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Database: PDB
Entry: 4HDK
LinkDB: 4HDK
Original site: 4HDK 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       02-OCT-12   4HDK              
TITLE     CRYSTAL STRUCTURE OF ARSAB IN COMPLEX WITH PHLOROGLUCINOL             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ARSA;                                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.4.2.21;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ARSB;                                                      
COMPND   8 CHAIN: B;                                                            
COMPND   9 EC: 2.4.2.21;                                                        
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SPOROMUSA OVATA;                                
SOURCE   3 ORGANISM_TAXID: 2378;                                                
SOURCE   4 GENE: ARSA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: JE13607;                                   
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PARSAB22;                                 
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: SPOROMUSA OVATA;                                
SOURCE  12 ORGANISM_TAXID: 2378;                                                
SOURCE  13 GENE: ARSB;                                                          
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: JE13607;                                   
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PARSAB22                                  
KEYWDS    TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.A.NEWMISTER,C.H.CHAN,J.C.ESCALANTE-SEMERENA,I.RAYMENT               
REVDAT   2   30-JAN-13 4HDK    1       JRNL                                     
REVDAT   1   24-OCT-12 4HDK    0                                                
JRNL        AUTH   S.A.NEWMISTER,C.H.CHAN,J.C.ESCALANTE-SEMERENA,I.RAYMENT      
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE FUNCTION OF THE NICOTINATE      
JRNL        TITL 2 MONONUCLEOTIDE:PHENOL/P-CRESOL PHOSPHORIBOSYLTRANSFERASE     
JRNL        TITL 3 (ARSAB) ENZYME FROM SPOROMUSA OVATA.                         
JRNL        REF    BIOCHEMISTRY                  V.  51  8571 2012              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   23039029                                                     
JRNL        DOI    10.1021/BI301142H                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 100357                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5004                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6363                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.15                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2540                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 322                          
REMARK   3   BIN FREE R VALUE                    : 0.3140                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4779                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 501                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.48000                                              
REMARK   3    B22 (A**2) : 0.62000                                              
REMARK   3    B33 (A**2) : -1.10000                                             
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.079         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.081         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.054         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.408         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5013 ; 0.025 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6821 ; 2.483 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   699 ; 5.900 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   179 ;36.998 ;24.469       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   856 ;14.841 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;18.424 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   829 ; 0.281 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3689 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   4                                                                      
REMARK   4 4HDK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB075331.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 100657                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 9.900                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39900                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12.5% MEPEG5000, 100 MM MOPS, 20 MM      
REMARK 280  NACL, 10 MM PHLOROGLUCINOL, 12% ETHYLENE GLYCOL , PH 7.1, VAPOR     
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
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       26.38900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       76.19400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.68250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       76.19400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.38900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.68250            
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.                         
