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Database: PDB
Entry: 3V4Z
LinkDB: 3V4Z
Original site: 3V4Z 
HEADER    LIGASE                                  15-DEC-11   3V4Z              
TITLE     D-ALANINE--D-ALANINE LIGASE FROM YERSINIA PESTIS                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: D-ALA-D-ALA LIGASE, D-ALANYLALANINE SYNTHETASE;             
COMPND   5 EC: 6.3.2.4;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: YERSINIA PESTIS;                                
SOURCE   3 ORGANISM_TAXID: 214092;                                              
SOURCE   4 STRAIN: CO92;                                                        
SOURCE   5 GENE: DDL, DDLB, Y3624, YPO0557, YP_3627;                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMCSG7                                    
KEYWDS    STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS     
KEYWDS   2 DISEASES, CSGID, PEPTIDOGLYCAN SYNTHESIS, LIGASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.OSIPIUK,B.NOCEK,R.MULLIGAN,L.PAPAZISI,W.F.ANDERSON,A.JOACHIMIAK,    
AUTHOR   2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)        
REVDAT   1   28-DEC-11 3V4Z    0                                                
JRNL        AUTH   J.OSIPIUK,B.NOCEK,R.MULLIGAN,L.PAPAZISI,W.F.ANDERSON,        
JRNL        AUTH 2 A.JOACHIMIAK                                                 
JRNL        TITL   D-ALANINE--D-ALANINE LIGASE FROM YERSINIA PESTIS.            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.69 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) : 2.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 18203                          
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) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.289                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 927                             
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) : 2.69                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.76                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1141                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.83                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3010                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 69                           
REMARK   3   BIN FREE R VALUE                    : 0.5030                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4399                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 17                                      
REMARK   3   SOLVENT ATOMS            : 23                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 70.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.64000                                             
REMARK   3    B22 (A**2) : -3.64000                                             
REMARK   3    B33 (A**2) : 5.46000                                              
REMARK   3    B12 (A**2) : -1.82000                                             
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.402         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.305         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 32.364        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.894                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4497 ; 0.014 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6091 ; 1.871 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   575 ; 6.445 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   181 ;36.155 ;25.028       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   760 ;19.730 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;20.748 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   701 ; 0.109 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3342 ; 0.008 ; 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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   306                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.6619 -27.9739  -9.3727              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0059 T22:   0.0952                                     
REMARK   3      T33:   0.0879 T12:  -0.0141                                     
REMARK   3      T13:   0.0149 T23:  -0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8487 L22:   0.8480                                     
