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Database: PDB
Entry: 5AG2
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HEADER    OXIDOREDUCTASE                          27-JAN-15   5AG2              
TITLE     SOD-3 AZIDE COMPLEX                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [MN] 2, MITOCHONDRIAL;                
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: MANGANESE SUPEROXIDE DISMUTASE;                             
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;                         
SOURCE   3 ORGANISM_TAXID: 6239;                                                
SOURCE   4 STRAIN: N2;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: OX326A;                                    
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PTRC99A                                    
KEYWDS    OXIDOREDUCTASE, MANGANESE                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.J.HUNTER,C.H.TRINH,R.BONETTA,E.E.STEWART,D.E.CABELLI,T.HUNTER       
REVDAT   1   13-JAN-16 5AG2    0                                                
JRNL        AUTH   G.J.HUNTER,C.H.TRINH,R.BONETTA,E.E.STEWART,D.E.CABELLI,      
JRNL        AUTH 2 T.HUNTER                                                     
JRNL        TITL   THE STRUCTURE OF THE CAENORHABDITIS ELEGANS MANGANESE        
JRNL        TITL 2 SUPEROXIDE DISMUTASE MNSOD-3-AZIDE COMPLEX.                  
JRNL        REF    PROTEIN SCI.                  V.  24  1777 2015              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   26257399                                                     
JRNL        DOI    10.1002/PRO.2768                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.77 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,NICHOLLS,WINN,LONG,VAGIN                     
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.58                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.90                          
REMARK   3   NUMBER OF REFLECTIONS             : 44455                          
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 + TEST SET) : 0.18614                         
REMARK   3   R VALUE            (WORKING SET) : 0.18455                         
REMARK   3   FREE R VALUE                     : 0.21573                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2363                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.766                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.812                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3228                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.97                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.242                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 164                          
REMARK   3   BIN FREE R VALUE                    : 0.266                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3138                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 384                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) :  31.396                        
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.17                                                
REMARK   3    B22 (A**2) : -1.17                                                
REMARK   3    B33 (A**2) : 2.34                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.115         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.110         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.075         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.196         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3288 ; 0.011 ; 0.019       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4466 ; 1.363 ; 1.932       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   398 ; 5.599 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   166 ;32.151 ;25.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   553 ;13.039 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;11.073 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   468 ; 0.099 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2533 ; 0.007 ; 0.021       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1570 ; 0.816 ; 1.691       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1961 ; 1.403 ; 2.525       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1717 ; 1.085 ; 1.822       
REMARK   3   LONG RANGE B REFINED ATOMS (A**2)    :  5523 ; 5.769 ;15.719       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  :    2                                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     1                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   193                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.6580   6.0590  -0.7910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0678 T22:   0.0220                                     
REMARK   3      T33:   0.1150 T12:   0.0339                                     
REMARK   3      T13:   0.0415 T23:   0.0360                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2414 L22:   1.9331                                     
REMARK   3      L33:   1.5895 L12:   0.3511                                     
REMARK   3      L13:  -0.0356 L23:  -0.8882                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0256 S12:  -0.0489 S13:  -0.1367                       
REMARK   3      S21:  -0.1681 S22:  -0.1656 S23:  -0.4049                       
REMARK   3      S31:   0.3029 S32:   0.1629 S33:   0.1912                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     2                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     0        C   194                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.6520  -2.6260  14.3540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0492 T22:   0.1296                                     
REMARK   3      T33:   0.0876 T12:   0.0070                                     
REMARK   3      T13:   0.0441 T23:   0.0565                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4187 L22:   1.1962                                     
REMARK   3      L33:   1.1065 L12:  -0.1751                                     
REMARK   3      L13:   0.2885 L23:  -0.4205                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0011 S12:  -0.3145 S13:  -0.0640                       
REMARK   3      S21:   0.1603 S22:   0.0978 S23:   0.2396                       
REMARK   3      S31:  -0.0595 S32:  -0.2497 S33:  -0.0989                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED :  MASK                                                
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   :   1.20                                        
REMARK   3   ION PROBE RADIUS   :   0.80                                        
REMARK   3   SHRINKAGE RADIUS   :   0.80                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT                    
REMARK   3  U VALUES WITH TLS ADDED                                             
REMARK   4                                                                      
REMARK   4 5AG2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JAN-15.                  
