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Database: PDB
Entry: 3R23
LinkDB: 3R23
Original site: 3R23 
HEADER    LIGASE                                  12-MAR-11   3R23              
TITLE     CRYSTAL STRUCTURE OF D-ALANINE--D-ALANINE LIGASE FROM BACILLUS        
TITLE    2 ANTHRACIS                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: D-ALA-D-ALA LIGASE, D-ALANYLALANINE SYNTHETASE;             
COMPND   5 EC: 6.3.2.4;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;                             
SOURCE   3 ORGANISM_COMMON: ANTHRAX,ANTHRAX BACTERIUM;                          
SOURCE   4 ORGANISM_TAXID: 198094;                                              
SOURCE   5 STRAIN: AMES;                                                        
SOURCE   6 GENE: BAS2435, BA_2610, DDL, DDLB, GBAA_2610;                        
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 MAGIC;                                
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PMCSG7                                    
KEYWDS    STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS     
KEYWDS   2 DISEASES, CSGID, ALPHA-BETA STRUCTURE, LIGASE, CYTOSOL               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.KIM,R.MULLIGAN,J.HASSEMAN,W.F.ANDERSON,A.JOACHIMIAK,CENTER FOR      
AUTHOR   2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)                   
REVDAT   2   06-APR-11 3R23    1       AUTHOR                                   
REVDAT   1   30-MAR-11 3R23    0                                                
JRNL        AUTH   Y.KIM,R.MULLIGAN,J.HASSEMAN,W.F.ANDERSON,A.JOACHIMIAK,       
JRNL        AUTH 2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES        
JRNL        AUTH 3 (CSGID)                                                      
JRNL        TITL   CRYSTAL STRUCTURE OF D-ALANINE--D-ALANINE LIGASE FROM        
JRNL        TITL 2 BACILLUS ANTHRACIS                                           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
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 : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.24                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 24525                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.150                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
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 40.2434 -  5.3651    0.99     2445   217  0.2044 0.2594        
REMARK   3     2  5.3651 -  4.2599    0.99     2353   210  0.1493 0.1868        
REMARK   3     3  4.2599 -  3.7219    0.99     2327   206  0.1513 0.2053        
REMARK   3     4  3.7219 -  3.3818    0.99     2285   202  0.1982 0.2686        
REMARK   3     5  3.3818 -  3.1395    0.98     2248   200  0.2128 0.2949        
REMARK   3     6  3.1395 -  2.9545    0.97     2253   200  0.2148 0.2783        
REMARK   3     7  2.9545 -  2.8065    0.96     2203   196  0.2159 0.3163        
REMARK   3     8  2.8065 -  2.6844    0.96     2188   194  0.2284 0.3297        
REMARK   3     9  2.6844 -  2.5811    0.94     2155   191  0.2346 0.3080        
REMARK   3    10  2.5811 -  2.4920    0.90     2068   184  0.2228 0.3376        
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              : 0.29                                          
REMARK   3   B_SOL              : 20.11                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.600           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.17                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 16.49710                                             
REMARK   3    B22 (A**2) : 8.36930                                              
REMARK   3    B33 (A**2) : 7.67160                                              
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      :  0.012           4826                                  
REMARK   3   ANGLE     :  1.518           6500                                  
REMARK   3   CHIRALITY :  0.103            746                                  
REMARK   3   PLANARITY :  0.008            825                                  
REMARK   3   DIHEDRAL  : 16.891           1846                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  25.1696  36.8127  66.3870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0209 T22:   0.0958                                     
REMARK   3      T33:   0.0835 T12:  -0.0302                                     
REMARK   3      T13:   0.0109 T23:  -0.0172                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0067 L22:   0.1432                                     
