GenomeNet

Database: PDB
Entry: 2AW9
LinkDB: 2AW9
Original site: 2AW9 
HEADER    OXIDOREDUCTASE                          31-AUG-05   2AW9              
TITLE     SUPEROXIDE DISMUTASE WITH MANGANESE FROM DEINOCOCCUS RADIODURANS      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [MN];                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: MNSOD;                                                      
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE   3 ORGANISM_TAXID: 1299;                                                
SOURCE   4 GENE: SODA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)GOLD;                             
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.TANAKA,M.R.SAWAYA,S.CHAN,L.J.PERRY                                  
REVDAT   3   13-JUL-11 2AW9    1       VERSN                                    
REVDAT   2   24-FEB-09 2AW9    1       VERSN                                    
REVDAT   1   22-AUG-06 2AW9    0                                                
JRNL        AUTH   S.TANAKA,M.R.SAWAYA,S.CHAN,L.J.PERRY                         
JRNL        TITL   CRYSTAL STRUCTURE OF MANGANESE SUPEROXIDE DISMUTASE FROM     
JRNL        TITL 2 DEINOCOCCUS RADIODURANS                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 62.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 11008                          
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) : 0.170                           
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 572                             
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 605                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.28                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3340                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 31                           
REMARK   3   BIN FREE R VALUE                    : 0.4130                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3287                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 25                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.11000                                             
REMARK   3    B22 (A**2) : -4.47000                                             
REMARK   3    B33 (A**2) : 8.08000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 4.59000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.332         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.277         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.357        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3375 ; 0.010 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2892 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4589 ; 1.742 ; 1.917       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6731 ; 0.956 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   414 ; 7.430 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   176 ;37.663 ;24.886       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   513 ;16.974 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;13.944 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   476 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3858 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   696 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   775 ; 0.231 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2805 ; 0.190 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1699 ; 0.193 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1773 ; 0.097 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    76 ; 0.101 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     6 ; 0.161 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):     9 ; 0.208 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.236 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2626 ; 0.805 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   854 ; 0.145 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3291 ; 0.991 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1572 ; 1.584 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1298 ; 2.568 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     211      1                      
REMARK   3           1     B      1       B     211      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3072 ;  0.05 ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   3072 ;  0.13 ;  0.50           
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     1        A   213                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.6681  16.4545   5.8683              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1846 T22:  -0.1396                                     
REMARK   3      T33:   0.0939 T12:  -0.0108                                     
REMARK   3      T13:   0.0380 T23:  -0.0975                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8133 L22:   3.6846                                     
REMARK   3      L33:   1.1026 L12:   0.0181                                     
REMARK   3      L13:  -0.0267 L23:  -1.0123                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0222 S12:   0.0312 S13:  -0.0675                       
REMARK   3      S21:   0.3591 S22:  -0.0823 S23:   0.1046                       
REMARK   3      S31:  -0.0984 S32:   0.0151 S33:   0.1045                       
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 :   B     1        B   211                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.0314  19.1377 -22.8558              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2405 T22:  -0.0007                                     
REMARK   3      T33:   0.1578 T12:   0.0405                                     