REMARK 100 THE PDBE ID CODE IS EBI-62815.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-AUG-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX10.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : SI(III)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (MARMOSAIC 225)                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46922                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.77                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.38                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.9                               
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.70                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.3                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.00                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 3DC5                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.6                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.8M AMMONIUM SULPHATE, 0.1M             
REMARK 280  BICINE PH 9.0                                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.80500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       41.03000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       41.03000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       34.40250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       41.03000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       41.03000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      103.20750            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       41.03000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       41.03000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       34.40250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       41.03000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       41.03000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      103.20750            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       68.80500            
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 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.2 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2133   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH C2145   LIES ON A SPECIAL POSITION.                         
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     0                                                      
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     LYS A   1    CG   CD   CE   NZ                                   
REMARK 470     LYS A  90    CG   CD   CE   NZ                                   
REMARK 470     LYS A 130    CG   CD   CE   NZ                                   
REMARK 470     LYS C  90    CG   CD   CE   NZ                                   
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   O    HOH A  2050     O    HOH A  2051              2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  29      -61.10   -106.45                                   
REMARK 500    ASN A 141     -118.68     54.43                                   
REMARK 500    LYS A 166     -130.86     53.38                                   
REMARK 500    ASP C  84       79.53   -110.80                                   
REMARK 500    ASN C 141     -118.86     54.05                                   
REMARK 500    TYR C 161      -20.32   -141.51                                   
REMARK 500    LYS C 166     -134.93     55.07                                   
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 195  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  26   NE2                                                    
REMARK 620 2 ASP A 155   OD2  83.9                                              
REMARK 620 3 HOH A2096   O   168.9  85.3                                        
REMARK 620 4 HIS A  74   NE2  93.9 100.9  90.5                                  
REMARK 620 5 AZI A 196   N3  104.6 171.4  86.3  77.2                            
REMARK 620 6 HIS A 159   NE2  91.8 114.2  90.5 144.9  67.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 195  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 159   NE2                                                    
REMARK 620 2 HIS C  26   NE2  90.2                                              
REMARK 620 3 ASP C 155   OD2 111.7  84.7                                        
REMARK 620 4 AZI C 196   N3   71.0  98.6 175.8                                  
REMARK 620 5 HOH C2108   O    92.3 170.5  85.8  90.9                            
REMARK 620 6 HIS C  74   NE2 147.9  92.4 100.4  77.0  90.4                      
REMARK 620 N                    1     2     3     4     5                       