REMARK   3      L33:   0.0889 L12:  -0.0016                                     
REMARK   3      L13:   0.0031 L23:   0.1077                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0175 S12:   0.0243 S13:  -0.0187                       
REMARK   3      S21:  -0.0447 S22:  -0.0522 S23:   0.1368                       
REMARK   3      S31:  -0.0535 S32:  -0.0381 S33:   0.0301                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2806  50.9485  91.3041              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1773 T22:   0.0249                                     
REMARK   3      T33:   0.1026 T12:   0.0134                                     
REMARK   3      T13:   0.1478 T23:  -0.1217                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0518 L22:   0.0097                                     
REMARK   3      L33:   0.0542 L12:  -0.0274                                     
REMARK   3      L13:   0.0053 L23:   0.0018                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0230 S12:  -0.0240 S13:  -0.0267                       
REMARK   3      S21:   0.0420 S22:   0.0148 S23:   0.0141                       
REMARK   3      S31:  -0.1429 S32:   0.0110 S33:  -0.0189                       
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 3R23 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB064391.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25302                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
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     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 44.900                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.15700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.81700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.040                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: HKL3000, PHENIX                                       
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 20% W/V POLYETHYLENE     
REMARK 280  GLYCOL MONOMETHYL ETHER 5,000, VAPOR DIFFUSION, SITTING DROP,       
REMARK 280  TEMPERATURE 100K, PH 6.5, 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       32.93900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.19000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.59350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.19000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.93900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.59350            
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: 3110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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     SER A    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     PHE A   304                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     GLY B   141                                                      
REMARK 465     SER B   142                                                      
REMARK 465     SER B   143                                                      
REMARK 465     VAL B   144                                                      
REMARK 465     PHE B   304                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP B 151    CG   OD1  OD2                                       
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 A  11     -127.54     46.03                                   
REMARK 500    LEU A 121       73.22     62.64                                   
REMARK 500    SER A 143      -70.79    -51.06                                   
REMARK 500    VAL A 243      -32.47     72.15                                   
REMARK 500    TYR A 244      156.72    179.26                                   
REMARK 500    SER B  11     -124.31     60.05                                   
REMARK 500    VAL B 243      -29.91     72.21                                   
REMARK 500    TYR B 244      156.51    174.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    VAL A 243        -10.98                                           
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 EDO A 311                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 312                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 311                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 312                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: IDP01207   RELATED DB: TARGETDB                          
DBREF  3R23 A    1   304  UNP    Q81Q29   DDL_BACAN        1    304             
DBREF  3R23 B    1   304  UNP    Q81Q29   DDL_BACAN        1    304             
SEQADV 3R23 SER A   -2  UNP  Q81Q29              EXPRESSION TAG                 
