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Database: PDB
Entry: 3Q62
LinkDB: 3Q62
Original site: 3Q62 
HEADER    LYASE                                   30-DEC-10   3Q62              
TITLE     CRYSTAL STRUCTURE OF 3-HYDROXYDECANOYL-(ACYL CARRIER PROTEIN)         
TITLE    2 DEHYDRATASE FROM YERSINIA PESTIS                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 3-HYDROXYDECANOYL-[ACYL-CARRIER-PROTEIN] DEHYDRATASE;      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: BETA-HYDROXYDECANOYL THIOESTER DEHYDRASE;                   
COMPND   5 EC: 4.2.1.60;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: YERSINIA PSEUDOTUBERCULOSIS;                    
SOURCE   3 ORGANISM_TAXID: 214092;                                              
SOURCE   4 STRAIN: CO92;                                                        
SOURCE   5 GENE: FABA, YPTB1450;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 MAGIC;                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMCSG7                                    
KEYWDS    STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS     
KEYWDS   2 DISEASES, CSGID, ALPHA-BETA FOLD, HOTDOG FOLD, LYASE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.ZHANG,N.MALTSEVA,K.KWON,W.F.ANDERSON,A.JOACHIMIAK,CENTER FOR        
AUTHOR   2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)                   
REVDAT   1   12-JAN-11 3Q62    0                                                
JRNL        AUTH   R.ZHANG,N.MALTSEVA,K.KWON,W.F.ANDERSON,A.JOACHIMIAK,CSGID    
JRNL        TITL   CRYSTAL STRUCTURE OF 3-HYDROXYDECANOYL-(ACYL CARRIER         
JRNL        TITL 2 PROTEIN) DEHYDRATASE FROM YERSINIA PESTIS                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.18                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 57089                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.151                           
REMARK   3   R VALUE            (WORKING SET) : 0.149                           
REMARK   3   FREE R VALUE                     : 0.187                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2901                            
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 26.1897 -  3.0134    1.00     5684   327  0.1555 0.1721        
REMARK   3     2  3.0134 -  2.3923    1.00     5556   263  0.1579 0.2037        
REMARK   3     3  2.3923 -  2.0901    1.00     5472   281  0.1400 0.1700        
REMARK   3     4  2.0901 -  1.8990    1.00     5409   285  0.1312 0.1810        
REMARK   3     5  1.8990 -  1.7629    1.00     5393   287  0.1247 0.1876        
REMARK   3     6  1.7629 -  1.6590    1.00     5370   312  0.1237 0.1846        
REMARK   3     7  1.6590 -  1.5759    1.00     5357   263  0.1333 0.1864        
REMARK   3     8  1.5759 -  1.5074    1.00     5355   304  0.1390 0.1929        
REMARK   3     9  1.5074 -  1.4493    1.00     5349   267  0.1803 0.2313        
REMARK   3    10  1.4493 -  1.3993    0.98     5243   312  0.2325 0.2906        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.72                                          
REMARK   3   K_SOL              : 0.40                                          
REMARK   3   B_SOL              : 43.17                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.08                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.78400                                             
REMARK   3    B22 (A**2) : -0.77940                                             
REMARK   3    B33 (A**2) : 3.56340                                              
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      :  0.005           2904                                  
REMARK   3   ANGLE     :  1.063           3933                                  
REMARK   3   CHIRALITY :  0.069            410                                  
REMARK   3   PLANARITY :  0.004            517                                  
REMARK   3   DIHEDRAL  : 15.166           1114                                  
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 3Q62 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063239.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57207                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.66900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: HKL-3000, MOLREP                                      