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: 5020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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     GLY A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A    77                                                      
REMARK 465     ALA A    78                                                      
REMARK 465     TYR A    79                                                      
REMARK 465     ASP A   209                                                      
REMARK 465     SER A   210                                                      
REMARK 465     ARG A   211                                                      
REMARK 465     ARG A   344                                                      
REMARK 465     GLY A   345                                                      
REMARK 465     GLY A   346                                                      
REMARK 465     LYS A   347                                                      
REMARK 465     ALA A   348                                                      
REMARK 465     ASN A   349                                                      
REMARK 465     ALA A   350                                                      
REMARK 465     MET B     1                                                      
REMARK 465     MET B    71                                                      
REMARK 465     ALA B    72                                                      
REMARK 465     THR B    73                                                      
REMARK 465     ASP B    74                                                      
REMARK 465     GLN B    75                                                      
REMARK 465     GLN B    76                                                      
REMARK 465     ALA B   335                                                      
REMARK 465     GLN B   336                                                      
REMARK 465     ASP B   337                                                      
REMARK 465     GLY B   338                                                      
REMARK 465     PRO B   339                                                      
REMARK 465     GLY B   340                                                      
REMARK 465     ALA B   341                                                      
REMARK 465     LEU B   342                                                      
REMARK 465     ARG B   343                                                      
REMARK 465     GLN B   344                                                      
REMARK 465     SER B   345                                                      
REMARK 465     LYS B   346                                                      
REMARK 465     ASP B   347                                                      
REMARK 465     VAL B   348                                                      
REMARK 465     ARG B   349                                                      
REMARK 465     ASP B   350                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH2  ARG B   104     O    HOH B   694              1.98            
REMARK 500   O    HOH B   654     O    HOH B   780              2.05            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 176   CD    GLU A 176   OE2    -0.083                       
REMARK 500    THR A 270   N     THR A 270   CA     -0.145                       
REMARK 500    GLU A 312   CD    GLU A 312   OE2    -0.077                       
REMARK 500    GLU A 319   CD    GLU A 319   OE2    -0.075                       
REMARK 500    GLU B  18   CD    GLU B  18   OE2     0.082                       
REMARK 500    GLU B 159   CD    GLU B 159   OE2    -0.069                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ARG A 259   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 259   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    LEU A 307   O   -  C   -  N   ANGL. DEV. =  11.2 DEGREES          
REMARK 500    ARG B 104   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG B 154   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    PRO B 193   C   -  N   -  CD  ANGL. DEV. = -15.0 DEGREES          
REMARK 500    ARG B 243   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG B 243   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    MET B 299   CG  -  SD  -  CE  ANGL. DEV. = -10.0 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    ILE A  93      -68.51   -100.93                                   
REMARK 500    ASP A 265     -121.17   -137.58                                   
REMARK 500    SER A 290      -86.69   -126.74                                   
REMARK 500    HIS B  35     -112.45     45.99                                   
REMARK 500    ASP B 249     -111.40   -103.87                                   
REMARK 500    SER B 274      -85.79   -128.93                                   
REMARK 500    ALA B 281       -4.56     79.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLU A 308        24.9      L          L   OUTSIDE RANGE           
REMARK 500    ILE B 261        24.7      L          L   OUTSIDE RANGE           