SEQADV 3R23 ASN A   -1  UNP  Q81Q29              EXPRESSION TAG                 
SEQADV 3R23 ALA A    0  UNP  Q81Q29              EXPRESSION TAG                 
SEQADV 3R23 SER B   -2  UNP  Q81Q29              EXPRESSION TAG                 
SEQADV 3R23 ASN B   -1  UNP  Q81Q29              EXPRESSION TAG                 
SEQADV 3R23 ALA B    0  UNP  Q81Q29              EXPRESSION TAG                 
SEQRES   1 A  307  SER ASN ALA MSE ARG ILE GLY VAL ILE MSE GLY GLY VAL          
SEQRES   2 A  307  SER SER GLU LYS GLN VAL SER ILE MSE THR GLY ASN GLU          
SEQRES   3 A  307  MSE ILE ALA ASN LEU ASP LYS ASN LYS TYR GLU ILE VAL          
SEQRES   4 A  307  PRO ILE THR LEU ASN GLU LYS MSE ASP LEU ILE GLU LYS          
SEQRES   5 A  307  ALA LYS ASP ILE ASP PHE ALA LEU LEU ALA LEU HIS GLY          
SEQRES   6 A  307  LYS TYR GLY GLU ASP GLY THR VAL GLN GLY THR LEU GLU          
SEQRES   7 A  307  SER LEU GLY ILE PRO TYR SER GLY SER ASN MSE LEU SER          
SEQRES   8 A  307  SER GLY ILE CYS MSE ASP LYS ASN ILE SER LYS LYS ILE          
SEQRES   9 A  307  LEU ARG TYR GLU GLY ILE GLU THR PRO ASP TRP ILE GLU          
SEQRES  10 A  307  LEU THR LYS MSE GLU ASP LEU ASN PHE ASP GLU LEU ASP          
SEQRES  11 A  307  LYS LEU GLY PHE PRO LEU VAL VAL LYS PRO ASN SER GLY          
SEQRES  12 A  307  GLY SER SER VAL GLY VAL LYS ILE VAL TYR ASP LYS ASP          
SEQRES  13 A  307  GLU LEU ILE SER MSE LEU GLU THR VAL PHE GLU TRP ASP          
SEQRES  14 A  307  SER GLU VAL VAL ILE GLU LYS TYR ILE LYS GLY GLU GLU          
SEQRES  15 A  307  ILE THR CYS SER ILE PHE ASP GLY LYS GLN LEU PRO ILE          
SEQRES  16 A  307  ILE SER ILE ARG HIS ALA ALA GLU PHE PHE ASP TYR ASN          
SEQRES  17 A  307  ALA LYS TYR ASP ASP ALA SER THR ILE GLU GLU VAL ILE          
SEQRES  18 A  307  GLU LEU PRO ALA GLU LEU LYS GLU ARG VAL ASN LYS ALA          
SEQRES  19 A  307  SER LEU ALA CYS TYR LYS ALA LEU LYS CYS SER VAL TYR          
SEQRES  20 A  307  ALA ARG VAL ASP MSE MSE VAL LYS ASP GLY ILE PRO TYR          
SEQRES  21 A  307  VAL MSE GLU VAL ASN THR LEU PRO GLY MSE THR GLN ALA          
SEQRES  22 A  307  SER LEU LEU PRO LYS SER ALA ASP ALA ALA GLY ILE HIS          
SEQRES  23 A  307  TYR SER LYS LEU LEU ASP MSE ILE ILE GLU THR SER LEU          
SEQRES  24 A  307  ARG VAL ARG LYS GLU GLU GLY PHE                              
SEQRES   1 B  307  SER ASN ALA MSE ARG ILE GLY VAL ILE MSE GLY GLY VAL          
SEQRES   2 B  307  SER SER GLU LYS GLN VAL SER ILE MSE THR GLY ASN GLU          
SEQRES   3 B  307  MSE ILE ALA ASN LEU ASP LYS ASN LYS TYR GLU ILE VAL          
SEQRES   4 B  307  PRO ILE THR LEU ASN GLU LYS MSE ASP LEU ILE GLU LYS          
SEQRES   5 B  307  ALA LYS ASP ILE ASP PHE ALA LEU LEU ALA LEU HIS GLY          
SEQRES   6 B  307  LYS TYR GLY GLU ASP GLY THR VAL GLN GLY THR LEU GLU          
SEQRES   7 B  307  SER LEU GLY ILE PRO TYR SER GLY SER ASN MSE LEU SER          
SEQRES   8 B  307  SER GLY ILE CYS MSE ASP LYS ASN ILE SER LYS LYS ILE          
SEQRES   9 B  307  LEU ARG TYR GLU GLY ILE GLU THR PRO ASP TRP ILE GLU          
SEQRES  10 B  307  LEU THR LYS MSE GLU ASP LEU ASN PHE ASP GLU LEU ASP          
SEQRES  11 B  307  LYS LEU GLY PHE PRO LEU VAL VAL LYS PRO ASN SER GLY          
SEQRES  12 B  307  GLY SER SER VAL GLY VAL LYS ILE VAL TYR ASP LYS ASP          
SEQRES  13 B  307  GLU LEU ILE SER MSE LEU GLU THR VAL PHE GLU TRP ASP          
SEQRES  14 B  307  SER GLU VAL VAL ILE GLU LYS TYR ILE LYS GLY GLU GLU          
SEQRES  15 B  307  ILE THR CYS SER ILE PHE ASP GLY LYS GLN LEU PRO ILE          
SEQRES  16 B  307  ILE SER ILE ARG HIS ALA ALA GLU PHE PHE ASP TYR ASN          
SEQRES  17 B  307  ALA LYS TYR ASP ASP ALA SER THR ILE GLU GLU VAL ILE          
SEQRES  18 B  307  GLU LEU PRO ALA GLU LEU LYS GLU ARG VAL ASN LYS ALA          
SEQRES  19 B  307  SER LEU ALA CYS TYR LYS ALA LEU LYS CYS SER VAL TYR          
SEQRES  20 B  307  ALA ARG VAL ASP MSE MSE VAL LYS ASP GLY ILE PRO TYR          
SEQRES  21 B  307  VAL MSE GLU VAL ASN THR LEU PRO GLY MSE THR GLN ALA          
SEQRES  22 B  307  SER LEU LEU PRO LYS SER ALA ASP ALA ALA GLY ILE HIS          
SEQRES  23 B  307  TYR SER LYS LEU LEU ASP MSE ILE ILE GLU THR SER LEU          
SEQRES  24 B  307  ARG VAL ARG LYS GLU GLU GLY PHE                              
