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Database: PDB
Entry: 2DFC
LinkDB: 2DFC
Original site: 2DFC 
HEADER    HYDROLASE                               28-FEB-06   2DFC              
TITLE     XYLANASE II FROM TRICODERMA REESEI AT 293K                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDO-1,4-BETA-XYLANASE 2;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: XYLANASE 2, 1,4-BETA-D-XYLAN XYLANOHYDROLASE 2;             
COMPND   5 EC: 3.2.1.8                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HYPOCREA JECORINA;                              
SOURCE   3 ORGANISM_TAXID: 51453                                                
KEYWDS    BENT BETA SHEET, HYDROLASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.HARATA,T.AKIBA                                                      
REVDAT   2   24-FEB-09 2DFC    1       VERSN                                    
REVDAT   1   11-JUL-06 2DFC    0                                                
JRNL        AUTH   N.WATANABE,T.AKIBA,R.KANAI,K.HARATA                          
JRNL        TITL   STRUCTURE OF AN ORTHORHOMBIC FORM OF XYLANASE II             
JRNL        TITL 2 FROM TRICHODERMA REESEI AND ANALYSIS OF THERMAL              
JRNL        TITL 3 DISPLACEMENT.                                                
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  62   784 2006              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   16790934                                                     
JRNL        DOI    10.1107/S0907444906017379                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.19 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   CROSS-VALIDATION METHOD           : NULL                           
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.106                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.122                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 3354                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 67625                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 1499                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 1                                             
REMARK   3   SOLVENT ATOMS      : 208                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL                    
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL                    
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : NULL                    
REMARK   3   NUMBER OF RESTRAINTS                     : NULL                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.013                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.029                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.035                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.098                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.099                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : NULL                    
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL                    
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL                    
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL                    
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2DFC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-MAR-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB025351.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-NOV-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-18B                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.15                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (TRUNCATE)                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67093                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : 0.04600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.19                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39200                            
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: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1ENX                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4M AMMONIUM SULFATE, 0.1M BICINE,      
REMARK 280  0.15M SODIUM IODIDE, 1.6% PROTEIN, PH 9.0, VAPOR DIFFUSION,         
REMARK 280  SITTING DROP, TEMPERATURE 298K                                      
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       24.77500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.25000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.01500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       35.25000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.77500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       30.01500            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 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    TRP A  39   CG  -  CD1 -  NE1 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    TRP A  39   CD1 -  NE1 -  CE2 ANGL. DEV. =  12.3 DEGREES          
REMARK 500    TRP A  39   NE1 -  CE2 -  CD2 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    GLY A 101   C   -  N   -  CA  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    ARG A 119   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A 122   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    TYR A 137   CB  -  CG  -  CD1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 145   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    HIS A 155   CG  -  ND1 -  CE1 ANGL. DEV. =   7.1 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    ASP A 170     -144.30   -104.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 394        DISTANCE =  5.17 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 191                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2DFB   RELATED DB: PDB                                   
