37                                   
REMARK 500    TYR A 165      -20.93   -147.86                                   
REMARK 500    LYS A 170     -135.43     50.46                                   
REMARK 500    ASN B 142     -121.49     52.36                                   
REMARK 500    TYR B 165      -19.03   -146.96                                   
REMARK 500    LYS B 170     -135.97     58.22                                   
REMARK 500    ASN C 142     -122.56     52.35                                   
REMARK 500    TYR C 165      -17.42   -147.50                                   
REMARK 500    LYS C 170     -137.38     55.31                                   
REMARK 500    ASN D 142     -126.22     58.64                                   
REMARK 500    TYR D 165      -17.50   -146.88                                   
REMARK 500    LYS D 170     -135.05     54.08                                   
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                              MN A 200  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  26   NE2                                                    
REMARK 620 2 HIS A  74   NE2  88.4                                              
REMARK 620 3 ASP A 159   OD2  82.7 108.4                                        
REMARK 620 4 HIS A 163   NE2  89.9 136.4 114.6                                  
REMARK 620 5 HOH A 201   O   175.0  88.5  94.6  95.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 200  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  26   NE2                                                    
REMARK 620 2 HIS B  74   NE2  86.9                                              
REMARK 620 3 ASP B 159   OD2  84.2 112.2                                        
REMARK 620 4 HIS B 163   NE2  85.7 130.1 115.9                                  
REMARK 620 5 HOH B 202   O   176.6  93.2  92.6  96.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 200  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  26   NE2                                                    
REMARK 620 2 HIS C  74   NE2  87.5                                              
REMARK 620 3 ASP C 159   OD2  84.9 110.9                                        
REMARK 620 4 HIS C 163   NE2  90.0 131.0 117.6                                  
REMARK 620 5 HOH C 203   O   174.6  87.4  95.4  94.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 200  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  26   NE2                                                    
REMARK 620 2 HIS D  74   NE2  85.4                                              
REMARK 620 3 ASP D 159   OD2  85.4 114.5                                        
REMARK 620 4 HIS D 163   NE2  88.0 130.0 114.3                                  
REMARK 620 5 HOH D 204   O   175.7  91.5  98.6  91.8                            
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 200                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 200                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 200                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 200                  
DBREF  1PL4 A    1   198  UNP    P04179   SODM_HUMAN      25    222             
DBREF  1PL4 B    1   198  UNP    P04179   SODM_HUMAN      25    222             
DBREF  1PL4 C    1   198  UNP    P04179   SODM_HUMAN      25    222             
DBREF  1PL4 D    1   198  UNP    P04179   SODM_HUMAN      25    222             
SEQADV 1PL4 PHE A  166  UNP  P04179    TYR   190 ENGINEERED                     
SEQADV 1PL4 PHE B  166  UNP  P04179    TYR   190 ENGINEERED                     
SEQADV 1PL4 PHE C  166  UNP  P04179    TYR   190 ENGINEERED                     
SEQADV 1PL4 PHE D  166  UNP  P04179    TYR   190 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 TYR 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 PHE 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 TYR 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 PHE 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                                                  
SEQRES   1 C  198  LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR GLY ALA          
SEQRES   2 C  198  LEU GLU PRO HIS ILE ASN ALA GLN ILE MET GLN LEU HIS          
SEQRES   3 C  198  HIS SER LYS HIS HIS ALA ALA TYR VAL ASN ASN LEU ASN          
SEQRES   4 C  198  VAL THR GLU GLU LYS TYR GLN GLU ALA LEU ALA LYS GLY          
SEQRES   5 C  198  ASP VAL THR ALA GLN ILE ALA LEU GLN PRO ALA LEU LYS          
SEQRES   6 C  198  PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE TRP          
SEQRES   7 C  198  THR ASN LEU SER PRO ASN GLY GLY GLY GLU PRO LYS GLY          
SEQRES   8 C  198  GLU LEU LEU GLU ALA ILE LYS ARG ASP PHE GLY SER PHE          
