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Database: PDB
Entry: 4EOU
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Original site: 4EOU 
HEADER    LYASE                                   15-APR-12   4EOU              
TITLE     CRYSTAL STRUCTURE OF E. COLI DIHYDRODIPICOLINATE SYNTHASE WITH        
TITLE    2 PYRUVATE AND SUCCINIC SEMI-ALDEHYDE BOUND IN ACTIVE SITE             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDRODIPICOLINATE SYNTHASE;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: DHDPS;                                                      
COMPND   5 EC: 4.2.1.52                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 STRAIN: XL1-BLUE;                                                    
SOURCE   5 OTHER_DETAILS: HARBORING PLASMID PJG001                              
KEYWDS    ALPHA/BETA BARREL, TIM BARREL, AMINO-ACID BIOSYNTHESIS, SCHIFF BASE,  
KEYWDS   2 LYASE                                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.A.BOUGHTON,R.C.J.DOBSON,C.A.HUTTON                                  
REVDAT   5   06-DEC-23 4EOU    1       REMARK                                   
REVDAT   4   13-SEP-23 4EOU    1       REMARK LINK                              
REVDAT   3   25-JUL-12 4EOU    1       JRNL                                     
REVDAT   2   06-JUN-12 4EOU    1       JRNL                                     
REVDAT   1   25-APR-12 4EOU    0                                                
SPRSDE     25-APR-12 4EOU      3UBS                                             
JRNL        AUTH   B.A.BOUGHTON,R.C.DOBSON,C.A.HUTTON                           
JRNL        TITL   THE CRYSTAL STRUCTURE OF DIHYDRODIPICOLINATE SYNTHASE FROM   
JRNL        TITL 2 ESCHERICHIA COLI WITH BOUND PYRUVATE AND SUCCINIC ACID       
JRNL        TITL 3 SEMIALDEHYDE: UNAMBIGUOUS RESOLUTION OF THE STEREOCHEMISTRY  
JRNL        TITL 4 OF THE CONDENSATION PRODUCT.                                 
JRNL        REF    PROTEINS                      V.  80  2117 2012              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   22552955                                                     
JRNL        DOI    10.1002/PROT.24106                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 35072                          
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) : 0.146                           
REMARK   3   R VALUE            (WORKING SET) : 0.143                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2110                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2550                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.79                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1570                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 51                           
REMARK   3   BIN FREE R VALUE                    : 0.2240                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4378                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 16                                      
REMARK   3   SOLVENT ATOMS            : 459                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.14000                                             
REMARK   3    B22 (A**2) : -0.14000                                             
REMARK   3    B33 (A**2) : 0.20000                                              
REMARK   3    B12 (A**2) : -0.07000                                             
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): 0.196         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.180         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.099         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.069         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4503 ; 0.019 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6129 ; 1.940 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   594 ; 6.515 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   176 ;37.210 ;24.432       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   744 ;15.778 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    27 ;17.125 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   740 ; 0.123 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3351 ; 0.010 ; 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   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER 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:                                           
REMARK   3  HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT                    
REMARK   3  U VALUES      : REFINED INDIVIDUALLY                                
