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Database: PDB
Entry: 3D3U
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Original site: 3D3U 
HEADER    TRANSFERASE                             12-MAY-08   3D3U              
TITLE     CRYSTAL STRUCTURE OF 4-HYDROXYBUTYRATE COA-TRANSFERASE (ABFT-2) FROM  
TITLE    2 PORPHYROMONAS GINGIVALIS. NORTHEAST STRUCTURAL GENOMICS CONSORTIUM   
TITLE    3 TARGET PGR26                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 4-HYDROXYBUTYRATE COA-TRANSFERASE;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PORPHYROMONAS GINGIVALIS;                       
SOURCE   3 ORGANISM_TAXID: 242619;                                              
SOURCE   4 STRAIN: W83;                                                         
SOURCE   5 ATCC: BAA-308;                                                       
SOURCE   6 GENE: ABFT-2, PG_1956;                                               
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21                                     
KEYWDS    ALPHA-BETA PROTEIN, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE     
KEYWDS   2 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG,          
KEYWDS   3 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.FOROUHAR,H.NEELY,X.-Z.ZHANG,W.N.PRICE II,M.HUSSAIN,J.SEETHARAMAN,   
AUTHOR   2 R.XIAO,K.CONOVER,K.CUNNINGHAM,L.-C.MA,C.K.HO,J.K.EVERETT,T.B.ACTON,  
AUTHOR   3 G.T.MONTELIONE,J.F.HUNT,L.TONG,NORTHEAST STRUCTURAL GENOMICS         
AUTHOR   4 CONSORTIUM (NESG)                                                    
REVDAT   5   24-JAN-18 3D3U    1       AUTHOR JRNL                              
REVDAT   4   25-OCT-17 3D3U    1       REMARK                                   
REVDAT   3   13-JUL-11 3D3U    1       VERSN                                    
REVDAT   2   24-FEB-09 3D3U    1       VERSN                                    
REVDAT   1   15-JUL-08 3D3U    0                                                
JRNL        AUTH   F.FOROUHAR,H.NEELY,X.-Z.ZHANG,W.N.PRICE II,M.HUSSAIN,        
JRNL        AUTH 2 J.SEETHARAMAN,R.XIAO,K.CONOVER,K.CUNNINGHAM,L.-C.MA,C.K.HO,  
JRNL        AUTH 3 J.K.EVERETT,T.B.ACTON,G.T.MONTELIONE,J.F.HUNT,L.TONG         
JRNL        TITL   CRYSTAL STRUCTURE OF 4-HYDROXYBUTYRATE COA-TRANSFERASE       
JRNL        TITL 2 (ABFT-2) FROM PORPHYROMONAS GINGIVALIS.                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0003                                      
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.35                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 10089                          
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) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 505                             
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 648                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2340                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 34                           
REMARK   3   BIN FREE R VALUE                    : 0.3320                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3018                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 20                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 28.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.43000                                              
REMARK   3    B22 (A**2) : -1.98000                                             
REMARK   3    B33 (A**2) : 0.55000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.406         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.302         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.071        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.923                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.880                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3077 ; 0.033 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4157 ; 2.806 ; 1.948       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   382 ; 7.975 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   141 ;40.745 ;23.688       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   534 ;25.220 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;16.766 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   465 ; 0.177 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2327 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1633 ; 0.299 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2105 ; 0.350 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   104 ; 0.198 ; 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):    17 ; 0.340 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.121 ; 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):  1973 ; 1.219 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3104 ; 2.075 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1229 ; 3.575 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1053 ; 5.599 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
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   430                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.3542   5.1715  15.1827              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0329 T22:   0.0237                                     
REMARK   3      T33:  -0.0019 T12:   0.0121                                     
REMARK   3      T13:   0.0016 T23:  -0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6884 L22:   1.3709                                     
REMARK   3      L33:   1.4346 L12:   0.3462                                     
REMARK   3      L13:  -0.1697 L23:  -1.1791                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0297 S12:   0.0584 S13:  -0.1483                       
REMARK   3      S21:  -0.0810 S22:   0.0072 S23:  -0.0954                       
REMARK   3      S31:   0.1341 S32:  -0.0506 S33:   0.0225                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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: THE FRIEDEL PAIRS WERE USED IN PHASING.   