REMARK   3      L33:   0.7556 L12:  -0.2365                                     
REMARK   3      L13:   0.0787 L23:   0.6026                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0237 S12:   0.0282 S13:  -0.1207                       
REMARK   3      S21:  -0.0035 S22:   0.0802 S23:   0.0703                       
REMARK   3      S31:  -0.0003 S32:   0.0026 S33:  -0.0565                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   306                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.7133 -35.2272  -4.4591              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0711 T22:   0.2165                                     
REMARK   3      T33:   0.1560 T12:  -0.0286                                     
REMARK   3      T13:   0.0302 T23:  -0.0323                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1354 L22:   1.6172                                     
REMARK   3      L33:   1.5455 L12:  -0.6053                                     
REMARK   3      L13:   0.0245 L23:   1.2801                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0577 S12:   0.1184 S13:   0.2146                       
REMARK   3      S21:  -0.1417 S22:   0.0418 S23:  -0.0666                       
REMARK   3      S31:  -0.1868 S32:   0.1052 S33:   0.0159                       
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   3  THE INPUT. U VALUES: WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 3V4Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB069601.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-AUG-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SBC-3                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18282                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 31.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 9.900                              
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.10                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.89000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.430                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP, HKL3000                                       
REMARK 200 STARTING MODEL: 1IOW                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE, 0.1 M SODIUM   
REMARK 280  CACODYLATE, 50% PEG-200, PH 6.5, VAPOR DIFFUSION, SITTING DROP,     
REMARK 280  TEMPERATURE 289K                                                    
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       36.76800            
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       73.53600            
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       73.53600            
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       36.76800            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     VAL A   208                                                      
REMARK 465     PHE A   209                                                      
REMARK 465     TYR A   210                                                      
REMARK 465     ASP A   211                                                      
REMARK 465     TYR A   212                                                      
REMARK 465     ASP A   213                                                      
REMARK 465     ALA A   214                                                      
REMARK 465     LYS A   215                                                      
REMARK 465     TYR A   216                                                      
REMARK 465     LEU A   217                                                      
REMARK 465     SER A   218                                                      
REMARK 465     ASP A   219                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     GLU B   148                                                      
REMARK 465     GLY B   149                                                      
REMARK 465     SER B   150                                                      
REMARK 465     SER B   151                                                      
REMARK 465     VAL B   152                                                      
REMARK 465     GLY B   207                                                      
REMARK 465     VAL B   208                                                      
REMARK 465     PHE B   209                                                      