MODRES 3R23 MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE A    7  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE A   19  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE A   24  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE A   44  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE A   86  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE A   93  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE A  118  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE A  158  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE A  249  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE A  250  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE A  259  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE A  267  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE A  290  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE B    7  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE B   19  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE B   24  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE B   44  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE B   86  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE B   93  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE B  118  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE B  158  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE B  249  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE B  250  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE B  259  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE B  267  MET  SELENOMETHIONINE                                   
MODRES 3R23 MSE B  290  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A   7       8                                                       
HET    MSE  A  19       8                                                       
HET    MSE  A  24       8                                                       
HET    MSE  A  44       8                                                       
HET    MSE  A  86       8                                                       
HET    MSE  A  93       8                                                       
HET    MSE  A 118       8                                                       
HET    MSE  A 158       8                                                       
HET    MSE  A 249       8                                                       
HET    MSE  A 250       8                                                       
HET    MSE  A 259       8                                                       
HET    MSE  A 267       8                                                       
HET    MSE  A 290       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B   7       8                                                       
HET    MSE  B  19       8                                                       
HET    MSE  B  24       8                                                       
HET    MSE  B  44       8                                                       
HET    MSE  B  86       8                                                       
HET    MSE  B  93       8                                                       
HET    MSE  B 118       8                                                       
HET    MSE  B 158       8                                                       
HET    MSE  B 249       8                                                       
HET    MSE  B 250       8                                                       
HET    MSE  B 259       8                                                       
HET    MSE  B 267       8                                                       
HET    MSE  B 290       8                                                       
HET    EDO  A 311       4                                                       
HET    EDO  A 312       4                                                       
HET    EDO  B 311       4                                                       
HET    EDO  B 312       4                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  MSE    28(C5 H11 N O2 SE)                                           
FORMUL   3  EDO    4(C2 H6 O2)                                                  
FORMUL   7  HOH   *234(H2 O)                                                    
HELIX    1   1 VAL A   10  LEU A   28  1                                  19    
HELIX    2   2 GLU A   42  MSE A   44  5                                   3    
HELIX    3   3 ASP A   45  ALA A   50  1                                   6    
HELIX    4   4 GLY A   62  ASP A   67  1                                   6    
HELIX    5   5 GLY A   68  GLY A   78  1                                  11    
HELIX    6   6 ASN A   85  MSE A   93  1                                   9    
HELIX    7   7 ASP A   94  GLU A  105  1                                  12    
HELIX    8   8 ASP A  151  GLU A  164  1                                  14    
HELIX    9   9 PRO A  221  LEU A  239  1                                  19    