REMARK   3  PROGRAM CNS 1.2 HAS ALSO BEEN USED IN REFINEMENT                    
REMARK   4                                                                      
REMARK   4 3D3U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000047557.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4C                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97900                            
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21251                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.350                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.11200                            
REMARK 200  R SYM                      (I) : 0.09700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.4300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.32400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.250                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SNB, SOLVE, RESOLVE                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THE STRUCTURE FACTOR FILE CONTAINS FRIEDEL PAIRS             
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 20 MM TRIS-HCL PH      
REMARK 280  7.5, 100 MM NACL, 5 MM ACETYL-COA. RESERVOIR SOLUTION: 200 MM       
REMARK 280  AMMONIUM CITRATE PH 5.0, 20% PEG 3350, VAPOR DIFFUSION, SITTING     
REMARK 280  DROP, TEMPERATURE 292K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       27.34200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.75200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.63950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       46.75200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.34200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.63950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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     1                                                      
REMARK 465     ASN A    81                                                      
REMARK 465     PHE A    82                                                      
REMARK 465     LEU A    83                                                      
REMARK 465     GLU A    84                                                      
REMARK 465     GLY A    85                                                      
REMARK 465     ASN A    86                                                      
REMARK 465     SER A    87                                                      
REMARK 465     ARG A    88                                                      
REMARK 465     PRO A    89                                                      
REMARK 465     ALA A    90                                                      
REMARK 465     SER A    91                                                      
REMARK 465     ARG A    92                                                      
REMARK 465     ASP A    93                                                      
REMARK 465     ARG A    94                                                      
REMARK 465     ARG A    95                                                      
REMARK 465     VAL A    96                                                      
REMARK 465     ASP A    97                                                      
REMARK 465     PHE A    98                                                      
REMARK 465     ILE A    99                                                      
REMARK 465     PRO A   100                                                      
REMARK 465     PRO A   190                                                      
REMARK 465     ALA A   191                                                      
REMARK 465     ALA A   323                                                      
REMARK 465     SER A   324                                                      
REMARK 465     GLU A   325                                                      
REMARK 465     SER A   326                                                      
REMARK 465     ILE A   327                                                      
REMARK 465     GLY A   328                                                      