REMARK   3      T13:   0.1608 T23:  -0.1284                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4057 L22:   2.8699                                     
REMARK   3      L33:   1.9063 L12:  -0.2293                                     
REMARK   3      L13:  -0.1355 L23:   0.0907                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0116 S12:   0.3028 S13:  -0.2119                       
REMARK   3      S21:  -1.1666 S22:  -0.1090 S23:  -0.3161                       
REMARK   3      S31:  -0.0493 S32:  -0.1316 S33:   0.1206                       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2AW9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB034387.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUN-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5499                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL, SI(111)            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DCS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11594                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 90.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.6                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.3297                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.23500                            
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: EPMR                                                  
REMARK 200 STARTING MODEL: 1Y67                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MAGNESIUM CHLORIDE, TRIS-                
REMARK 280  HYDROCHLORIDE, PEG 4000, PH 8.5, VAPOR DIFFUSION, SITTING DROP,     
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       41.74950            
REMARK 290   SMTRY3   2  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 ASYMMETRIC UNIT CONTAINS A DIMER WHICH CORRESPONDS TO    
REMARK 300 THE BIOLOGICAL 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 465     GLN A    94                                                      
REMARK 465     ASN A    95                                                      
REMARK 465     GLY A    96                                                      
REMARK 465     PRO A   214                                                      
REMARK 465     ARG A   215                                                      
REMARK 465     GLY A   216                                                      
REMARK 465     SER A   217                                                      
REMARK 465     ALA A   218                                                      
REMARK 465     ALA A   219                                                      
REMARK 465     ALA A   220                                                      
REMARK 465     LEU A   221                                                      
REMARK 465     GLU A   222                                                      
REMARK 465     HIS A   223                                                      
REMARK 465     HIS A   224                                                      
REMARK 465     HIS A   225                                                      
REMARK 465     HIS A   226                                                      
REMARK 465     HIS A   227                                                      
REMARK 465     HIS A   228                                                      
REMARK 465     MET B     0                                                      
REMARK 465     GLN B    94                                                      
REMARK 465     ASN B    95                                                      
REMARK 465     GLY B    96                                                      
REMARK 465     LEU B   212                                                      
REMARK 465     VAL B   213                                                      
REMARK 465     PRO B   214                                                      
REMARK 465     ARG B   215                                                      
REMARK 465     GLY B   216                                                      
REMARK 465     SER B   217                                                      
REMARK 465     ALA B   218                                                      
REMARK 465     ALA B   219                                                      
REMARK 465     ALA B   220                                                      
REMARK 465     LEU B   221                                                      
REMARK 465     GLU B   222                                                      
REMARK 465     HIS B   223                                                      
REMARK 465     HIS B   224                                                      
REMARK 465     HIS B   225                                                      
REMARK 465     HIS B   226                                                      
REMARK 465     HIS B   227                                                      
REMARK 465     HIS B   228                                                      
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    ARG A 186   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 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  30      -61.09   -106.33                                   
REMARK 500    ASN A 151     -116.66     48.73                                   
REMARK 500    TYR A 179       -5.81   -143.93                                   
REMARK 500    GLN A 184     -125.76     48.52                                   
REMARK 500    LYS B  30      -60.35   -103.92                                   
REMARK 500    LEU B  43       -6.70    -60.00                                   
REMARK 500    ASN B 151     -122.42     48.53                                   