DBREF  2DFC A    1   190  UNP    P36217   XYN2_TRIRE      33    222             
SEQADV 2DFC PCA A    1  UNP  P36217    GLN    33 MODIFIED RESIDUE               
SEQRES   1 A  190  PCA THR ILE GLN PRO GLY THR GLY TYR ASN ASN GLY TYR          
SEQRES   2 A  190  PHE TYR SER TYR TRP ASN ASP GLY HIS GLY GLY VAL THR          
SEQRES   3 A  190  TYR THR ASN GLY PRO GLY GLY GLN PHE SER VAL ASN TRP          
SEQRES   4 A  190  SER ASN SER GLY ASN PHE VAL GLY GLY LYS GLY TRP GLN          
SEQRES   5 A  190  PRO GLY THR LYS ASN LYS VAL ILE ASN PHE SER GLY SER          
SEQRES   6 A  190  TYR ASN PRO ASN GLY ASN SER TYR LEU SER VAL TYR GLY          
SEQRES   7 A  190  TRP SER ARG ASN PRO LEU ILE GLU TYR TYR ILE VAL GLU          
SEQRES   8 A  190  ASN PHE GLY THR TYR ASN PRO SER THR GLY ALA THR LYS          
SEQRES   9 A  190  LEU GLY GLU VAL THR SER ASP GLY SER VAL TYR ASP ILE          
SEQRES  10 A  190  TYR ARG THR GLN ARG VAL ASN GLN PRO SER ILE ILE GLY          
SEQRES  11 A  190  THR ALA THR PHE TYR GLN TYR TRP SER VAL ARG ARG ASN          
SEQRES  12 A  190  HIS ARG SER SER GLY SER VAL ASN THR ALA ASN HIS PHE          
SEQRES  13 A  190  ASN ALA TRP ALA GLN GLN GLY LEU THR LEU GLY THR MET          
SEQRES  14 A  190  ASP TYR GLN ILE VAL ALA VAL GLU GLY TYR PHE SER SER          
SEQRES  15 A  190  GLY SER ALA SER ILE THR VAL SER                              
MODRES 2DFC PCA A    1  GLU  PYROGLUTAMIC ACID                                  
HET    PCA  A   1       8                                                       
HET    IOD  A 191       1                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM     IOD IODIDE ION                                                       
FORMUL   1  PCA    C5 H7 N O3                                                   
FORMUL   2  IOD    I 1-                                                         
FORMUL   3  HOH   *208(H2 O)                                                    
HELIX    1   1 THR A  152  GLN A  162  1                                  11    
SHEET    1   A 9 GLY A   6  ASN A  10  0                                        
SHEET    2   A 9 TYR A  13  ASN A  19 -1  O  TYR A  13   N  ASN A  10           
SHEET    3   A 9 ASN A  44  TRP A  51 -1  O  GLY A  50   N  PHE A  14           
SHEET    4   A 9 THR A 168  TYR A 179 -1  O  GLN A 172   N  TRP A  51           
SHEET    5   A 9 SER A  72  ARG A  81 -1  N  TYR A  77   O  ILE A 173           
SHEET    6   A 9 ILE A  85  PHE A  93 -1  O  TYR A  87   N  GLY A  78           
SHEET    7   A 9 ALA A 132  ARG A 141  1  O  SER A 139   N  VAL A  90           
SHEET    8   A 9 SER A 113  GLN A 125 -1  N  ARG A 122   O  PHE A 134           
SHEET    9   A 9 THR A 103  SER A 110 -1  N  LEU A 105   O  ILE A 117           
SHEET    1   B 5 VAL A  25  ASN A  29  0                                        
SHEET    2   B 5 GLN A  34  TRP A  39 -1  O  ASN A  38   N  THR A  26           
SHEET    3   B 5 SER A 182  SER A 190 -1  O  GLY A 183   N  TRP A  39           
SHEET    4   B 5 VAL A  59  ASN A  69 -1  N  ASN A  69   O  SER A 182           
SHEET    5   B 5 GLY A 148  ASN A 151 -1  O  VAL A 150   N  ILE A  60           
LINK         C   PCA A   1                 N   THR A   2     1555   1555  1.33  
CISPEP   1 GLN A   52    PRO A   53          0        -1.59                     
CISPEP   2 ASN A   82    PRO A   83          0         8.38                     
SITE     1 AC1  2 ASN A  82  SER A 146                                          
CRYST1   49.550   60.030   70.500  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      0.020182  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016658  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014184        0.00000                         
HETATM    1  N   PCA A   1      29.904  42.860 -10.799  1.00 34.45           N  
ANISOU    1  N   PCA A   1     3573   4683   4835  -1169  -1199   1433       N  
HETATM    2  CA  PCA A   1      29.837  44.278 -11.026  1.00 36.15           C  
ANISOU    2  CA  PCA A   1     2687   4972   6076  -1382   -762   2252       C  
HETATM    3  CB  PCA A   1      30.860  44.487 -12.140  1.00 46.39           C  
ANISOU    3  CB  PCA A   1     3117   6563   7945   -553    496   3145       C  
HETATM    4  CG  PCA A   1      31.555  43.181 -12.368  1.00 48.48           C  
ANISOU    4  CG  PCA A   1     4291   6982   7147    -35    330   2574       C  
HETATM    5  CD  PCA A   1      30.853  42.191 -11.483  1.00 43.18           C  
ANISOU    5  CD  PCA A   1     3774   5925   6709   -489   -360   1797       C  
HETATM    6  OE  PCA A   1      31.049  40.977 -11.509  1.00 56.25           O  
ANISOU    6  OE  PCA A   1     5377   5826  10171  -1110   2836    456       O  
HETATM    7  C   PCA A   1      28.487  44.735 -11.561  1.00 33.07           C  
ANISOU    7  C   PCA A   1     2598   4909   5056  -1254   -725   1459       C  
HETATM    8  O   PCA A   1      27.728  43.878 -12.084  1.00 30.05           O  
ANISOU    8  O   PCA A   1     2790   4712   3915  -1307    -83   1263       O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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