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Database: PDB
Entry: 3K3P
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HEADER    LIGASE                                  03-OCT-09   3K3P              
TITLE     CRYSTAL STRUCTURE OF THE APO FORM OF D-ALANINE:D-ALANINE LIGASE (DDL) 
TITLE    2 FROM STREPTOCOCCUS MUTANS                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: D-ALANYLALANINE SYNTHETASE, D-ALA-D-ALA LIGASE;             
COMPND   5 EC: 6.3.2.4;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS MUTANS;                           
SOURCE   3 ORGANISM_TAXID: 1309;                                                
SOURCE   4 STRAIN: UA159;                                                       
SOURCE   5 GENE: DDL;                                                           
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: PET28A(+)                                 
KEYWDS    D-ALANYL-ALANINE SYNTHETASE, ATP-BINDING, CELL SHAPE, CELL WALL       
KEYWDS   2 BIOGENESIS/DEGRADATION, LIGASE, MAGNESIUM, MANGANESE, METAL-BINDING, 
KEYWDS   3 NUCLEOTIDE-BINDING, PEPTIDOGLYCAN SYNTHESIS                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.LU                                                                  
REVDAT   1   15-SEP-10 3K3P    0                                                
JRNL        AUTH   Y.LU,H.XU,X.ZHAO                                             
JRNL        TITL   CRYSTAL STRUCTURE OF THE APO FORM OF D-ALANINE:D-ALANINE     
JRNL        TITL 2 LIGASE (DDL) FROM STREPTOCOCCUS MUTANS                       
JRNL        REF    PROTEIN PEPT.LETT.            V.  17  1053 2010              
JRNL        REFN                   ISSN 0929-8665                               
JRNL        PMID   20522004                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.23 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.23                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 17.58                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 37611                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1921                            
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) : 2.23                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.29                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2628                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.71                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2420                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 141                          
REMARK   3   BIN FREE R VALUE                    : 0.3340                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4930                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 150                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.256         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.212         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5001 ; 0.023 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6766 ; 1.930 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   625 ; 7.000 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   208 ;36.461 ;25.577       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   909 ;15.943 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;23.728 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   804 ; 0.125 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3648 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2232 ; 0.215 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3421 ; 0.313 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   232 ; 0.149 ; 0.200       
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):    42 ; 0.227 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.122 ; 0.200       
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):  3156 ; 1.170 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5118 ; 2.105 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1845 ; 3.155 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1648 ; 4.752 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3K3P COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-OCT-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055506.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : SEALED TUBE                        
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : OXFORD DIFFRACTION ENHANCE ULTRA   
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54056                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : OXFORD ONYX CCD                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO                        
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37656                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.230                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 68.850                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.09200                            
REMARK 200  R SYM                      (I) : 0.09200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.60500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2I87                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M MAGNESIUM SULFATE, 0.05M HEPES,    
REMARK 280  1.2M LITHIUM SULFATE, PH 7.0, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 289K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,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       72.93333            
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       36.46667            
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: 3120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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     MET A   -33                                                      
REMARK 465     GLY A   -32                                                      
