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Database: PDB
Entry: 1LUR
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Original site: 1LUR 
HEADER    ISOMERASE                               23-MAY-02   1LUR              
TITLE     CRYSTAL STRUCTURE OF THE GALM/ALDOSE EPIMERASE HOMOLOGUE              
TITLE    2 FROM C. ELEGANS, NORTHEAST STRUCTURAL GENOMICS TARGET WR66           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALDOSE 1-EPIMERASE;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 5.1.3.3;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: NESG WR66                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;                         
SOURCE   3 ORGANISM_TAXID: 6239;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET14C                                    
KEYWDS    VITAMIN B12, METHYLTRANSFERASE, STRUCTURAL GENOMICS,                  
KEYWDS   2 STRUCTURE-BASED FUNCTION ASSIGNMENT, DECARBOXYLASE, PSI,             
KEYWDS   3 PROTEIN STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS          
KEYWDS   4 CONSORTIUM, NESG, ISOMERASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.P.KELLER,R.XIAO,L.MACDONALD,J.SHEN,T.ACTON,G.MONTELIONE,            
AUTHOR   2 J.F.HUNT,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)             
REVDAT   3   24-FEB-09 1LUR    1       VERSN                                    
REVDAT   2   25-JAN-05 1LUR    1       AUTHOR KEYWDS REMARK                     
REVDAT   1   29-JUL-03 1LUR    0                                                
JRNL        AUTH   J.P.KELLER,R.XIAO,L.MACDONALD,J.SHEN,T.ACTON,                
JRNL        AUTH 2 G.MONTELIONE,J.F.HUNT                                        
JRNL        TITL   CRYSTAL STRUCTURE OF THE GALM/ALDOSE EPIMERASE               
JRNL        TITL 2 HOMOLOGUE FROM C. ELEGANS, NORTHEAST STRUCTURAL              
JRNL        TITL 3 GENOMICS TARGET WR66                                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 60770                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : 5%                              
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 3006                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5096                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 398                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.51                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1LUR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUN-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB016291.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 3                                  
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                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : YALE MIRRORS                       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 131853                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -5.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY                : 3.360                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.3500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: CNS 1.1                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 600, LITHIUM SULFATE, TRISCL,        
REMARK 280  PEG 4000, GLYCEROL, PH 8.2, VAPOR DIFFUSION, HANGING DROP,          
REMARK 280  TEMPERATURE 294K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       45.50350            
REMARK 290   SMTRY3   2  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 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: MONOMERIC                         
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 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     MSE A   992                                                      
REMARK 465     SER A   993                                                      
