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Database: PDB
Entry: 3LST
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HEADER    TRANSFERASE                             12-FEB-10   3LST              
TITLE     CRYSTAL STRUCTURE OF CALO1, METHYLTRANSFERASE IN CALICHEAMICIN        
TITLE    2 BIOSYNTHESIS, SAH BOUND FORM                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALO1 METHYLTRANSFERASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MICROMONOSPORA ECHINOSPORA;                     
SOURCE   3 ORGANISM_COMMON: MICROMONOSPORA PURPUREA;                            
SOURCE   4 ORGANISM_TAXID: 1877;                                                
SOURCE   5 GENE: CALO1;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: B834 P(RARE2);                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET16B                                    
KEYWDS    CALICHEAMICIN, METHYLTRANSFERASE, CALO1, ENEDIYNE, SAH, STRUCTURAL    
KEYWDS   2 GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, CENTER FOR EUKARYOTIC 
KEYWDS   3 STRUCTURAL GENOMICS, CESG, TRANSFERASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.CHANG,S.SINGH,C.A.BINGMAN,J.S.THORSON,G.N.PHILLIPS JR.,CENTER FOR   
AUTHOR   2 EUKARYOTIC STRUCTURAL GENOMICS (CESG)                                
REVDAT   3   01-NOV-17 3LST    1       REMARK                                   
REVDAT   2   16-MAR-11 3LST    1       JRNL                                     
REVDAT   1   02-MAR-10 3LST    0                                                
JRNL        AUTH   A.CHANG,S.SINGH,C.A.BINGMAN,J.S.THORSON,G.N.PHILLIPS         
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF CALO1: A PUTATIVE ORSELLINIC  
JRNL        TITL 2 ACID METHYLTRANSFERASE IN THE CALICHEAMICIN-BIOSYNTHETIC     
JRNL        TITL 3 PATHWAY.                                                     
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  67   197 2011              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   21358050                                                     
JRNL        DOI    10.1107/S090744491100360X                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 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 : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.17                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.320                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 27959                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1411                            
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 48.1830 -  5.1690    1.00     2847   167  0.1730 0.2040        
REMARK   3     2  5.1690 -  4.1030    1.00     2771   142  0.1450 0.2050        
REMARK   3     3  4.1030 -  3.5850    1.00     2721   138  0.1690 0.2350        
REMARK   3     4  3.5850 -  3.2570    1.00     2743   131  0.2170 0.2370        
REMARK   3     5  3.2570 -  3.0240    1.00     2665   152  0.2280 0.2900        
REMARK   3     6  3.0240 -  2.8450    1.00     2708   130  0.2220 0.2850        
REMARK   3     7  2.8450 -  2.7030    1.00     2671   159  0.2290 0.2800        
REMARK   3     8  2.7030 -  2.5850    0.99     2639   126  0.2500 0.3310        
REMARK   3     9  2.5850 -  2.4860    0.93     2503   144  0.2450 0.3300        
REMARK   3    10  2.4860 -  2.4000    0.86     2280   122  0.2590 0.3030        
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              : 0.33                                          
REMARK   3   B_SOL              : 40.00                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.50800                                              
REMARK   3    B22 (A**2) : -2.32600                                             
REMARK   3    B33 (A**2) : 1.89100                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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      :  0.004           5222                                  
REMARK   3   ANGLE     :  0.717           7098                                  
REMARK   3   CHIRALITY :  0.049            808                                  
REMARK   3   PLANARITY :  0.002            938                                  
REMARK   3   DIHEDRAL  : 14.893           1882                                  
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 3LST 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_1000057685.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUL-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) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794, 0.9641                     
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL             
REMARK 200                                   MONOCHROMATER                      
REMARK 200  OPTICS                         : ADJUSTABLE FOCUSING MIRRORS IN K   
REMARK 200                                   -B GEOMETRY                        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28057                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : 12.30                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION 20MG/ML CALO1           
REMARK 280  PROTEIN, 20MM TRIS PH 8, MIXED IN A 1:1 RATIO WITH THE WELL         
REMARK 280  SOLUTION 20% MEPEG 5K, 0.2M GLYCINE, 0.1M BTP PH 7.0.               