REMARK 500    GLN B 184     -128.69     47.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A   45     THR A   46                 -137.52                    
REMARK 500 GLY B   45     THR B   46                 -141.55                    
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 229  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 236   O                                                      
REMARK 620 2 ASP A 173   OD2  77.8                                              
REMARK 620 3 HIS A  27   NE2 166.9  89.2                                        
REMARK 620 4 HIS A  81   NE2  92.2 108.0  90.3                                  
REMARK 620 5 HIS A 177   NE2  93.5 115.3  93.4 136.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 229  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  27   NE2                                                    
REMARK 620 2 HIS B  81   NE2  90.2                                              
REMARK 620 3 ASP B 173   OD2  95.2  97.4                                        
REMARK 620 4 HIS B 177   NE2  92.5 132.3 129.7                                  
REMARK 620 5 HOH B 240   O   171.3  81.4  83.6  94.9                            
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 229                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 229                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1Y67   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITHOUT MANGANESE.                                  
DBREF  2AW9 A    2   211  UNP    Q9RUV2   SODM_DEIRA       1    210             
DBREF  2AW9 B    2   211  UNP    Q9RUV2   SODM_DEIRA       1    210             
SEQADV 2AW9 MET A    0  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 ALA A    1  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 LEU A  212  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 VAL A  213  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 PRO A  214  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 ARG A  215  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 GLY A  216  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 SER A  217  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 ALA A  218  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 ALA A  219  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 ALA A  220  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 LEU A  221  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 GLU A  222  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 HIS A  223  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 2AW9 HIS A  224  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 2AW9 HIS A  225  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 2AW9 HIS A  226  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 2AW9 HIS A  227  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 2AW9 HIS A  228  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 2AW9 MET B    0  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 ALA B    1  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 LEU B  212  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 VAL B  213  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 PRO B  214  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 ARG B  215  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 GLY B  216  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 SER B  217  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 ALA B  218  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 ALA B  219  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 ALA B  220  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 LEU B  221  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 GLU B  222  UNP  Q9RUV2              CLONING ARTIFACT               
SEQADV 2AW9 HIS B  223  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 2AW9 HIS B  224  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 2AW9 HIS B  225  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 2AW9 HIS B  226  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 2AW9 HIS B  227  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 2AW9 HIS B  228  UNP  Q9RUV2              EXPRESSION TAG                 
SEQRES   1 A  229  MET ALA ALA TYR THR LEU PRO GLN LEU PRO TYR ALA TYR          
SEQRES   2 A  229  ASP ALA LEU GLU PRO HIS ILE ASP ALA ARG THR MET GLU          
SEQRES   3 A  229  ILE HIS HIS THR LYS HIS HIS GLN THR TYR VAL ASP ASN          
SEQRES   4 A  229  ALA ASN LYS ALA LEU GLU GLY THR GLU PHE ALA ASP LEU          
SEQRES   5 A  229  PRO VAL GLU GLN LEU ILE GLN GLN LEU ASP ARG VAL PRO          
SEQRES   6 A  229  ALA ASP LYS LYS GLY ALA LEU ARG ASN ASN ALA GLY GLY          
SEQRES   7 A  229  HIS ALA ASN HIS SER MET PHE TRP GLN ILE MET GLY GLN          
SEQRES   8 A  229  GLY GLN GLY GLN ASN GLY ALA ASN GLN PRO SER GLY GLU          
SEQRES   9 A  229  LEU LEU ASP ALA ILE ASN SER ALA PHE GLY SER PHE ASP          
SEQRES  10 A  229  ALA PHE LYS GLN LYS PHE GLU ASP ALA ALA LYS THR ARG          
SEQRES  11 A  229  PHE GLY SER GLY TRP ALA TRP LEU VAL VAL LYS ASP GLY          
SEQRES  12 A  229  LYS LEU ASP VAL VAL SER THR ALA ASN GLN ASP ASN PRO          
SEQRES  13 A  229  LEU MET GLY GLU ALA ILE ALA GLY VAL SER GLY THR PRO          
SEQRES  14 A  229  ILE LEU GLY VAL ASP VAL TRP GLU HIS ALA TYR TYR LEU          
SEQRES  15 A  229  ASN TYR GLN ASN ARG ARG PRO ASP TYR LEU ALA ALA PHE          
SEQRES  16 A  229  TRP ASN VAL VAL ASN TRP ASP GLU VAL SER LYS ARG TYR          
SEQRES  17 A  229  ALA ALA ALA LYS LEU VAL PRO ARG GLY SER ALA ALA ALA          
SEQRES  18 A  229  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B  229  MET ALA ALA TYR THR LEU PRO GLN LEU PRO TYR ALA TYR          
SEQRES   2 B  229  ASP ALA LEU GLU PRO HIS ILE ASP ALA ARG THR MET GLU          