REMARK 465     TYR A   329                                                      
REMARK 465     GLU A   330                                                      
REMARK 465     GLN A   331                                                      
REMARK 465     PHE A   332                                                      
REMARK 465     SER A   333                                                      
REMARK 465     GLY A   334                                                      
REMARK 465     SER A   335                                                      
REMARK 465     GLY A   336                                                      
REMARK 465     GLU A   375                                                      
REMARK 465     GLY A   376                                                      
REMARK 465     ALA A   377                                                      
REMARK 465     CYS A   378                                                      
REMARK 465     VAL A   379                                                      
REMARK 465     THR A   380                                                      
REMARK 465     GLU A   431                                                      
REMARK 465     LEU A   432                                                      
REMARK 465     GLU A   433                                                      
REMARK 465     HIS A   434                                                      
REMARK 465     HIS A   435                                                      
REMARK 465     HIS A   436                                                      
REMARK 465     HIS A   437                                                      
REMARK 465     HIS A   438                                                      
REMARK 465     HIS A   439                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    VAL A  11   CB    VAL A  11   CG1    -0.137                       
REMARK 500    TYR A  61   CB    TYR A  61   CG      0.121                       
REMARK 500    TYR A  61   CG    TYR A  61   CD2     0.093                       
REMARK 500    TYR A  61   CG    TYR A  61   CD1     0.083                       
REMARK 500    TYR A  61   CD1   TYR A  61   CE1     0.138                       
REMARK 500    TYR A  61   CE2   TYR A  61   CD2     0.117                       
REMARK 500    GLY A  63   N     GLY A  63   CA      0.124                       
REMARK 500    ALA A  65   CA    ALA A  65   CB      0.181                       
REMARK 500    PHE A 115   CE1   PHE A 115   CZ      0.128                       
REMARK 500    TYR A 141   CZ    TYR A 141   CE2    -0.079                       
REMARK 500    GLU A 182   CG    GLU A 182   CD      0.096                       
REMARK 500    GLU A 182   CD    GLU A 182   OE1     0.069                       
REMARK 500    PRO A 189   N     PRO A 189   CA      0.102                       
REMARK 500    LYS A 346   CB    LYS A 346   CG      0.177                       
REMARK 500    MET A 355   CG    MET A 355   SD      0.166                       
REMARK 500    PHE A 357   CZ    PHE A 357   CE2     0.135                       
REMARK 500    GLU A 392   CD    GLU A 392   OE1     0.088                       
REMARK 500    ARG A 399   CG    ARG A 399   CD      0.177                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A   6   CB  -  CG  -  CD1 ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ASP A  15   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ASP A  20   CB  -  CG  -  OD2 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ARG A  46   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    HIS A  67   CB  -  CA  -  C   ANGL. DEV. = -15.6 DEGREES          
REMARK 500    GLU A  71   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.0 DEGREES          
REMARK 500    CYS A 101   CA  -  CB  -  SG  ANGL. DEV. = -13.0 DEGREES          
REMARK 500    LEU A 109   CB  -  CG  -  CD2 ANGL. DEV. = -11.1 DEGREES          
REMARK 500    ASP A 181   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    LEU A 188   CA  -  CB  -  CG  ANGL. DEV. =  14.3 DEGREES          