REMARK 465     TYR B   210                                                      
REMARK 465     ASP B   211                                                      
REMARK 465     TYR B   212                                                      
REMARK 465     ASP B   213                                                      
REMARK 465     ALA B   214                                                      
REMARK 465     LYS B   215                                                      
REMARK 465     TYR B   216                                                      
REMARK 465     LEU B   217                                                      
REMARK 465     SER B   218                                                      
REMARK 465     ASP B   219                                                      
REMARK 465     LYS B   220                                                      
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 262   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    LEU A 292   CB  -  CG  -  CD1 ANGL. DEV. = -10.8 DEGREES          
REMARK 500    LEU B 125   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    ASP B 306   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 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    THR A  12       18.35   -144.04                                   
REMARK 500    THR A  48      -35.16    -37.18                                   
REMARK 500    GLU A  52      -30.00    -35.95                                   
REMARK 500    TYR A 114      144.82   -172.12                                   
REMARK 500    PHE A 122      -74.87    -38.66                                   
REMARK 500    GLU A 123       -9.83    -58.12                                   
REMARK 500    GLU A 148      -75.46    -49.40                                   
REMARK 500    SER A 150     -167.52    -77.45                                   
REMARK 500    PRO A 186     -177.70    -68.08                                   
REMARK 500    TRP A 253      167.21    178.04                                   
REMARK 500    GLU A 270      153.49    175.37                                   
REMARK 500    MET A 277       28.96   -143.20                                   
REMARK 500    THR A 278     -150.65    -63.78                                   
REMARK 500    HIS A 280        0.23    -69.17                                   
REMARK 500    ALA A 305      109.97    -51.91                                   
REMARK 500    THR B  42       -7.69    -57.53                                   
REMARK 500    GLN B 204      119.31   -172.09                                   
REMARK 500    PRO B 226      150.15    -45.61                                   
REMARK 500    SER B 230      172.60    -59.79                                   
REMARK 500    LEU B 269      -66.08   -124.75                                   
REMARK 500    ALA B 305       91.85    -65.17                                   
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 PGE B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: IDP00575   RELATED DB: TARGETDB                          
DBREF  3V4Z A    1   306  UNP    Q8ZIE7   DDL_YERPE        1    306             
DBREF  3V4Z B    1   306  UNP    Q8ZIE7   DDL_YERPE        1    306             
SEQADV 3V4Z SER A   -2  UNP  Q8ZIE7              EXPRESSION TAG                 
SEQADV 3V4Z ASN A   -1  UNP  Q8ZIE7              EXPRESSION TAG                 
SEQADV 3V4Z ALA A    0  UNP  Q8ZIE7              EXPRESSION TAG                 
SEQADV 3V4Z SER B   -2  UNP  Q8ZIE7              EXPRESSION TAG                 
SEQADV 3V4Z ASN B   -1  UNP  Q8ZIE7              EXPRESSION TAG                 
SEQADV 3V4Z ALA B    0  UNP  Q8ZIE7              EXPRESSION TAG                 
SEQRES   1 A  309  SER ASN ALA MET ALA GLU LYS VAL ALA VAL LEU LEU GLY          
SEQRES   2 A  309  GLY THR SER ALA GLU ARG GLU VAL SER LEU LEU SER GLY          
SEQRES   3 A  309  GLN ALA VAL LEU ALA GLY LEU LYS GLU ALA GLY ILE ASP          
SEQRES   4 A  309  ALA TYR GLY VAL ASP THR LYS ASP PHE PRO VAL THR GLN          
SEQRES   5 A  309  LEU LYS GLU GLN GLY PHE ASP LYS VAL PHE ILE ALA LEU          
SEQRES   6 A  309  HIS GLY ARG GLY GLY GLU ASP GLY THR LEU GLN GLY VAL          
SEQRES   7 A  309  LEU GLU PHE LEU GLN LEU PRO TYR THR GLY SER GLY VAL          
SEQRES   8 A  309  MET ALA SER ALA LEU THR MET ASP LYS LEU ARG THR LYS          
SEQRES   9 A  309  LEU VAL TRP GLN ALA LEU GLY LEU PRO ILE SER PRO TYR          
