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Database: PDB
Entry: 3LSU
LinkDB: 3LSU
Original site: 3LSU 
HEADER    OXIDOREDUCTASE                          12-FEB-10   3LSU              
TITLE     CRYSTAL STRUCTURE OF SOD2 FROM SACCHAROMYCES 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                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: YEAST;                                              
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: SOD2, YHR008C;                                                 
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_COMMON: YEAST;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: EG103;                                     
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: YEP352-SOD2                               
KEYWDS    MN SUPEROXIDE DISMUTASE, REDUCTIVE METHYLATION, MANGANESE, METAL-     
KEYWDS   2 BINDING, MITOCHONDRION, OXIDOREDUCTASE, PHOSPHOPROTEIN, TRANSIT      
KEYWDS   3 PEPTIDE                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.SHENG,D.CASCIO,J.S.VALENTINE                                        
REVDAT   2   01-NOV-17 3LSU    1       REMARK                                   
REVDAT   1   23-FEB-11 3LSU    0                                                
JRNL        AUTH   Y.SHENG,D.CASCIO,J.S.VALENTINE                               
JRNL        TITL   CRYSTAL STRUCTURE OF SOD2 FROM SACCHAROMYCES CEREVISIAE      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.5_2                                         
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.38                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 59978                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3032                            
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 32.3810 -  5.3060    0.98     2850   143  0.1620 0.1770        
REMARK   3     2  5.3060 -  4.2150    0.96     2799   146  0.1510 0.1480        
REMARK   3     3  4.2150 -  3.6830    0.96     2799   142  0.1380 0.1600        
REMARK   3     4  3.6830 -  3.3470    0.97     2815   146  0.1540 0.1890        
REMARK   3     5  3.3470 -  3.1070    0.97     2802   150  0.1690 0.1800        
REMARK   3     6  3.1070 -  2.9240    0.96     2802   145  0.1810 0.2230        
REMARK   3     7  2.9240 -  2.7770    0.96     2788   135  0.1820 0.2230        
REMARK   3     8  2.7770 -  2.6570    0.96     2809   144  0.1710 0.2360        
REMARK   3     9  2.6570 -  2.5550    0.95     2709   179  0.1690 0.2170        
REMARK   3    10  2.5550 -  2.4660    0.95     2788   141  0.1610 0.2120        
REMARK   3    11  2.4660 -  2.3890    0.95     2725   156  0.1620 0.2010        
REMARK   3    12  2.3890 -  2.3210    0.94     2764   147  0.1520 0.1820        
REMARK   3    13  2.3210 -  2.2600    0.94     2735   148  0.1550 0.1850        
REMARK   3    14  2.2600 -  2.2050    0.94     2700   152  0.1600 0.2230        
REMARK   3    15  2.2050 -  2.1550    0.94     2724   152  0.1560 0.2230        
REMARK   3    16  2.1550 -  2.1090    0.93     2683   148  0.1550 0.2140        
REMARK   3    17  2.1090 -  2.0670    0.93     2675   139  0.1560 0.1950        
REMARK   3    18  2.0670 -  2.0280    0.93     2750   135  0.1590 0.2230        
REMARK   3    19  2.0280 -  1.9910    0.85     2439   150  0.1550 0.1930        
REMARK   3    20  1.9910 -  1.9580    0.66     1915    95  0.1660 0.2460        
REMARK   3    21  1.9580 -  1.9260    0.56     1656    76  0.1730 0.2090        
REMARK   3    22  1.9260 -  1.8960    0.43     1219    63  0.1650 0.1920        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.38                                          
REMARK   3   B_SOL              : 39.98                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.84                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.04700                                              
REMARK   3    B22 (A**2) : 2.23300                                              
REMARK   3    B33 (A**2) : -4.28000                                             
REMARK   3    B12 (A**2) : -0.69400                                             
REMARK   3    B13 (A**2) : 1.87100                                              
REMARK   3    B23 (A**2) : -2.43700                                             
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      :  0.007           6858                                  
REMARK   3   ANGLE     :  1.045           9331                                  
REMARK   3   CHIRALITY :  0.073            901                                  
REMARK   3   PLANARITY :  0.041           1251                                  
REMARK   3   DIHEDRAL  : 24.702           2619                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 3LSU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000057686.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-APR-09                          
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+ DW                    
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : CONFOCAL MIRRORS VARIMAX HF        
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS HTC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59997                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 80.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.5                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 53.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.31400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 1.3.2                                          
REMARK 200 STARTING MODEL: PDB ENTRY 1QNM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM MALONATE, 20% PEG 3350, PH   
REMARK 280  7.0, VAPOR DIFFUSION, HANGING DROP, 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: 12380 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ILE A   207                                                      
REMARK 465     ILE C   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      -66.26   -105.27                                   
REMARK 500    GLU A  55       88.86   -154.81                                   
REMARK 500    ASN A 153     -126.57     59.90                                   
REMARK 500    TYR A 174      -12.78   -145.89                                   
REMARK 500    GLN A 179     -124.52     40.86                                   
REMARK 500    MLY B  29      -61.68   -105.27                                   
REMARK 500    THR B 100     -167.60   -124.96                                   