REMARK 280  CRYOPROTECTED WITH 20% ETHYLENE GLYCOL, 20% MEPEG 5K, 0.2M          
REMARK 280  GLYCINE, 0.1M BTP PH 7.0, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      120.48550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      120.48550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       31.75750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.80150            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       31.75750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.80150            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      120.48550            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       31.75750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       46.80150            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      120.48550            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       31.75750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       46.80150            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL UNIT IS A DIMER. THERE ARE HALF OF 2          
REMARK 300 BIOLOGICAL UNITS IN THE ASYMMETRIC UNIT. THE DIMER GENERATED FROM    
REMARK 300 THE MONOMER IN THE ASYMMETRIC UNIT BY THE OPERATIONS: X, -Y,-Z AND - 
REMARK 300 X, Y,-Z+1/2                                                          
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       93.60300            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      240.97100            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      120.48550            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 398  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 429  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MSE A     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     ARG A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     PRO A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     ARG A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     GLN B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 465     ARG B     5                                                      
REMARK 465     PRO B     6                                                      
REMARK 465     PRO B     7                                                      
REMARK 465     SER B     8                                                      
REMARK 465     ARG B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     GLY B    12                                                      
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    ARG A 133       69.29     63.92                                   
REMARK 500    ASP A 212     -178.88   -170.06                                   
REMARK 500    ILE A 253      -65.00   -108.53                                   
REMARK 500    LEU A 327       96.13    -62.79                                   
REMARK 500    ARG B 133       77.16     56.84                                   
REMARK 500    SER B 142      152.77    179.08                                   
REMARK 500    HIS B 220      152.28    -43.86                                   
REMARK 500    ASP B 223       42.26    -81.71                                   
REMARK 500    VAL B 272       30.52    -99.85                                   
REMARK 500    SER B 334        2.42    -69.74                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 346                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 347                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 346                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 347                 
DBREF  3LST A    1   345  UNP    Q8KNE5   Q8KNE5_MICEC     1    345             
DBREF  3LST B    1   345  UNP    Q8KNE5   Q8KNE5_MICEC     1    345             
SEQADV 3LST GLY A   -2  UNP  Q8KNE5              EXPRESSION TAG                 
SEQADV 3LST SER A   -1  UNP  Q8KNE5              EXPRESSION TAG                 
SEQADV 3LST HIS A    0  UNP  Q8KNE5              EXPRESSION TAG                 
SEQADV 3LST GLY B   -2  UNP  Q8KNE5              EXPRESSION TAG                 
SEQADV 3LST SER B   -1  UNP  Q8KNE5              EXPRESSION TAG                 
SEQADV 3LST HIS B    0  UNP  Q8KNE5              EXPRESSION TAG                 
SEQRES   1 A  348  GLY SER HIS MSE GLN ARG GLN ARG PRO PRO SER ARG ALA          