SEQRES  10 A  309  VAL ALA LEU ASN ARG GLN GLN PHE GLU THR LEU SER PRO          
SEQRES  11 A  309  GLU GLU LEU VAL ALA CYS VAL ALA LYS LEU GLY LEU PRO          
SEQRES  12 A  309  LEU ILE VAL LYS PRO SER HIS GLU GLY SER SER VAL GLY          
SEQRES  13 A  309  MET SER LYS VAL ASP HIS ALA SER GLU LEU GLN LYS ALA          
SEQRES  14 A  309  LEU VAL GLU ALA PHE GLN HIS ASP SER ASP VAL LEU ILE          
SEQRES  15 A  309  GLU LYS TRP LEU SER GLY PRO GLU PHE THR VAL ALA ILE          
SEQRES  16 A  309  LEU GLY ASP GLU VAL LEU PRO SER ILE ARG ILE GLN PRO          
SEQRES  17 A  309  PRO GLY VAL PHE TYR ASP TYR ASP ALA LYS TYR LEU SER          
SEQRES  18 A  309  ASP LYS THR GLN TYR PHE CYS PRO SER GLY LEU SER ASP          
SEQRES  19 A  309  GLU SER GLU GLN GLN LEU ALA ALA LEU ALA LEU GLN ALA          
SEQRES  20 A  309  TYR HIS ALA LEU ASP CYS SER GLY TRP GLY ARG VAL ASP          
SEQRES  21 A  309  VAL MET GLN ASP ARG ASP GLY HIS PHE TYR LEU LEU GLU          
SEQRES  22 A  309  VAL ASN THR SER PRO GLY MET THR SER HIS SER LEU VAL          
SEQRES  23 A  309  PRO MET ALA ALA ARG GLN TYR GLY LEU SER PHE SER GLN          
SEQRES  24 A  309  LEU VAL ALA ARG ILE LEU MET LEU ALA ASP                      
SEQRES   1 B  309  SER ASN ALA MET ALA GLU LYS VAL ALA VAL LEU LEU GLY          
SEQRES   2 B  309  GLY THR SER ALA GLU ARG GLU VAL SER LEU LEU SER GLY          
SEQRES   3 B  309  GLN ALA VAL LEU ALA GLY LEU LYS GLU ALA GLY ILE ASP          
SEQRES   4 B  309  ALA TYR GLY VAL ASP THR LYS ASP PHE PRO VAL THR GLN          
SEQRES   5 B  309  LEU LYS GLU GLN GLY PHE ASP LYS VAL PHE ILE ALA LEU          
SEQRES   6 B  309  HIS GLY ARG GLY GLY GLU ASP GLY THR LEU GLN GLY VAL          
SEQRES   7 B  309  LEU GLU PHE LEU GLN LEU PRO TYR THR GLY SER GLY VAL          
SEQRES   8 B  309  MET ALA SER ALA LEU THR MET ASP LYS LEU ARG THR LYS          
SEQRES   9 B  309  LEU VAL TRP GLN ALA LEU GLY LEU PRO ILE SER PRO TYR          
SEQRES  10 B  309  VAL ALA LEU ASN ARG GLN GLN PHE GLU THR LEU SER PRO          
SEQRES  11 B  309  GLU GLU LEU VAL ALA CYS VAL ALA LYS LEU GLY LEU PRO          
SEQRES  12 B  309  LEU ILE VAL LYS PRO SER HIS GLU GLY SER SER VAL GLY          
SEQRES  13 B  309  MET SER LYS VAL ASP HIS ALA SER GLU LEU GLN LYS ALA          
SEQRES  14 B  309  LEU VAL GLU ALA PHE GLN HIS ASP SER ASP VAL LEU ILE          
SEQRES  15 B  309  GLU LYS TRP LEU SER GLY PRO GLU PHE THR VAL ALA ILE          
SEQRES  16 B  309  LEU GLY ASP GLU VAL LEU PRO SER ILE ARG ILE GLN PRO          
SEQRES  17 B  309  PRO GLY VAL PHE TYR ASP TYR ASP ALA LYS TYR LEU SER          
SEQRES  18 B  309  ASP LYS THR GLN TYR PHE CYS PRO SER GLY LEU SER ASP          
SEQRES  19 B  309  GLU SER GLU GLN GLN LEU ALA ALA LEU ALA LEU GLN ALA          
SEQRES  20 B  309  TYR HIS ALA LEU ASP CYS SER GLY TRP GLY ARG VAL ASP          
SEQRES  21 B  309  VAL MET GLN ASP ARG ASP GLY HIS PHE TYR LEU LEU GLU          
SEQRES  22 B  309  VAL ASN THR SER PRO GLY MET THR SER HIS SER LEU VAL          
SEQRES  23 B  309  PRO MET ALA ALA ARG GLN TYR GLY LEU SER PHE SER GLN          
SEQRES  24 B  309  LEU VAL ALA ARG ILE LEU MET LEU ALA ASP                      
HET    PEG  A 502       7                                                       
HET    PGE  B 501      10                                                       
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     PGE TRIETHYLENE GLYCOL                                               
FORMUL   3  PEG    C4 H10 O3                                                    
FORMUL   4  PGE    C6 H14 O4                                                    
FORMUL   5  HOH   *23(H2 O)                                                     
HELIX    1   1 GLU A   15  GLY A   34  1                                  20    
HELIX    2   2 PRO A   46  LEU A   50  5                                   5    
HELIX    3   3 GLY A   70  GLN A   80  1                                  11    
HELIX    4   4 GLY A   87  MET A   95  1                                   9    
HELIX    5   5 ASP A   96  LEU A  107  1                                  12    
HELIX    6   6 ARG A  119  GLU A  123  1                                   5    
HELIX    7   7 SER A  126  ALA A  135  1                                  10    
HELIX    8   8 LYS A  136  GLY A  138  5                                   3    
HELIX    9   9 HIS A  159  SER A  161  5                                   3    