REMARK   4                                                                      
REMARK   4 4EOU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000071886.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JUL-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 10.0                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95364                            
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35072                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.10300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.36                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.700                              
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: PDB ENTRY 1YXC                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% W/V N-OCTYL-R-GLUCOPYRANOSIDE, 1.8    
REMARK 280  M POTASSIUM PHOSPHATE DIBASIC, PH 10.0, VAPOR DIFFUSION, HANGING    
REMARK 280  DROP, TEMPERATURE 277K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.57733            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       73.15467            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       73.15467            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       36.57733            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10580 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 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 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       73.15467            
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     LYS A  16    NZ                                                  
REMARK 470     LYS A  25    NZ                                                  
REMARK 470     LYS A 120    NZ                                                  
REMARK 470     LYS A 155    CD   CE   NZ                                        
REMARK 470     GLU A 175    OE1  OE2                                            
REMARK 470     LYS A 257    NZ                                                  
REMARK 470     LYS B  25    NZ                                                  
REMARK 470     ASP B  94    CG   OD1  OD2                                       
REMARK 470     LYS B 155    CD   CE   NZ                                        
REMARK 470     ARG B 212    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 219    CE   NZ                                             
REMARK 470     LYS B 257    NZ                                                  
REMARK 470     LYS B 287    CE   NZ                                             
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   N    MET B     1     O    HOH B   508              2.00            
REMARK 500   N    MET A     1     O    HOH A   508              2.02            
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    HIS A 118   CG    HIS A 118   CD2     0.062                       
REMARK 500    HIS B  53   CG    HIS B  53   CD2     0.065                       
REMARK 500    HIS B 240   CG    HIS B 240   CD2     0.067                       
REMARK 500    HIS B 288   CG    HIS B 288   CD2     0.070                       
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    LEU A 183   CB  -  CG  -  CD2 ANGL. DEV. = -10.6 DEGREES          
REMARK 500    ARG B 235   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 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    TYR A 107      -50.90     81.40                                   
REMARK 500    TYR B 107      -54.78     78.08                                   
REMARK 500    PRO B 249       31.20    -99.65                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 303   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A 123   O                                                      
REMARK 620 2 GLU A 124   O    67.9                                              
REMARK 620 3 THR A 126   O    70.3  88.3                                        
REMARK 620 4 HOH A 512   O    64.6  96.8 128.3                                  
REMARK 620 5 HOH A 557   O   116.2  69.2 149.7  76.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 301   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A 152   O                                                      
REMARK 620 2 VAL A 154   O    85.6                                              
REMARK 620 3 LYS A 155   O   145.6  63.8                                        
REMARK 620 4 ILE A 157   O   101.8  85.8  91.6                                  
REMARK 620 5 HOH A 514   O    79.9  96.1  87.8 177.5                            
REMARK 620 6 HOH A 568   O    93.8 175.8 115.6  98.4  79.7                      