REMARK 465     HIS A   994                                                      
REMARK 465     HIS A   995                                                      
REMARK 465     HIS A   996                                                      
REMARK 465     HIS A   997                                                      
REMARK 465     HIS A   998                                                      
REMARK 465     HIS A   999                                                      
REMARK 465     SER A  1000                                                      
REMARK 465     MSE A  1001                                                      
REMARK 465     PRO A  1240                                                      
REMARK 465     SER A  1241                                                      
REMARK 465     THR A  1242                                                      
REMARK 465     PRO A  1243                                                      
REMARK 465     MSE B  1992                                                      
REMARK 465     SER B  1993                                                      
REMARK 465     HIS B  1994                                                      
REMARK 465     HIS B  1995                                                      
REMARK 465     HIS B  1996                                                      
REMARK 465     HIS B  1997                                                      
REMARK 465     HIS B  1998                                                      
REMARK 465     HIS B  1999                                                      
REMARK 465     SER B  2000                                                      
REMARK 465     MSE B  2001                                                      
REMARK 465     PRO B  2240                                                      
REMARK 465     SER B  2241                                                      
REMARK 465     THR B  2242                                                      
REMARK 465     PRO B  2243                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     SER A 1218                                                       
REMARK 475     GLY A 1219                                                       
REMARK 475     LYS A 1220                                                       
REMARK 475     ASP A 1221                                                       
REMARK 475     ALA A 1222                                                       
REMARK 475     GLU A 1223                                                       
REMARK 475     GLU A 1224                                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    THR B2060   N   -  CA  -  C   ANGL. DEV. = -16.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A1003     -143.85   -118.71                                   
REMARK 500    ASN A1010     -164.67   -101.23                                   
REMARK 500    ASN A1066     -148.78     69.35                                   
REMARK 500    ALA A1130      146.94   -175.21                                   
REMARK 500    HIS A1163       40.63   -101.93                                   
REMARK 500    SER A1218       72.43   -150.10                                   
REMARK 500    ASP A1227       34.15    -98.93                                   
REMARK 500    ASP A1229       59.51    176.11                                   
REMARK 500    LYS A1237     -167.97    -74.94                                   
REMARK 500    THR A1238      -50.13   -149.90                                   
REMARK 500    ALA A1271       13.51    -68.59                                   
REMARK 500    ASP A1276       82.22   -176.89                                   
REMARK 500    ASN B2010     -168.59   -105.63                                   