REMARK 500    ASN B 153     -127.15     57.52                                   
REMARK 500    TYR B 174      -14.37   -148.95                                   
REMARK 500    GLN B 179     -128.00     48.87                                   
REMARK 500    MLY C  29      -70.50   -103.69                                   
REMARK 500    ASN C 153     -124.45     54.40                                   
REMARK 500    TYR C 174      -11.91   -146.72                                   
REMARK 500    GLN C 179     -126.00     43.90                                   
REMARK 500    MLY D  29      -67.27   -103.32                                   
REMARK 500    ASN D 153     -126.45     57.39                                   
REMARK 500    TYR D 174      -13.06   -149.15                                   
REMARK 500    GLN D 179     -128.16     44.58                                   
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 B 208  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 168   OD2                                                    
REMARK 620 2 HIS B  26   NE2  86.0                                              
REMARK 620 3 HIS B  81   NE2 115.4  94.3                                        
REMARK 620 4 HIS B 172   NE2 118.0  92.1 126.5                                  
REMARK 620 5 HOH B 214   O    87.6 173.0  91.1  88.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 208  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 168   OD2                                                    
REMARK 620 2 HIS A  81   NE2 112.3                                              
REMARK 620 3 HIS A 172   NE2 117.5 130.1                                        
REMARK 620 4 HIS A  26   NE2  87.5  94.3  90.9                                  
REMARK 620 5 HOH A 211   O    85.4  89.2  91.7 172.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 208  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 168   OD2                                                    
REMARK 620 2 HIS C  26   NE2  85.3                                              
REMARK 620 3 HIS C 172   NE2 119.6  92.4                                        
REMARK 620 4 HIS C  81   NE2 111.9  90.6 128.5                                  
REMARK 620 5 HOH C 212   O    87.9 172.7  93.4  89.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 208  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 168   OD2                                                    
REMARK 620 2 HIS D 172   NE2 118.6                                              
REMARK 620 3 HIS D  81   NE2 112.4 129.0                                        
REMARK 620 4 HIS D  26   NE2  84.4  94.3  90.9                                  
REMARK 620 5 HOH D 214   O    87.2  91.6  90.3 171.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 209  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GOL C 210   O1                                                     
REMARK 620 2 GLN C 179   OE1 169.4                                              
REMARK 620 3 GLN C 177   O    84.0  85.5                                        
REMARK 620 4 HOH C 222   O   108.0  72.3  83.1                                  
REMARK 620 5 HOH C 259   O    92.4  89.5 109.2 157.5                            
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 208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 209                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 209                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 210                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 209                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 210                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3BFR   RELATED DB: PDB                                   
REMARK 900 OUR ENTRY IS THE SAME PROTEIN BUT WITH MN(II) INSTEAD OF MN(III) IN  
REMARK 900 3BFR. OUR ENTRY HAS THE LYSINES METHYLATED                           
DBREF  3LSU A    1   207  UNP    P00447   SODM_YEAST      27    233             
DBREF  3LSU B    1   207  UNP    P00447   SODM_YEAST      27    233             
DBREF  3LSU C    1   207  UNP    P00447   SODM_YEAST      27    233             
DBREF  3LSU D    1   207  UNP    P00447   SODM_YEAST      27    233             
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 MLY          
SEQRES  15 A  207  ALA 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 MLY          
SEQRES  15 B  207  ALA 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 MLY          
SEQRES  15 C  207  ALA 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 MLY          
SEQRES  15 D  207  ALA 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 3LSU MLY A    1  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY A    8  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY A   29  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY A   54  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY A   63  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY A   72  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY A  105  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY A  119  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY A  124  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY A  138  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY A  145  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY A  181  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY A  182  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY A  187  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY A  196  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY A  206  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY B    1  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY B    8  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY B   29  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY B   54  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY B   63  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY B   72  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY B  105  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY B  119  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY B  124  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY B  138  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY B  145  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY B  181  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY B  182  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY B  187  