GenomeNet

Database: PDB
Entry: 4F6E
LinkDB: 4F6E
Original site: 4F6E 
HEADER    OXIDOREDUCTASE                          14-MAY-12   4F6E              
TITLE     CRYSTAL STRUCTURE OF THE K182R, A183P MUTANT MANGANESE SUPEROXIDE     
TITLE    2 DISMUTASE FROM SACCHROMYCES CEREVISIAE                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL;                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 559292;                                              
SOURCE   5 STRAIN: ATCC 204508 / S288C;                                         
SOURCE   6 GENE: SOD2, YHR008C;                                                 
SOURCE   7 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: EG110;                                     
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: YEP352-SOD2                               
KEYWDS    MN SUPEROXIDE DISMUTASE, DIMER INTERFACE, OXIDOREDUCTASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.SHENG,D.CASCIO,J.S.VALENTINE                                        
REVDAT   1   12-JUN-13 4F6E    0                                                
JRNL        AUTH   Y.SHENG,D.CASCIO,J.S.VALENTINE                               
JRNL        TITL   CRYSTAL STRUCTURE OF THE K182R, A183P MUTANT MANGANESE       
JRNL        TITL 2 SUPEROXIDE DISMUTASE FROM SACCHROMYCES CEREVISIAE            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.65                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 105020                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.164                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5252                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 37.6633 -  4.9665    0.98     3621   191  0.1649 0.1915        
REMARK   3     2  4.9665 -  3.9434    0.97     3564   188  0.1421 0.1639        
REMARK   3     3  3.9434 -  3.4453    0.97     3557   187  0.1566 0.1757        
REMARK   3     4  3.4453 -  3.1305    0.96     3540   186  0.1711 0.1795        
REMARK   3     5  3.1305 -  2.9062    0.96     3509   185  0.1843 0.2088        
REMARK   3     6  2.9062 -  2.7349    0.95     3478   183  0.1820 0.2287        
REMARK   3     7  2.7349 -  2.5980    0.94     3492   184  0.1759 0.2022        
REMARK   3     8  2.5980 -  2.4849    0.94     3465   182  0.1716 0.2005        
REMARK   3     9  2.4849 -  2.3893    0.94     3460   182  0.1728 0.2154        
REMARK   3    10  2.3893 -  2.3068    0.94     3429   181  0.1662 0.2027        
REMARK   3    11  2.3068 -  2.2347    0.93     3419   180  0.1583 0.1837        
REMARK   3    12  2.2347 -  2.1708    0.93     3417   180  0.1597 0.1723        
REMARK   3    13  2.1708 -  2.1137    0.93     3374   177  0.1596 0.2035        
REMARK   3    14  2.1137 -  2.0621    0.92     3388   178  0.1635 0.2139        
REMARK   3    15  2.0621 -  2.0153    0.92     3382   178  0.1637 0.1918        
REMARK   3    16  2.0153 -  1.9724    0.91     3343   176  0.1549 0.1884        
REMARK   3    17  1.9724 -  1.9329    0.91     3301   174  0.1559 0.2241        
REMARK   3    18  1.9329 -  1.8965    0.91     3338   176  0.1563 0.1969        
REMARK   3    19  1.8965 -  1.8626    0.90     3319   175  0.1551 0.2152        
REMARK   3    20  1.8626 -  1.8310    0.90     3310   174  0.1629 0.2123        
REMARK   3    21  1.8310 -  1.8015    0.90     3286   173  0.1613 0.1801        
REMARK   3    22  1.8015 -  1.7738    0.89     3294   173  0.1545 0.1994        
REMARK   3    23  1.7738 -  1.7477    0.89     3248   171  0.1602 0.2022        
REMARK   3    24  1.7477 -  1.7231    0.88     3276   172  0.1651 0.2018        
REMARK   3    25  1.7231 -  1.6998    0.88     3224   170  0.1641 0.1735        
REMARK   3    26  1.6998 -  1.6777    0.88     3227   170  0.1658 0.2321        
REMARK   3    27  1.6777 -  1.6567    0.88     3262   172  0.1748 0.2225        
REMARK   3    28  1.6567 -  1.6368    0.87     3167   166  0.1707 0.2187        
REMARK   3    29  1.6368 -  1.6177    0.81     2984   157  0.1808 0.2251        
REMARK   3    30  1.6177 -  1.5996    0.57     2094   111  0.1916 0.2329        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.86                                          
REMARK   3   K_SOL              : 0.40                                          
REMARK   3   B_SOL              : 42.61                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.820           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.67580                                              
REMARK   3    B22 (A**2) : -1.34200                                             
REMARK   3    B33 (A**2) : -1.33380                                             
REMARK   3    B12 (A**2) : -1.74430                                             
REMARK   3    B13 (A**2) : -0.38070                                             
REMARK   3    B23 (A**2) : 0.35770                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           6860                                  
REMARK   3   ANGLE     :  1.037           9348                                  
REMARK   3   CHIRALITY :  0.078            967                                  
REMARK   3   PLANARITY :  0.005           1197                                  
REMARK   3   DIHEDRAL  : 12.986           2468                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: all                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6978 -12.3594 -21.9457              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0135 T22:   0.0376                                     
REMARK   3      T33:   0.0425 T12:   0.0149                                     
REMARK   3      T13:   0.0235 T23:   0.0091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3130 L22:   0.4126                                     
REMARK   3      L33:   0.6710 L12:   0.2306                                     