REMARK 620 7 HOH A 588   O   138.9 130.8  67.2  99.7  77.9  48.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 303   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA B 123   O                                                      
REMARK 620 2 THR B 126   O    72.5                                              
REMARK 620 3 HOH B 500   O    68.0 133.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 301   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA B 152   O                                                      
REMARK 620 2 VAL B 154   O    81.9                                              
REMARK 620 3 LYS B 155   O   142.6  64.1                                        
REMARK 620 4 ILE B 157   O    99.9  82.9  91.3                                  
REMARK 620 5 HOH B 561   O    75.8  88.5  87.7 170.9                            
REMARK 620 6 HOH B 603   O   146.1 109.9  48.7 112.8  72.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 301                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 303                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 301                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 303                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1YXC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3DU0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1DHP   RELATED DB: PDB                                   
DBREF  4EOU A    1   292  UNP    P0A6L2   DAPA_ECOLI       1    292             
DBREF  4EOU B    1   292  UNP    P0A6L2   DAPA_ECOLI       1    292             
SEQRES   1 A  292  MET PHE THR GLY SER ILE VAL ALA ILE VAL THR PRO MET          
SEQRES   2 A  292  ASP GLU LYS GLY ASN VAL CYS ARG ALA SER LEU LYS LYS          
SEQRES   3 A  292  LEU ILE ASP TYR HIS VAL ALA SER GLY THR SER ALA ILE          
SEQRES   4 A  292  VAL SER VAL GLY THR THR GLY GLU SER ALA THR LEU ASN          
SEQRES   5 A  292  HIS ASP GLU HIS ALA ASP VAL VAL MET MET THR LEU ASP          
SEQRES   6 A  292  LEU ALA ASP GLY ARG ILE PRO VAL ILE ALA GLY THR GLY          
SEQRES   7 A  292  ALA ASN ALA THR ALA GLU ALA ILE SER LEU THR GLN ARG          
SEQRES   8 A  292  PHE ASN ASP SER GLY ILE VAL GLY CYS LEU THR VAL THR          
SEQRES   9 A  292  PRO TYR TYR ASN ARG PRO SER GLN GLU GLY LEU TYR GLN          
SEQRES  10 A  292  HIS PHE LYS ALA ILE ALA GLU HIS THR ASP LEU PRO GLN          
SEQRES  11 A  292  ILE LEU TYR ASN VAL PRO SER ARG THR GLY CYS ASP LEU          
SEQRES  12 A  292  LEU PRO GLU THR VAL GLY ARG LEU ALA LYS VAL LYS ASN          
SEQRES  13 A  292  ILE ILE GLY ILE LYF GLU ALA THR GLY ASN LEU THR ARG          
SEQRES  14 A  292  VAL ASN GLN ILE LYS GLU LEU VAL SER ASP ASP PHE VAL          
SEQRES  15 A  292  LEU LEU SER GLY ASP ASP ALA SER ALA LEU ASP PHE MET          
SEQRES  16 A  292  GLN LEU GLY GLY HIS GLY VAL ILE SER VAL THR ALA ASN          
SEQRES  17 A  292  VAL ALA ALA ARG ASP MET ALA GLN MET CYS LYS LEU ALA          
SEQRES  18 A  292  ALA GLU GLY HIS PHE ALA GLU ALA ARG VAL ILE ASN GLN          
SEQRES  19 A  292  ARG LEU MET PRO LEU HIS ASN LYS LEU PHE VAL GLU PRO          
SEQRES  20 A  292  ASN PRO ILE PRO VAL LYS TRP ALA CYS LYS GLU LEU GLY          
SEQRES  21 A  292  LEU VAL ALA THR ASP THR LEU ARG LEU PRO MET THR PRO          
SEQRES  22 A  292  ILE THR ASP SER GLY ARG GLU THR VAL ARG ALA ALA LEU          
SEQRES  23 A  292  LYS HIS ALA GLY LEU LEU                                      
SEQRES   1 B  292  MET PHE THR GLY SER ILE VAL ALA ILE VAL THR PRO MET          
SEQRES   2 B  292  ASP GLU LYS GLY ASN VAL CYS ARG ALA SER LEU LYS LYS          
SEQRES   3 B  292  LEU ILE ASP TYR HIS VAL ALA SER GLY THR SER ALA ILE          
SEQRES   4 B  292  VAL SER VAL GLY THR THR GLY GLU SER ALA THR LEU ASN          
SEQRES   5 B  292  HIS ASP GLU HIS ALA ASP VAL VAL MET MET THR LEU ASP          
SEQRES   6 B  292  LEU ALA ASP GLY ARG ILE PRO VAL ILE ALA GLY THR GLY          
SEQRES   7 B  292  ALA ASN ALA THR ALA GLU ALA ILE SER LEU THR GLN ARG          
SEQRES   8 B  292  PHE ASN ASP SER GLY ILE VAL GLY CYS LEU THR VAL THR          
SEQRES   9 B  292  PRO TYR TYR ASN ARG PRO SER GLN GLU GLY LEU TYR GLN          
SEQRES  10 B  292  HIS PHE LYS ALA ILE ALA GLU HIS THR ASP LEU PRO GLN          
SEQRES  11 B  292  ILE LEU TYR ASN VAL PRO SER ARG THR GLY CYS ASP LEU          
SEQRES  12 B  292  LEU PRO GLU THR VAL GLY ARG LEU ALA LYS VAL LYS ASN          
SEQRES  13 B  292  ILE ILE GLY ILE LYF GLU ALA THR GLY ASN LEU THR ARG          
SEQRES  14 B  292  VAL ASN GLN ILE LYS GLU LEU VAL SER ASP ASP PHE VAL          
SEQRES  15 B  292  LEU LEU SER GLY ASP ASP ALA SER ALA LEU ASP PHE MET          
