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Database: PDB
Entry: 1GV3
LinkDB: 1GV3
Original site: 1GV3 
HEADER    MANGANESE SUPEROXIDE DISMUTASE          05-FEB-02   1GV3              
TITLE     THE 2.0 ANGSTROM RESOLUTION STRUCTURE OF THE CATALYTIC                
TITLE    2 PORTION OF A CYANOBACTERIAL MEMBRANE-BOUND MANGANESE                 
TITLE    3 SUPEROXIDE DISMUTASE                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MANGANESE SUPEROXIDE DISMUTASE;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: HELICAL HAIRPIN, ALPHA/BETA DOMAIN, RESIDUES               
COMPND   5  30-270;                                                             
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ANABAENA SP.;                                   
SOURCE   3 ORGANISM_TAXID: 103690;                                              
SOURCE   4 STRAIN: PCC 7120;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET-3A                                    
KEYWDS    MANGANESE SUPEROXIDE DISMUTASE, ANABAENA PCC 7120, CRYSTAL            
KEYWDS   2 STRUCTURE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.ATZENHOFER,G.REGELSBERGER,U.JACOB,R.HUBER,G.A.PESCHEK,              
AUTHOR   2 C.OBINGER                                                            
REVDAT   3   24-FEB-09 1GV3    1       VERSN                                    
REVDAT   2   16-JAN-03 1GV3    1       COMPND DBREF                             
REVDAT   1   08-AUG-02 1GV3    0                                                
JRNL        AUTH   W.ATZENHOFER,G.REGELSBERGER,U.JACOB,G.A.PESCHEK,             
JRNL        AUTH 2 P.FURTMULLER,R.HUBER,C.OBINGER                               
JRNL        TITL   THE 2.0A RESOLUTION STRUCTURE OF THE CATALYTIC               
JRNL        TITL 2 PORTION OF A CYANOBACTERIAL MEMBRANE-BOUND                   
JRNL        TITL 3 MANGANESE SUPEROXIDE DISMUTASE                               
JRNL        REF    J.MOL.BIOL.                   V. 321   479 2002              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   12162960                                                     
JRNL        DOI    10.1016/S0022-2836(02)00624-1                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.0  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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100                            
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000                          
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 33267                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.191                        
REMARK   3   BIN FREE R VALUE                    : 0.212                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3440                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 166                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.69                                                 
REMARK   3    B22 (A**2) : 1.69                                                 
REMARK   3    B33 (A**2) : -3.39                                                
REMARK   3    B12 (A**2) : 0.34                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.0057                          
REMARK   3   BOND ANGLES            (DEGREES) : 1.248                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.33  ; 1.50                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.33  ; 2.00                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.13  ; 2.00                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.55  ; 2.50                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1GV3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  05-FEB-02.                 
REMARK 100 THE PDBE ID CODE IS EBI-9391.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 287.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 3                                  
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 ROTATING ANODE              
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.518                              
REMARK 200  MONOCHROMATOR                  : GRAPHIT                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35333                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.030                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.570                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: 1MNG                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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        0.00000            