REMARK   3      L13:   0.3548 L23:   0.2606                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0204 S12:  -0.0406 S13:  -0.0269                       
REMARK   3      S21:  -0.0101 S22:  -0.0165 S23:  -0.0023                       
REMARK   3      S31:  -0.0116 S32:  -0.0095 S33:   0.0015                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4F6E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072512.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-OCT-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
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 FR-E+ SUPERBRIGHT           
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : CONFOCAL MIRRORS VARIMAX HR        
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS HTC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 105023                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.653                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.2                               
REMARK 200  DATA REDUNDANCY                : 3.820                              
REMARK 200  R MERGE                    (I) : 0.03500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.6900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 70.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.790                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3LSU                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRI-AMMONIUM CITRATE, 20% (W/V)    
REMARK 280  POLYETHYLENE GLYCOL 3350, PH 7.0, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11570 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 33010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, B, 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 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     MLY B   206                                                      
REMARK 465     ILE B   207                                                      
REMARK 465     MLY D   206                                                      
REMARK 465     ILE D   207                                                      
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    MLY A  29      -65.19   -107.17                                   
REMARK 500    GLN A 129       76.56   -102.54                                   
REMARK 500    ASN A 153     -122.82     58.03                                   
REMARK 500    TYR A 174      -15.19   -148.52                                   
REMARK 500    GLN A 179     -127.81     46.08                                   
REMARK 500    MLY B  29      -66.17   -106.31                                   
REMARK 500    GLN B 129       78.58   -100.77                                   
REMARK 500    ASN B 153     -124.70     57.73                                   
REMARK 500    TYR B 174      -16.56   -146.00                                   
REMARK 500    GLN B 179     -127.90     46.50                                   
REMARK 500    MLY C  29      -65.16   -105.17                                   
REMARK 500    GLN C 129       79.66   -102.01                                   
REMARK 500    ASN C 153     -124.44     59.76                                   
REMARK 500    TYR C 174      -17.70   -147.01                                   
REMARK 500    GLN C 179     -128.85     46.30                                   
REMARK 500    MLY D  29      -64.43   -105.86                                   
REMARK 500    GLN D 129       75.13   -103.06                                   
REMARK 500    ASN D 153     -122.94     57.45                                   
REMARK 500    TYR D 174      -17.39   -145.83                                   
REMARK 500    GLN D 179     -129.44     44.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN B  87        24.7      L          L   OUTSIDE RANGE           
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 301  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 168   OD2                                                    
REMARK 620 2 HIS A  81   NE2 113.1                                              
REMARK 620 3 HIS A 172   NE2 119.0 127.8                                        
REMARK 620 4 HIS A  26   NE2  83.5  89.3  93.5                                  
REMARK 620 5 HOH A 403   O    88.8  91.8  92.2 172.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 301  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 168   OD2                                                    
REMARK 620 2 HIS C  81   NE2 113.2                                              
REMARK 620 3 HIS C 172   NE2 118.6 128.2                                        
REMARK 620 4 HIS C  26   NE2  85.0  92.1  90.7                                  
REMARK 620 5 HOH C 402   O    86.9  91.0  93.2 171.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 302  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 168   OD2                                                    
REMARK 620 2 HIS D  81   NE2 113.3                                              
REMARK 620 3 HIS D  26   NE2  85.0  94.3                                        
REMARK 620 4 HIS D 172   NE2 120.3 126.5  90.8                                  
REMARK 620 5 HOH D 403   O    86.5  89.7 171.4  93.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 301  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 168   OD2                                                    
REMARK 620 2 HIS B  26   NE2  83.8                                              
REMARK 620 3 HIS B 172   NE2 119.2  91.8                                        
REMARK 620 4 HOH B 401   O    86.6 170.4  93.5                                  
REMARK 620 5 HIS B  81   NE2 113.0  92.6 127.7  90.5                            
