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Database: PDB
Entry: 6OSU
LinkDB: 6OSU
Original site: 6OSU 
HEADER    HYDROLASE                               02-MAY-19   6OSU              
TITLE     CRYSTAL STRUCTURE OF THE D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACD FROM
TITLE    2 FRANCISELLA TULARENSIS                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANYL-D-ALANINE CARBOXYPEPTIDASE (PENICILLIN BINDING    
COMPND   3 PROTEIN) FAMILY PROTEIN;                                             
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: D-ALANYL-D-ALANINE CARBOXYPEPTIDASE FAMILY PROTEIN;         
COMPND   6 EC: 3.4.16.4;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: FRANCISELLA TULARENSIS SUBSP. TULARENSIS        
SOURCE   3 (STRAIN SCHU S4 / SCHU 4);                                           
SOURCE   4 ORGANISM_TAXID: 177416;                                              
SOURCE   5 VARIANT: SCHU S4 / SCHU 4;                                           
SOURCE   6 GENE: DACD, FTT_1029, BZ14_1819;                                     
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: BL21 DE3 (GOLD)                           
KEYWDS    SERINE PROTEASE, PENICILLIN BINDING PROTEIN, STRUCTURAL GENOMICS,     
KEYWDS   2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID,        
KEYWDS   3 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.KIM,P.STOGIOS,T.SKARINA,R.DI,A.JOACHIMIAK,CENTER FOR STRUCTURAL     
AUTHOR   2 GENOMICS OF INFECTIOUS DISEASES (CSGID)                              
REVDAT   1   15-MAY-19 6OSU    0                                                
JRNL        AUTH   Y.KIM,P.STOGIOS,T.SKARINA,R.DI,A.JOACHIMIAK,                 
JRNL        AUTH 2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES        
JRNL        AUTH 3 (CSGID)                                                      
JRNL        TITL   CRYSTAL STRUCTURE OF THE D-ALANYL-D-ALANINE CARBOXYPEPTIDASE 
JRNL        TITL 2 DACD FROM FRANCISELLA TULARENSIS                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.44 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.13_2998: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.44                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.320                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 17084                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 837                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 33.5015 -  4.4310    0.99     2748   135  0.1455 0.1954        
REMARK   3     2  4.4310 -  3.5183    1.00     2715   147  0.1661 0.2020        
REMARK   3     3  3.5183 -  3.0739    1.00     2723   133  0.2153 0.2899        
REMARK   3     4  3.0739 -  2.7930    1.00     2716   154  0.2357 0.2809        
REMARK   3     5  2.7930 -  2.5929    1.00     2691   139  0.2489 0.2768        
REMARK   3     6  2.5929 -  2.4401    0.97     2654   129  0.2862 0.2920        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.680           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 53.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 75.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           3220                                  
REMARK   3   ANGLE     :  0.555           4368                                  
REMARK   3   CHIRALITY :  0.044            499                                  
REMARK   3   PLANARITY :  0.004            570                                  
REMARK   3   DIHEDRAL  : 15.826           1962                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 29 THROUGH 55 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  40.7750  71.9762  75.7519              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6053 T22:   0.7456                                     
REMARK   3      T33:   0.6933 T12:   0.0945                                     
REMARK   3      T13:  -0.0988 T23:  -0.0179                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1806 L22:   0.5400                                     
REMARK   3      L33:   8.7383 L12:   0.3534                                     
REMARK   3      L13:   3.1932 L23:   0.4920                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0528 S12:   0.0716 S13:  -0.0250                       
REMARK   3      S21:   0.2336 S22:   0.0188 S23:  -0.0217                       
REMARK   3      S31:  -0.3074 S32:  -1.1759 S33:   0.2206                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 56 THROUGH 215 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  21.9220  62.6685  34.7532              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3055 T22:   0.4266                                     
REMARK   3      T33:   0.4647 T12:   0.0696                                     
REMARK   3      T13:  -0.0213 T23:   0.0312                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8637 L22:   3.6253                                     