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 CL A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 13X A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 13X B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4HDM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4HDR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4HDS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4HDN   RELATED DB: PDB                                   
DBREF  4HDK A    1   350  UNP    F6MZ55   F6MZ55_9FIRM     5    350             
DBREF  4HDK B    1   350  UNP    F6MZ56   F6MZ56_9FIRM     1    350             
SEQADV 4HDK GLY A   -1  UNP  F6MZ55              EXPRESSION TAG                 
SEQADV 4HDK GLY A    0  UNP  F6MZ55              EXPRESSION TAG                 
SEQRES   1 A  348  GLY GLY MET SER LEU LEU GLN ALA THR VAL ALA LYS ILE          
SEQRES   2 A  348  MET ARG PRO ASP THR VAL ILE LYS ASP GLN VAL LYS THR          
SEQRES   3 A  348  LYS LEU ALA GLY VAL LEU GLN SER ALA GLY SER LEU GLY          
SEQRES   4 A  348  ARG LEU GLU ASP MET VAL GLU GLN TYR ALA GLY ILE THR          
SEQRES   5 A  348  GLY GLU LEU ASN PRO ALA LEU PRO LYS PRO CYS MET VAL          
SEQRES   6 A  348  VAL ALA SER ALA ASP HIS GLY VAL ALA ARG ARG VAL VAL          
SEQRES   7 A  348  SER ALA TYR PRO ILE GLU THR THR ILE HIS MET THR ALA          
SEQRES   8 A  348  ASN TYR LEU ILE SER GLN GLY ALA SER ALA ASN ALA PHE          
SEQRES   9 A  348  ALA ASN PHE CYS GLY ALA ASP MET VAL VAL VAL ASP MET          
SEQRES  10 A  348  GLY VAL ALA GLY ASP LEU SER TYR VAL PRO GLY LEU TRP          
SEQRES  11 A  348  HIS ARG LYS ILE ALA TYR GLY THR GLN ASP PHE THR GLU          
SEQRES  12 A  348  GLY PRO ALA MET THR ARG GLU GLN ALA ILE GLN ALA VAL          
SEQRES  13 A  348  GLU THR GLY ILE ASP ILE VAL ASN ASP ARG VAL LYS HIS          
SEQRES  14 A  348  GLY ASN ARG CYS PHE CYS LEU GLY GLU MET GLY ILE GLY          
SEQRES  15 A  348  ASN THR THR SER SER ALA THR ILE VAL GLY ALA PHE THR          
SEQRES  16 A  348  GLY LEU ALA PRO GLU LYS VAL THR GLY ARG GLY THR GLY          
SEQRES  17 A  348  ILE SER ASP SER ARG LEU LYS THR LYS MET GLU ILE VAL          
SEQRES  18 A  348  GLY ARG ALA LEU ALA VAL ASN LYS PRO ASN PRO GLN ASP          
SEQRES  19 A  348  GLY LEU ASP VAL LEU ALA LYS VAL GLY GLY PHE GLU LEU          
SEQRES  20 A  348  GLY ALA LEU ALA GLY VAL ILE LEU GLY SER ALA ALA ASN          
SEQRES  21 A  348  ARG CYS ALA VAL VAL ILE ASP GLY LEU ASN THR THR ALA          
SEQRES  22 A  348  ALA ALA LEU ILE ALA ASN VAL ILE HIS PRO LEU SER LYS          
SEQRES  23 A  348  GLU TYR MET PHE ALA SER HIS LEU SER GLY GLU PRO ALA          
SEQRES  24 A  348  HIS SER ILE ALA LEU ARG GLN LEU GLN LEU GLU ALA CYS          
SEQRES  25 A  348  LEU GLU LEU GLY VAL ARG LEU GLY GLU GLY ILE GLY ALA          
SEQRES  26 A  348  SER MET VAL VAL ASP MET LEU TYR VAL ALA ILE LYS LEU          
SEQRES  27 A  348  LEU ASN ASN ARG GLY GLY LYS ALA ASN ALA                      
SEQRES   1 B  350  MET LEU GLU GLU LEU ILE ALA ALA ILE LYS PRO LEU ASP          
SEQRES   2 B  350  SER ILE ALA MET GLU GLN CYS GLN ARG ARG VAL ASP ASN          
SEQRES   3 B  350  LEU THR LYS PRO LEU ASN SER LEU HIS SER PHE GLU HIS          
SEQRES   4 B  350  ILE ALA CYS LYS LEU ALA GLY ILE SER GLY ASN PRO ARG          
SEQRES   5 B  350  PRO ARG ALA LEU GLU LYS SER ILE ILE ILE MET ALA ALA          
SEQRES   6 B  350  ASP ASN GLY VAL ALA MET ALA THR ASP GLN GLN GLN MET          
SEQRES   7 B  350  THR THR ALA ALA ARG LEU THR GLY PHE CYS GLN GLY GLN          
SEQRES   8 B  350  ALA PRO ILE GLN VAL PHE ALA ALA HIS VAL GLN ALA ARG          
SEQRES   9 B  350  LEU ILE MET VAL ASP ILE GLY VAL ALA ALA ASP LEU PRO          
SEQRES  10 B  350  HIS SER PRO ALA VAL CYS ARG LYS LYS LEU ALA TYR GLY          
SEQRES  11 B  350  SER ARG ASN SER THR GLU GLY PRO ALA MET THR ARG GLN          
SEQRES  12 B  350  GLN ALA ILE GLN ALA ILE GLU VAL GLY VAL ARG ILE ALA          
SEQRES  13 B  350  GLN ALA GLU ILE ALA ARG GLY CYS GLN VAL ILE GLY LEU          
SEQRES  14 B  350  GLY GLU MET GLY LEU GLY GLY LEU ALA ALA ALA MET ALA          
SEQRES  15 B  350  ILE VAL ALA CYS CYS HIS GLY GLN PRO LEU PRO GLY LEU          
SEQRES  16 B  350  ALA GLY ARG GLU ALA GLU LEU VAL ASN THR ALA ILE ALA          
SEQRES  17 B  350  VAL ASN ARG PRO ASN ALA ALA ASP PRO LEU ASP ILE LEU          
SEQRES  18 B  350  THR LYS VAL GLY GLY LEU ALA ILE ALA GLY LEU VAL GLY          
SEQRES  19 B  350  VAL ILE LEU GLY ALA ALA ALA GLY ARG ALA ALA VAL VAL          
SEQRES  20 B  350  LEU ASP GLY LEU ALA THR SER THR ALA ALA LEU ILE ALA          
SEQRES  21 B  350  ILE ASN LEU VAL PRO ASP VAL LYS PRO TYR LEU ILE GLY          
SEQRES  22 B  350  SER HIS PHE ALA ALA GLU PRO ALA HIS GLU THR ALA LEU          
SEQRES  23 B  350  ALA LEU LEU ASP VAL PRO ALA TYR LEU GLN LEU LYS MET          
SEQRES  24 B  350  ASN LEU GLY GLU GLY THR GLY ALA ALA LEU GLY MET SER          
SEQRES  25 B  350  VAL ILE ASN ALA THR LEU HIS MET LEU ASN ASP MET LYS          
SEQRES  26 B  350  THR PHE GLY GLU ALA GLU VAL ALA VAL ALA GLN ASP GLY          
SEQRES  27 B  350  PRO GLY ALA LEU ARG GLN SER LYS ASP VAL ARG ASP              
HET     CL  A 701       1                                                       
HET    13X  A 702       9                                                       
HET    EDO  A 703       4                                                       
HET    EDO  B 401       4                                                       
HET    13X  B 402       9                                                       