REMARK 500    ASP A 209   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    LEU A 225   CB  -  CG  -  CD2 ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ARG A 226   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ASP A 293   CB  -  CG  -  OD2 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    LEU A 314   CB  -  CG  -  CD2 ANGL. DEV. =  10.9 DEGREES          
REMARK 500    ARG A 343   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    MET A 355   CG  -  SD  -  CE  ANGL. DEV. =  10.8 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    LEU A  22       69.76   -112.00                                   
REMARK 500    PRO A  24      143.42    -39.75                                   
REMARK 500    ALA A  33     -118.71     81.17                                   
REMARK 500    GLU A  52     -102.35   -104.61                                   
REMARK 500    ASN A  53       69.59   -102.79                                   
REMARK 500    HIS A  58     -171.64   -170.96                                   
REMARK 500    MET A  59     -108.80   -138.45                                   
REMARK 500    ASP A  64       67.34    -31.77                                   
REMARK 500    ALA A  65      -80.72    -71.39                                   
REMARK 500    PRO A  66       79.87    -41.27                                   
REMARK 500    HIS A  67      -34.63   -152.47                                   
REMARK 500    SER A  74       -6.54     79.98                                   
REMARK 500    PHE A 103      -45.86    -29.44                                   
REMARK 500    ARG A 111       22.99    -77.45                                   
REMARK 500    GLN A 112       -6.14   -159.53                                   
REMARK 500    PRO A 116       69.69    -67.38                                   
REMARK 500    ASN A 128     -167.57   -111.67                                   
REMARK 500    ASP A 140     -102.08     12.77                                   
REMARK 500    GLU A 182      130.21    178.05                                   
REMARK 500    ALA A 185      140.46    -32.02                                   
REMARK 500    SER A 193      161.67    147.51                                   
REMARK 500    ASP A 194      -91.37    -35.98                                   
REMARK 500    HIS A 237       79.95   -152.60                                   
REMARK 500    THR A 242     -160.08   -122.44                                   
REMARK 500    ASN A 255       -7.77   -144.61                                   
REMARK 500    LYS A 259      127.34    -29.82                                   
REMARK 500    ASP A 293       21.65    -70.68                                   
REMARK 500    TYR A 294      -59.37   -142.89                                   
REMARK 500    LEU A 318       10.87    -60.11                                   
REMARK 500    ASN A 384       41.74    -43.42                                   
REMARK 500    GLU A 385      -70.69   -122.02                                   
REMARK 500    GLU A 392      -19.69    -42.52                                   
REMARK 500    LEU A 403      -52.94    -23.77                                   
REMARK 500    ARG A 429        6.70    176.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: PGR26   RELATED DB: TARGETDB                             
DBREF  3D3U A    1   431  UNP    Q7MTJ6   Q7MTJ6_PORGI     1    431             
SEQADV 3D3U GLY A  192  UNP  Q7MTJ6    ILE   192 EXPRESSION TAG                 
SEQADV 3D3U LEU A  432  UNP  Q7MTJ6              EXPRESSION TAG                 
SEQADV 3D3U GLU A  433  UNP  Q7MTJ6              EXPRESSION TAG                 
SEQADV 3D3U HIS A  434  UNP  Q7MTJ6              EXPRESSION TAG                 
SEQADV 3D3U HIS A  435  UNP  Q7MTJ6              EXPRESSION TAG                 
SEQADV 3D3U HIS A  436  UNP  Q7MTJ6              EXPRESSION TAG                 
SEQADV 3D3U HIS A  437  UNP  Q7MTJ6              EXPRESSION TAG                 