REMARK 500    ASN B2066     -151.37     64.45                                   
REMARK 500    ASN B2070       19.01     59.77                                   
REMARK 500    ALA B2222      132.10     62.77                                   
REMARK 500    ASP B2229       55.69   -169.01                                   
REMARK 500    ALA B2271       32.48    -77.28                                   
REMARK 500    ASP B2276       99.14   -167.53                                   
REMARK 500    LYS B2286     -168.20   -116.50                                   
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 SO4 A 4001                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 4002                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: WR66   RELATED DB: TARGETDB                              
DBREF  1LUR A 1001  1330  UNP    Q966D4   Q966D4_CAEEL     1    330             
DBREF  1LUR B 2001  2330  UNP    Q966D4   Q966D4_CAEEL     1    330             
SEQADV 1LUR MSE A  992  UNP  Q966D4              EXPRESSION TAG                 
SEQADV 1LUR SER A  993  UNP  Q966D4              EXPRESSION TAG                 
SEQADV 1LUR HIS A  994  UNP  Q966D4              EXPRESSION TAG                 
SEQADV 1LUR HIS A  995  UNP  Q966D4              EXPRESSION TAG                 
SEQADV 1LUR HIS A  996  UNP  Q966D4              EXPRESSION TAG                 
SEQADV 1LUR HIS A  997  UNP  Q966D4              EXPRESSION TAG                 
SEQADV 1LUR HIS A  998  UNP  Q966D4              EXPRESSION TAG                 
SEQADV 1LUR HIS A  999  UNP  Q966D4              EXPRESSION TAG                 
SEQADV 1LUR SER A 1000  UNP  Q966D4              EXPRESSION TAG                 
SEQADV 1LUR MSE A 1001  UNP  Q966D4    MET     1 MODIFIED RESIDUE               
SEQADV 1LUR MSE A 1082  UNP  Q966D4    MET    82 MODIFIED RESIDUE               
SEQADV 1LUR MSE A 1181  UNP  Q966D4    MET   181 MODIFIED RESIDUE               
SEQADV 1LUR MSE B 1992  UNP  Q966D4              EXPRESSION TAG                 
SEQADV 1LUR SER B 1993  UNP  Q966D4              EXPRESSION TAG                 
SEQADV 1LUR HIS B 1994  UNP  Q966D4              EXPRESSION TAG                 
SEQADV 1LUR HIS B 1995  UNP  Q966D4              EXPRESSION TAG                 
SEQADV 1LUR HIS B 1996  UNP  Q966D4              EXPRESSION TAG                 
SEQADV 1LUR HIS B 1997  UNP  Q966D4              EXPRESSION TAG                 
SEQADV 1LUR HIS B 1998  UNP  Q966D4              EXPRESSION TAG                 
SEQADV 1LUR HIS B 1999  UNP  Q966D4              EXPRESSION TAG                 
SEQADV 1LUR SER B 2000  UNP  Q966D4              EXPRESSION TAG                 
SEQADV 1LUR MSE B 2001  UNP  Q966D4    MET     1 MODIFIED RESIDUE               
SEQADV 1LUR MSE B 2082  UNP  Q966D4    MET    82 MODIFIED RESIDUE               
SEQADV 1LUR MSE B 2181  UNP  Q966D4    MET   181 MODIFIED RESIDUE               
SEQRES   1 A  339  MSE SER HIS HIS HIS HIS HIS HIS SER MSE ALA SER GLY          
SEQRES   2 A  339  PHE ILE GLU ILE ALA ASN LYS GLN GLY LEU THR ALA THR          
SEQRES   3 A  339  LEU LEU PRO PHE GLY ALA THR LEU ALA LYS LEU THR PHE          
SEQRES   4 A  339  PRO ASP LYS ASN GLY LYS ASN GLN ASP LEU VAL LEU GLY          
SEQRES   5 A  339  PHE ASP THR ILE ASP GLU PHE GLU LYS ASP ALA ALA SER          
SEQRES   6 A  339  ILE GLY LYS THR VAL GLY ARG VAL ALA ASN ARG ILE LYS          
SEQRES   7 A  339  ASN SER THR LEU HIS PHE ASP GLY LYS GLN TYR THR MSE          
SEQRES   8 A  339  THR PRO ASN ASN GLY PRO HIS TYR LEU HIS GLY GLY PRO          
SEQRES   9 A  339  ASN GLY LEU GLY TYR ARG LYS TRP GLU VAL VAL ARG HIS          
SEQRES  10 A  339  ALA PRO GLU SER VAL SER PHE SER VAL ARG ALA ASN GLU          
SEQRES  11 A  339  GLN ASP ASP GLY LEU PRO GLY ASP ALA LYS ILE ASP VAL          
SEQRES  12 A  339  THR TYR THR VAL ASN ASP ARG ASN GLN LEU ILE ILE GLU          