SEQRES   9 C  198  ASP LYS PHE LYS GLU LYS LEU THR ALA ALA SER VAL GLY          
SEQRES  10 C  198  VAL GLN GLY SER GLY TRP GLY TRP LEU GLY PHE ASN LYS          
SEQRES  11 C  198  GLU ARG GLY HIS LEU GLN ILE ALA ALA CYS PRO ASN GLN          
SEQRES  12 C  198  ASP PRO LEU GLN GLY THR THR GLY LEU ILE PRO LEU LEU          
SEQRES  13 C  198  GLY ILE ASP VAL TRP GLU HIS ALA TYR PHE LEU GLN TYR          
SEQRES  14 C  198  LYS ASN VAL ARG PRO ASP TYR LEU LYS ALA ILE TRP ASN          
SEQRES  15 C  198  VAL ILE ASN TRP GLU ASN VAL THR GLU ARG TYR MET ALA          
SEQRES  16 C  198  CYS LYS LYS                                                  
SEQRES   1 D  198  LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR GLY ALA          
SEQRES   2 D  198  LEU GLU PRO HIS ILE ASN ALA GLN ILE MET GLN LEU HIS          
SEQRES   3 D  198  HIS SER LYS HIS HIS ALA ALA TYR VAL ASN ASN LEU ASN          
SEQRES   4 D  198  VAL THR GLU GLU LYS TYR GLN GLU ALA LEU ALA LYS GLY          
SEQRES   5 D  198  ASP VAL THR ALA GLN ILE ALA LEU GLN PRO ALA LEU LYS          
SEQRES   6 D  198  PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE TRP          
SEQRES   7 D  198  THR ASN LEU SER PRO ASN GLY GLY GLY GLU PRO LYS GLY          
SEQRES   8 D  198  GLU LEU LEU GLU ALA ILE LYS ARG ASP PHE GLY SER PHE          
SEQRES   9 D  198  ASP LYS PHE LYS GLU LYS LEU THR ALA ALA SER VAL GLY          
SEQRES  10 D  198  VAL GLN GLY SER GLY TRP GLY TRP LEU GLY PHE ASN LYS          
SEQRES  11 D  198  GLU ARG GLY HIS LEU GLN ILE ALA ALA CYS PRO ASN GLN          
SEQRES  12 D  198  ASP PRO LEU GLN GLY THR THR GLY LEU ILE PRO LEU LEU          
SEQRES  13 D  198  GLY ILE ASP VAL TRP GLU HIS ALA TYR PHE LEU GLN TYR          
SEQRES  14 D  198  LYS ASN VAL ARG PRO ASP TYR LEU LYS ALA ILE TRP ASN          
SEQRES  15 D  198  VAL ILE ASN TRP GLU ASN VAL THR GLU ARG TYR MET ALA          
SEQRES  16 D  198  CYS LYS LYS                                                  
HET     MN  A 200       1                                                       
HET     MN  B 200       1                                                       
HET     MN  C 200       1                                                       
HET     MN  D 200       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   9  HOH   *680(H2 O)                                                    
HELIX    1   1 ASN A   19  LYS A   29  1                                  11    
HELIX    2   2 LYS A   29  LYS A   51  1                                  23    
HELIX    3   3 ASP A   53  LEU A   60  1                                   8    
HELIX    4   4 LEU A   60  ASN A   80  1                                  21    
HELIX    5   5 LYS A   90  GLY A  102  1                                  13    
HELIX    6   6 SER A  103  GLY A  117  1                                  15    
HELIX    7   7 PRO A  145  GLY A  151  1                                   7    
HELIX    8   8 TRP A  161  ALA A  164  5                                   4    
HELIX    9   9 TYR A  165  LYS A  170  1                                   6    
HELIX   10  10 VAL A  172  TRP A  181  1                                  10    
HELIX   11  11 ASN A  182  ILE A  184  5                                   3    
HELIX   12  12 ASN A  185  CYS A  196  1                                  12    
HELIX   13  13 ASN B   19  LYS B   29  1                                  11    
HELIX   14  14 LYS B   29  LYS B   51  1                                  23    
HELIX   15  15 ASP B   53  ASN B   80  1                                  28    
HELIX   16  16 LYS B   90  GLY B  102  1                                  13    
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    
HELIX   24  24 ASN C   19  LYS C   29  1                                  11    
HELIX   25  25 LYS C   29  LYS C   51  1                                  23    
HELIX   26  26 ASP C   53  LEU C   60  1                                   8    
HELIX   27  27 LEU C   60  ASN C   80  1                                  21    
HELIX   28  28 LYS C   90  GLY C  102  1                                  13    
HELIX   29  29 SER C  103  GLY C  117  1                                  15    
HELIX   30  30 PRO C  145  GLY C  151  1                                   7    
HELIX   31  31 TRP C  161  ALA C  164  5                                   4    
HELIX   32  32 TYR C  165  LYS C  170  1                                   6    
HELIX   33  33 VAL C  172  TRP C  181  1                                  10    
HELIX   34  34 ASN C  182  ILE C  184  5                                   3    
HELIX   35  35 ASN C  185  ALA C  195  1                                  11    