REMARK   3      L33:   4.3795 L12:   0.4641                                     
REMARK   3      L13:   1.0258 L23:   1.0889                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0295 S12:   0.3514 S13:   0.0351                       
REMARK   3      S21:  -0.2737 S22:  -0.0665 S23:   0.1696                       
REMARK   3      S31:  -0.2042 S32:  -0.0436 S33:   0.1377                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 216 THROUGH 268 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.1870  33.6039  38.8346              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0818 T22:   0.5921                                     
REMARK   3      T33:   0.9240 T12:  -0.1567                                     
REMARK   3      T13:   0.1042 T23:  -0.0209                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0986 L22:   4.9260                                     
REMARK   3      L33:   4.5132 L12:   0.5781                                     
REMARK   3      L13:   0.9336 L23:   0.1368                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0413 S12:  -0.2546 S13:  -0.6404                       
REMARK   3      S21:   0.5351 S22:  -0.0606 S23:   1.0141                       
REMARK   3      S31:   1.1902 S32:  -0.5462 S33:  -0.0463                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 269 THROUGH 326 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  27.4069  53.1406  44.0609              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5366 T22:   0.4358                                     
REMARK   3      T33:   0.5558 T12:   0.0601                                     
REMARK   3      T13:  -0.0331 T23:   0.0561                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1759 L22:   5.4086                                     
REMARK   3      L33:   3.6993 L12:   1.2026                                     
REMARK   3      L13:   0.9776 L23:   1.7003                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0026 S12:   0.0113 S13:  -0.4641                       
REMARK   3      S21:   0.3986 S22:  -0.1551 S23:   0.1203                       
REMARK   3      S31:   0.6688 S32:   0.1630 S33:   0.0891                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 327 THROUGH 371 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  25.9537  78.5273  62.5644              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5683 T22:   0.5892                                     
REMARK   3      T33:   0.4553 T12:  -0.0508                                     
REMARK   3      T13:  -0.0276 T23:   0.0030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0856 L22:   3.6667                                     
REMARK   3      L33:   2.6270 L12:  -0.7827                                     
REMARK   3      L13:  -0.5270 L23:   0.6158                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0944 S12:  -0.6245 S13:   0.0907                       
REMARK   3      S21:   0.5042 S22:   0.1942 S23:  -0.0153                       
REMARK   3      S31:  -0.4539 S32:   0.3523 S33:  -0.1372                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 372 THROUGH 420 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  23.3743  89.3108  64.9926              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8152 T22:   0.5080                                     
REMARK   3      T33:   0.4623 T12:   0.0498                                     
REMARK   3      T13:  -0.0340 T23:  -0.0331                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6332 L22:   9.6502                                     
REMARK   3      L33:   2.6338 L12:   0.4034                                     
REMARK   3      L13:  -0.4378 L23:   0.8087                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0233 S12:  -0.1052 S13:   0.6152                       
REMARK   3      S21:  -0.0265 S22:  -0.0942 S23:   0.5458                       
REMARK   3      S31:  -1.0720 S32:  -0.1021 S33:   0.1479                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 421 THROUGH 441 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  23.4490  94.5428  65.8334              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0369 T22:   0.7649                                     
REMARK   3      T33:   0.6812 T12:   0.0620                                     
REMARK   3      T13:  -0.0221 T23:  -0.0948                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7900 L22:   8.3668                                     
REMARK   3      L33:   2.5075 L12:   1.9390                                     
REMARK   3      L13:  -0.9027 L23:   3.1832                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2561 S12:  -0.6775 S13:   0.8341                       