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        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       75.66000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       43.68232            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       23.09333            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       75.66000            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       43.68232            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       23.09333            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       75.66000            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       43.68232            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       23.09333            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       87.36464            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       46.18667            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       87.36464            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       46.18667            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       87.36464            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       46.18667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
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 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     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     PRO A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     ASN A     9                                                      
REMARK 465     VAL A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     PRO A    13                                                      
REMARK 465     VAL A    14                                                      
REMARK 465     GLN A    15                                                      
REMARK 465     THR A    16                                                      
REMARK 465     THR A    17                                                      
REMARK 465     THR A    18                                                      
REMARK 465     PRO A    19                                                      
REMARK 465     THR A    20                                                      
REMARK 465     THR A    21                                                      
REMARK 465     ASP A    22                                                      
REMARK 465     LYS A    23                                                      
REMARK 465     ARG A    24                                                      
REMARK 465     GLN A   239                                                      
REMARK 465     SER A   240                                                      
REMARK 465     ASN A   241                                                      
REMARK 465     SER A   242                                                      
REMARK 465     HIS A   243                                                      
REMARK 465     HIS A   244                                                      
REMARK 465     HIS A   245                                                      
REMARK 465     HIS A   246                                                      
REMARK 465     HIS A   247                                                      
REMARK 465     HIS A   248                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ASN B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     PRO B     7                                                      
REMARK 465     THR B     8                                                      
REMARK 465     ASN B     9                                                      
REMARK 465     VAL B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     PRO B    13                                                      
REMARK 465     VAL B    14                                                      
REMARK 465     GLN B    15                                                      
REMARK 465     THR B    16                                                      
REMARK 465     THR B    17                                                      
REMARK 465     THR B    18                                                      
REMARK 465     PRO B    19                                                      
REMARK 465     THR B    20                                                      
REMARK 465     THR B    21                                                      
REMARK 465     ASP B    22                                                      
REMARK 465     LYS B    23                                                      
REMARK 465     ARG B    24                                                      
REMARK 465     GLN B   239                                                      
REMARK 465     SER B   240                                                      
REMARK 465     ASN B   241                                                      
REMARK 465     SER B   242                                                      
REMARK 465     HIS B   243                                                      
REMARK 465     HIS B   244                                                      
REMARK 465     HIS B   245                                                      
REMARK 465     HIS B   246                                                      
REMARK 465     HIS B   247                                                      
REMARK 465     HIS B   248                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 238    CA   C    O    CB   CG   CD   NE   CZ   NH1  NH2    
REMARK 470     ARG B 238    CA   C    O    CB   CG   CD   NE   CZ   NH1  NH2    
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CG1  ILE A    29  -  O    HOH A  2078              1.40            