SEQRES   2 A  348  GLY GLY ASP MSE ASP ARG LEU GLN SER ALA LEU ALA LEU          
SEQRES   3 A  348  TYR GLU GLU ALA MSE GLY TYR THR TYR ALA ALA ALA LEU          
SEQRES   4 A  348  ARG ALA ALA ALA ALA VAL GLY VAL ALA ASP HIS LEU VAL          
SEQRES   5 A  348  ASP GLY PRO ARG THR PRO ALA GLU LEU ALA ALA ALA THR          
SEQRES   6 A  348  GLY THR ASP ALA ASP ALA LEU ARG ARG VAL LEU ARG LEU          
SEQRES   7 A  348  LEU ALA VAL ARG ASP VAL VAL ARG GLU SER ASP GLY ARG          
SEQRES   8 A  348  PHE ALA LEU THR ASP LYS GLY ALA ALA LEU ARG SER ASP          
SEQRES   9 A  348  SER PRO VAL PRO ALA ARG ALA GLY ILE LEU MSE PHE THR          
SEQRES  10 A  348  ASP THR MSE PHE TRP THR MSE SER HIS ARG VAL ALA SER          
SEQRES  11 A  348  ALA LEU GLY PRO GLU ARG PRO ALA PHE ALA ASP ILE PHE          
SEQRES  12 A  348  GLY SER SER LEU ASP ALA TYR PHE ASP GLY ASP ALA GLU          
SEQRES  13 A  348  VAL GLU ALA LEU TYR TYR GLU GLY MSE GLU THR VAL SER          
SEQRES  14 A  348  ALA ALA GLU HIS LEU ILE LEU ALA ARG ALA GLY ASP PHE          
SEQRES  15 A  348  PRO ALA THR GLY THR VAL ALA ASP VAL GLY GLY GLY ARG          
SEQRES  16 A  348  GLY GLY PHE LEU LEU THR VAL LEU ARG GLU HIS PRO GLY          
SEQRES  17 A  348  LEU GLN GLY VAL LEU LEU ASP ARG ALA GLU VAL VAL ALA          
SEQRES  18 A  348  ARG HIS ARG LEU ASP ALA PRO ASP VAL ALA GLY ARG TRP          
SEQRES  19 A  348  LYS VAL VAL GLU GLY ASP PHE LEU ARG GLU VAL PRO HIS          
SEQRES  20 A  348  ALA ASP VAL HIS VAL LEU LYS ARG ILE LEU HIS ASN TRP          
SEQRES  21 A  348  GLY ASP GLU ASP SER VAL ARG ILE LEU THR ASN CYS ARG          
SEQRES  22 A  348  ARG VAL MSE PRO ALA HIS GLY ARG VAL LEU VAL ILE ASP          
SEQRES  23 A  348  ALA VAL VAL PRO GLU GLY ASN ASP ALA HIS GLN SER LYS          
SEQRES  24 A  348  GLU MSE ASP PHE MSE MSE LEU ALA ALA ARG THR GLY GLN          
SEQRES  25 A  348  GLU ARG THR ALA ALA GLU LEU GLU PRO LEU PHE THR ALA          
SEQRES  26 A  348  ALA GLY LEU ARG LEU ASP ARG VAL VAL GLY THR SER SER          
SEQRES  27 A  348  VAL MSE SER ILE ALA VAL GLY VAL PRO ALA                      
SEQRES   1 B  348  GLY SER HIS MSE GLN ARG GLN ARG PRO PRO SER ARG ALA          
SEQRES   2 B  348  GLY GLY ASP MSE ASP ARG LEU GLN SER ALA LEU ALA LEU          
SEQRES   3 B  348  TYR GLU GLU ALA MSE GLY TYR THR TYR ALA ALA ALA LEU          
SEQRES   4 B  348  ARG ALA ALA ALA ALA VAL GLY VAL ALA ASP HIS LEU VAL          
SEQRES   5 B  348  ASP GLY PRO ARG THR PRO ALA GLU LEU ALA ALA ALA THR          
SEQRES   6 B  348  GLY THR ASP ALA ASP ALA LEU ARG ARG VAL LEU ARG LEU          
SEQRES   7 B  348  LEU ALA VAL ARG ASP VAL VAL ARG GLU SER ASP GLY ARG          
SEQRES   8 B  348  PHE ALA LEU THR ASP LYS GLY ALA ALA LEU ARG SER ASP          
SEQRES   9 B  348  SER PRO VAL PRO ALA ARG ALA GLY ILE LEU MSE PHE THR          
SEQRES  10 B  348  ASP THR MSE PHE TRP THR MSE SER HIS ARG VAL ALA SER          
SEQRES  11 B  348  ALA LEU GLY PRO GLU ARG PRO ALA PHE ALA ASP ILE PHE          
SEQRES  12 B  348  GLY SER SER LEU ASP ALA TYR PHE ASP GLY ASP ALA GLU          
SEQRES  13 B  348  VAL GLU ALA LEU TYR TYR GLU GLY MSE GLU THR VAL SER          
SEQRES  14 B  348  ALA ALA GLU HIS LEU ILE LEU ALA ARG ALA GLY ASP PHE          
SEQRES  15 B  348  PRO ALA THR GLY THR VAL ALA ASP VAL GLY GLY GLY ARG          
SEQRES  16 B  348  GLY GLY PHE LEU LEU THR VAL LEU ARG GLU HIS PRO GLY          
SEQRES  17 B  348  LEU GLN GLY VAL LEU LEU ASP ARG ALA GLU VAL VAL ALA          
SEQRES  18 B  348  ARG HIS ARG LEU ASP ALA PRO ASP VAL ALA GLY ARG TRP          
SEQRES  19 B  348  LYS VAL VAL GLU GLY ASP PHE LEU ARG GLU VAL PRO HIS          
SEQRES  20 B  348  ALA ASP VAL HIS VAL LEU LYS ARG ILE LEU HIS ASN TRP          
SEQRES  21 B  348  GLY ASP GLU ASP SER VAL ARG ILE LEU THR ASN CYS ARG          
SEQRES  22 B  348  ARG VAL MSE PRO ALA HIS GLY ARG VAL LEU VAL ILE ASP          
SEQRES  23 B  348  ALA VAL VAL PRO GLU GLY ASN ASP ALA HIS GLN SER LYS          
SEQRES  24 B  348  GLU MSE ASP PHE MSE MSE LEU ALA ALA ARG THR GLY GLN          
SEQRES  25 B  348  GLU ARG THR ALA ALA GLU LEU GLU PRO LEU PHE THR ALA          
SEQRES  26 B  348  ALA GLY LEU ARG LEU ASP ARG VAL VAL GLY THR SER SER          
SEQRES  27 B  348  VAL MSE SER ILE ALA VAL GLY VAL PRO ALA                      