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 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 303                 
DBREF  4F6E A    2   207  UNP    P00447   SODM_YEAST      28    233             
DBREF  4F6E B    2   207  UNP    P00447   SODM_YEAST      28    233             
DBREF  4F6E C    2   207  UNP    P00447   SODM_YEAST      28    233             
DBREF  4F6E D    2   207  UNP    P00447   SODM_YEAST      28    233             
SEQADV 4F6E MLY A    1  UNP  P00447              EXPRESSION TAG                 
SEQADV 4F6E ARG A  182  UNP  P00447    LYS   208 ENGINEERED MUTATION            
SEQADV 4F6E PRO A  183  UNP  P00447    ALA   209 ENGINEERED MUTATION            
SEQADV 4F6E MLY B    1  UNP  P00447              EXPRESSION TAG                 
SEQADV 4F6E ARG B  182  UNP  P00447    LYS   208 ENGINEERED MUTATION            
SEQADV 4F6E PRO B  183  UNP  P00447    ALA   209 ENGINEERED MUTATION            
SEQADV 4F6E MLY C    1  UNP  P00447              EXPRESSION TAG                 
SEQADV 4F6E ARG C  182  UNP  P00447    LYS   208 ENGINEERED MUTATION            
SEQADV 4F6E PRO C  183  UNP  P00447    ALA   209 ENGINEERED MUTATION            
SEQADV 4F6E MLY D    1  UNP  P00447              EXPRESSION TAG                 
SEQADV 4F6E ARG D  182  UNP  P00447    LYS   208 ENGINEERED MUTATION            
SEQADV 4F6E PRO D  183  UNP  P00447    ALA   209 ENGINEERED MUTATION            
SEQRES   1 A  207  MLY VAL THR LEU PRO ASP LEU MLY TRP ASP PHE GLY ALA          
SEQRES   2 A  207  LEU GLU PRO TYR ILE SER GLY GLN ILE ASN GLU LEU HIS          
SEQRES   3 A  207  TYR THR MLY HIS HIS GLN THR TYR VAL ASN GLY PHE ASN          
SEQRES   4 A  207  THR ALA VAL ASP GLN PHE GLN GLU LEU SER ASP LEU LEU          
SEQRES   5 A  207  ALA MLY GLU PRO SER PRO ALA ASN ALA ARG MLY MET ILE          
SEQRES   6 A  207  ALA ILE GLN GLN ASN ILE MLY PHE HIS GLY GLY GLY PHE          
SEQRES   7 A  207  THR ASN HIS CYS LEU PHE TRP GLU ASN LEU ALA PRO GLU          
SEQRES   8 A  207  SER GLN GLY GLY GLY GLU PRO PRO THR GLY ALA LEU ALA          
SEQRES   9 A  207  MLY ALA ILE ASP GLU GLN PHE GLY SER LEU ASP GLU LEU          
SEQRES  10 A  207  ILE MLY LEU THR ASN THR MLY LEU ALA GLY VAL GLN GLY          
SEQRES  11 A  207  SER GLY TRP ALA PHE ILE VAL MLY ASN LEU SER ASN GLY          
SEQRES  12 A  207  GLY MLY LEU ASP VAL VAL GLN THR TYR ASN GLN ASP THR          
SEQRES  13 A  207  VAL THR GLY PRO LEU VAL PRO LEU VAL ALA ILE ASP ALA          
SEQRES  14 A  207  TRP GLU HIS ALA TYR TYR LEU GLN TYR GLN ASN MLY ARG          
SEQRES  15 A  207  PRO ASP TYR PHE MLY ALA ILE TRP ASN VAL VAL ASN TRP          
SEQRES  16 A  207  MLY GLU ALA SER ARG ARG PHE ASP ALA GLY MLY ILE              
SEQRES   1 B  207  MLY VAL THR LEU PRO ASP LEU MLY TRP ASP PHE GLY ALA          
SEQRES   2 B  207  LEU GLU PRO TYR ILE SER GLY GLN ILE ASN GLU LEU HIS          
SEQRES   3 B  207  TYR THR MLY HIS HIS GLN THR TYR VAL ASN GLY PHE ASN          
SEQRES   4 B  207  THR ALA VAL ASP GLN PHE GLN GLU LEU SER ASP LEU LEU          
SEQRES   5 B  207  ALA MLY GLU PRO SER PRO ALA ASN ALA ARG MLY MET ILE          
SEQRES   6 B  207  ALA ILE GLN GLN ASN ILE MLY PHE HIS GLY GLY GLY PHE          
SEQRES   7 B  207  THR ASN HIS CYS LEU PHE TRP GLU ASN LEU ALA PRO GLU          
SEQRES   8 B  207  SER GLN GLY GLY GLY GLU PRO PRO THR GLY ALA LEU ALA          
SEQRES   9 B  207  MLY ALA ILE ASP GLU GLN PHE GLY SER LEU ASP GLU LEU          
SEQRES  10 B  207  ILE MLY LEU THR ASN THR MLY LEU ALA GLY VAL GLN GLY          
SEQRES  11 B  207  SER GLY TRP ALA PHE ILE VAL MLY ASN LEU SER ASN GLY          
SEQRES  12 B  207  GLY MLY LEU ASP VAL VAL GLN THR TYR ASN GLN ASP THR          
SEQRES  13 B  207  VAL THR GLY PRO LEU VAL PRO LEU VAL ALA ILE ASP ALA          
SEQRES  14 B  207  TRP GLU HIS ALA TYR TYR LEU GLN TYR GLN ASN MLY ARG          
SEQRES  15 B  207  PRO ASP TYR PHE MLY ALA ILE TRP ASN VAL VAL ASN TRP          
SEQRES  16 B  207  MLY GLU ALA SER ARG ARG PHE ASP ALA GLY MLY ILE              
SEQRES   1 C  207  MLY VAL THR LEU PRO ASP LEU MLY TRP ASP PHE GLY ALA          
SEQRES   2 C  207  LEU GLU PRO TYR ILE SER GLY GLN ILE ASN GLU LEU HIS          
SEQRES   3 C  207  TYR THR MLY HIS HIS GLN THR TYR VAL ASN GLY PHE ASN          
SEQRES   4 C  207  THR ALA VAL ASP GLN PHE GLN GLU LEU SER ASP LEU LEU          
SEQRES   5 C  207  ALA MLY GLU PRO SER PRO ALA ASN ALA ARG MLY MET ILE          
SEQRES   6 C  207  ALA ILE GLN GLN ASN ILE MLY PHE HIS GLY GLY GLY PHE          
SEQRES   7 C  207  THR ASN HIS CYS LEU PHE TRP GLU ASN LEU ALA PRO GLU          
SEQRES   8 C  207  SER GLN GLY GLY GLY GLU PRO PRO THR GLY ALA LEU ALA          
SEQRES   9 C  207  MLY ALA ILE ASP GLU GLN PHE GLY SER LEU ASP GLU LEU          
SEQRES  10 C  207  ILE MLY LEU THR ASN THR MLY LEU ALA GLY VAL GLN GLY          
SEQRES  11 C  207  SER GLY TRP ALA PHE ILE VAL MLY ASN LEU SER ASN GLY          
SEQRES  12 C  207  GLY MLY LEU ASP VAL VAL GLN THR TYR ASN GLN ASP THR          
SEQRES  13 C  207  VAL THR GLY PRO LEU VAL PRO LEU VAL ALA ILE ASP ALA          
SEQRES  14 C  207  TRP GLU HIS ALA TYR TYR LEU GLN TYR GLN ASN MLY ARG          
SEQRES  15 C  207  PRO ASP TYR PHE MLY ALA ILE TRP ASN VAL VAL ASN TRP          
SEQRES  16 C  207  MLY GLU ALA SER ARG ARG PHE ASP ALA GLY MLY ILE              
SEQRES   1 D  207  MLY VAL THR LEU PRO ASP LEU MLY TRP ASP PHE GLY ALA          
SEQRES   2 D  207  LEU GLU PRO TYR ILE SER GLY GLN ILE ASN GLU LEU HIS          
SEQRES   3 D  207  TYR THR MLY HIS HIS GLN THR TYR VAL ASN GLY PHE ASN          
SEQRES   4 D  207  THR ALA VAL ASP GLN PHE GLN GLU LEU SER ASP LEU LEU          
SEQRES   5 D  207  ALA MLY GLU PRO SER PRO ALA ASN ALA ARG MLY MET ILE          
SEQRES   6 D  207  ALA ILE GLN GLN ASN ILE MLY PHE HIS GLY GLY GLY PHE          
SEQRES   7 D  207  THR ASN HIS CYS LEU PHE TRP GLU ASN LEU ALA PRO GLU          
SEQRES   8 D  207  SER GLN GLY GLY GLY GLU PRO PRO THR GLY ALA LEU ALA          