REMARK 465     SER A   -31                                                      
REMARK 465     SER A   -30                                                      
REMARK 465     HIS A   -29                                                      
REMARK 465     HIS A   -28                                                      
REMARK 465     HIS A   -27                                                      
REMARK 465     HIS A   -26                                                      
REMARK 465     HIS A   -25                                                      
REMARK 465     HIS A   -24                                                      
REMARK 465     SER A   -23                                                      
REMARK 465     SER A   -22                                                      
REMARK 465     GLY A   -21                                                      
REMARK 465     LEU A   -20                                                      
REMARK 465     VAL A   -19                                                      
REMARK 465     PRO A   -18                                                      
REMARK 465     ARG A   -17                                                      
REMARK 465     GLY A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     MET A   -13                                                      
REMARK 465     ALA A   -12                                                      
REMARK 465     SER A   -11                                                      
REMARK 465     MET A   -10                                                      
REMARK 465     THR A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     GLN A    -6                                                      
REMARK 465     GLN A    -5                                                      
REMARK 465     MET A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     ARG A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLU A    61                                                      
REMARK 465     THR A    62                                                      
REMARK 465     MET A   177                                                      
REMARK 465     GLY A   178                                                      
REMARK 465     SER A   179                                                      
REMARK 465     SER A   180                                                      
REMARK 465     VAL A   181                                                      
REMARK 465     GLY A   182                                                      
REMARK 465     LYS A   237                                                      
REMARK 465     ASP A   238                                                      
REMARK 465     VAL A   239                                                      
REMARK 465     ALA A   240                                                      
REMARK 465     PHE A   241                                                      
REMARK 465     TYR A   242                                                      
REMARK 465     ASP A   243                                                      
REMARK 465     TYR A   244                                                      
REMARK 465     GLU A   245                                                      
REMARK 465     ALA A   246                                                      
REMARK 465     LYS A   247                                                      
REMARK 465     TYR A   248                                                      
REMARK 465     ILE A   249                                                      
REMARK 465     ASP A   250                                                      
REMARK 465     ASN A   251                                                      
REMARK 465     LYS A   252                                                      
REMARK 465     ILE A   253                                                      
REMARK 465     GLN A   311                                                      
REMARK 465     TRP A   312                                                      
REMARK 465     HIS A   347                                                      
REMARK 465     LEU A   348                                                      
REMARK 465     VAL A   349                                                      
REMARK 465     MET B   -33                                                      
REMARK 465     GLY B   -32                                                      
REMARK 465     SER B   -31                                                      
REMARK 465     SER B   -30                                                      
REMARK 465     HIS B   -29                                                      
REMARK 465     HIS B   -28                                                      
REMARK 465     HIS B   -27                                                      
REMARK 465     HIS B   -26                                                      
REMARK 465     HIS B   -25                                                      
REMARK 465     HIS B   -24                                                      
REMARK 465     SER B   -23                                                      
REMARK 465     SER B   -22                                                      
REMARK 465     GLY B   -21                                                      
REMARK 465     LEU B   -20                                                      
REMARK 465     VAL B   -19                                                      
REMARK 465     PRO B   -18                                                      
REMARK 465     ARG B   -17                                                      
REMARK 465     GLY B   -16                                                      
REMARK 465     SER B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     MET B   -13                                                      