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY B  196  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY B  206  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY C    1  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY C    8  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY C   29  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY C   54  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY C   63  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY C   72  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY C  105  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY C  119  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY C  124  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY C  138  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY C  145  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY C  181  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY C  182  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY C  187  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY C  196  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY C  206  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY D    1  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY D    8  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY D   29  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY D   54  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY D   63  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY D   72  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY D  105  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY D  119  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY D  124  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY D  138  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY D  145  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY D  181  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY D  182  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY D  187  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY D  196  LYS  N-DIMETHYL-LYSINE                                  
MODRES 3LSU MLY D  206  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 182      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 182      11                                                       
HET    MLY  B 187      11                                                       
HET    MLY  B 196      11                                                       
HET    MLY  B 206      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 182      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 182      11                                                       
HET    MLY  D 187      11                                                       
HET    MLY  D 196      11                                                       
HET    MLY  D 206      11                                                       
HET     MN  A 208       1                                                       
HET     MN  B 208       1                                                       
HET    GOL  B 209       6                                                       
HET     MN  C 208       1                                                       
HET     NA  C 209       1                                                       
HET    GOL  C 210       6                                                       
HET     MN  D 208       1                                                       
HET    GOL  D 209       6                                                       
HET    GOL  D 210       6                                                       
HETNAM     MLY N-DIMETHYL-LYSINE                                                
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     GOL GLYCEROL                                                         
HETNAM      NA SODIUM ION                                                       
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MLY    64(C8 H18 N2 O2)                                             
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   7  GOL    4(C3 H8 O3)                                                  
FORMUL   9   NA    NA 1+                                                        
FORMUL  14  HOH   *421(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 TRP A  170  ALA A  173  5                                   4    
HELIX    9   9 TYR A  174  GLN A  179  1                                   6    
HELIX   10  10 MLY A  181  ILE A  189  1                                   9    
HELIX   11  11 TRP A  190  VAL A  193  5                                   4    
HELIX   12  12 ASN A  194  GLY A  205  1                                  12    
HELIX   13  13 ASP B   10  GLU B   15  5                                   6    
HELIX   14  14 SER B   19  MLY B   29  1                                  11    
HELIX   15  15 MLY B   29  GLU B   55  1                                  27    
HELIX   16  16 SER B   57  ASN B   87  1                                  31    
HELIX   17  17 PRO B   90  GLY B   94  5                                   5    
HELIX   18  18 THR B  100  GLY B  112  1                                  13    
HELIX   19  19 SER B  113  GLY B  127  1                                  15    
HELIX   20  20 SER B  141  GLY B  143  5                                   3    
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  ILE C  189  1                                   9    
HELIX   35  35 TRP C  190  VAL C  193  5                                   4    
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 MLY A 145  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  PHE B 135   O  VAL B 149           
SHEET    3   B 3 LEU B 161  ASP B 168 -1  O  LEU B 164   N  ILE B 136           
SHEET    1   C 3 LEU C 146  TYR C 152  0                                        
SHEET    2   C 3 GLY C 132  ASN C 139 -1  N  PHE C 135   O  VAL C 149           
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  1.33  
LINK         C   MLY A  72                 N   PHE A  73     1555   1555  1.32  
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  1.33  
LINK         C   MLY A 119                 N   LEU A 120     1555   1555  1.33  
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  1.32  
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   MLY A 182     1555   1555  1.32  
LINK         C   MLY A 182                 N   ALA A 183     1555   1555  1.33  
LINK         C   PHE A 186                 N   MLY A 187     1555   1555  1.32  