HET    EDO  B 403       4                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     13X BENZENE-1,3,5-TRIOL                                              
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     13X PHLOROGLUCINOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  13X    2(C6 H6 O3)                                                  
FORMUL   5  EDO    3(C2 H6 O2)                                                  
FORMUL   9  HOH   *501(H2 O)                                                    
HELIX    1   1 SER A    2  ILE A   11  1                                  10    
HELIX    2   2 ASP A   15  LEU A   30  1                                  16    
HELIX    3   3 GLY A   37  GLY A   51  1                                  15    
HELIX    4   4 HIS A   69  VAL A   75  5                                   7    
HELIX    5   5 GLU A   82  ILE A   93  1                                  12    
HELIX    6   6 ALA A   97  CYS A  106  1                                  10    
HELIX    7   7 THR A  146  LYS A  166  1                                  21    
HELIX    8   8 GLY A  180  GLY A  194  1                                  15    
HELIX    9   9 ALA A  196  GLY A  202  1                                   7    
HELIX   10  10 THR A  214  LYS A  227  1                                  14    
HELIX   11  11 ASP A  232  GLY A  241  1                                  10    
HELIX   12  12 GLY A  242  ASN A  258  1                                  17    
HELIX   13  13 GLY A  266  HIS A  280  1                                  15    
HELIX   14  14 LEU A  282  GLU A  285  5                                   4    
HELIX   15  15 GLU A  295  LEU A  305  1                                  11    
HELIX   16  16 GLY A  320  ASN A  342  1                                  19    
HELIX   17  17 GLU B    3  ALA B    8  1                                   6    
HELIX   18  18 ASP B   13  LEU B   27  1                                  15    
HELIX   19  19 HIS B   35  GLY B   49  1                                  15    
HELIX   20  20 THR B   79  GLN B   89  1                                  11    
HELIX   21  21 ALA B   92  GLN B  102  1                                  11    
HELIX   22  22 THR B  141  ARG B  162  1                                  22    
HELIX   23  23 GLY B  175  GLY B  189  1                                  15    
HELIX   24  24 ALA B  196  ARG B  211  1                                  16    
HELIX   25  25 ASP B  216  GLY B  225  1                                  10    
HELIX   26  26 GLY B  226  GLY B  242  1                                  17    
HELIX   27  27 GLY B  250  VAL B  264  1                                  15    
HELIX   28  28 PRO B  265  PRO B  269  5                                   5    
HELIX   29  29 ALA B  281  ASP B  290  1                                  10    
HELIX   30  30 GLY B  304  MET B  324  1                                  21    
HELIX   31  31 THR B  326  VAL B  332  1                                   7    
SHEET    1   A 6 TRP A 128  HIS A 129  0                                        
SHEET    2   A 6 ASP A 109  GLY A 116  1  N  ASP A 114   O  TRP A 128           
SHEET    3   A 6 LYS A  59  ALA A  67  1  N  MET A  62   O  ASP A 109           
SHEET    4   A 6 ASN A 169  MET A 177  1  O  CYS A 173   N  VAL A  63           
SHEET    5   A 6 ALA A 261  VAL A 263  1  O  VAL A 263   N  PHE A 172           
SHEET    6   A 6 MET A 287  PHE A 288  1  O  PHE A 288   N  VAL A 262           
SHEET    1   B 6 VAL B 122  ARG B 124  0                                        
SHEET    2   B 6 ALA B 103  GLY B 111  1  N  MET B 107   O  CYS B 123           
SHEET    3   B 6 LYS B  58  ALA B  65  1  N  ILE B  60   O  ARG B 104           
SHEET    4   B 6 VAL B 166  MET B 172  1  O  GLY B 168   N  SER B  59           
SHEET    5   B 6 ALA B 245  VAL B 247  1  O  ALA B 245   N  ILE B 167           
SHEET    6   B 6 LEU B 271  ILE B 272  1  O  ILE B 272   N  VAL B 246           
CISPEP   1 PRO B  193    GLY B  194          0       -10.12                     
SITE     1 AC1  3 HIS A 129  ARG A 130  ARG B 132                               
SITE     1 AC2 10 MET A  87  MET A 177  GLU A 319  HOH A 871                    
SITE     2 AC2 10 HOH A 878  THR B  28  LYS B  29  PRO B  30                    
SITE     3 AC2 10 PHE B 327  HOH B 507                                          
SITE     1 AC3  6 GLY A 178  GLY A 180  ASN A 181  THR A 182                    
SITE     2 AC3  6 HOH A 847  HOH A 916                                          
SITE     1 AC4  4 ASN A 104  PHE A 105  HIS B 319  HOH B 501                    
SITE     1 AC5  7 VAL A  29  ALA A  33  ARG B  83  GLY B  86                    
SITE     2 AC5  7 ALA B  92  PRO B  93  GLU B 303                               
SITE     1 AC6  6 PHE A 105  ASP A 328  HIS B 100  SER B 312                    
SITE     2 AC6  6 ASN B 315  HOH B 550                                          
CRYST1   52.778   77.365  152.388  90.00  90.00  90.00 P 21 21 21    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      0.018947  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012926  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006562        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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