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 195                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI A 196                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN C 195                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI C 196                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1195                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1195                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A1196                 
DBREF  5AG2 A    1   194  UNP    P41977   SODM2_CAEEL     25    218             
DBREF  5AG2 C    1   194  UNP    P41977   SODM2_CAEEL     25    218             
SEQADV 5AG2 MET A    0  UNP  P41977              EXPRESSION TAG                 
SEQADV 5AG2 MET C    0  UNP  P41977              EXPRESSION TAG                 
SEQRES   1 A  195  MET LYS HIS THR LEU PRO ASP LEU PRO PHE ASP TYR ALA          
SEQRES   2 A  195  ASP LEU GLU PRO VAL ILE SER HIS GLU ILE MET GLN LEU          
SEQRES   3 A  195  HIS HIS GLN LYS HIS HIS ALA THR TYR VAL ASN ASN LEU          
SEQRES   4 A  195  ASN GLN ILE GLU GLU LYS LEU HIS GLU ALA VAL SER LYS          
SEQRES   5 A  195  GLY ASN LEU LYS GLU ALA ILE ALA LEU GLN PRO ALA LEU          
SEQRES   6 A  195  LYS PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE          
SEQRES   7 A  195  TRP THR ASN LEU ALA LYS ASP GLY GLY GLU PRO SER LYS          
SEQRES   8 A  195  GLU LEU MET ASP THR ILE LYS ARG ASP PHE GLY SER LEU          
SEQRES   9 A  195  ASP ASN LEU GLN LYS ARG LEU SER ASP ILE THR ILE ALA          
SEQRES  10 A  195  VAL GLN GLY SER GLY TRP GLY TRP LEU GLY TYR OCS LYS          
SEQRES  11 A  195  LYS ASP LYS ILE LEU LYS ILE ALA THR CYS ALA ASN GLN          
SEQRES  12 A  195  ASP PRO LEU GLU GLY MET VAL PRO LEU PHE GLY ILE ASP          
SEQRES  13 A  195  VAL TRP GLU HIS ALA TYR TYR LEU GLN TYR LYS ASN VAL          
SEQRES  14 A  195  ARG PRO ASP TYR VAL HIS ALA ILE TRP LYS ILE ALA ASN          
SEQRES  15 A  195  TRP LYS ASN ILE SER GLU ARG PHE ALA ASN ALA ARG GLN          
SEQRES   1 C  195  MET LYS HIS THR LEU PRO ASP LEU PRO PHE ASP TYR ALA          
SEQRES   2 C  195  ASP LEU GLU PRO VAL ILE SER HIS GLU ILE MET GLN LEU          
SEQRES   3 C  195  HIS HIS GLN LYS HIS HIS ALA THR TYR VAL ASN ASN LEU          
SEQRES   4 C  195  ASN GLN ILE GLU GLU LYS LEU HIS GLU ALA VAL SER LYS          
SEQRES   5 C  195  GLY ASN LEU LYS GLU ALA ILE ALA LEU GLN PRO ALA LEU          
SEQRES   6 C  195  LYS PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE          
SEQRES   7 C  195  TRP THR ASN LEU ALA LYS ASP GLY GLY GLU PRO SER LYS          
SEQRES   8 C  195  GLU LEU MET ASP THR ILE LYS ARG ASP PHE GLY SER LEU          
SEQRES   9 C  195  ASP ASN LEU GLN LYS ARG LEU SER ASP ILE THR ILE ALA          
SEQRES  10 C  195  VAL GLN GLY SER GLY TRP GLY TRP LEU GLY TYR OCS LYS          
SEQRES  11 C  195  LYS ASP LYS ILE LEU LYS ILE ALA THR CYS ALA ASN GLN          
SEQRES  12 C  195  ASP PRO LEU GLU GLY MET VAL PRO LEU PHE GLY ILE ASP          
SEQRES  13 C  195  VAL TRP GLU HIS ALA TYR TYR LEU GLN TYR LYS ASN VAL          
SEQRES  14 C  195  ARG PRO ASP TYR VAL HIS ALA ILE TRP LYS ILE ALA ASN          
SEQRES  15 C  195  TRP LYS ASN ILE SER GLU ARG PHE ALA ASN ALA ARG GLN          
MODRES 5AG2 OCS A  128  CYS  CYSTEINESULFONIC ACID                              
MODRES 5AG2 OCS C  128  CYS  CYSTEINESULFONIC ACID                              
HET    OCS  A 128       9                                                       
HET     MN  A 195       1                                                       
HET    AZI  A 196       3                                                       
HET    OCS  C 128       9                                                       
HET     MN  C 195       1                                                       
HET    AZI  C 196       3                                                       
HET    ACT  A1195       4                                                       
HET    SO4  C1195       5                                                       
HET    MLI  A1196       7                                                       
HETNAM     AZI AZIDE ION                                                        
HETNAM     MLI MALONATE ION                                                     
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ACT ACETATE ION                                                      
HETNAM     OCS CYSTEINESULFONIC ACID                                            
FORMUL   3  AZI    2(N3 1-)                                                     
FORMUL   4  MLI    C3 H2 O4 2-                                                  
FORMUL   5   MN    2(MN 2+)                                                     
FORMUL   6  SO4    O4 S 2-                                                      
FORMUL   7  ACT    C2 H3 O2 1-                                                  
FORMUL   8  OCS    2(C3 H7 N O5 S)                                              
FORMUL   9  HOH   *384(H2 O)                                                    