MODRES 3LST MSE A   14  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE A   28  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE A  112  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE A  117  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE A  121  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE A  162  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE A  273  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE A  298  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE A  301  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE A  302  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE A  337  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE B   14  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE B   28  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE B  112  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE B  117  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE B  121  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE B  162  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE B  273  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE B  298  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE B  301  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE B  302  MET  SELENOMETHIONINE                                   
MODRES 3LST MSE B  337  MET  SELENOMETHIONINE                                   
HET    MSE  A  14       8                                                       
HET    MSE  A  28       8                                                       
HET    MSE  A 112       8                                                       
HET    MSE  A 117       8                                                       
HET    MSE  A 121       8                                                       
HET    MSE  A 162       8                                                       
HET    MSE  A 273       8                                                       
HET    MSE  A 298       8                                                       
HET    MSE  A 301       8                                                       
HET    MSE  A 302       8                                                       
HET    MSE  A 337       8                                                       
HET    MSE  B  14       8                                                       
HET    MSE  B  28       8                                                       
HET    MSE  B 112       8                                                       
HET    MSE  B 117       8                                                       
HET    MSE  B 121       8                                                       
HET    MSE  B 162       8                                                       
HET    MSE  B 273       8                                                       
HET    MSE  B 298       8                                                       
HET    MSE  B 301       8                                                       
HET    MSE  B 302       8                                                       
HET    MSE  B 337       8                                                       
HET    SAH  A 346      26                                                       
HET    EDO  A 347       4                                                       
HET    SAH  B 346      26                                                       
HET    EDO  B 347       4                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  MSE    22(C5 H11 N O2 SE)                                           
FORMUL   3  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL   4  EDO    2(C2 H6 O2)                                                  
FORMUL   7  HOH   *181(H2 O)                                                    
HELIX    1   1 ASP A   15  MSE A   28  1                                  14    
HELIX    2   2 TYR A   30  GLY A   43  1                                  14    
HELIX    3   3 VAL A   44  VAL A   49  5                                   6    
HELIX    4   4 THR A   54  GLY A   63  1                                  10    
HELIX    5   5 ASP A   65  ARG A   79  1                                  15    
HELIX    6   6 GLY A   95  ARG A   99  5                                   5    
HELIX    7   7 ALA A  106  THR A  114  1                                   9    