SEQRES  16 B  292  GLN LEU GLY GLY HIS GLY VAL ILE SER VAL THR ALA ASN          
SEQRES  17 B  292  VAL ALA ALA ARG ASP MET ALA GLN MET CYS LYS LEU ALA          
SEQRES  18 B  292  ALA GLU GLY HIS PHE ALA GLU ALA ARG VAL ILE ASN GLN          
SEQRES  19 B  292  ARG LEU MET PRO LEU HIS ASN LYS LEU PHE VAL GLU PRO          
SEQRES  20 B  292  ASN PRO ILE PRO VAL LYS TRP ALA CYS LYS GLU LEU GLY          
SEQRES  21 B  292  LEU VAL ALA THR ASP THR LEU ARG LEU PRO MET THR PRO          
SEQRES  22 B  292  ILE THR ASP SER GLY ARG GLU THR VAL ARG ALA ALA LEU          
SEQRES  23 B  292  LYS HIS ALA GLY LEU LEU                                      
MODRES 4EOU LYF A  161  LYS                                                     
MODRES 4EOU LYF B  161  LYS                                                     
HET    LYF  A 161      21                                                       
HET    LYF  B 161      21                                                       
HET      K  A 301       1                                                       
HET    GOL  A 302       6                                                       
HET      K  A 303       1                                                       
HET      K  B 301       1                                                       
HET    GOL  B 302       6                                                       
HET      K  B 303       1                                                       
HETNAM     LYF (2E,4S)-2-{[(5S)-5-AMINO-5-CARBOXYPENTYL]IMINO}-4-               
HETNAM   2 LYF  HYDROXYHEPTANEDIOIC ACID                                        
HETNAM       K POTASSIUM ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  LYF    2(C13 H22 N2 O7)                                             
FORMUL   3    K    4(K 1+)                                                      
FORMUL   4  GOL    2(C3 H8 O3)                                                  
FORMUL   9  HOH   *459(H2 O)                                                    
HELIX    1   1 CYS A   20  GLY A   35  1                                  16    
HELIX    2   2 GLU A   47  LEU A   51  5                                   5    
HELIX    3   3 ASN A   52  ASP A   68  1                                  17    
HELIX    4   4 ALA A   81  PHE A   92  1                                  12    
HELIX    5   5 SER A  111  HIS A  125  1                                  15    
HELIX    6   6 VAL A  135  GLY A  140  1                                   6    
HELIX    7   7 LEU A  144  ALA A  152  1                                   9    
HELIX    8   8 THR A  168  GLU A  175  1                                   8    
HELIX    9   9 ASP A  187  LEU A  197  1                                  11    
HELIX   10  10 VAL A  205  VAL A  209  5                                   5    
HELIX   11  11 ALA A  210  GLU A  223  1                                  14    
HELIX   12  12 HIS A  225  LEU A  243  1                                  19    
HELIX   13  13 PRO A  249  LEU A  259  1                                  11    
HELIX   14  14 THR A  275  ALA A  289  1                                  15    
HELIX   15  15 CYS B   20  GLY B   35  1                                  16    
HELIX   16  16 GLU B   47  LEU B   51  5                                   5    
HELIX   17  17 ASN B   52  ASP B   68  1                                  17    
HELIX   18  18 ALA B   81  ARG B   91  1                                  11    
HELIX   19  19 SER B  111  HIS B  125  1                                  15    
HELIX   20  20 VAL B  135  GLY B  140  1                                   6    
HELIX   21  21 LEU B  144  ALA B  152  1                                   9    
HELIX   22  22 THR B  168  GLU B  175  1                                   8    
HELIX   23  23 ASP B  187  LEU B  197  1                                  11    
HELIX   24  24 VAL B  205  VAL B  209  5                                   5    
HELIX   25  25 ALA B  210  GLU B  223  1                                  14    
HELIX   26  26 HIS B  225  LEU B  243  1                                  19    
HELIX   27  27 PRO B  249  LEU B  259  1                                  11    
HELIX   28  28 THR B  275  ALA B  289  1                                  15    
SHEET    1   A 9 GLY A   4  ALA A   8  0                                        
SHEET    2   A 9 ALA A  38  SER A  41  1  O  VAL A  40   N  VAL A   7           
SHEET    3   A 9 VAL A  73  GLY A  76  1  O  ILE A  74   N  SER A  41           
SHEET    4   A 9 GLY A  99  VAL A 103  1  O  LEU A 101   N  ALA A  75           
SHEET    5   A 9 GLN A 130  ASN A 134  1  O  ILE A 131   N  THR A 102           