HELIX   36  36 ASN D   19  LYS D   29  1                                  11    
HELIX   37  37 LYS D   29  LYS D   51  1                                  23    
HELIX   38  38 ASP D   53  ASN D   80  1                                  28    
HELIX   39  39 GLY D   91  GLY D  102  1                                  12    
HELIX   40  40 SER D  103  GLY D  117  1                                  15    
HELIX   41  41 PRO D  145  GLY D  151  1                                   7    
HELIX   42  42 TRP D  161  ALA D  164  5                                   4    
HELIX   43  43 TYR D  165  LYS D  170  1                                   6    
HELIX   44  44 VAL D  172  TRP D  181  1                                  10    
HELIX   45  45 ASN D  182  ILE D  184  5                                   3    
HELIX   46  46 ASN D  185  ALA D  195  1                                  11    
SHEET    1   A 3 HIS A 134  PRO A 141  0                                        
SHEET    2   A 3 GLY A 122  ASN A 129 -1  N  TRP A 125   O  ALA A 138           
SHEET    3   A 3 ILE A 153  ASP A 159 -1  O  LEU A 156   N  LEU A 126           
SHEET    1   B 3 HIS B 134  PRO B 141  0                                        
SHEET    2   B 3 GLY B 122  ASN B 129 -1  N  ASN B 129   O  HIS B 134           
SHEET    3   B 3 ILE B 153  ASP B 159 -1  O  ILE B 158   N  GLY B 124           
SHEET    1   C 3 HIS C 134  PRO C 141  0                                        
SHEET    2   C 3 GLY C 122  ASN C 129 -1  N  ASN C 129   O  HIS C 134           
SHEET    3   C 3 ILE C 153  ASP C 159 -1  O  ILE C 158   N  GLY C 124           
SHEET    1   D 3 HIS D 134  PRO D 141  0                                        
SHEET    2   D 3 GLY D 122  ASN D 129 -1  N  ASN D 129   O  HIS D 134           
SHEET    3   D 3 ILE D 153  ASP D 159 -1  O  LEU D 155   N  LEU D 126           
LINK         NE2 HIS A  26                MN    MN A 200     1555   1555  2.18  
LINK         NE2 HIS A  74                MN    MN A 200     1555   1555  2.22  
LINK         OD2 ASP A 159                MN    MN A 200     1555   1555  2.05  
LINK         NE2 HIS A 163                MN    MN A 200     1555   1555  2.16  
LINK         NE2 HIS B  26                MN    MN B 200     1555   1555  2.21  
LINK         NE2 HIS B  74                MN    MN B 200     1555   1555  2.14  
LINK         OD2 ASP B 159                MN    MN B 200     1555   1555  1.96  
LINK         NE2 HIS B 163                MN    MN B 200     1555   1555  2.21  
LINK         NE2 HIS C  26                MN    MN C 200     1555   1555  2.20  
LINK         NE2 HIS C  74                MN    MN C 200     1555   1555  2.20  
LINK         OD2 ASP C 159                MN    MN C 200     1555   1555  2.03  
LINK         NE2 HIS C 163                MN    MN C 200     1555   1555  2.19  
LINK         NE2 HIS D  26                MN    MN D 200     1555   1555  2.16  
LINK         NE2 HIS D  74                MN    MN D 200     1555   1555  2.15  
LINK         OD2 ASP D 159                MN    MN D 200     1555   1555  2.01  
LINK         NE2 HIS D 163                MN    MN D 200     1555   1555  2.16  
LINK        MN    MN A 200                 O   HOH A 201     1555   1555  1.98  
LINK        MN    MN B 200                 O   HOH B 202     1555   1555  2.10  
LINK        MN    MN C 200                 O   HOH C 203     1555   1555  1.99  
LINK        MN    MN D 200                 O   HOH D 204     1555   1555  1.89  
CISPEP   1 GLU A   15    PRO A   16          0        -0.42                     
CISPEP   2 GLU B   15    PRO B   16          0        -1.62                     
CISPEP   3 GLU C   15    PRO C   16          0         0.42                     
CISPEP   4 GLU D   15    PRO D   16          0        -0.29                     
SITE     1 AC1  5 HIS A  26  HIS A  74  ASP A 159  HIS A 163                    
SITE     2 AC1  5 HOH A 201                                                     
SITE     1 AC2  5 HIS B  26  HIS B  74  ASP B 159  HIS B 163                    
SITE     2 AC2  5 HOH B 202                                                     
SITE     1 AC3  5 HIS C  26  HIS C  74  ASP C 159  HIS C 163                    
SITE     2 AC3  5 HOH C 203                                                     
SITE     1 AC4  5 HIS D  26  HIS D  74  ASP D 159  HIS D 163                    
SITE     2 AC4  5 HOH D 204                                                     
CRYST1   73.689   77.711  135.795  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013571  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012868  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007364        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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