REMARK   3      S21:   0.0152 S22:  -0.3871 S23:   0.5928                       
REMARK   3      S31:  -1.0963 S32:  -0.1639 S33:   0.0120                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6OSU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000241279.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-MAR-18                          
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               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 X 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DIALS, XIA2                        
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17114                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.440                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.44                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: HKL-3000, MOLREP                                      
REMARK 200 STARTING MODEL: PDBID 4K91                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 %(W/V) PEG 6000, 0.1 M CALCIUM        
REMARK 280  CHLORIDE, 0.1 M HEPES PH 7.5, 10 MM PENICILLIN G, VAPOR             
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 289K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       65.78500            
REMARK 290   SMTRY3   2  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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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     SER A    18                                                      
REMARK 465     ASN A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     ALA A    21                                                      
REMARK 465     PRO A    22                                                      
REMARK 465     ASN A    23                                                      
REMARK 465     ILE A    24                                                      
REMARK 465     SER A    25                                                      
REMARK 465     ALA A    26                                                      
REMARK 465     TYR A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     GLY A   442                                                      
REMARK 465     TRP A   443                                                      
REMARK 465     TRP A   444                                                      
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    ALA A  80     -146.67     58.79                                   
REMARK 500    TYR A 121       55.05     72.17                                   
REMARK 500    GLN A 189      115.51   -161.79                                   
REMARK 500    PRO A 270     -174.86    -62.80                                   
REMARK 500    MET A 294      -63.05   -135.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: CSGID-IDP02286   RELATED DB: TARGETTRACK                 
DBREF  6OSU A   21   444  UNP    Q5NG28   Q5NG28_FRATT    21    444             
SEQADV 6OSU SER A   18  UNP  Q5NG28              EXPRESSION TAG                 
SEQADV 6OSU ASN A   19  UNP  Q5NG28              EXPRESSION TAG                 
SEQADV 6OSU ALA A   20  UNP  Q5NG28              EXPRESSION TAG                 
SEQRES   1 A  427  SER ASN ALA ALA PRO ASN ILE SER ALA TYR SER ASP PRO          
SEQRES   2 A  427  TYR PHE ASN GLY ALA ASN GLY LEU ALA GLN LYS ASP ILE          
SEQRES   3 A  427  ILE ILE ARG PRO ALA ASN ILE GLU LEU ASP ALA PRO ALA          
SEQRES   4 A  427  TRP VAL THR MET ASP TYR ARG THR GLY ASP ILE VAL SER          
SEQRES   5 A  427  GLU LYS ASN MET ASP VAL ARG ARG ALA PRO ALA SER LEU          
SEQRES   6 A  427  THR LYS ILE MET THR SER TYR ILE VAL ALA SER GLU ILE          
SEQRES   7 A  427  LYS ALA GLY ASN LEU SER TRP ASP THR MET ILE PRO ILE          
SEQRES   8 A  427  SER GLU ASN ALA ALA SER THR GLY GLY SER LYS MET TYR          
SEQRES   9 A  427  VAL LYS ALA GLY ALA LYS VAL SER VAL ARG ASN LEU VAL          
SEQRES  10 A  427  THR GLY MET ASP VAL VAL SER GLY ASN ASP ALA THR ILE          
SEQRES  11 A  427  ALA LEU ALA GLU TYR ILE GLY GLY THR THR GLN ALA PHE          
SEQRES  12 A  427  THR ASP LEU MET ASN GLN THR ALA LYS ALA ILE GLY MET          
SEQRES  13 A  427  ASN ASN THR HIS PHE ALA ASN PRO ASP GLY LEU PRO GLY          
SEQRES  14 A  427  GLY GLU GLN TYR THR THR ALA HIS ASP MET ALA LEU LEU          
SEQRES  15 A  427  ALA ARG SER TYR ILE TYR ASN PHE PRO GLU ALA TYR LYS          
SEQRES  16 A  427  VAL TYR ASP ASP LYS GLY LEU VAL TRP ASN ALA THR LYS          
SEQRES  17 A  427  GLN ASP SER VAL SER ILE ALA ASP ARG LYS GLN CYS LEU          
SEQRES  18 A  427  PRO LYS PHE ASP ARG ALA THR GLY ASN VAL ILE GLU SER          
SEQRES  19 A  427  TYR THR VAL LYS ASP LEU ASP ASP GLN ALA LYS ASP LYS          
SEQRES  20 A  427  CYS ASN LYS LEU PHE PRO LYS GLY ASP ASN PHE VAL LEU          
SEQRES  21 A  427  GLN ASN ASN ARG ASN ARG LEU LEU PHE THR PHE ASP GLY          