SEQRES   9 D  207  MLY ALA ILE ASP GLU GLN PHE GLY SER LEU ASP GLU LEU          
SEQRES  10 D  207  ILE MLY LEU THR ASN THR MLY LEU ALA GLY VAL GLN GLY          
SEQRES  11 D  207  SER GLY TRP ALA PHE ILE VAL MLY ASN LEU SER ASN GLY          
SEQRES  12 D  207  GLY MLY LEU ASP VAL VAL GLN THR TYR ASN GLN ASP THR          
SEQRES  13 D  207  VAL THR GLY PRO LEU VAL PRO LEU VAL ALA ILE ASP ALA          
SEQRES  14 D  207  TRP GLU HIS ALA TYR TYR LEU GLN TYR GLN ASN MLY ARG          
SEQRES  15 D  207  PRO ASP TYR PHE MLY ALA ILE TRP ASN VAL VAL ASN TRP          
SEQRES  16 D  207  MLY GLU ALA SER ARG ARG PHE ASP ALA GLY MLY ILE              
MODRES 4F6E MLY A    1  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY A    8  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY A   29  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY A   54  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY A   63  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY A   72  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY A  105  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY A  119  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY A  124  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY A  138  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY A  145  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY A  181  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY A  187  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY A  196  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY A  206  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY B    1  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY B    8  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY B   29  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY B   54  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY B   63  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY B   72  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY B  105  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY B  119  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY B  124  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY B  138  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY B  145  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY B  181  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY B  187  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY B  196  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY C    1  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY C    8  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY C   29  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY C   54  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY C   63  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY C   72  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY C  105  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY C  119  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY C  124  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY C  138  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY C  145  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY C  181  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY C  187  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY C  196  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY C  206  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY D    1  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY D    8  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY D   29  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY D   54  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY D   63  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY D   72  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY D  105  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY D  119  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY D  124  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY D  138  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY D  145  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY D  181  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY D  187  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4F6E MLY D  196  LYS  N-DIMETHYL-LYSINE                                  
HET    MLY  A   1      11                                                       
HET    MLY  A   8      11                                                       
HET    MLY  A  29      11                                                       
HET    MLY  A  54      11                                                       
HET    MLY  A  63      11                                                       
HET    MLY  A  72      11                                                       
HET    MLY  A 105      11                                                       
HET    MLY  A 119      11                                                       
HET    MLY  A 124      11                                                       
HET    MLY  A 138      11                                                       
HET    MLY  A 145      11                                                       
HET    MLY  A 181      11                                                       
HET    MLY  A 187      11                                                       
HET    MLY  A 196      11                                                       
HET    MLY  A 206      11                                                       
HET    MLY  B   1      11                                                       
HET    MLY  B   8      11                                                       
HET    MLY  B  29      11                                                       
HET    MLY  B  54      11                                                       