REMARK 465     ALA B   -12                                                      
REMARK 465     SER B   -11                                                      
REMARK 465     MET B   -10                                                      
REMARK 465     THR B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     GLN B    -6                                                      
REMARK 465     GLN B    -5                                                      
REMARK 465     MET B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     ARG B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLU B    61                                                      
REMARK 465     THR B    62                                                      
REMARK 465     MET B   177                                                      
REMARK 465     GLY B   178                                                      
REMARK 465     SER B   179                                                      
REMARK 465     SER B   180                                                      
REMARK 465     VAL B   181                                                      
REMARK 465     LYS B   237                                                      
REMARK 465     ASP B   238                                                      
REMARK 465     VAL B   239                                                      
REMARK 465     ALA B   240                                                      
REMARK 465     PHE B   241                                                      
REMARK 465     TYR B   242                                                      
REMARK 465     ASP B   243                                                      
REMARK 465     TYR B   244                                                      
REMARK 465     GLU B   245                                                      
REMARK 465     ALA B   246                                                      
REMARK 465     LYS B   247                                                      
REMARK 465     TYR B   248                                                      
REMARK 465     ILE B   249                                                      
REMARK 465     ASP B   250                                                      
REMARK 465     ASN B   251                                                      
REMARK 465     LYS B   252                                                      
REMARK 465     ILE B   253                                                      
REMARK 465     GLN B   311                                                      
REMARK 465     TRP B   312                                                      
REMARK 465     HIS B   347                                                      
REMARK 465     LEU B   348                                                      
REMARK 465     VAL B   349                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     SER B   60   OG                                                  
DBREF  3K3P A    1   349  UNP    P95803   DDL_STRMU        1    349             
DBREF  3K3P B    1   349  UNP    P95803   DDL_STRMU        1    349             
SEQADV 3K3P MET A  -33  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P GLY A  -32  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P SER A  -31  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P SER A  -30  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P HIS A  -29  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P HIS A  -28  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P HIS A  -27  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P HIS A  -26  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P HIS A  -25  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P HIS A  -24  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P SER A  -23  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P SER A  -22  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P GLY A  -21  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P LEU A  -20  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P VAL A  -19  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P PRO A  -18  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P ARG A  -17  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P GLY A  -16  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P SER A  -15  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P HIS A  -14  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P MET A  -13  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P ALA A  -12  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P SER A  -11  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P MET A  -10  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P THR A   -9  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P GLY A   -8  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P GLY A   -7  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P GLN A   -6  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P GLN A   -5  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P MET A   -4  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P GLY A   -3  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P ARG A   -2  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P GLY A   -1  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P SER A    0  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P MET B  -33  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P GLY B  -32  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P SER B  -31  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P SER B  -30  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P HIS B  -29  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P HIS B  -28  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P HIS B  -27  