SEQRES  13 A  339  HIS HIS ALA THR CYS ASP THR PRO GLY LEU LEU ALA LEU          
SEQRES  14 A  339  THR ASN HIS ALA TYR TRP ASN LEU ASP GLY SER ASP THR          
SEQRES  15 A  339  VAL ALA GLU HIS PHE LEU GLU MSE GLU ALA ASP GLU PHE          
SEQRES  16 A  339  VAL GLU VAL ASP ASP THR PHE CYS PRO THR GLY ALA ILE          
SEQRES  17 A  339  ARG SER VAL THR ASP THR GLY PHE ASP PHE ARG SER GLY          
SEQRES  18 A  339  LYS GLN LEU LYS GLU SER GLY LYS ASP ALA GLU GLU LEU          
SEQRES  19 A  339  LEU ASP LEU ASP ASN ASP LEU VAL ILE THR LYS LYS THR          
SEQRES  20 A  339  PRO PRO SER THR PRO SER THR TYR LEU ARG PHE TRP SER          
SEQRES  21 A  339  GLU LYS SER GLY ILE GLU LEU SER ILE THR THR SER TYR          
SEQRES  22 A  339  PRO VAL ILE HIS LEU TYR ALA SER LYS PHE LEU ASP CYS          
SEQRES  23 A  339  LYS GLY LYS LYS GLY GLU HIS TYR LYS ALA ASN LYS ALA          
SEQRES  24 A  339  LEU ALA ILE GLU PRO GLN PHE HIS SER ALA ALA PRO ASN          
SEQRES  25 A  339  PHE ASP HIS PHE PRO ASP VAL SER LEU ARG PRO GLY ASP          
SEQRES  26 A  339  HIS TYR CYS GLN GLU ILE VAL TYR THR PHE SER HIS VAL          
SEQRES  27 A  339  ASN                                                          
SEQRES   1 B  339  MSE SER HIS HIS HIS HIS HIS HIS SER MSE ALA SER GLY          
SEQRES   2 B  339  PHE ILE GLU ILE ALA ASN LYS GLN GLY LEU THR ALA THR          
SEQRES   3 B  339  LEU LEU PRO PHE GLY ALA THR LEU ALA LYS LEU THR PHE          
SEQRES   4 B  339  PRO ASP LYS ASN GLY LYS ASN GLN ASP LEU VAL LEU GLY          
SEQRES   5 B  339  PHE ASP THR ILE ASP GLU PHE GLU LYS ASP ALA ALA SER          
SEQRES   6 B  339  ILE GLY LYS THR VAL GLY ARG VAL ALA ASN ARG ILE LYS          
SEQRES   7 B  339  ASN SER THR LEU HIS PHE ASP GLY LYS GLN TYR THR MSE          
SEQRES   8 B  339  THR PRO ASN ASN GLY PRO HIS TYR LEU HIS GLY GLY PRO          
SEQRES   9 B  339  ASN GLY LEU GLY TYR ARG LYS TRP GLU VAL VAL ARG HIS          
SEQRES  10 B  339  ALA PRO GLU SER VAL SER PHE SER VAL ARG ALA ASN GLU          
SEQRES  11 B  339  GLN ASP ASP GLY LEU PRO GLY ASP ALA LYS ILE ASP VAL          
SEQRES  12 B  339  THR TYR THR VAL ASN ASP ARG ASN GLN LEU ILE ILE GLU          
SEQRES  13 B  339  HIS HIS ALA THR CYS ASP THR PRO GLY LEU LEU ALA LEU          
SEQRES  14 B  339  THR ASN HIS ALA TYR TRP ASN LEU ASP GLY SER ASP THR          
SEQRES  15 B  339  VAL ALA GLU HIS PHE LEU GLU MSE GLU ALA ASP GLU PHE          
SEQRES  16 B  339  VAL GLU VAL ASP ASP THR PHE CYS PRO THR GLY ALA ILE          
SEQRES  17 B  339  ARG SER VAL THR ASP THR GLY PHE ASP PHE ARG SER GLY          
SEQRES  18 B  339  LYS GLN LEU LYS GLU SER GLY LYS ASP ALA GLU GLU LEU          
SEQRES  19 B  339  LEU ASP LEU ASP ASN ASP LEU VAL ILE THR LYS LYS THR          
SEQRES  20 B  339  PRO PRO SER THR PRO SER THR TYR LEU ARG PHE TRP SER          
SEQRES  21 B  339  GLU LYS SER GLY ILE GLU LEU SER ILE THR THR SER TYR          
SEQRES  22 B  339  PRO VAL ILE HIS LEU TYR ALA SER LYS PHE LEU ASP CYS          
SEQRES  23 B  339  LYS GLY LYS LYS GLY GLU HIS TYR LYS ALA ASN LYS ALA          
SEQRES  24 B  339  LEU ALA ILE GLU PRO GLN PHE HIS SER ALA ALA PRO ASN          
SEQRES  25 B  339  PHE ASP HIS PHE PRO ASP VAL SER LEU ARG PRO GLY ASP          
SEQRES  26 B  339  HIS TYR CYS GLN GLU ILE VAL TYR THR PHE SER HIS VAL          
SEQRES  27 B  339  ASN                                                          
MODRES 1LUR MSE A 1082  MET  SELENOMETHIONINE                                   
MODRES 1LUR MSE A 1181  MET  SELENOMETHIONINE                                   
MODRES 1LUR MSE B 2082  MET  SELENOMETHIONINE                                   
MODRES 1LUR MSE B 2181  MET  SELENOMETHIONINE                                   
HET    MSE  A1082       8                                                       