HET    MLY  B  63      11                                                       
HET    MLY  B  72      11                                                       
HET    MLY  B 105      11                                                       
HET    MLY  B 119      11                                                       
HET    MLY  B 124      11                                                       
HET    MLY  B 138      11                                                       
HET    MLY  B 145      11                                                       
HET    MLY  B 181      11                                                       
HET    MLY  B 187      11                                                       
HET    MLY  B 196      11                                                       
HET    MLY  C   1      11                                                       
HET    MLY  C   8      11                                                       
HET    MLY  C  29      11                                                       
HET    MLY  C  54      11                                                       
HET    MLY  C  63      11                                                       
HET    MLY  C  72      11                                                       
HET    MLY  C 105      11                                                       
HET    MLY  C 119      11                                                       
HET    MLY  C 124      11                                                       
HET    MLY  C 138      11                                                       
HET    MLY  C 145      11                                                       
HET    MLY  C 181      11                                                       
HET    MLY  C 187      11                                                       
HET    MLY  C 196      11                                                       
HET    MLY  C 206      11                                                       
HET    MLY  D   1      11                                                       
HET    MLY  D   8      11                                                       
HET    MLY  D  29      11                                                       
HET    MLY  D  54      11                                                       
HET    MLY  D  63      11                                                       
HET    MLY  D  72      11                                                       
HET    MLY  D 105      11                                                       
HET    MLY  D 119      11                                                       
HET    MLY  D 124      11                                                       
HET    MLY  D 138      11                                                       
HET    MLY  D 145      11                                                       
HET    MLY  D 181      11                                                       
HET    MLY  D 187      11                                                       
HET    MLY  D 196      11                                                       
HET     MN  A 301       1                                                       
HET     MN  B 301       1                                                       
HET     MN  C 301       1                                                       
HET    TRS  C 302       8                                                       
HET    MLY  D 301      11                                                       
HET     MN  D 302       1                                                       
HET    GOL  D 303       6                                                       
HETNAM     MLY N-DIMETHYL-LYSINE                                                
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETNAM     GOL GLYCEROL                                                         
HETSYN     TRS TRIS BUFFER                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MLY    59(C8 H18 N2 O2)                                             
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   8  TRS    C4 H12 N O3 1+                                               
FORMUL  11  GOL    C3 H8 O3                                                     
FORMUL  12  HOH   *555(H2 O)                                                    
HELIX    1   1 ASP A   10  GLU A   15  5                                   6    
HELIX    2   2 SER A   19  MLY A   29  1                                  11    
HELIX    3   3 MLY A   29  GLU A   55  1                                  27    
HELIX    4   4 SER A   57  ASN A   87  1                                  31    
HELIX    5   5 PRO A   90  GLY A   94  5                                   5    
HELIX    6   6 THR A  100  GLY A  112  1                                  13    
HELIX    7   7 SER A  113  GLY A  127  1                                  15    
HELIX    8   8 SER A  141  GLY A  143  5                                   3    
HELIX    9   9 TRP A  170  ALA A  173  5                                   4    
HELIX   10  10 TYR A  174  GLN A  179  1                                   6    
HELIX   11  11 MLY A  181  TRP A  190  1                                  10    
HELIX   12  12 ASN A  191  VAL A  193  5                                   3    
HELIX   13  13 ASN A  194  GLY A  205  1                                  12    
HELIX   14  14 ASP B   10  GLU B   15  5                                   6    
HELIX   15  15 SER B   19  MLY B   29  1                                  11    
HELIX   16  16 MLY B   29  GLU B   55  1                                  27    
HELIX   17  17 SER B   57  ASN B   87  1                                  31    
HELIX   18  18 PRO B   90  GLY B   94  5                                   5    