SHEET    6   A 9 ILE A 157  GLU A 162  1  O  LYF A 161   N  LEU A 132           
SHEET    7   A 9 VAL A 182  SER A 185  1  O  LEU A 184   N  GLU A 162           
SHEET    8   A 9 GLY A 201  SER A 204  1  O  ILE A 203   N  SER A 185           
SHEET    9   A 9 GLY A   4  ALA A   8  1  N  ILE A   6   O  SER A 204           
SHEET    1   B 9 GLY B   4  ALA B   8  0                                        
SHEET    2   B 9 ALA B  38  SER B  41  1  O  VAL B  40   N  VAL B   7           
SHEET    3   B 9 VAL B  73  GLY B  76  1  O  ILE B  74   N  ILE B  39           
SHEET    4   B 9 GLY B  99  VAL B 103  1  O  LEU B 101   N  ALA B  75           
SHEET    5   B 9 GLN B 130  ASN B 134  1  O  ILE B 131   N  CYS B 100           
SHEET    6   B 9 ILE B 157  GLU B 162  1  O  LYF B 161   N  LEU B 132           
SHEET    7   B 9 VAL B 182  SER B 185  1  O  LEU B 184   N  GLU B 162           
SHEET    8   B 9 GLY B 201  SER B 204  1  O  ILE B 203   N  SER B 185           
SHEET    9   B 9 GLY B   4  ALA B   8  1  N  ILE B   6   O  SER B 204           
LINK         C   ILE A 160                 N   LYF A 161     1555   1555  1.33  
LINK         C   LYF A 161                 N   GLU A 162     1555   1555  1.33  
LINK         C   ILE B 160                 N   LYF B 161     1555   1555  1.35  
LINK         C   LYF B 161                 N   GLU B 162     1555   1555  1.34  
LINK         O   ALA A 123                 K     K A 303     1555   1555  2.92  
LINK         O   GLU A 124                 K     K A 303     1555   1555  3.22  
LINK         O   THR A 126                 K     K A 303     1555   1555  2.70  
LINK         O   ALA A 152                 K     K A 301     1555   1555  2.69  
LINK         O   VAL A 154                 K     K A 301     1555   1555  2.64  
LINK         O   LYS A 155                 K     K A 301     1555   1555  3.25  
LINK         O   ILE A 157                 K     K A 301     1555   1555  2.63  
LINK         K     K A 301                 O   HOH A 514     1555   1555  2.84  
LINK         K     K A 301                 O   HOH A 568     1555   1555  2.70  
LINK         K     K A 301                 O   HOH A 588     1555   1555  3.22  
LINK         K     K A 303                 O   HOH A 512     1555   1555  2.85  
LINK         K     K A 303                 O   HOH A 557     1555   1555  3.15  
LINK         O   ALA B 123                 K     K B 303     1555   1555  2.82  
LINK         O   THR B 126                 K     K B 303     1555   1555  2.59  
LINK         O   ALA B 152                 K     K B 301     1555   1555  2.75  
LINK         O   VAL B 154                 K     K B 301     1555   1555  2.68  
LINK         O   LYS B 155                 K     K B 301     1555   1555  3.27  
LINK         O   ILE B 157                 K     K B 301     1555   1555  2.64  
LINK         K     K B 301                 O   HOH B 561     1555   1555  3.01  
LINK         K     K B 301                 O   HOH B 603     1555   1555  3.44  
LINK         K     K B 303                 O   HOH B 500     1555   1555  2.88  
CISPEP   1 ASN A  248    PRO A  249          0         8.61                     
CISPEP   2 LEU A  269    PRO A  270          0        13.01                     
CISPEP   3 ASN B  248    PRO B  249          0         3.10                     
CISPEP   4 LEU B  269    PRO B  270          0        13.62                     
SITE     1 AC1  6 ALA A 152  VAL A 154  LYS A 155  ILE A 157                    
SITE     2 AC1  6 HOH A 514  HOH A 568                                          
SITE     1 AC2  7 SER A  48  ALA A  49  TYR A 106  HOH A 462                    
SITE     2 AC2  7 HOH A 585  ASN B  80  TYR B 107                               
SITE     1 AC3  4 ALA A 123  GLU A 124  THR A 126  HOH A 512                    
SITE     1 AC4  5 ALA B 152  VAL B 154  LYS B 155  ILE B 157                    
SITE     2 AC4  5 HOH B 561                                                     
SITE     1 AC5  9 ASN A  80  SER B  48  ALA B  49  GLY B  78                    
SITE     2 AC5  9 VAL B 103  TYR B 106  HOH B 411  HOH B 431                    
SITE     3 AC5  9 HOH B 547                                                     
SITE     1 AC6  3 ALA B 123  THR B 126  HOH B 500                               
CRYST1  121.172  121.172  109.732  90.00  90.00 120.00 P 31 2 1     12          
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      0.008253  0.004765  0.000000        0.00000                         
SCALE2      0.000000  0.009529  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009113        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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