SEQADV 3D3U HIS A  438  UNP  Q7MTJ6              EXPRESSION TAG                 
SEQADV 3D3U HIS A  439  UNP  Q7MTJ6              EXPRESSION TAG                 
SEQRES   1 A  439  MET GLN TRP GLN GLU LEU TYR ARG GLN ARG VAL CYS SER          
SEQRES   2 A  439  ALA ASP GLU ALA VAL VAL ASP SER LEU LYS PRO GLY THR          
SEQRES   3 A  439  LYS VAL VAL PHE GLY HIS ALA ALA ALA ALA PRO VAL ARG          
SEQRES   4 A  439  PHE SER GLN ALA MET TYR ARG GLN ARG GLU LYS LEU GLU          
SEQRES   5 A  439  ASN ILE THR VAL PHE HIS MET LEU TYR PHE GLY ASP ALA          
SEQRES   6 A  439  PRO HIS LEU ALA PRO GLU MET ARG SER HIS VAL HIS PRO          
SEQRES   7 A  439  THR LEU ASN PHE LEU GLU GLY ASN SER ARG PRO ALA SER          
SEQRES   8 A  439  ARG ASP ARG ARG VAL ASP PHE ILE PRO CYS HIS PHE HIS          
SEQRES   9 A  439  GLU VAL PRO GLU LEU PHE ARG GLN GLY PHE PHE PRO LEU          
SEQRES  10 A  439  ASP VAL ALA VAL VAL GLN VAL SER THR PRO ASN GLU GLU          
SEQRES  11 A  439  GLY TYR CYS SER PHE GLY VAL SER CYS ASP TYR THR LYS          
SEQRES  12 A  439  ALA ALA ALA GLU CYS ALA PRO VAL VAL VAL ALA GLU VAL          
SEQRES  13 A  439  ASN LYS GLN MET PRO PHE ILE GLY GLY GLU ASN LEU ILE          
SEQRES  14 A  439  HIS ILE SER LYS LEU THR HIS ILE ILE GLU VAL ASP GLU          
SEQRES  15 A  439  PRO ILE ALA GLU VAL LEU PRO PRO ALA GLY SER ASP LEU          
SEQRES  16 A  439  GLU LEU ARG ILE GLY GLN ASN CYS ALA SER LEU ILE LYS          
SEQRES  17 A  439  ASP GLY ASP THR LEU GLN LEU GLY ILE GLY GLY ILE PRO          
SEQRES  18 A  439  ASP ALA VAL LEU ARG ALA LEU GLU GLY HIS LYS ASP LEU          
SEQRES  19 A  439  GLY ILE HIS THR GLU MET PHE THR ASP GLY VAL MET ARG          
SEQRES  20 A  439  MET ILE ARG LYS GLY ILE ILE ASN GLY LYS LYS LYS THR          
SEQRES  21 A  439  LEU HIS PRO GLU LYS VAL VAL THR SER LEU ILE PHE GLY          
SEQRES  22 A  439  SER LYS GLU LEU TYR ASP PHE VAL ASN ASN ASN PRO VAL          
SEQRES  23 A  439  ILE GLU CYS TYR PRO VAL ASP TYR ILE ASN ASN PRO ASP          
SEQRES  24 A  439  VAL ILE GLY LYS ASN ASP ARG MET VAL SER ILE ASN SER          
SEQRES  25 A  439  CYS LEU GLU MET ASP LEU MET GLY GLN ALA ALA SER GLU          
SEQRES  26 A  439  SER ILE GLY TYR GLU GLN PHE SER GLY SER GLY GLY GLN          
SEQRES  27 A  439  VAL ASP PHE LEU ARG GLY ALA LYS ARG SER LYS GLY GLY          
SEQRES  28 A  439  ILE SER ILE MET ALA PHE PRO SER THR ALA LYS LYS GLY          
SEQRES  29 A  439  THR GLU SER ARG ILE VAL PRO ILE LEU LYS GLU GLY ALA          
SEQRES  30 A  439  CYS VAL THR THR GLY ARG ASN GLU VAL ASP TYR VAL VAL          
SEQRES  31 A  439  THR GLU TYR GLY VAL ALA ARG LEU ARG GLY ALA THR LEU          
SEQRES  32 A  439  ARG GLN ARG ALA GLU ALA LEU THR ALA ILE ALA HIS PRO          
SEQRES  33 A  439  ASP PHE ARG PRO ALA LEU GLU GLU GLU ILE ARG ARG ARG          
SEQRES  34 A  439  PHE GLU LEU GLU HIS HIS HIS HIS HIS HIS                      
FORMUL   2  HOH   *20(H2 O)                                                     
HELIX    1   1 TRP A    3  VAL A   11  1                                   9    
HELIX    2   2 SER A   13  LEU A   22  1                                  10    
HELIX    3   3 HIS A   32  ALA A   36  5                                   5    
HELIX    4   4 PRO A   37  GLN A   47  1                                  11    
HELIX    5   5 ALA A   69  ARG A   73  5                                   5    
HELIX    6   6 HIS A  102  HIS A  104  5                                   3    
HELIX    7   7 GLU A  105  ARG A  111  1                                   7    
HELIX    8   8 TYR A  141  ALA A  149  1                                   9    
HELIX    9   9 SER A  172  LEU A  174  5                                   3    
HELIX   10  10 SER A  193  SER A  205  1                                  13    
HELIX   11  11 GLY A  218  ALA A  227  1                                  10    
HELIX   12  12 THR A  242  LYS A  251  1                                  10    
HELIX   13  13 SER A  274  ASN A  282  1                                   9    
HELIX   14  14 PRO A  291  ASN A  296  1                                   6    