HELIX   19  19 THR B  100  GLY B  112  1                                  13    
HELIX   20  20 SER B  113  GLY B  127  1                                  15    
HELIX   21  21 TRP B  170  ALA B  173  5                                   4    
HELIX   22  22 TYR B  174  GLN B  179  1                                   6    
HELIX   23  23 MLY B  181  TRP B  190  1                                  10    
HELIX   24  24 ASN B  191  VAL B  193  5                                   3    
HELIX   25  25 ASN B  194  GLY B  205  1                                  12    
HELIX   26  26 SER C   19  MLY C   29  1                                  11    
HELIX   27  27 MLY C   29  GLU C   55  1                                  27    
HELIX   28  28 SER C   57  ASN C   87  1                                  31    
HELIX   29  29 PRO C   90  GLY C   94  5                                   5    
HELIX   30  30 THR C  100  GLY C  112  1                                  13    
HELIX   31  31 SER C  113  GLY C  127  1                                  15    
HELIX   32  32 TRP C  170  ALA C  173  5                                   4    
HELIX   33  33 TYR C  174  GLN C  179  1                                   6    
HELIX   34  34 MLY C  181  TRP C  190  1                                  10    
HELIX   35  35 ASN C  191  VAL C  193  5                                   3    
HELIX   36  36 ASN C  194  GLY C  205  1                                  12    
HELIX   37  37 SER D   19  MLY D   29  1                                  11    
HELIX   38  38 MLY D   29  GLU D   55  1                                  27    
HELIX   39  39 SER D   57  ASN D   87  1                                  31    
HELIX   40  40 PRO D   90  GLY D   94  5                                   5    
HELIX   41  41 THR D  100  GLY D  112  1                                  13    
HELIX   42  42 SER D  113  GLY D  127  1                                  15    
HELIX   43  43 TRP D  170  ALA D  173  5                                   4    
HELIX   44  44 TYR D  174  GLN D  179  1                                   6    
HELIX   45  45 MLY D  181  TRP D  190  1                                  10    
HELIX   46  46 ASN D  191  VAL D  193  5                                   3    
HELIX   47  47 ASN D  194  GLY D  205  1                                  12    
SHEET    1   A 3 LEU A 146  TYR A 152  0                                        
SHEET    2   A 3 GLY A 132  ASN A 139 -1  N  VAL A 137   O  ASP A 147           
SHEET    3   A 3 LEU A 161  ASP A 168 -1  O  LEU A 164   N  ILE A 136           
SHEET    1   B 3 LEU B 146  TYR B 152  0                                        
SHEET    2   B 3 GLY B 132  ASN B 139 -1  N  VAL B 137   O  ASP B 147           
SHEET    3   B 3 LEU B 161  ASP B 168 -1  O  LEU B 164   N  ILE B 136           
SHEET    1   C 3 MLY C 145  TYR C 152  0                                        
SHEET    2   C 3 GLY C 132  ASN C 139 -1  N  VAL C 137   O  ASP C 147           
SHEET    3   C 3 LEU C 161  ASP C 168 -1  O  LEU C 164   N  ILE C 136           
SHEET    1   D 3 MLY D 145  TYR D 152  0                                        
SHEET    2   D 3 GLY D 132  ASN D 139 -1  N  VAL D 137   O  ASP D 147           
SHEET    3   D 3 LEU D 161  ASP D 168 -1  O  LEU D 164   N  ILE D 136           
LINK         C   MLY A   1                 N   VAL A   2     1555   1555  1.33  
LINK         C   LEU A   7                 N   MLY A   8     1555   1555  1.33  
LINK         C   MLY A   8                 N   TRP A   9     1555   1555  1.33  
LINK         C   THR A  28                 N   MLY A  29     1555   1555  1.33  
LINK         C   MLY A  29                 N   HIS A  30     1555   1555  1.33  
LINK         C   ALA A  53                 N   MLY A  54     1555   1555  1.33  
LINK         C   MLY A  54                 N   GLU A  55     1555   1555  1.33  
LINK         C   ARG A  62                 N   MLY A  63     1555   1555  1.33  
LINK         C   MLY A  63                 N   MET A  64     1555   1555  1.33  
LINK         C   ILE A  71                 N   MLY A  72     1555   1555  1.34  
LINK         C   MLY A  72                 N   PHE A  73     1555   1555  1.33  
LINK         C   ALA A 104                 N   MLY A 105     1555   1555  1.33  
LINK         C   MLY A 105                 N   ALA A 106     1555   1555  1.33  
LINK         C   ILE A 118                 N   MLY A 119     1555   1555  1.34  
LINK         C   MLY A 119                 N   LEU A 120     1555   1555  1.32  
LINK         C   THR A 123                 N   MLY A 124     1555   1555  1.33  
LINK         C   MLY A 124                 N   LEU A 125     1555   1555  1.33  
LINK         C   VAL A 137                 N   MLY A 138     1555   1555  1.33  
LINK         C   MLY A 138                 N   ASN A 139     1555   1555  1.33  
LINK         C   GLY A 144                 N   MLY A 145     1555   1555  1.33  
LINK         C   MLY A 145                 N   LEU A 146     1555   1555  1.33  
LINK         C   ASN A 180                 N   MLY A 181     1555   1555  1.33  
LINK         C   MLY A 181                 N   ARG A 182     1555   1555  1.33  
LINK         C   PHE A 186                 N   MLY A 187     1555   1555  1.33  
LINK         C   MLY A 187                 N   ALA A 188     1555   1555  1.33  
LINK         C   TRP A 195                 N   MLY A 196     1555   1555  1.33  
LINK         C   MLY A 196                 N   GLU A 197     1555   1555  1.33  
LINK         C   GLY A 205                 N   MLY A 206     1555   1555  1.33  
LINK         C   MLY A 206                 N   ILE A 207     1555   1555  1.33  
LINK         C   MLY B   1                 N   VAL B   2     1555   1555  1.33  
LINK         C   LEU B   7                 N   MLY B   8     1555   1555  1.33  
LINK         C   MLY B   8                 N   TRP B   9     1555   1555  1.33  