HET    MSE  A1181       8                                                       
HET    MSE  B2082       8                                                       
HET    MSE  B2181       8                                                       
HET    SO4  A4001       5                                                       
HET    SO4  B4002       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    4(C5 H11 N O2 SE)                                            
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  HOH   *398(H2 O)                                                    
HELIX    1   1 PRO A 1020  ALA A 1023  5                                   4    
HELIX    2   2 THR A 1046  ASP A 1053  1                                   8    
HELIX    3   3 GLY A 1097  ARG A 1101  5                                   5    
HELIX    4   4 GLU A 1121  GLY A 1125  1                                   5    
HELIX    5   5 LYS A 1280  GLY A 1282  5                                   3    
HELIX    6   6 ALA A 1300  PHE A 1304  5                                   5    
HELIX    7   7 PRO B 2020  ALA B 2023  5                                   4    
HELIX    8   8 THR B 2046  ASP B 2053  1                                   8    
HELIX    9   9 GLY B 2097  ARG B 2101  5                                   5    
HELIX   10  10 GLU B 2121  GLY B 2125  1                                   5    
HELIX   11  11 LYS B 2216  GLY B 2219  5                                   4    
HELIX   12  12 LYS B 2280  GLY B 2282  5                                   3    
HELIX   13  13 ALA B 2300  PHE B 2304  5                                   5    
SHEET    1   A 4 ILE A1006  ALA A1009  0                                        
SHEET    2   A 4 THR A1015  LEU A1019 -1  O  LEU A1018   N  ILE A1006           
SHEET    3   A 4 THR A1024  PRO A1031 -1  O  LYS A1027   N  THR A1017           
SHEET    4   A 4 ASN A1037  ASP A1039 -1  O  GLN A1038   N  PHE A1030           
SHEET    1   B 2 THR A1060  VAL A1061  0                                        
SHEET    2   B 2 THR A1161  ASN A1162 -1  O  THR A1161   N  VAL A1061           
SHEET    1   C 2 ARG A1067  ILE A1068  0                                        
SHEET    2   C 2 TYR A1090  LEU A1091 -1  N  TYR A1090   O  ILE A1068           
SHEET    1   D 2 THR A1072  PHE A1075  0                                        
SHEET    2   D 2 LYS A1078  THR A1081 -1  O  LYS A1078   N  PHE A1075           
SHEET    1   E 9 GLU A1104  ALA A1109  0                                        
SHEET    2   E 9 SER A1112  ASN A1120 -1  O  SER A1116   N  GLU A1104           
SHEET    3   E 9 ASP A1129  VAL A1138 -1  O  ILE A1132   N  VAL A1117           
SHEET    4   E 9 GLN A1143  THR A1151 -1  O  ILE A1145   N  THR A1137           
SHEET    5   E 9 TYR A1318  HIS A1328 -1  O  TYR A1324   N  LEU A1144           
SHEET    6   E 9 ILE A1256  THR A1262 -1  N  THR A1261   O  VAL A1323           
SHEET    7   E 9 LEU A1247  TRP A1250 -1  N  PHE A1249   O  LEU A1258           
SHEET    8   E 9 PHE A1178  MSE A1181 -1  N  PHE A1178   O  TRP A1250           
SHEET    9   E 9 LYS A1213  GLN A1214 -1  O  LYS A1213   N  LEU A1179           
SHEET    1   F 2 GLY A1156  LEU A1157  0                                        
SHEET    2   F 2 SER A1311  LEU A1312 -1  O  LEU A1312   N  GLY A1156           
SHEET    1   G 6 TYR A1165  TRP A1166  0                                        
SHEET    2   G 6 LEU A1291  GLN A1296 -1  O  LEU A1291   N  TRP A1166           
SHEET    3   G 6 VAL A1266  TYR A1270 -1  N  HIS A1268   O  GLU A1294           
SHEET    4   G 6 ASP A1229  ILE A1234 -1  N  ASN A1230   O  LEU A1269           
SHEET    5   G 6 ALA A1183  VAL A1189 -1  N  GLU A1185   O  VAL A1233           
SHEET    6   G 6 PRO A1195  SER A1201 -1  O  ARG A1200   N  PHE A1186           
SHEET    1   H 2 CYS A1277  LYS A1278  0                                        