HELIX    1   1 SER A   19  LYS A   29  1                                  11    
HELIX    2   2 LYS A   29  GLY A   52  1                                  24    
HELIX    3   3 ASN A   53  LEU A   60  1                                   8    
HELIX    4   4 LEU A   60  ASN A   80  1                                  21    
HELIX    5   5 SER A   89  GLY A  101  1                                  13    
HELIX    6   6 SER A  102  ALA A  116  1                                  15    
HELIX    7   7 TRP A  157  ALA A  160  5                                   4    
HELIX    8   8 TYR A  161  LYS A  166  1                                   6    
HELIX    9   9 VAL A  168  TRP A  177  1                                  10    
HELIX   10  10 ASN A  181  ARG A  193  1                                  13    
HELIX   11  11 SER C   19  LYS C   29  1                                  11    
HELIX   12  12 LYS C   29  GLY C   52  1                                  24    
HELIX   13  13 ASN C   53  LEU C   60  1                                   8    
HELIX   14  14 LEU C   60  ASN C   80  1                                  21    
HELIX   15  15 SER C   89  GLY C  101  1                                  13    
HELIX   16  16 SER C  102  ALA C  116  1                                  15    
HELIX   17  17 TRP C  157  ALA C  160  5                                   4    
HELIX   18  18 TYR C  161  LYS C  166  1                                   6    
HELIX   19  19 VAL C  168  TRP C  177  1                                  10    
HELIX   20  20 ASN C  181  ARG C  193  1                                  13    
SHEET    1  AA 3 ILE A 133  ALA A 140  0                                        
SHEET    2  AA 3 GLY A 121  OCS A 128 -1  O  TRP A 122   N  CYS A 139           
SHEET    3  AA 3 VAL A 149  ASP A 155 -1  O  VAL A 149   N  TYR A 127           
SHEET    1  CA 3 ILE C 133  ALA C 140  0                                        
SHEET    2  CA 3 GLY C 121  OCS C 128 -1  O  TRP C 122   N  CYS C 139           
SHEET    3  CA 3 VAL C 149  ASP C 155 -1  O  VAL C 149   N  TYR C 127           
LINK         C   TYR A 127                 N   OCS A 128     1555   1555  1.33  
LINK         C   OCS A 128                 N   LYS A 129     1555   1555  1.33  
LINK        MN    MN A 195                 NE2 HIS A  26     1555   1555  2.25  
LINK        MN    MN A 195                 OD2 ASP A 155     1555   1555  2.03  
LINK        MN    MN A 195                 O   HOH A2096     1555   1555  2.24  
LINK        MN    MN A 195                 NE2 HIS A  74     1555   1555  2.16  
LINK        MN    MN A 195                 NE2 HIS A 159     1555   1555  2.20  
LINK        MN    MN A 195                 N3  AZI A 196     1555   1555  2.77  
LINK         C   TYR C 127                 N   OCS C 128     1555   1555  1.34  
LINK         C   OCS C 128                 N   LYS C 129     1555   1555  1.33  
LINK        MN    MN C 195                 NE2 HIS C  74     1555   1555  2.18  
LINK        MN    MN C 195                 O   HOH C2108     1555   1555  2.15  
LINK        MN    MN C 195                 OD2 ASP C 155     1555   1555  2.11  
LINK        MN    MN C 195                 NE2 HIS C  26     1555   1555  2.17  
LINK        MN    MN C 195                 NE2 HIS C 159     1555   1555  2.11  
LINK        MN    MN C 195                 N3  AZI C 196     1555   1555  2.64  
CISPEP   1 GLU A   15    PRO A   16          0         9.98                     
CISPEP   2 GLU C   15    PRO C   16          0         8.28                     
SITE     1 AC1  6 HIS A  26  HIS A  74  ASP A 155  HIS A 159                    
SITE     2 AC1  6 AZI A 196  HOH A2096                                          
SITE     1 AC2  8 HIS A  26  HIS A  30  HIS A  31  TYR A  34                    
SITE     2 AC2  8 HIS A  74  HIS A 159   MN A 195  HOH A2048                    
SITE     1 AC3  6 HIS C  26  HIS C  74  ASP C 155  HIS C 159                    
SITE     2 AC3  6 AZI C 196  HOH C2108                                          
SITE     1 AC4  8 HIS C  26  HIS C  30  HIS C  31  TYR C  34                    
SITE     2 AC4  8 HIS C  74  HIS C 159   MN C 195  HOH C2049                    
SITE     1 AC5  3 HIS A   2  THR A   3  HIS A  71                               
SITE     1 AC6  2 LYS C  51  ASN C  53                                          
SITE     1 AC7 10 ASN A 167  VAL A 168  HOH A2044  HOH A2050                    
SITE     2 AC7 10 HOH A2056  HOH A2184  HOH A2185  HOH A2186                    
SITE     3 AC7 10 HOH A2187  HOH A2188                                          
CRYST1   82.060   82.060  137.610  90.00  90.00  90.00 P 41 21 2    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      0.012186  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012186  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007267        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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