LINK         C   THR B  28                 N   MLY B  29     1555   1555  1.33  
LINK         C   MLY B  29                 N   HIS B  30     1555   1555  1.33  
LINK         C   ALA B  53                 N   MLY B  54     1555   1555  1.33  
LINK         C   MLY B  54                 N   GLU B  55     1555   1555  1.33  
LINK         C   ARG B  62                 N   MLY B  63     1555   1555  1.33  
LINK         C   MLY B  63                 N   MET B  64     1555   1555  1.33  
LINK         C   ILE B  71                 N   MLY B  72     1555   1555  1.33  
LINK         C   MLY B  72                 N   PHE B  73     1555   1555  1.33  
LINK         C   ALA B 104                 N   MLY B 105     1555   1555  1.33  
LINK         C   MLY B 105                 N   ALA B 106     1555   1555  1.33  
LINK         C   ILE B 118                 N   MLY B 119     1555   1555  1.33  
LINK         C   MLY B 119                 N   LEU B 120     1555   1555  1.33  
LINK         C   THR B 123                 N   MLY B 124     1555   1555  1.33  
LINK         C   MLY B 124                 N   LEU B 125     1555   1555  1.33  
LINK         C   VAL B 137                 N   MLY B 138     1555   1555  1.33  
LINK         C   MLY B 138                 N   ASN B 139     1555   1555  1.33  
LINK         C   GLY B 144                 N   MLY B 145     1555   1555  1.33  
LINK         C   MLY B 145                 N   LEU B 146     1555   1555  1.33  
LINK         C   ASN B 180                 N   MLY B 181     1555   1555  1.33  
LINK         C   MLY B 181                 N   ARG B 182     1555   1555  1.33  
LINK         C   PHE B 186                 N   MLY B 187     1555   1555  1.33  
LINK         C   MLY B 187                 N   ALA B 188     1555   1555  1.33  
LINK         C   TRP B 195                 N   MLY B 196     1555   1555  1.33  
LINK         C   MLY B 196                 N   GLU B 197     1555   1555  1.33  
LINK         C   MLY C   1                 N   VAL C   2     1555   1555  1.33  
LINK         C   LEU C   7                 N   MLY C   8     1555   1555  1.33  
LINK         C   MLY C   8                 N   TRP C   9     1555   1555  1.33  
LINK         C   THR C  28                 N   MLY C  29     1555   1555  1.33  
LINK         C   MLY C  29                 N   HIS C  30     1555   1555  1.33  
LINK         C   ALA C  53                 N   MLY C  54     1555   1555  1.33  
LINK         C   MLY C  54                 N   GLU C  55     1555   1555  1.33  
LINK         C   ARG C  62                 N   MLY C  63     1555   1555  1.33  
LINK         C   MLY C  63                 N   MET C  64     1555   1555  1.33  
LINK         C   ILE C  71                 N   MLY C  72     1555   1555  1.33  
LINK         C   MLY C  72                 N   PHE C  73     1555   1555  1.33  
LINK         C   ALA C 104                 N   MLY C 105     1555   1555  1.33  
LINK         C   MLY C 105                 N   ALA C 106     1555   1555  1.33  
LINK         C   ILE C 118                 N   MLY C 119     1555   1555  1.33  
LINK         C   MLY C 119                 N   LEU C 120     1555   1555  1.33  
LINK         C   THR C 123                 N   MLY C 124     1555   1555  1.33  
LINK         C   MLY C 124                 N   LEU C 125     1555   1555  1.33  
LINK         C   VAL C 137                 N   MLY C 138     1555   1555  1.33  
LINK         C   MLY C 138                 N   ASN C 139     1555   1555  1.33  
LINK         C   GLY C 144                 N   MLY C 145     1555   1555  1.33  
LINK         C   MLY C 145                 N   LEU C 146     1555   1555  1.33  
LINK         C   ASN C 180                 N   MLY C 181     1555   1555  1.33  
LINK         C   MLY C 181                 N   ARG C 182     1555   1555  1.33  
LINK         C   PHE C 186                 N   MLY C 187     1555   1555  1.33  
LINK         C   MLY C 187                 N   ALA C 188     1555   1555  1.33  
LINK         C   TRP C 195                 N   MLY C 196     1555   1555  1.34  
LINK         C   MLY C 196                 N   GLU C 197     1555   1555  1.33  
LINK         C   GLY C 205                 N   MLY C 206     1555   1555  1.33  
LINK         C   GLY D 205                 N   MLY D 301     1555   1555  1.33  
LINK         C   MLY C 206                 N   ILE C 207     1555   1555  1.33  
LINK         C   MLY D   1                 N   VAL D   2     1555   1555  1.33  
LINK         C   LEU D   7                 N   MLY D   8     1555   1555  1.33  
LINK         C   MLY D   8                 N   TRP D   9     1555   1555  1.33  
LINK         C   THR D  28                 N   MLY D  29     1555   1555  1.33  
LINK         C   MLY D  29                 N   HIS D  30     1555   1555  1.33  
LINK         C   ALA D  53                 N   MLY D  54     1555   1555  1.32  
LINK         C   MLY D  54                 N   GLU D  55     1555   1555  1.33  
LINK         C   ARG D  62                 N   MLY D  63     1555   1555  1.33  
LINK         C   MLY D  63                 N   MET D  64     1555   1555  1.32  
LINK         C   ILE D  71                 N   MLY D  72     1555   1555  1.33  
LINK         C   MLY D  72                 N   PHE D  73     1555   1555  1.33  
LINK         C   ALA D 104                 N   MLY D 105     1555   1555  1.33  
LINK         C   MLY D 105                 N   ALA D 106     1555   1555  1.33  
LINK         C   ILE D 118                 N   MLY D 119     1555   1555  1.33  
LINK         C   MLY D 119                 N   LEU D 120     1555   1555  1.33  
LINK         C   THR D 123                 N   MLY D 124     1555   1555  1.33  
LINK         C   MLY D 124                 N   LEU D 125     1555   1555  1.33  
LINK         C   VAL D 137                 N   MLY D 138     1555   1555  1.33  