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P HIS B  -26  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P HIS B  -25  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P HIS B  -24  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P SER B  -23  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P SER B  -22  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P GLY B  -21  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P LEU B  -20  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P VAL B  -19  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P PRO B  -18  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P ARG B  -17  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P GLY B  -16  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P SER B  -15  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P HIS B  -14  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P MET B  -13  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P ALA B  -12  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P SER B  -11  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P MET B  -10  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P THR B   -9  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P GLY B   -8  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P GLY B   -7  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P GLN B   -6  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P GLN B   -5  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P MET B   -4  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P GLY B   -3  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P ARG B   -2  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P GLY B   -1  UNP  P95803              EXPRESSION TAG                 
SEQADV 3K3P SER B    0  UNP  P95803              EXPRESSION TAG                 
SEQRES   1 A  383  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  383  LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY          
SEQRES   3 A  383  GLY GLN GLN MET GLY ARG GLY SER MET SER LYS GLU THR          
SEQRES   4 A  383  LEU VAL LEU LEU TYR GLY GLY ARG SER ALA GLU ARG ASP          
SEQRES   5 A  383  VAL SER VAL LEU SER ALA GLU SER VAL MET ARG ALA ILE          
SEQRES   6 A  383  ASN TYR ASP ASN PHE LEU VAL LYS THR TYR PHE ILE THR          
SEQRES   7 A  383  GLN ALA GLY ASP PHE ILE LYS THR GLN GLU PHE ASP SER          
SEQRES   8 A  383  GLN PRO SER GLU THR ASP LYS LEU MET THR ASN ASP THR          
SEQRES   9 A  383  ILE ILE ALA SER GLN LYS ILE LYS PRO SER ASP ILE TYR          
SEQRES  10 A  383  GLU GLU GLU ALA VAL VAL PHE PRO VAL LEU HIS GLY PRO          
SEQRES  11 A  383  MET GLY GLU ASP GLY SER ILE GLN GLY PHE LEU GLU VAL          
SEQRES  12 A  383  LEU LYS MET PRO TYR VAL GLY THR ASN ILE LEU SER SER          
SEQRES  13 A  383  SER VAL ALA MET ASP LYS ILE THR THR ASN GLN VAL LEU          
SEQRES  14 A  383  GLU SER ALA THR THR ILE PRO GLN VAL ALA TYR VAL ALA          
SEQRES  15 A  383  LEU ILE GLU GLY GLU PRO LEU GLU SER LYS LEU ALA GLU          
SEQRES  16 A  383  VAL GLU GLU LYS LEU ILE TYR PRO VAL PHE VAL LYS PRO          
SEQRES  17 A  383  ALA ASN MET GLY SER SER VAL GLY ILE SER LYS ALA GLU          
SEQRES  18 A  383  ASN ARG THR ASP LEU LYS GLN ALA ILE ALA LEU ALA LEU          
SEQRES  19 A  383  LYS TYR ASP SER ARG VAL LEU ILE GLU GLN GLY VAL ASP          
SEQRES  20 A  383  ALA ARG GLU ILE GLU VAL GLY ILE LEU GLY ASN THR ASP          
SEQRES  21 A  383  VAL LYS THR THR LEU PRO GLY GLU ILE VAL LYS ASP VAL          
SEQRES  22 A  383  ALA PHE TYR ASP TYR GLU ALA LYS TYR ILE ASP ASN LYS          
SEQRES  23 A  383  ILE THR MET ALA ILE PRO ALA GLU ILE ASP PRO VAL ILE          
SEQRES  24 A  383  VAL GLU LYS MET ARG ASP TYR ALA ALA THR ALA PHE ARG          
SEQRES  25 A  383  THR LEU GLY CYS CYS GLY LEU SER ARG CYS ASP PHE PHE          
SEQRES  26 A  383  LEU THR GLU ASP GLY LYS VAL TYR LEU ASN GLU LEU ASN          
SEQRES  27 A  383  THR MET PRO GLY PHE THR GLN TRP SER MET TYR PRO LEU          
SEQRES  28 A  383  LEU TRP GLU ASN MET GLY LEU SER TYR SER VAL LEU ILE          
SEQRES  29 A  383  GLU GLU LEU VAL SER LEU ALA LYS GLU MET PHE ASP LYS          
SEQRES  30 A  383  ARG GLU SER HIS LEU VAL                                      
SEQRES   1 B  383  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  383  LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY          
SEQRES   3 B  383  GLY GLN GLN MET GLY ARG GLY SER MET SER LYS GLU THR          
SEQRES   4 B  383  LEU VAL LEU LEU TYR GLY GLY ARG SER ALA GLU ARG ASP          
SEQRES   5 B  383  VAL SER VAL LEU SER ALA GLU SER VAL MET ARG ALA ILE          
SEQRES   6 B  383  ASN TYR ASP ASN PHE LEU VAL LYS THR TYR PHE ILE THR          
SEQRES   7 B  383  GLN ALA GLY ASP PHE ILE LYS THR GLN GLU PHE ASP SER          
SEQRES   8 B  383  GLN PRO SER GLU THR ASP LYS LEU MET THR ASN ASP THR          
SEQRES   9 B  383  ILE ILE ALA SER GLN LYS ILE LYS PRO SER ASP ILE TYR          
SEQRES  10 B  383  GLU GLU GLU ALA VAL VAL PHE PRO VAL LEU HIS GLY PRO          
SEQRES  11 B  383  MET GLY GLU ASP GLY SER ILE GLN GLY PHE LEU GLU VAL          
SEQRES  12 B  383  LEU LYS MET PRO TYR VAL GLY THR ASN ILE LEU SER SER          
SEQRES  13 B  383  SER VAL ALA MET ASP LYS ILE THR THR ASN GLN VAL LEU          
SEQRES  14 B  383  GLU SER ALA THR THR ILE PRO GLN VAL ALA TYR VAL ALA          
SEQRES  15 B  383  LEU ILE GLU GLY GLU PRO LEU GLU SER LYS LEU ALA GLU          
SEQRES  16 B  383  VAL GLU GLU LYS LEU ILE TYR PRO VAL PHE VAL LYS PRO          
SEQRES  17 B  383  ALA ASN MET GLY SER SER VAL GLY ILE SER LYS ALA GLU          
SEQRES  18 B  383  ASN ARG THR ASP LEU LYS GLN ALA ILE ALA LEU ALA LEU          
SEQRES  19 B  383  LYS TYR ASP SER ARG VAL LEU ILE GLU GLN GLY VAL ASP          
SEQRES  20 B  383  ALA ARG GLU ILE GLU VAL GLY ILE LEU GLY ASN THR ASP          
SEQRES  21 B  383  VAL LYS THR THR LEU PRO GLY GLU ILE VAL LYS ASP VAL          