REMARK 200 STARTING MODEL: PDB ENTRY 1MKB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 33.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 6.0, 1.0M K/NA TARTRATE,     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   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       21.21650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.19200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.33400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.19200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.21650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       25.33400            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG A   137                                                      
REMARK 465     LYS A   138                                                      
REMARK 465     ASN A   170                                                      
REMARK 465     ALA A   171                                                      
REMARK 465     PHE A   172                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B   170                                                      
REMARK 465     ALA B   171                                                      
REMARK 465     PHE B   172                                                      
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    ASP A  75       68.54   -161.91                                   
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 MES A 175                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 173                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: IDP90513   RELATED DB: TARGETDB                          
DBREF  3Q62 A    1   172  UNP    Q66CF3   FABA_YERPS       1    172             
DBREF  3Q62 B    1   172  UNP    Q66CF3   FABA_YERPS       1    172             
SEQADV 3Q62 SER A   -2  UNP  Q66CF3              EXPRESSION TAG                 
SEQADV 3Q62 ASN A   -1  UNP  Q66CF3              EXPRESSION TAG                 
SEQADV 3Q62 ALA A    0  UNP  Q66CF3              EXPRESSION TAG                 
SEQADV 3Q62 SER B   -2  UNP  Q66CF3              EXPRESSION TAG                 
SEQADV 3Q62 ASN B   -1  UNP  Q66CF3              EXPRESSION TAG                 
SEQADV 3Q62 ALA B    0  UNP  Q66CF3              EXPRESSION TAG                 
SEQRES   1 A  175  SER ASN ALA MET VAL ASP LYS ARG GLU SER TYR THR LYS          
SEQRES   2 A  175  GLU ASP LEU GLU ALA SER GLY ARG GLY GLU LEU PHE GLY          
SEQRES   3 A  175  ALA GLY GLY PRO PRO LEU PRO ALA GLY ASN MET LEU MET          
SEQRES   4 A  175  MET ASP ARG ILE VAL LYS MET ILE GLU ASP GLY GLY SER          
SEQRES   5 A  175  HIS ASN LYS GLY TYR VAL GLU ALA GLU LEU ASP ILE ASN          
SEQRES   6 A  175  PRO ASP LEU TRP PHE PHE GLY CYS HIS PHE ILE GLY ASP          
SEQRES   7 A  175  PRO VAL MET PRO GLY CYS LEU GLY LEU ASP ALA MET TRP          
SEQRES   8 A  175  GLN LEU VAL GLY PHE TYR LEU GLY TRP LEU GLY GLY GLU          
SEQRES   9 A  175  GLY LYS GLY ARG ALA LEU GLY VAL GLY GLU VAL LYS PHE          
SEQRES  10 A  175  THR GLY GLN VAL LEU PRO ASP ALA LYS LYS VAL THR TYR          
SEQRES  11 A  175  ARG ILE ASN PHE LYS ARG VAL ILE MET ARG LYS LEU ILE          
SEQRES  12 A  175  MET GLY VAL ALA ASP GLY GLU VAL LEU VAL ASP GLY LYS          
SEQRES  13 A  175  VAL ILE TYR THR ALA THR ASP LEU LYS VAL GLY LEU PHE          
SEQRES  14 A  175  LYS ASP THR ASN ALA PHE                                      
SEQRES   1 B  175  SER ASN ALA MET VAL ASP LYS ARG GLU SER TYR THR LYS          
SEQRES   2 B  175  GLU ASP LEU GLU ALA SER GLY ARG GLY GLU LEU PHE GLY          
SEQRES   3 B  175  ALA GLY GLY PRO PRO LEU PRO ALA GLY ASN MET LEU MET          
SEQRES   4 B  175  MET ASP ARG ILE VAL LYS MET ILE GLU ASP GLY GLY SER          
SEQRES   5 B  175  HIS ASN LYS GLY TYR VAL GLU ALA GLU LEU ASP ILE ASN          
SEQRES   6 B  175  PRO ASP LEU TRP PHE PHE GLY CYS HIS PHE ILE GLY ASP          
SEQRES   7 B  175  PRO VAL MET PRO GLY CYS LEU GLY LEU ASP ALA MET TRP          
SEQRES   8 B  175  GLN LEU VAL GLY PHE TYR LEU GLY TRP LEU GLY GLY GLU          
SEQRES   9 B  175  GLY LYS GLY ARG ALA LEU GLY VAL GLY GLU VAL LYS PHE          
