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Entry: 1K6A
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HEADER    HYDROLASE                               15-OCT-01   1K6A              
TITLE     STRUCTURAL STUDIES ON THE MOBILITY IN THE ACTIVE SITE OF              
TITLE    2 THE THERMOASCUS AURANTIACUS XYLANASE I                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: XYLANASE I;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ENDO-1,4-BETA-XYLANASE;                                     
COMPND   5 EC: 3.2.1.8                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOASCUS AURANTIACUS;                        
SOURCE   3 ORGANISM_TAXID: 5087;                                                
SOURCE   4 STRAIN: IMI 216529                                                   
KEYWDS    ALTERNATE CONFORMATIONS, ACTIVE SITE MOBILITY, HYDROLASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.LO LEGGIO,S.KALOGIANNIS,K.ECKERT,S.C.M.TEIXEIRA,M.K.BHAT,           
AUTHOR   2 C.ANDREI,R.W.PICKERSGILL,S.LARSEN                                    
REVDAT   4   24-FEB-09 1K6A    1       VERSN                                    
REVDAT   3   01-APR-03 1K6A    1       JRNL                                     
REVDAT   2   18-DEC-02 1K6A    1       REMARK                                   
REVDAT   1   03-JUL-02 1K6A    0                                                
SPRSDE     03-JUL-02 1K6A      1FXM                                             
JRNL        AUTH   L.LO LEGGIO,S.KALOGIANNIS,K.ECKERT,S.C.TEIXEIRA,             
JRNL        AUTH 2 M.K.BHAT,C.ANDREI,R.W.PICKERSGILL,S.LARSEN                   
JRNL        TITL   SUBSTRATE SPECIFICITY AND SUBSITE MOBILITY IN T.             
JRNL        TITL 2 AURANTIACUS XYLANASE 10A.                                    
JRNL        REF    FEBS LETT.                    V. 509   303 2001              
JRNL        REFN                   ISSN 0014-5793                               
JRNL        PMID   11741607                                                     
JRNL        DOI    10.1016/S0014-5793(01)03177-5                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.C.M.TEIXEIRA,L.LO LEGGIO,R.PICKERSGILL,C.CARDIN            
REMARK   1  TITL   ANISOTROPIC REFINEMENT OF THE STRUCTURE OF                   
REMARK   1  TITL 2 THERMOASCUS AURANTIACUS XYLANASE I                           
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  57   385 2001              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  DOI    10.1107/S0907444900019089                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   L.LO LEGGIO,S.KALOGIANNIS,M.K.BHAT,R.W.PICKERSGILL           
REMARK   1  TITL   HIGH RESOLUTION STRUCTURE AND SEQUENCE OF                    
REMARK   1  TITL 2 T.AURANTIACUS XYLANASE I: IMPLICATIONS FOR THE               
REMARK   1  TITL 3 EVOLUTION OF THERMOSTABILITY IN FAMILY 10                    
REMARK   1  TITL 4 XYLANASES AND ENZYMES WITH (BETA)ALPHA-BARREL                
REMARK   1  TITL 5 ARCHITECTURE                                                 
REMARK   1  REF    PROTEINS                      V.  36   295 1999              
REMARK   1  REFN                   ISSN 0887-3585                               
REMARK   1  DOI    10.1002/(SICI)1097-0134(19990815)36:3<295::AID-PROT          
REMARK   1  DOI  2 4>3.3.CO;2-Y                                                 
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   R.NATESH,P.BHANUMOORTHY,P.J.VITHAYATHIL,K.SEKAR,             
REMARK   1  AUTH 2 S.RAMAKUMAR,M.A.VISWAMITRA                                   
REMARK   1  TITL   CRYSTAL STRUCTURE AT 1.8A RESOLUTION AND PROPOSED            
REMARK   1  TITL 2 AMINO ACID SEQUENCE OF A THERMOSTABLE XYLANASE               
REMARK   1  TITL 3 FROM THERMOASCUS AURANTIACUS                                 
REMARK   1  REF    J.MOL.BIOL.                   V. 288   999 1999              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  DOI    10.1006/JMBI.1999.2727                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.14 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) : 1.14                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 80.9                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
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) : 0.109                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.116                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.146                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.300                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 4019                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 76489                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.106                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.113                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.142                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.300                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 3650                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 68979                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 4541                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 0                                             
REMARK   3   SOLVENT ATOMS      : 199                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 2518.01                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 2089.00                 
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 17                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 23110                   