HELIX   10  10 GLU A  162  GLN A  172  1                                  11    
HELIX   11  11 SER A  230  ALA A  247  1                                  18    
HELIX   12  12 SER A  281  GLY A  291  1                                  11    
HELIX   13  13 SER A  293  LEU A  304  1                                  12    
HELIX   14  14 GLU B   15  ALA B   33  1                                  19    
HELIX   15  15 PRO B   46  LEU B   50  5                                   5    
HELIX   16  16 GLY B   70  GLN B   80  1                                  11    
HELIX   17  17 GLY B   87  THR B   94  1                                   8    
HELIX   18  18 ASP B   96  GLY B  108  1                                  13    
HELIX   19  19 ARG B  119  LEU B  125  1                                   7    
HELIX   20  20 SER B  126  CYS B  133  1                                   8    
HELIX   21  21 VAL B  134  GLY B  138  5                                   5    
HELIX   22  22 GLU B  162  PHE B  171  1                                  10    
HELIX   23  23 SER B  230  LEU B  248  1                                  19    
HELIX   24  24 SER B  281  GLY B  291  1                                  11    
HELIX   25  25 SER B  293  LEU B  304  1                                  12    
SHEET    1   A 3 ALA A  37  ASP A  41  0                                        
SHEET    2   A 3 VAL A   5  LEU A   9  1  N  VAL A   5   O  TYR A  38           
SHEET    3   A 3 LYS A  57  ILE A  60  1  O  PHE A  59   N  ALA A   6           
SHEET    1   B 4 TYR A 114  ASN A 118  0                                        
SHEET    2   B 4 ASP A 176  LYS A 181 -1  O  ILE A 179   N  VAL A 115           
SHEET    3   B 4 LEU A 141  PRO A 145 -1  N  LYS A 144   O  LEU A 178           
SHEET    4   B 4 SER A 155  VAL A 157 -1  O  VAL A 157   N  LEU A 141           
SHEET    1   C 4 GLU A 196  VAL A 197  0                                        
SHEET    2   C 4 GLU A 187  LEU A 193 -1  N  LEU A 193   O  GLU A 196           
SHEET    3   C 4 ILE A 201  GLN A 204 -1  O  ILE A 203   N  GLU A 187           
SHEET    4   C 4 GLN A 222  PHE A 224 -1  O  GLN A 222   N  GLN A 204           
SHEET    1   D 4 GLU A 196  VAL A 197  0                                        
SHEET    2   D 4 GLU A 187  LEU A 193 -1  N  LEU A 193   O  GLU A 196           
SHEET    3   D 4 TRP A 253  GLN A 260 -1  O  VAL A 258   N  PHE A 188           
SHEET    4   D 4 PHE A 266  ASN A 272 -1  O  TYR A 267   N  MET A 259           
SHEET    1   E 3 ALA B  37  ASP B  41  0                                        
SHEET    2   E 3 VAL B   5  LEU B   9  1  N  VAL B   7   O  VAL B  40           
SHEET    3   E 3 LYS B  57  ILE B  60  1  O  PHE B  59   N  ALA B   6           
SHEET    1   F 4 TYR B 114  ASN B 118  0                                        
SHEET    2   F 4 ASP B 176  LYS B 181 -1  O  VAL B 177   N  LEU B 117           
SHEET    3   F 4 LEU B 141  PRO B 145 -1  N  LYS B 144   O  LEU B 178           
SHEET    4   F 4 SER B 155  VAL B 157 -1  O  VAL B 157   N  LEU B 141           
SHEET    1   G 5 GLN B 222  PHE B 224  0                                        
SHEET    2   G 5 GLU B 196  GLN B 204 -1  N  ARG B 202   O  PHE B 224           
SHEET    3   G 5 GLU B 187  LEU B 193 -1  N  GLU B 187   O  ILE B 203           
SHEET    4   G 5 TRP B 253  GLN B 260 -1  O  VAL B 258   N  PHE B 188           
SHEET    5   G 5 PHE B 266  ASN B 272 -1  O  GLU B 270   N  ASP B 257           
CISPEP   1 LEU A  139    PRO A  140          0         0.75                     
CISPEP   2 GLY A  185    PRO A  186          0         3.13                     
CISPEP   3 CYS A  225    PRO A  226          0        10.21                     
CISPEP   4 LEU B  139    PRO B  140          0        -0.02                     
CISPEP   5 GLY B  185    PRO B  186          0         4.23                     
CISPEP   6 CYS B  225    PRO B  226          0         0.34                     
SITE     1 AC1  4 ALA A  25  ALA A  28  PHE A 294  ALA B  25                    
SITE     1 AC2  4 PRO A 113  LYS A 181  ASP A 261  TYR A 267                    
CRYST1  100.637  100.637  110.304  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      0.009937  0.005737  0.000000        0.00000                         
SCALE2      0.000000  0.011474  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009066        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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