LINK         C   MLY D 138                 N   ASN D 139     1555   1555  1.33  
LINK         C   GLY D 144                 N   MLY D 145     1555   1555  1.33  
LINK         C   MLY D 145                 N   LEU D 146     1555   1555  1.33  
LINK         C   ASN D 180                 N   MLY D 181     1555   1555  1.33  
LINK         C   MLY D 181                 N   ARG D 182     1555   1555  1.33  
LINK         C   PHE D 186                 N   MLY D 187     1555   1555  1.33  
LINK         C   MLY D 187                 N   ALA D 188     1555   1555  1.33  
LINK         C   TRP D 195                 N   MLY D 196     1555   1555  1.33  
LINK         C   MLY D 196                 N   GLU D 197     1555   1555  1.33  
LINK         OD2 ASP A 168                MN    MN A 301     1555   1555  2.11  
LINK         OD2 ASP C 168                MN    MN C 301     1555   1555  2.12  
LINK         OD2 ASP D 168                MN    MN D 302     1555   1555  2.12  
LINK         OD2 ASP B 168                MN    MN B 301     1555   1555  2.14  
LINK         NE2 HIS A  81                MN    MN A 301     1555   1555  2.21  
LINK         NE2 HIS C  81                MN    MN C 301     1555   1555  2.21  
LINK         NE2 HIS A 172                MN    MN A 301     1555   1555  2.22  
LINK         NE2 HIS B  26                MN    MN B 301     1555   1555  2.22  
LINK         NE2 HIS C 172                MN    MN C 301     1555   1555  2.22  
LINK         NE2 HIS B 172                MN    MN B 301     1555   1555  2.24  
LINK         NE2 HIS D  81                MN    MN D 302     1555   1555  2.25  
LINK        MN    MN B 301                 O   HOH B 401     1555   1555  2.26  
LINK         NE2 HIS B  81                MN    MN B 301     1555   1555  2.26  
LINK         NE2 HIS D  26                MN    MN D 302     1555   1555  2.26  
LINK         NE2 HIS C  26                MN    MN C 301     1555   1555  2.26  
LINK         NE2 HIS D 172                MN    MN D 302     1555   1555  2.27  
LINK        MN    MN C 301                 O   HOH C 402     1555   1555  2.27  
LINK         NE2 HIS A  26                MN    MN A 301     1555   1555  2.28  
LINK        MN    MN D 302                 O   HOH D 403     1555   1555  2.28  
LINK        MN    MN A 301                 O   HOH A 403     1555   1555  2.38  
CISPEP   1 GLU A   15    PRO A   16          0         0.50                     
CISPEP   2 GLU B   15    PRO B   16          0         9.15                     
CISPEP   3 GLU C   15    PRO C   16          0         6.18                     
CISPEP   4 GLU D   15    PRO D   16          0         6.45                     
SITE     1 AC1  5 HIS A  26  HIS A  81  ASP A 168  HIS A 172                    
SITE     2 AC1  5 HOH A 403                                                     
SITE     1 AC2  5 HIS B  26  HIS B  81  ASP B 168  HIS B 172                    
SITE     2 AC2  5 HOH B 401                                                     
SITE     1 AC3  5 HIS C  26  HIS C  81  ASP C 168  HIS C 172                    
SITE     2 AC3  5 HOH C 402                                                     
SITE     1 AC4  8 PHE A  11  GLY A  12  GLY A  20  GLN A  21                    
SITE     2 AC4  8 HOH A 447  GLN C 179  MLY C 181  HOH C 433                    
SITE     1 AC5  5 HIS D  26  HIS D  81  ASP D 168  HIS D 172                    
SITE     2 AC5  5 HOH D 403                                                     
SITE     1 AC6  7 GLU B  15  GLY B  20  GLN B  21  TYR D 178                    
SITE     2 AC6  7 MLY D 181  ASP D 184  HOH D 520                               
CRYST1   65.540   66.250   66.620 112.58 103.63 110.27 P 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      0.015258  0.005634  0.007651        0.00000                         
SCALE2      0.000000  0.016091  0.009558        0.00000                         
SCALE3      0.000000  0.000000  0.017965        0.00000                         
HETATM    1  N   MLY A   1     -30.156 -10.656 -23.354  1.00 21.32           N  
ANISOU    1  N   MLY A   1     2012   3245   2843    213     44   -474       N  
HETATM    2  CA  MLY A   1     -29.984 -11.771 -24.277  1.00 16.49           C  
ANISOU    2  CA  MLY A   1     1414   2614   2238    191     44   -431       C  
HETATM    3  CB  MLY A   1     -31.277 -12.587 -24.350  1.00 20.86           C  
ANISOU    3  CB  MLY A   1     1917   3222   2787    165     50   -457       C  
HETATM    4  CG  MLY A   1     -31.217 -13.781 -25.302  1.00 19.95           C  
ANISOU    4  CG  MLY A   1     1810   3090   2679    140     48   -417       C  
HETATM    5  CD  MLY A   1     -32.574 -14.477 -25.341  1.00 25.80           C  
ANISOU    5  CD  MLY A   1     2499   3889   3416    114     51   -447       C  
HETATM    6  CE  MLY A   1     -32.457 -15.922 -25.795  1.00 36.43           C  
ANISOU    6  CE  MLY A   1     3851   5234   4758     67     61   -403       C  
HETATM    7  NZ  MLY A   1     -33.261 -16.828 -24.909  1.00 44.61           N  
ANISOU    7  NZ  MLY A   1     4848   6337   5766      7     90   -414       N  
HETATM    8  CH1 MLY A   1     -34.580 -16.210 -24.697  1.00 34.70           C  
ANISOU    8  CH1 MLY A   1     3539   5134   4510     24     83   -479       C  
HETATM    9  CH2 MLY A   1     -33.480 -18.075 -25.653  1.00 46.90           C  
ANISOU    9  CH2 MLY A   1     5137   6626   6059    -30     86   -383       C  
HETATM   10  C   MLY A   1     -29.647 -11.252 -25.666  1.00 17.94           C  
ANISOU   10  C   MLY A   1     1632   2738   2448    233      7   -420       C  
HETATM   11  O   MLY A   1     -30.432 -10.507 -26.248  1.00 17.02           O  
ANISOU   11  O   MLY A   1     1501   2618   2346    270    -26   -460       O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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