REMARK 500   CD1  ILE A    29  -  O    HOH A  2078              1.31            
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 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    ALA A  53      -46.24   -146.27                                   
REMARK 500    LYS A  65      -60.39   -104.32                                   
REMARK 500    ASN A 184     -116.84     45.69                                   
REMARK 500    TYR A 206       -2.57   -145.33                                   
REMARK 500    GLN A 211     -123.60     54.98                                   
REMARK 500    ALA B  53      -44.49   -144.86                                   
REMARK 500    ASN B 184     -117.69     46.45                                   
REMARK 500    TYR B 206       -2.10   -147.90                                   
REMARK 500    GLN B 211     -128.90     56.08                                   
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 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 A1238  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 117   NE2                                                    
REMARK 620 2 HIS A 204   NE2 137.0                                              
REMARK 620 3 HIS A  62   NE2  86.7  87.8                                        
REMARK 620 4 ASP A 200   OD2 105.8 116.5  87.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B1238  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 200   OD2                                                    
REMARK 620 2 HIS B 117   NE2 107.9                                              
REMARK 620 3 HIS B  62   NE2  92.5  86.1                                        
REMARK 620 4 HIS B 204   NE2 115.0 137.1  94.0                                  
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  MN A1238                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN B1238                 
DBREF  1GV3 A    1     1  PDB    1GV3     1GV3             1      1             
DBREF  1GV3 A    2   242  UNP    Q8Z0M1   Q8Z0M1_ANASP    30    270             
DBREF  1GV3 A  243   248  PDB    1GV3     1GV3           243    248             
DBREF  1GV3 B    1     1  PDB    1GV3     1GV3             1      1             
DBREF  1GV3 B    2   242  UNP    Q8Z0M1   Q8Z0M1_ANASP    30    270             
DBREF  1GV3 B  243   248  PDB    1GV3     1GV3           243    248             
SEQADV 1GV3 VAL A  179  UNP  Q8Z0M1    ILE   207 CONFLICT                       
SEQADV 1GV3 ASN A  187  UNP  Q8Z0M1    SER   215 CONFLICT                       
SEQADV 1GV3 VAL B  179  UNP  Q8Z0M1    ILE   207 CONFLICT                       
SEQADV 1GV3 ASN B  187  UNP  Q8Z0M1    SER   215 CONFLICT                       
SEQRES   1 A  248  MET ALA ALA ASN SER LEU PRO THR ASN VAL ALA SER PRO          
SEQRES   2 A  248  VAL GLN THR THR THR PRO THR THR ASP LYS ARG SER ILE          
SEQRES   3 A  248  GLY PHE ILE ASP ARG GLN LEU GLY THR ASN PRO ALA GLU          
SEQRES   4 A  248  LEU PRO PRO LEU PRO TYR GLY TYR ASP ALA LEU GLU LYS          
SEQRES   5 A  248  ALA ILE ASP ALA GLU THR MET LYS LEU HIS HIS ASP LYS          
SEQRES   6 A  248  HIS HIS ALA ALA TYR VAL ASN ASN LEU ASN ASN ALA LEU          
SEQRES   7 A  248  LYS LYS HIS PRO GLU LEU GLN ASN SER SER VAL GLU ALA          
SEQRES   8 A  248  LEU LEU ARG ASP LEU ASN SER VAL PRO GLU ASP ILE ARG          
SEQRES   9 A  248  THR THR VAL ARG ASN ASN GLY GLY GLY HIS LEU ASN HIS          
SEQRES  10 A  248  THR ILE PHE TRP GLN ILE MET SER PRO ASP GLY GLY GLY          
SEQRES  11 A  248  GLN PRO THR GLY ASP ILE ALA GLN GLU ILE ASN GLN THR          
SEQRES  12 A  248  PHE GLY SER PHE GLU GLU PHE LYS LYS GLN PHE ASN GLN          
SEQRES  13 A  248  ALA GLY GLY ASP ARG PHE GLY SER GLY TRP VAL TRP LEU          
SEQRES  14 A  248  VAL ARG ASN PRO GLN GLY GLN LEU GLN VAL VAL SER THR          
SEQRES  15 A  248  PRO ASN GLN ASP ASN PRO ILE MET GLU GLY SER TYR PRO          
SEQRES  16 A  248  ILE MET GLY ASN ASP VAL TRP GLU HIS ALA TYR TYR LEU          
SEQRES  17 A  248  ARG TYR GLN ASN ARG ARG PRO GLU TYR LEU ASN ASN TRP          
SEQRES  18 A  248  TRP ASN VAL VAL ASN TRP SER GLU ILE ASN ARG ARG THR          
SEQRES  19 A  248  GLN ALA SER ARG GLN SER ASN SER HIS HIS HIS HIS HIS          
SEQRES  20 A  248  HIS                                                          
SEQRES   1 B  248  MET ALA ALA ASN SER LEU PRO THR ASN VAL ALA SER PRO          
SEQRES   2 B  248  VAL GLN THR THR THR PRO THR THR ASP LYS ARG SER ILE          
SEQRES   3 B  248  GLY PHE ILE ASP ARG GLN LEU GLY THR ASN PRO ALA GLU          
SEQRES   4 B  248  LEU PRO PRO LEU PRO TYR GLY TYR ASP ALA LEU GLU LYS          
SEQRES   5 B  248  ALA ILE ASP ALA GLU THR MET LYS LEU HIS HIS ASP LYS          
SEQRES   6 B  248  HIS HIS ALA ALA TYR VAL ASN ASN LEU ASN ASN ALA LEU          
SEQRES   7 B  248  LYS LYS HIS PRO GLU LEU GLN ASN SER SER VAL GLU ALA          
SEQRES   8 B  248  LEU LEU ARG ASP LEU ASN SER VAL PRO GLU ASP ILE ARG          
SEQRES   9 B  248  THR THR VAL ARG ASN ASN GLY GLY GLY HIS LEU ASN HIS          
SEQRES  10 B  248  THR ILE PHE TRP GLN ILE MET SER PRO ASP GLY GLY GLY          