SEQRES   3 B  229  ILE HIS HIS THR LYS HIS HIS GLN THR TYR VAL ASP ASN          
SEQRES   4 B  229  ALA ASN LYS ALA LEU GLU GLY THR GLU PHE ALA ASP LEU          
SEQRES   5 B  229  PRO VAL GLU GLN LEU ILE GLN GLN LEU ASP ARG VAL PRO          
SEQRES   6 B  229  ALA ASP LYS LYS GLY ALA LEU ARG ASN ASN ALA GLY GLY          
SEQRES   7 B  229  HIS ALA ASN HIS SER MET PHE TRP GLN ILE MET GLY GLN          
SEQRES   8 B  229  GLY GLN GLY GLN ASN GLY ALA ASN GLN PRO SER GLY GLU          
SEQRES   9 B  229  LEU LEU ASP ALA ILE ASN SER ALA PHE GLY SER PHE ASP          
SEQRES  10 B  229  ALA PHE LYS GLN LYS PHE GLU ASP ALA ALA LYS THR ARG          
SEQRES  11 B  229  PHE GLY SER GLY TRP ALA TRP LEU VAL VAL LYS ASP GLY          
SEQRES  12 B  229  LYS LEU ASP VAL VAL SER THR ALA ASN GLN ASP ASN PRO          
SEQRES  13 B  229  LEU MET GLY GLU ALA ILE ALA GLY VAL SER GLY THR PRO          
SEQRES  14 B  229  ILE LEU GLY VAL ASP VAL TRP GLU HIS ALA TYR TYR LEU          
SEQRES  15 B  229  ASN TYR GLN ASN ARG ARG PRO ASP TYR LEU ALA ALA PHE          
SEQRES  16 B  229  TRP ASN VAL VAL ASN TRP ASP GLU VAL SER LYS ARG TYR          
SEQRES  17 B  229  ALA ALA ALA LYS LEU VAL PRO ARG GLY SER ALA ALA ALA          
SEQRES  18 B  229  LEU GLU HIS HIS HIS HIS HIS HIS                              
HET     MN  A 229       1                                                       
HET     MN  B 229       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   5  HOH   *25(H2 O)                                                     
HELIX    1   1 ASP A   20  LYS A   30  1                                  11    
HELIX    2   2 LYS A   30  GLU A   44  1                                  15    
HELIX    3   3 PRO A   52  ILE A   57  1                                   6    
HELIX    4   4 PRO A   64  ASP A   66  5                                   3    
HELIX    5   5 LYS A   67  ILE A   87  1                                  21    
HELIX    6   6 SER A  101  GLY A  113  1                                  13    
HELIX    7   7 SER A  114  ARG A  129  1                                  16    
HELIX    8   8 ASN A  154  MET A  157  5                                   4    
HELIX    9   9 GLY A  158  GLY A  163  1                                   6    
HELIX   10  10 TRP A  175  ALA A  178  5                                   4    
HELIX   11  11 TYR A  179  GLN A  184  1                                   6    
HELIX   12  12 ARG A  186  TRP A  195  1                                  10    
HELIX   13  13 ASN A  199  LYS A  211  1                                  13    
HELIX   14  14 ASP B   20  LYS B   30  1                                  11    
HELIX   15  15 LYS B   30  GLU B   44  1                                  15    
HELIX   16  16 PRO B   52  ILE B   57  1                                   6    
HELIX   17  17 PRO B   64  ASP B   66  5                                   3    
HELIX   18  18 LYS B   67  ILE B   87  1                                  21    
HELIX   19  19 SER B  101  GLY B  113  1                                  13    
HELIX   20  20 SER B  114  THR B  128  1                                  15    
HELIX   21  21 ASN B  154  LEU B  156  5                                   3    
HELIX   22  22 MET B  157  GLY B  163  1                                   7    
HELIX   23  23 TRP B  175  ALA B  178  5                                   4    
HELIX   24  24 TYR B  179  GLN B  184  1                                   6    
HELIX   25  25 ARG B  186  VAL B  198  1                                  13    
HELIX   26  26 ASN B  199  LYS B  211  1                                  13    
SHEET    1   A 3 LYS A 143  ALA A 150  0                                        
SHEET    2   A 3 GLY A 133  LYS A 140 -1  N  TRP A 136   O  VAL A 147           
SHEET    3   A 3 THR A 167  ASP A 173 -1  O  ILE A 169   N  LEU A 137           
SHEET    1   B 3 LYS B 143  ALA B 150  0                                        
SHEET    2   B 3 GLY B 133  LYS B 140 -1  N  TRP B 136   O  VAL B 147           
SHEET    3   B 3 THR B 167  ASP B 173 -1  O  LEU B 170   N  LEU B 137           
LINK        MN    MN A 229                 O   HOH A 236     1555   1555  2.63  
LINK        MN    MN A 229                 OD2 ASP A 173     1555   1555  1.85  
LINK        MN    MN A 229                 NE2 HIS A  27     1555   1555  2.35  
LINK        MN    MN A 229                 NE2 HIS A  81     1555   1555  2.19  
LINK        MN    MN A 229                 NE2 HIS A 177     1555   1555  2.16  
LINK        MN    MN B 229                 NE2 HIS B  27     1555   1555  2.19  
LINK        MN    MN B 229                 NE2 HIS B  81     1555   1555  2.34  
LINK        MN    MN B 229                 OD2 ASP B 173     1555   1555  1.90  
LINK        MN    MN B 229                 NE2 HIS B 177     1555   1555  2.07  
LINK        MN    MN B 229                 O   HOH B 240     1555   1555  2.20  
CISPEP   1 GLU A   16    PRO A   17          0        -2.05                     
CISPEP   2 GLU B   16    PRO B   17          0        -1.08                     
SITE     1 AC1  5 HIS A  27  HIS A  81  ASP A 173  HIS A 177                    
SITE     2 AC1  5 HOH A 236                                                     
SITE     1 AC2  5 HIS B  27  HIS B  81  ASP B 173  HIS B 177                    
SITE     2 AC2  5 HOH B 240                                                     
CRYST1   43.833   83.499   65.495  90.00 105.79  90.00 P 1 21 1      4          
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      0.022814  0.000000  0.006452        0.00000                         
SCALE2      0.000000  0.011976  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015867        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system