HELIX   15  15 ASN A  297  ASN A  304  1                                   8    
HELIX   16  16 GLY A  337  LYS A  346  1                                  10    
HELIX   17  17 THR A  402  ALA A  414  1                                  13    
HELIX   18  18 ASP A  417  ARG A  428  1                                  12    
SHEET    1   A 6 VAL A  76  THR A  79  0                                        
SHEET    2   A 6 ILE A  54  PHE A  57  1  N  VAL A  56   O  HIS A  77           
SHEET    3   A 6 LYS A  27  PHE A  30  1  N  VAL A  28   O  THR A  55           
SHEET    4   A 6 VAL A 119  SER A 125  1  O  VAL A 121   N  VAL A  29           
SHEET    5   A 6 VAL A 151  ASN A 157  1  O  ASN A 157   N  VAL A 124           
SHEET    6   A 6 HIS A 176  VAL A 180  1  O  VAL A 180   N  VAL A 156           
SHEET    1   B 2 TYR A 132  SER A 134  0                                        
SHEET    2   B 2 LEU A 168  HIS A 170 -1  O  ILE A 169   N  CYS A 133           
SHEET    1   C 9 GLY A 164  GLY A 165  0                                        
SHEET    2   C 9 ILE A 287  CYS A 289  1  O  CYS A 289   N  GLY A 164           
SHEET    3   C 9 VAL A 266  THR A 268  1  N  VAL A 266   O  GLU A 288           
SHEET    4   C 9 GLY A 235  HIS A 237  1  N  ILE A 236   O  VAL A 267           
SHEET    5   C 9 THR A 212  LEU A 215  1  N  LEU A 213   O  HIS A 237           
SHEET    6   C 9 MET A 307  ASN A 311  1  O  ILE A 310   N  GLN A 214           
SHEET    7   C 9 ILE A 352  ALA A 356  1  O  ILE A 354   N  SER A 309           
SHEET    8   C 9 TYR A 388  THR A 391  1  O  VAL A 390   N  MET A 355           
SHEET    9   C 9 GLY A 394  ARG A 397 -1  O  GLY A 394   N  THR A 391           
SHEET    1   D 2 MET A 316  ASP A 317  0                                        
SHEET    2   D 2 ILE A 369  VAL A 370  1  O  VAL A 370   N  MET A 316           
SHEET    1   E 2 THR A 360  ALA A 361  0                                        
SHEET    2   E 2 GLU A 366  SER A 367 -1  O  GLU A 366   N  ALA A 361           
LINK         C   ALA A  43                 N   MET A  44     1555   1555  1.32  
LINK         C   MET A  44                 N   TYR A  45     1555   1555  1.33  
LINK         C   HIS A  58                 N   MET A  59     1555   1555  1.34  
LINK         C   MET A  59                 N   LEU A  60     1555   1555  1.33  
LINK         C   GLU A  71                 N   MET A  72     1555   1555  1.33  
LINK         C   MET A  72                 N   ARG A  73     1555   1555  1.34  
LINK         C   GLN A 159                 N   MET A 160     1555   1555  1.34  
LINK         C   MET A 160                 N   PRO A 161     1555   1555  1.33  
LINK         C   GLU A 239                 N   MET A 240     1555   1555  1.33  
LINK         C   MET A 240                 N   PHE A 241     1555   1555  1.29  
LINK         C   VAL A 245                 N   MET A 246     1555   1555  1.35  
LINK         C   MET A 246                 N   ARG A 247     1555   1555  1.30  
LINK         C   ARG A 247                 N   MET A 248     1555   1555  1.32  
LINK         C   MET A 248                 N   ILE A 249     1555   1555  1.33  
LINK         C   ARG A 306                 N   MET A 307     1555   1555  1.31  
LINK         C   MET A 307                 N   VAL A 308     1555   1555  1.34  
LINK         C   GLU A 315                 N   MET A 316     1555   1555  1.32  
LINK         C   MET A 316                 N   ASP A 317     1555   1555  1.33  
LINK         C   LEU A 318                 N   MET A 319     1555   1555  1.34  
LINK         C   MET A 319                 N   GLY A 320     1555   1555  1.32  
LINK         C   ILE A 354                 N   MET A 355     1555   1555  1.35  
LINK         C   MET A 355                 N   ALA A 356     1555   1555  1.31  
CRYST1   54.684   87.279   93.504  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018287  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011458  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010695        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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