SHEET    2   H 2 HIS A1284  TYR A1285 -1  O  TYR A1285   N  CYS A1277           
SHEET    1   I 4 ILE B2006  ALA B2009  0                                        
SHEET    2   I 4 THR B2015  LEU B2019 -1  O  LEU B2018   N  ILE B2006           
SHEET    3   I 4 THR B2024  PRO B2031 -1  O  THR B2029   N  THR B2015           
SHEET    4   I 4 ASN B2037  ASP B2039 -1  O  GLN B2038   N  PHE B2030           
SHEET    1   J 2 THR B2060  VAL B2061  0                                        
SHEET    2   J 2 THR B2161  ASN B2162 -1  O  THR B2161   N  VAL B2061           
SHEET    1   K 2 ARG B2067  ILE B2068  0                                        
SHEET    2   K 2 TYR B2090  LEU B2091 -1  N  TYR B2090   O  ILE B2068           
SHEET    1   L 2 THR B2072  PHE B2075  0                                        
SHEET    2   L 2 LYS B2078  THR B2081 -1  O  TYR B2080   N  LEU B2073           
SHEET    1   M 9 GLU B2104  ALA B2109  0                                        
SHEET    2   M 9 SER B2112  ASN B2120 -1  O  SER B2112   N  ALA B2109           
SHEET    3   M 9 ASP B2129  VAL B2138 -1  O  VAL B2134   N  PHE B2115           
SHEET    4   M 9 GLN B2143  THR B2151 -1  O  ILE B2145   N  THR B2137           
SHEET    5   M 9 TYR B2318  HIS B2328 -1  O  TYR B2324   N  LEU B2144           
SHEET    6   M 9 ILE B2256  THR B2262 -1  N  SER B2259   O  THR B2325           
SHEET    7   M 9 LEU B2247  TRP B2250 -1  N  PHE B2249   O  LEU B2258           
SHEET    8   M 9 PHE B2178  MSE B2181 -1  N  PHE B2178   O  TRP B2250           
SHEET    9   M 9 LYS B2213  GLN B2214 -1  O  LYS B2213   N  LEU B2179           
SHEET    1   N 2 GLY B2156  LEU B2157  0                                        
SHEET    2   N 2 SER B2311  LEU B2312 -1  O  LEU B2312   N  GLY B2156           
SHEET    1   O 6 TYR B2165  TRP B2166  0                                        
SHEET    2   O 6 LEU B2291  GLN B2296 -1  O  LEU B2291   N  TRP B2166           
SHEET    3   O 6 VAL B2266  TYR B2270 -1  N  HIS B2268   O  GLU B2294           
SHEET    4   O 6 ASP B2229  ILE B2234 -1  N  ASN B2230   O  LEU B2269           
SHEET    5   O 6 ALA B2183  VAL B2189 -1  N  VAL B2187   O  ASP B2231           
SHEET    6   O 6 PRO B2195  SER B2201 -1  O  ARG B2200   N  PHE B2186           
SHEET    1   P 2 CYS B2277  LYS B2278  0                                        
SHEET    2   P 2 HIS B2284  TYR B2285 -1  O  TYR B2285   N  CYS B2277           
LINK         C   THR A1081                 N   MSE A1082     1555   1555  1.33  
LINK         C   MSE A1082                 N   THR A1083     1555   1555  1.33  
LINK         C   GLU A1180                 N   MSE A1181     1555   1555  1.33  
LINK         C   MSE A1181                 N   GLU A1182     1555   1555  1.33  
LINK         C   THR B2081                 N   MSE B2082     1555   1555  1.33  
LINK         C   MSE B2082                 N   THR B2083     1555   1555  1.33  
LINK         C   GLU B2180                 N   MSE B2181     1555   1555  1.33  
LINK         C   MSE B2181                 N   GLU B2182     1555   1555  1.33  
CISPEP   1 GLY A 1062    ARG A 1063          0         0.35                     
CISPEP   2 GLY B 2062    ARG B 2063          0         0.25                     
SITE     1 AC1  1 LYS A1273                                                     
SITE     1 AC2  6 THR B2072  HIS B2074  ASN B2303  HOH B3030                    
SITE     2 AC2  6 HOH B3209  HOH B3337                                          
CRYST1   50.808   91.007   83.701  90.00 100.67  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019682  0.000000  0.003708        0.00000                         
SCALE2      0.000000  0.010988  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012157        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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