SEQRES  22 A  427  ALA ASP GLY MET LYS THR GLY HIS THR ASP ALA ALA GLY          
SEQRES  23 A  427  TYR CYS LEU VAL SER SER ALA LYS GLN ASP GLY GLU ARG          
SEQRES  24 A  427  PHE ILE SER VAL VAL LEU GLY THR THR SER SER ALA LYS          
SEQRES  25 A  427  ARG ASP SER GLU SER ALA LYS LEU LEU ARG TYR ALA LEU          
SEQRES  26 A  427  SER LYS TYR GLU ASN VAL LEU LEU TYR LYS ALA ASN SER          
SEQRES  27 A  427  PRO VAL THR ILE SER ALA ASP ASN ILE PRO ASN ALA LYS          
SEQRES  28 A  427  ALA GLY GLN LYS LEU THR VAL ALA SER ASN GLN ASN ILE          
SEQRES  29 A  427  TYR LYS THR VAL PRO LYS THR TYR VAL PRO TYR LEU LYS          
SEQRES  30 A  427  GLN GLY ILE GLU PHE ASN PRO ASN LEU ASN ALA PRO ILE          
SEQRES  31 A  427  LYS THR GLY GLN THR VAL GLY ASN LEU VAL ILE THR LEU          
SEQRES  32 A  427  GLY ASP THR LYS GLU GLU ILE ALA SER ILE PRO VAL VAL          
SEQRES  33 A  427  ALA MET ASN ASN VAL SER GLN LYS GLY TRP TRP                  
HET     CL  A 501       1                                                       
HET    EDO  A 502       4                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2   CL    CL 1-                                                        
FORMUL   3  EDO    C2 H6 O2                                                     
FORMUL   4  HOH   *36(H2 O)                                                     
HELIX    1 AA1 GLY A   34  ALA A   39  1                                   6    
HELIX    2 AA2 PRO A   79  SER A   81  5                                   3    
HELIX    3 AA3 LEU A   82  ALA A   97  1                                  16    
HELIX    4 AA4 SER A  109  SER A  114  1                                   6    
HELIX    5 AA5 VAL A  130  VAL A  140  1                                  11    
HELIX    6 AA6 GLY A  142  GLY A  155  1                                  14    
HELIX    7 AA7 THR A  156  GLY A  172  1                                  17    
HELIX    8 AA8 THR A  192  PHE A  207  1                                  16    
HELIX    9 AA9 PHE A  207  LYS A  212  1                                   6    
HELIX   10 AB1 VAL A  213  ASP A  216  5                                   4    
HELIX   11 AB2 SER A  230  LEU A  238  1                                   9    
HELIX   12 AB3 ASP A  258  PHE A  269  1                                  12    
HELIX   13 AB4 ARG A  283  PHE A  288  1                                   6    
HELIX   14 AB5 SER A  326  LYS A  344  1                                  19    
HELIX   15 AB6 THR A  388  PRO A  391  5                                   4    
SHEET    1 AA1 5 ILE A  67  LYS A  71  0                                        
SHEET    2 AA1 5 ALA A  56  ASP A  61 -1  N  THR A  59   O  SER A  69           
SHEET    3 AA1 5 GLU A 315  THR A 324 -1  O  ILE A 318   N  MET A  60           
SHEET    4 AA1 5 GLY A 303  GLN A 312 -1  N  SER A 308   O  SER A 319           
SHEET    5 AA1 5 ALA A 291  THR A 299 -1  N  GLY A 297   O  CYS A 305           
SHEET    1 AA2 2 MET A 105  PRO A 107  0                                        
SHEET    2 AA2 2 LYS A 127  SER A 129 -1  O  VAL A 128   N  ILE A 106           
SHEET    1 AA3 3 ASP A 227  VAL A 229  0                                        
SHEET    2 AA3 3 GLY A 218  ASN A 222 -1  N  ASN A 222   O  ASP A 227           
SHEET    3 AA3 3 PHE A 275  ASN A 279 -1  O  GLN A 278   N  LEU A 219           
SHEET    1 AA4 2 LYS A 240  PHE A 241  0                                        
SHEET    2 AA4 2 VAL A 248  GLU A 250 -1  O  ILE A 249   N  LYS A 240           
SHEET    1 AA5 2 TYR A 345  TYR A 351  0                                        
SHEET    2 AA5 2 ILE A 381  PRO A 386 -1  O  VAL A 385   N  GLU A 346           
SHEET    1 AA6 5 VAL A 357  SER A 360  0                                        
SHEET    2 AA6 5 LYS A 372  ALA A 376 -1  O  LEU A 373   N  ILE A 359           
SHEET    3 AA6 5 GLU A 426  ALA A 434 -1  O  VAL A 433   N  ALA A 376           
SHEET    4 AA6 5 THR A 412  LEU A 420 -1  N  ILE A 418   O  ILE A 427           
SHEET    5 AA6 5 LEU A 393  PHE A 399 -1  N  GLY A 396   O  VAL A 417           
SSBOND   1 CYS A  237    CYS A  265                          1555   1555  2.03  
CISPEP   1 GLY A  293    MET A  294          0         3.00                     
CISPEP   2 ALA A  405    PRO A  406          0         4.68                     
SITE     1 AC1  4 ASP A  61  ARG A  63  ARG A 316  ASN A 347                    
SITE     1 AC2  4 SER A 118  VAL A 140  SER A 141  ARG A 281                    
CRYST1   40.780  131.570   46.060  90.00 107.36  90.00 P 1 21 1      2          
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      0.024522  0.000000  0.007666        0.00000                         
SCALE2      0.000000  0.007601  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022747        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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