SEQRES  10 B  175  THR GLY GLN VAL LEU PRO ASP ALA LYS LYS VAL THR TYR          
SEQRES  11 B  175  ARG ILE ASN PHE LYS ARG VAL ILE MET ARG LYS LEU ILE          
SEQRES  12 B  175  MET GLY VAL ALA ASP GLY GLU VAL LEU VAL ASP GLY LYS          
SEQRES  13 B  175  VAL ILE TYR THR ALA THR ASP LEU LYS VAL GLY LEU PHE          
SEQRES  14 B  175  LYS ASP THR ASN ALA PHE                                      
HET    MES  A 175      12                                                       
HET    MES  A 173      24                                                       
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
FORMUL   3  MES    2(C6 H13 N O4 S)                                             
FORMUL   5  HOH   *434(H2 O)                                                    
HELIX    1   1 THR A    9  ARG A   18  1                                  10    
HELIX    2   2 ALA A   31  LEU A   35  5                                   5    
HELIX    3   3 LEU A   65  HIS A   71  1                                   7    
HELIX    4   4 PRO A   79  LEU A   98  1                                  20    
HELIX    5   5 THR B    9  ARG B   18  1                                  10    
HELIX    6   6 ALA B   31  LEU B   35  5                                   5    
HELIX    7   7 LEU B   65  HIS B   71  1                                   7    
HELIX    8   8 PRO B   79  LEU B   98  1                                  20    
SHEET    1   A12 ARG A  39  ILE A  44  0                                        
SHEET    2   A12 TYR A  54  ASP A  60 -1  O  TYR A  54   N  ILE A  44           
SHEET    3   A12 LYS A 124  ILE A 135 -1  O  ILE A 129   N  VAL A  55           
SHEET    4   A12 MET A 141  VAL A 150 -1  O  MET A 141   N  ILE A 135           
SHEET    5   A12 LYS A 153  PHE A 166 -1  O  ILE A 155   N  VAL A 148           
SHEET    6   A12 LYS A 103  VAL A 109 -1  N  LEU A 107   O  LYS A 162           
SHEET    7   A12 VAL B 112  PHE B 114 -1  O  VAL B 112   N  VAL A 109           
SHEET    8   A12 LYS B 153  PHE B 166 -1  O  THR B 157   N  LYS B 113           
SHEET    9   A12 ILE B 140  VAL B 150 -1  N  VAL B 148   O  ILE B 155           
SHEET   10   A12 LYS B 124  MET B 136 -1  N  LYS B 132   O  VAL B 143           
SHEET   11   A12 TYR B  54  ASP B  60 -1  N  LEU B  59   O  VAL B 125           
SHEET   12   A12 ARG B  39  ILE B  44 -1  N  LYS B  42   O  GLU B  56           
SHEET    1   B12 ARG A  39  ILE A  44  0                                        
SHEET    2   B12 TYR A  54  ASP A  60 -1  O  TYR A  54   N  ILE A  44           
SHEET    3   B12 LYS A 124  ILE A 135 -1  O  ILE A 129   N  VAL A  55           
SHEET    4   B12 MET A 141  VAL A 150 -1  O  MET A 141   N  ILE A 135           
SHEET    5   B12 LYS A 153  PHE A 166 -1  O  ILE A 155   N  VAL A 148           
SHEET    6   B12 VAL A 112  PHE A 114 -1  N  LYS A 113   O  THR A 157           
SHEET    7   B12 LYS B 103  VAL B 109 -1  O  VAL B 109   N  VAL A 112           
SHEET    8   B12 LYS B 153  PHE B 166 -1  O  LYS B 162   N  LEU B 107           
SHEET    9   B12 ILE B 140  VAL B 150 -1  N  VAL B 148   O  ILE B 155           
SHEET   10   B12 LYS B 124  MET B 136 -1  N  LYS B 132   O  VAL B 143           
SHEET   11   B12 TYR B  54  ASP B  60 -1  N  LEU B  59   O  VAL B 125           
SHEET   12   B12 ARG B  39  ILE B  44 -1  N  LYS B  42   O  GLU B  56           
CISPEP   1 HIS A   71    PHE A   72          0        -6.48                     
CISPEP   2 HIS B   71    PHE B   72          0        -6.64                     
SITE     1 AC1  5 GLY A 116  GLN A 117  HOH A 218  HOH A 249                    
SITE     2 AC1  5 LEU B 107                                                     
SITE     1 AC2  9 ARG A 105  LEU A 107  PHE A 166  ASP A 168                    
SITE     2 AC2  9 THR A 169  HOH A 187  PHE B 114  GLY B 116                    
SITE     3 AC2  9 GLN B 117                                                     
CRYST1   42.433   50.668  132.384  90.00  90.00  90.00 P 21 21 21    8          
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      0.023567  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.019736  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007554        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system