HELIX    8   8 ASP A  115  ARG A  124  1                                  10    
HELIX    9   9 ARG A  124  LEU A  129  1                                   6    
HELIX   10  10 ALA A  135  GLY A  141  1                                   7    
HELIX   11  11 SER A  143  ASP A  149  1                                   7    
HELIX   12  12 ASP A  151  ALA A  168  1                                  18    
HELIX   13  13 GLU A  169  GLY A  177  1                                   9    
HELIX   14  14 GLY A  193  HIS A  203  1                                  11    
HELIX   15  15 ARG A  213  ALA A  218  1                                   6    
HELIX   16  16 ALA A  224  ALA A  228  5                                   5    
HELIX   17  17 ILE A  253  TRP A  257  5                                   5    
HELIX   18  18 GLY A  258  VAL A  272  1                                  15    
HELIX   19  19 HIS A  293  ALA A  305  1                                  13    
HELIX   20  20 THR A  312  ALA A  323  1                                  12    
HELIX   21  21 ASP B   15  MSE B   28  1                                  14    
HELIX   22  22 TYR B   30  GLY B   43  1                                  14    
HELIX   23  23 VAL B   44  LEU B   48  5                                   5    
HELIX   24  24 THR B   54  GLY B   63  1                                  10    
HELIX   25  25 ASP B   65  ARG B   79  1                                  15    
HELIX   26  26 GLY B   95  ARG B   99  5                                   5    
HELIX   27  27 ALA B  106  THR B  114  1                                   9    
HELIX   28  28 ASP B  115  ARG B  124  1                                  10    
HELIX   29  29 ALA B  126  GLY B  130  5                                   5    
HELIX   30  30 ALA B  135  GLY B  141  1                                   7    
HELIX   31  31 SER B  143  ASP B  151  1                                   9    
HELIX   32  32 ASP B  151  GLY B  177  1                                  27    
HELIX   33  33 GLY B  193  HIS B  203  1                                  11    
HELIX   34  34 ARG B  213  ALA B  218  1                                   6    
HELIX   35  35 ALA B  224  ALA B  228  5                                   5    
HELIX   36  36 ILE B  253  TRP B  257  5                                   5    
HELIX   37  37 GLY B  258  VAL B  272  1                                  15    
HELIX   38  38 HIS B  293  ARG B  306  1                                  14    
HELIX   39  39 THR B  312  ALA B  323  1                                  12    
SHEET    1   A 2 VAL A  82  SER A  85  0                                        
SHEET    2   A 2 ARG A  88  LEU A  91 -1  O  ALA A  90   N  ARG A  83           
SHEET    1   B 7 TRP A 231  GLU A 235  0                                        
SHEET    2   B 7 LEU A 206  ASP A 212  1  N  LEU A 210   O  VAL A 234           
SHEET    3   B 7 GLY A 183  VAL A 188  1  N  VAL A 185   O  VAL A 209           
SHEET    4   B 7 VAL A 247  LYS A 251  1  O  VAL A 249   N  ALA A 186           
SHEET    5   B 7 ARG A 278  ASP A 283  1  O  LEU A 280   N  HIS A 248           
SHEET    6   B 7 SER A 338  PRO A 344 -1  O  ALA A 340   N  VAL A 281           
SHEET    7   B 7 LEU A 325  GLY A 332 -1  N  ARG A 329   O  VAL A 341           
SHEET    1   C 2 VAL B  82  SER B  85  0                                        
SHEET    2   C 2 ARG B  88  LEU B  91 -1  O  ARG B  88   N  SER B  85           
SHEET    1   D 7 TRP B 231  GLU B 235  0                                        
SHEET    2   D 7 GLN B 207  ASP B 212  1  N  LEU B 210   O  VAL B 234           
SHEET    3   D 7 THR B 184  VAL B 188  1  N  VAL B 185   O  VAL B 209           
SHEET    4   D 7 VAL B 247  LYS B 251  1  O  VAL B 247   N  ALA B 186           
SHEET    5   D 7 ARG B 278  ASP B 283  1  O  LEU B 280   N  HIS B 248           
SHEET    6   D 7 SER B 338  PRO B 344 -1  O  SER B 338   N  ASP B 283           
SHEET    7   D 7 LEU B 325  VAL B 331 -1  N  ARG B 329   O  VAL B 341           
LINK         C   ASP A  13                 N   MSE A  14     1555   1555  1.33  
LINK         C   MSE A  14                 N   ASP A  15     1555   1555  1.33  
LINK         C   ALA A  27                 N   MSE A  28     1555   1555  1.33  
LINK         C   MSE A  28                 N   GLY A  29     1555   1555  1.33  