HELIX   10  10 SER A  271  ALA A  280  1                                  10    
HELIX   11  11 HIS A  283  GLU A  302  1                                  20    
HELIX   12  12 VAL B   10  LEU B   28  1                                  19    
HELIX   13  13 GLU B   42  MSE B   44  5                                   3    
HELIX   14  14 ASP B   45  ALA B   50  1                                   6    
HELIX   15  15 LYS B   51  ILE B   53  5                                   3    
HELIX   16  16 GLY B   62  ASP B   67  1                                   6    
HELIX   17  17 GLY B   68  LEU B   77  1                                  10    
HELIX   18  18 ASN B   85  ASP B   94  1                                  10    
HELIX   19  19 ASP B   94  GLU B  105  1                                  12    
HELIX   20  20 ASN B  122  ASP B  127  1                                   6    
HELIX   21  21 ASP B  153  ASP B  166  1                                  14    
HELIX   22  22 PRO B  221  LEU B  239  1                                  19    
HELIX   23  23 SER B  271  ALA B  280  1                                  10    
HELIX   24  24 HIS B  283  GLY B  303  1                                  21    
SHEET    1   A 3 TYR A  33  THR A  39  0                                        
SHEET    2   A 3 MSE A   1  MSE A   7  1  N  MSE A   7   O  ILE A  38           
SHEET    3   A 3 PHE A  55  LEU A  58  1  O  LEU A  57   N  GLY A   4           
SHEET    1   B 4 TRP A 112  THR A 116  0                                        
SHEET    2   B 4 GLU A 168  LYS A 173 -1  O  ILE A 171   N  ILE A 113           
SHEET    3   B 4 LEU A 133  PRO A 137 -1  N  LYS A 136   O  VAL A 170           
SHEET    4   B 4 LYS A 147  VAL A 149 -1  O  VAL A 149   N  LEU A 133           
SHEET    1   C 4 LYS A 188  GLN A 189  0                                        
SHEET    2   C 4 GLU A 178  PHE A 185 -1  N  PHE A 185   O  LYS A 188           
SHEET    3   C 4 ILE A 193  HIS A 197 -1  O  ILE A 193   N  THR A 181           
SHEET    4   C 4 THR A 213  VAL A 217 -1  O  ILE A 214   N  ARG A 196           
SHEET    1   D 4 LYS A 188  GLN A 189  0                                        
SHEET    2   D 4 GLU A 178  PHE A 185 -1  N  PHE A 185   O  LYS A 188           
SHEET    3   D 4 TYR A 244  LYS A 252 -1  O  MSE A 249   N  ILE A 180           
SHEET    4   D 4 ILE A 255  ASN A 262 -1  O  ASN A 262   N  ARG A 246           
SHEET    1   E 2 GLU A 200  PHE A 202  0                                        
SHEET    2   E 2 LYS A 207  ASP A 209 -1  O  LYS A 207   N  PHE A 202           
SHEET    1   F 3 TYR B  33  THR B  39  0                                        
SHEET    2   F 3 MSE B   1  MSE B   7  1  N  ILE B   3   O  VAL B  36           
SHEET    3   F 3 PHE B  55  LEU B  58  1  O  LEU B  57   N  GLY B   4           
SHEET    1   G 4 TRP B 112  THR B 116  0                                        
SHEET    2   G 4 GLU B 168  LYS B 173 -1  O  ILE B 171   N  ILE B 113           
SHEET    3   G 4 LEU B 133  PRO B 137 -1  N  LYS B 136   O  VAL B 170           
SHEET    4   G 4 LYS B 147  VAL B 149 -1  O  VAL B 149   N  LEU B 133           
SHEET    1   H 4 LYS B 188  GLN B 189  0                                        
SHEET    2   H 4 GLU B 178  PHE B 185 -1  N  PHE B 185   O  LYS B 188           
SHEET    3   H 4 ILE B 193  HIS B 197 -1  O  ILE B 195   N  GLU B 179           
SHEET    4   H 4 THR B 213  GLU B 216 -1  O  GLU B 216   N  SER B 194           
SHEET    1   I 4 LYS B 188  GLN B 189  0                                        
SHEET    2   I 4 GLU B 178  PHE B 185 -1  N  PHE B 185   O  LYS B 188           
SHEET    3   I 4 ALA B 245  LYS B 252 -1  O  VAL B 247   N  CYS B 182           
SHEET    4   I 4 ILE B 255  ASN B 262 -1  O  MSE B 259   N  ASP B 248           
SHEET    1   J 2 GLU B 200  PHE B 202  0                                        
SHEET    2   J 2 LYS B 207  ASP B 209 -1  O  LYS B 207   N  PHE B 202           
LINK         C   ALA A   0                 N   MSE A   1     1555   1555  1.32  
LINK         C   MSE A   1                 N   ARG A   2     1555   1555  1.32  
LINK         C   ILE A   6                 N   MSE A   7     1555   1555  1.33  
LINK         C   MSE A   7                 N   GLY A   8     1555   1555  1.32  
LINK         C   ILE A  18                 N   MSE A  19     1555   1555  1.32  
LINK         C   MSE A  19                 N   THR A  20     1555   1555  1.33  
LINK         C   GLU A  23                 N   MSE A  24     1555   1555  1.34  
LINK         C   MSE A  24                 N   ILE A  25     1555   1555  1.33  