SEQRES  11 B  248  GLN PRO THR GLY ASP ILE ALA GLN GLU ILE ASN GLN THR          
SEQRES  12 B  248  PHE GLY SER PHE GLU GLU PHE LYS LYS GLN PHE ASN GLN          
SEQRES  13 B  248  ALA GLY GLY ASP ARG PHE GLY SER GLY TRP VAL TRP LEU          
SEQRES  14 B  248  VAL ARG ASN PRO GLN GLY GLN LEU GLN VAL VAL SER THR          
SEQRES  15 B  248  PRO ASN GLN ASP ASN PRO ILE MET GLU GLY SER TYR PRO          
SEQRES  16 B  248  ILE MET GLY ASN ASP VAL TRP GLU HIS ALA TYR TYR LEU          
SEQRES  17 B  248  ARG TYR GLN ASN ARG ARG PRO GLU TYR LEU ASN ASN TRP          
SEQRES  18 B  248  TRP ASN VAL VAL ASN TRP SER GLU ILE ASN ARG ARG THR          
SEQRES  19 B  248  GLN ALA SER ARG GLN SER ASN SER HIS HIS HIS HIS HIS          
SEQRES  20 B  248  HIS                                                          
HET     MN  A1238       1                                                       
HET     MN  B1238       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   5  HOH   *166(H2 O1)                                                   
HELIX    1   1 ASP A   55  LYS A   65  1                                  11    
HELIX    2   2 LYS A   65  LYS A   80  1                                  16    
HELIX    3   3 HIS A   81  SER A   87  5                                   7    
HELIX    4   4 SER A   88  ASP A   95  1                                   8    
HELIX    5   5 LEU A   96  VAL A   99  5                                   4    
HELIX    6   6 ILE A  103  ILE A  123  1                                  21    
HELIX    7   7 THR A  133  GLY A  145  1                                  13    
HELIX    8   8 SER A  146  ARG A  161  1                                  16    
HELIX    9   9 ASN A  187  GLY A  192  5                                   6    
HELIX   10  10 TRP A  202  ALA A  205  5                                   4    
HELIX   11  11 TYR A  206  GLN A  211  1                                   6    
HELIX   12  12 ARG A  213  TRP A  221  1                                   9    
HELIX   13  13 TRP A  222  VAL A  224  5                                   3    
HELIX   14  14 ASN A  226  SER A  237  1                                  12    
HELIX   15  15 ASP B   55  LYS B   65  1                                  11    
HELIX   16  16 LYS B   65  LYS B   80  1                                  16    
HELIX   17  17 HIS B   81  GLN B   85  5                                   5    
HELIX   18  18 SER B   88  ASP B   95  1                                   8    
HELIX   19  19 LEU B   96  VAL B   99  5                                   4    
HELIX   20  20 ILE B  103  ILE B  123  1                                  21    
HELIX   21  21 THR B  133  GLY B  145  1                                  13    
HELIX   22  22 SER B  146  ARG B  161  1                                  16    
HELIX   23  23 ASN B  187  GLY B  192  5                                   6    
HELIX   24  24 TRP B  202  ALA B  205  5                                   4    
HELIX   25  25 TYR B  206  GLN B  211  1                                   6    
HELIX   26  26 ARG B  213  TRP B  222  1                                  10    
HELIX   27  27 ASN B  226  SER B  237  1                                  12    
SHEET    1  AA 3 LEU A 177  PRO A 183  0                                        
SHEET    2  AA 3 GLY A 165  ARG A 171 -1  O  TRP A 166   N  THR A 182           
SHEET    3  AA 3 TYR A 194  ASP A 200 -1  O  TYR A 194   N  ARG A 171           
SHEET    1  BA 3 LEU B 177  PRO B 183  0                                        
SHEET    2  BA 3 GLY B 165  ARG B 171 -1  O  TRP B 166   N  THR B 182           
SHEET    3  BA 3 TYR B 194  ASP B 200 -1  O  TYR B 194   N  ARG B 171           
LINK        MN    MN A1238                 NE2 HIS A 117     1555   1555  2.16  
LINK        MN    MN A1238                 NE2 HIS A 204     1555   1555  2.23  
LINK        MN    MN A1238                 NE2 HIS A  62     1555   1555  2.20  
LINK        MN    MN A1238                 OD2 ASP A 200     1555   1555  2.02  
LINK        MN    MN B1238                 NE2 HIS B 117     1555   1555  2.20  
LINK        MN    MN B1238                 NE2 HIS B  62     1555   1555  2.15  
LINK        MN    MN B1238                 NE2 HIS B 204     1555   1555  2.17  
LINK        MN    MN B1238                 OD2 ASP B 200     1555   1555  1.99  
CISPEP   1 ASN A   36    PRO A   37          0        -0.32                     
CISPEP   2 ASN B   36    PRO B   37          0        -0.31                     
SITE     1 AC1  5 HIS A  62  HIS A 117  ASP A 200  HIS A 204                    
SITE     2 AC1  5 HOH A2079                                                     
SITE     1 AC2  5 HIS B  62  HIS B 117  ASP B 200  HIS B 204                    
SITE     2 AC2  5 HOH B2087                                                     
CRYST1  151.320  151.320   69.280  90.00  90.00 120.00 H 3          18          
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      0.006608  0.003815  0.000000        0.00000                         
SCALE2      0.000000  0.007631  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014434        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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