LINK         C   LEU A 111                 N   MSE A 112     1555   1555  1.33  
LINK         C   MSE A 112                 N   PHE A 113     1555   1555  1.33  
LINK         C   THR A 116                 N   MSE A 117     1555   1555  1.33  
LINK         C   MSE A 117                 N   PHE A 118     1555   1555  1.33  
LINK         C   THR A 120                 N   MSE A 121     1555   1555  1.33  
LINK         C   MSE A 121                 N   SER A 122     1555   1555  1.33  
LINK         C   GLY A 161                 N   MSE A 162     1555   1555  1.33  
LINK         C   MSE A 162                 N   GLU A 163     1555   1555  1.33  
LINK         C   VAL A 272                 N   MSE A 273     1555   1555  1.33  
LINK         C   MSE A 273                 N   PRO A 274     1555   1555  1.34  
LINK         C   GLU A 297                 N   MSE A 298     1555   1555  1.33  
LINK         C   MSE A 298                 N   ASP A 299     1555   1555  1.33  
LINK         C   PHE A 300                 N   MSE A 301     1555   1555  1.33  
LINK         C   MSE A 301                 N   MSE A 302     1555   1555  1.33  
LINK         C   MSE A 302                 N   LEU A 303     1555   1555  1.33  
LINK         C   VAL A 336                 N   MSE A 337     1555   1555  1.33  
LINK         C   MSE A 337                 N   SER A 338     1555   1555  1.33  
LINK         C   ASP B  13                 N   MSE B  14     1555   1555  1.33  
LINK         C   MSE B  14                 N   ASP B  15     1555   1555  1.33  
LINK         C   ALA B  27                 N   MSE B  28     1555   1555  1.33  
LINK         C   MSE B  28                 N   GLY B  29     1555   1555  1.33  
LINK         C   LEU B 111                 N   MSE B 112     1555   1555  1.33  
LINK         C   MSE B 112                 N   PHE B 113     1555   1555  1.33  
LINK         C   THR B 116                 N   MSE B 117     1555   1555  1.33  
LINK         C   MSE B 117                 N   PHE B 118     1555   1555  1.33  
LINK         C   THR B 120                 N   MSE B 121     1555   1555  1.33  
LINK         C   MSE B 121                 N   SER B 122     1555   1555  1.33  
LINK         C   GLY B 161                 N   MSE B 162     1555   1555  1.33  
LINK         C   MSE B 162                 N   GLU B 163     1555   1555  1.33  
LINK         C   VAL B 272                 N   MSE B 273     1555   1555  1.33  
LINK         C   MSE B 273                 N   PRO B 274     1555   1555  1.34  
LINK         C   GLU B 297                 N   MSE B 298     1555   1555  1.33  
LINK         C   MSE B 298                 N   ASP B 299     1555   1555  1.33  
LINK         C   PHE B 300                 N   MSE B 301     1555   1555  1.33  
LINK         C   MSE B 301                 N   MSE B 302     1555   1555  1.33  
LINK         C   MSE B 302                 N   LEU B 303     1555   1555  1.33  
LINK         C   VAL B 336                 N   MSE B 337     1555   1555  1.33  
LINK         C   MSE B 337                 N   SER B 338     1555   1555  1.33  
CISPEP   1 THR A   62    GLY A   63          0        -3.33                     
CISPEP   2 PHE B  140    GLY B  141          0        -3.83                     
SITE     1 AC1 14 SER A 166  GLY A 189  GLY A 190  ASP A 212                    
SITE     2 AC1 14 ARG A 213  VAL A 216  ASP A 237  PHE A 238                    
SITE     3 AC1 14 LYS A 251  ARG A 252  ILE A 253  TRP A 257                    
SITE     4 AC1 14 HOH A 359  HOH A 390                                          
SITE     1 AC2  4 GLU A  26  TYR A  32  ARG A  79  HOH A 381                    
SITE     1 AC3 12 GLY B 189  ASP B 212  ARG B 213  VAL B 216                    
SITE     2 AC3 12 GLY B 236  ASP B 237  PHE B 238  LYS B 251                    
SITE     3 AC3 12 ARG B 252  ILE B 253  TRP B 257  HOH B 354                    
SITE     1 AC4  4 GLU B  26  GLY B  29  TYR B  32  ARG B  79                    
CRYST1   63.515   93.603  240.971  90.00  90.00  90.00 C 2 2 21     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015744  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010683  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004150        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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