LINK         C   LYS A  43                 N   MSE A  44     1555   1555  1.32  
LINK         C   MSE A  44                 N   ASP A  45     1555   1555  1.33  
LINK         C   ASN A  85                 N   MSE A  86     1555   1555  1.32  
LINK         C   MSE A  86                 N   LEU A  87     1555   1555  1.33  
LINK         C   CYS A  92                 N   MSE A  93     1555   1555  1.33  
LINK         C   MSE A  93                 N   ASP A  94     1555   1555  1.33  
LINK         C   LYS A 117                 N   MSE A 118     1555   1555  1.33  
LINK         C   MSE A 118                 N   GLU A 119     1555   1555  1.34  
LINK         C   SER A 157                 N   MSE A 158     1555   1555  1.34  
LINK         C   MSE A 158                 N   LEU A 159     1555   1555  1.34  
LINK         C   ASP A 248                 N   MSE A 249     1555   1555  1.34  
LINK         C   MSE A 249                 N   MSE A 250     1555   1555  1.34  
LINK         C   MSE A 250                 N   VAL A 251     1555   1555  1.33  
LINK         C   VAL A 258                 N   MSE A 259     1555   1555  1.33  
LINK         C   MSE A 259                 N   GLU A 260     1555   1555  1.33  
LINK         C   GLY A 266                 N   MSE A 267     1555   1555  1.32  
LINK         C   MSE A 267                 N   THR A 268     1555   1555  1.33  
LINK         C   ASP A 289                 N   MSE A 290     1555   1555  1.32  
LINK         C   MSE A 290                 N   ILE A 291     1555   1555  1.33  
LINK         C   ALA B   0                 N   MSE B   1     1555   1555  1.33  
LINK         C   MSE B   1                 N   ARG B   2     1555   1555  1.33  
LINK         C   ILE B   6                 N   MSE B   7     1555   1555  1.33  
LINK         C   MSE B   7                 N   GLY B   8     1555   1555  1.33  
LINK         C   ILE B  18                 N   MSE B  19     1555   1555  1.33  
LINK         C   MSE B  19                 N   THR B  20     1555   1555  1.33  
LINK         C   GLU B  23                 N   MSE B  24     1555   1555  1.33  
LINK         C   MSE B  24                 N   ILE B  25     1555   1555  1.33  
LINK         C   LYS B  43                 N   MSE B  44     1555   1555  1.33  
LINK         C   MSE B  44                 N   ASP B  45     1555   1555  1.33  
LINK         C   ASN B  85                 N   MSE B  86     1555   1555  1.33  
LINK         C   MSE B  86                 N   LEU B  87     1555   1555  1.32  
LINK         C   CYS B  92                 N   MSE B  93     1555   1555  1.32  
LINK         C   MSE B  93                 N   ASP B  94     1555   1555  1.33  
LINK         C   LYS B 117                 N   MSE B 118     1555   1555  1.33  
LINK         C   MSE B 118                 N   GLU B 119     1555   1555  1.33  
LINK         C   SER B 157                 N   MSE B 158     1555   1555  1.33  
LINK         C   MSE B 158                 N   LEU B 159     1555   1555  1.33  
LINK         C   ASP B 248                 N   MSE B 249     1555   1555  1.33  
LINK         C   MSE B 249                 N   MSE B 250     1555   1555  1.33  
LINK         C   MSE B 250                 N   VAL B 251     1555   1555  1.33  
LINK         C   VAL B 258                 N   MSE B 259     1555   1555  1.32  
LINK         C   MSE B 259                 N   GLU B 260     1555   1555  1.33  
LINK         C   GLY B 266                 N   MSE B 267     1555   1555  1.32  
LINK         C   MSE B 267                 N   THR B 268     1555   1555  1.33  
LINK         C   ASP B 289                 N   MSE B 290     1555   1555  1.33  
LINK         C   MSE B 290                 N   ILE B 291     1555   1555  1.33  
CISPEP   1 PHE A  131    PRO A  132          0        -3.55                     
CISPEP   2 PHE B  131    PRO B  132          0         0.05                     
SITE     1 AC1  5 LYS A  95  LYS A 136  MSE A 259  GLU A 260                    
SITE     2 AC1  5 HOH A 401                                                     
SITE     1 AC2  4 LYS A  32  TYR A  33  ASP A 289  GLU A 293                    
SITE     1 AC3  6 CYS B  92  LYS B  95  SER B  98  LYS B  99                    
SITE     2 AC3  6 MSE B 259  VAL B 261                                          
SITE     1 AC4  2 TYR A 204  GLU B 260                                          
CRYST1   65.878   83.187  128.380  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      0.015180  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012021  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007789        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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