LINK         C   MLY A 187                 N   ALA A 188     1555   1555  1.33  
LINK         C   TRP A 195                 N   MLY A 196     1555   1555  1.32  
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 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  1.34  
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   MLY B 182     1555   1555  1.33  
LINK         C   MLY B 182                 N   ALA B 183     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   GLY B 205                 N   MLY B 206     1555   1555  1.33  
LINK         C   MLY B 206                 N   ILE B 207     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  1.32  
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   MLY C 182     1555   1555  1.32  
LINK         C   MLY C 182                 N   ALA C 183     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  1.33  
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   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  1.33  
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  1.33  
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  1.32  
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   MLY D 182     1555   1555  1.33  
LINK         C   MLY D 182                 N   ALA D 183     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         C   GLY D 205                 N   MLY D 206     1555   1555  1.33  
LINK         C   MLY D 206                 N   ILE D 207     1555   1555  1.33  
LINK         OD2 ASP B 168                MN    MN B 208     1555   1555  2.03  
LINK         OD2 ASP A 168                MN    MN A 208     1555   1555  2.04  
LINK         OD2 ASP C 168                MN    MN C 208     1555   1555  2.04  
LINK         OD2 ASP D 168                MN    MN D 208     1555   1555  2.07  
LINK         NE2 HIS B  26                MN    MN B 208     1555   1555  2.18  
LINK         NE2 HIS D 172                MN    MN D 208     1555   1555  2.19  
LINK         NE2 HIS A  81                MN    MN A 208     1555   1555  2.20  
LINK         NE2 HIS D  81                MN    MN D 208     1555   1555  2.21  
LINK         NE2 HIS A 172                MN    MN A 208     1555   1555  2.22  
LINK         NE2 HIS B  81                MN    MN B 208     1555   1555  2.22  
LINK         NE2 HIS C  26                MN    MN C 208     1555   1555  2.23  
LINK         NE2 HIS C 172                MN    MN C 208     1555   1555  2.23  
LINK         NE2 HIS B 172                MN    MN B 208     1555   1555  2.24  
LINK         NE2 HIS C  81                MN    MN C 208     1555   1555  2.24  
LINK         NE2 HIS A  26                MN    MN A 208     1555   1555  2.27  
LINK         NE2 HIS D  26                MN    MN D 208     1555   1555  2.29  
LINK        NA    NA C 209                 O1  GOL C 210     1555   1555  2.67  
LINK         OE1 GLN C 179                NA    NA C 209     1555   1555  2.73  
LINK         O   GLN C 177                NA    NA C 209     1555   1555  2.73  
LINK        MN    MN C 208                 O   HOH C 212     1555   1555  2.27  
LINK        MN    MN D 208                 O   HOH D 214     1555   1555  2.29  
LINK        MN    MN B 208                 O   HOH B 214     1555   1555  2.33  
LINK        MN    MN A 208                 O   HOH A 211     1555   1555  2.35  
LINK        NA    NA C 209                 O   HOH C 222     1555   1555  2.58  
LINK        NA    NA C 209                 O   HOH C 259     1555   1555  2.62  
CISPEP   1 GLU A   15    PRO A   16          0         1.94                     
CISPEP   2 GLU B   15    PRO B   16          0         6.62                     
CISPEP   3 GLU C   15    PRO C   16          0         6.66                     
CISPEP   4 GLU D   15    PRO D   16          0         5.83                     
SITE     1 AC1  5 HIS A  26  HIS A  81  ASP A 168  HIS A 172                    
SITE     2 AC1  5 HOH A 211                                                     
SITE     1 AC2  5 HIS B  26  HIS B  81  ASP B 168  HIS B 172                    
SITE     2 AC2  5 HOH B 214                                                     
SITE     1 AC3  4 MLY A   8  GLN A  93  ASN A 194  HOH B 230                    
SITE     1 AC4  5 HIS C  26  HIS C  81  ASP C 168  HIS C 172                    
SITE     2 AC4  5 HOH C 212                                                     
SITE     1 AC5  5 GLN C 177  GLN C 179  GOL C 210  HOH C 222                    
SITE     2 AC5  5 HOH C 259                                                     
SITE     1 AC6  8 GLY A  12  GLU A  15  GLN C 177  TYR C 178                    
SITE     2 AC6  8 MLY C 181  ASP C 184   NA C 209  HOH C 259                    
SITE     1 AC7  5 HIS D  26  HIS D  81  ASP D 168  HIS D 172                    
SITE     2 AC7  5 HOH D 214                                                     
SITE     1 AC8  7 GLU B  15  GLY B  20  GLN B  21  TYR D 178                    
SITE     2 AC8  7 MLY D 181  ASP D 184  HOH D 257                               
SITE     1 AC9  6 GLU B  15  PRO B  16  ILE B  18  SER B  19                    
SITE     2 AC9  6 GLN B 177  PRO D  16                                          
CRYST1   63.657   64.933   66.550 109.36 106.35 109.68 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      0.015709  0.005619  0.008233        0.00000                         
SCALE2      0.000000  0.016356  0.008753        0.00000                         
SCALE3      0.000000  0.000000  0.017761        0.00000                         
HETATM    1  N   MLY A   1      -4.631  17.174  35.553  1.00 42.50           N  
HETATM    2  CA  MLY A   1      -3.641  18.133  36.024  1.00 35.21           C  
HETATM    3  CB  MLY A   1      -4.276  19.392  36.677  1.00 31.39           C  
HETATM    4  CG  MLY A   1      -3.343  20.237  37.632  1.00 37.41           C  
HETATM    5  CD  MLY A   1      -3.884  21.643  38.118  1.00 42.54           C  
HETATM    6  CE  MLY A   1      -2.901  22.613  38.753  1.00 51.62           C  
HETATM    7  NZ  MLY A   1      -2.578  23.856  38.013  1.00 58.11           N  
HETATM    8  CH1 MLY A   1      -2.928  23.689  36.612  1.00 57.80           C  
HETATM    9  CH2 MLY A   1      -1.135  24.116  38.115  1.00 57.81           C  
HETATM   10  C   MLY A   1      -2.647  17.522  37.017  1.00 31.30           C  
HETATM   11  O   MLY A   1      -3.002  17.131  38.076  1.00 35.18           O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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