SEQRES  22 B  383  ALA PHE TYR ASP TYR GLU ALA LYS TYR ILE ASP ASN LYS          
SEQRES  23 B  383  ILE THR MET ALA ILE PRO ALA GLU ILE ASP PRO VAL ILE          
SEQRES  24 B  383  VAL GLU LYS MET ARG ASP TYR ALA ALA THR ALA PHE ARG          
SEQRES  25 B  383  THR LEU GLY CYS CYS GLY LEU SER ARG CYS ASP PHE PHE          
SEQRES  26 B  383  LEU THR GLU ASP GLY LYS VAL TYR LEU ASN GLU LEU ASN          
SEQRES  27 B  383  THR MET PRO GLY PHE THR GLN TRP SER MET TYR PRO LEU          
SEQRES  28 B  383  LEU TRP GLU ASN MET GLY LEU SER TYR SER VAL LEU ILE          
SEQRES  29 B  383  GLU GLU LEU VAL SER LEU ALA LYS GLU MET PHE ASP LYS          
SEQRES  30 B  383  ARG GLU SER HIS LEU VAL                                      
FORMUL   3  HOH   *150(H2 O)                                                    
HELIX    1   1 GLU A   16  ILE A   31  1                                  16    
HELIX    2   2 ILE A   72  SER A   74  5                                   3    
HELIX    3   3 LYS A   78  TYR A   83  5                                   6    
HELIX    4   4 GLY A  101  LEU A  110  1                                  10    
HELIX    5   5 ASN A  118  ASP A  127  1                                  10    
HELIX    6   6 ASP A  127  THR A  139  1                                  13    
HELIX    7   7 PRO A  154  LEU A  166  1                                  13    
HELIX    8   8 ASN A  188  ASP A  203  1                                  16    
HELIX    9   9 ASP A  262  LEU A  280  1                                  19    
HELIX   10  10 SER A  313  MET A  322  1                                  10    
HELIX   11  11 SER A  325  SER A  346  1                                  22    
HELIX   12  12 GLU B   16  ILE B   31  1                                  16    
HELIX   13  13 ILE B   72  SER B   74  5                                   3    
HELIX   14  14 LYS B   78  TYR B   83  5                                   6    
HELIX   15  15 GLY B  101  LEU B  110  1                                  10    
HELIX   16  16 ASN B  118  ASP B  127  1                                  10    
HELIX   17  17 ASP B  127  THR B  139  1                                  13    
HELIX   18  18 PRO B  154  LEU B  166  1                                  13    
HELIX   19  19 ASN B  188  ASP B  203  1                                  16    
HELIX   20  20 ASP B  262  GLY B  281  1                                  20    
HELIX   21  21 SER B  313  MET B  322  1                                  10    
HELIX   22  22 SER B  325  SER B  346  1                                  22    
SHEET    1   A 5 LYS A  76  ILE A  77  0                                        
SHEET    2   A 5 PHE A  49  PHE A  55 -1  N  PHE A  49   O  ILE A  77           
SHEET    3   A 5 PHE A  36  ILE A  43 -1  N  PHE A  42   O  ILE A  50           
SHEET    4   A 5 GLU A   4  GLY A  11  1  N  LEU A   6   O  LYS A  39           
SHEET    5   A 5 VAL A  88  VAL A  92  1  O  VAL A  92   N  LEU A   9           
SHEET    1   B 4 TYR A 146  ILE A 150  0                                        
SHEET    2   B 4 ARG A 205  GLN A 210 -1  O  VAL A 206   N  LEU A 149           
SHEET    3   B 4 VAL A 170  PRO A 174 -1  N  LYS A 173   O  LEU A 207           
SHEET    4   B 4 SER A 184  ALA A 186 -1  O  SER A 184   N  VAL A 172           
SHEET    1   C 3 LYS A 228  THR A 229  0                                        
SHEET    2   C 3 ARG A 215  GLY A 223 -1  N  LEU A 222   O  LYS A 228           
SHEET    3   C 3 GLY A 233  ILE A 235 -1  O  GLY A 233   N  GLU A 218           
SHEET    1   D 4 LYS A 228  THR A 229  0                                        
SHEET    2   D 4 ARG A 215  GLY A 223 -1  N  LEU A 222   O  LYS A 228           
SHEET    3   D 4 GLY A 284  LEU A 292 -1  O  PHE A 290   N  ILE A 217           
SHEET    4   D 4 VAL A 298  ASN A 304 -1  O  GLU A 302   N  ASP A 289           
SHEET    1   E 5 LYS B  76  ILE B  77  0                                        
SHEET    2   E 5 PHE B  49  PHE B  55 -1  N  PHE B  49   O  ILE B  77           
SHEET    3   E 5 PHE B  36  ILE B  43 -1  N  PHE B  42   O  ILE B  50           
SHEET    4   E 5 GLU B   4  GLY B  11  1  N  GLU B   4   O  LEU B  37           
SHEET    5   E 5 VAL B  88  VAL B  92  1  O  PHE B  90   N  VAL B   7           
SHEET    1   F 4 TYR B 146  ILE B 150  0                                        
SHEET    2   F 4 ARG B 205  GLN B 210 -1  O  VAL B 206   N  LEU B 149           
SHEET    3   F 4 VAL B 170  PRO B 174 -1  N  PHE B 171   O  GLU B 209           
SHEET    4   F 4 SER B 184  ALA B 186 -1  O  ALA B 186   N  VAL B 170           
SHEET    1   G 3 LYS B 228  THR B 229  0                                        
SHEET    2   G 3 ARG B 215  GLY B 223 -1  N  LEU B 222   O  LYS B 228           
SHEET    3   G 3 GLY B 233  ILE B 235 -1  O  GLY B 233   N  GLU B 218           
SHEET    1   H 4 LYS B 228  THR B 229  0                                        
SHEET    2   H 4 ARG B 215  GLY B 223 -1  N  LEU B 222   O  LYS B 228           
SHEET    3   H 4 GLY B 284  LEU B 292 -1  O  PHE B 290   N  ILE B 217           
SHEET    4   H 4 VAL B 298  ASN B 304 -1  O  ASN B 304   N  ARG B 287           
CISPEP   1 TYR A  168    PRO A  169          0        -1.54                     
CISPEP   2 ILE A  257    PRO A  258          0        -2.65                     
CISPEP   3 TYR B  168    PRO B  169          0        -6.08                     
CISPEP   4 ILE B  257    PRO B  258          0        -3.94                     
CRYST1   79.502   79.502  109.400  90.00  90.00 120.00 P 32          6          
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      0.012578  0.007262  0.000000        0.00000                         
SCALE2      0.000000  0.014524  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009141        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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