REMARK   3   NUMBER OF RESTRAINTS                     : 29211                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.014                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.028                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.029                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.085                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.091                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.042                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.005                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.048                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.054                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1K6A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-OCT-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB014613.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL; NULL                         
REMARK 200  TEMPERATURE           (KELVIN) : 293; 293                           
REMARK 200  PH                             : 5.1; 7.8                           
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : SRS; SRS                           
REMARK 200  BEAMLINE                       : PX9.6; PX9.6                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL                            
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87; 0.87                         
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL; NULL                         
REMARK 200  DETECTOR MANUFACTURER          : NULL; NULL                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 80508                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.140                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : 1.14                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.7                               
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; NULL                        
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: SHELX                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6K, PHOSPHATE CITRATE BUFFER,        
REMARK 280  PH 5.1, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K. PEG        
REMARK 280  6K, EDTA, TRIS, PH 7.8, VAPOR DIFFUSION, HANGING DROP,              
REMARK 280  TEMPERATURE 298K                                                    
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       29.62000            
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 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     GLN A   303                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A   1    NE2                                                 
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    GLU A 131   CD    GLU A 131   OE1     0.096                       
REMARK 500    GLU A 131   CD    GLU A 131   OE2    -0.091                       
REMARK 500    SER A 244   CB    SER A 244   OG     -0.080                       
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    ARG A  13   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    TYR A  68   CB  -  CG  -  CD2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    TYR A  68   CB  -  CG  -  CD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG A  81   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A 124   CG  -  CD  -  NE  ANGL. DEV. = -16.5 DEGREES          
REMARK 500    ARG A 124   NE  -  CZ  -  NH1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ARG A 124   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    ARG A 161   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG A 190   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG A 195   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ASP A 271   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A 271   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    TRP A 275   CB  -  CG  -  CD2 ANGL. DEV. =   8.3 DEGREES          
REMARK 500    ARG A 276   CD  -  NE  -  CZ  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    ARG A 276   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ASP A 300   CB  -  CG  -  OD1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ASP A 300   CB  -  CG  -  OD2 ANGL. DEV. = -10.3 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    ASN A  47      -23.93   -143.47                                   
REMARK 500    GLU A 237       45.83   -144.87                                   
REMARK 500    VAL A 269      -67.37    -93.74                                   
REMARK 500    THR A 280       64.53     32.92                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    GLN A   8         0.10    SIDE_CHAIN                              
REMARK 500    GLN A 158         0.12    SIDE_CHAIN                              
REMARK 500    GLN A 193         0.09    SIDE_CHAIN                              
REMARK 500    GLN A 259         0.11    SIDE_CHAIN                              
REMARK 500    ASP A 300         0.08    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FXM   RELATED DB: PDB                                   
REMARK 900 1FXM CONTAINS THERMOASCUS AURANTIACUS XYLANASE I: STRUCTURE          
REMARK 900 OBTAINED BY ANISOTROPIC REFINEMENT                                   
REMARK 900 RELATED ID: 1TAX   RELATED DB: PDB                                   
REMARK 900 1TAX CONTAINS THERMOASCUS AURANTIACUS XYLANASE I: STRUCTURE          
REMARK 900 OBTAINED BY ISOTROPIC REFINEMENT                                     
DBREF  1K6A A    1   303  UNP    P23360   XYNA_THEAU      27    329             
SEQRES   1 A  303  GLN ALA ALA GLN SER VAL ASP GLN LEU ILE LYS ALA ARG          
SEQRES   2 A  303  GLY LYS VAL TYR PHE GLY VAL ALA THR ASP GLN ASN ARG          
SEQRES   3 A  303  LEU THR THR GLY LYS ASN ALA ALA ILE ILE GLN ALA ASP          
SEQRES   4 A  303  PHE GLY GLN VAL THR PRO GLU ASN SER MET LYS TRP ASP          
SEQRES   5 A  303  ALA THR GLU PRO SER GLN GLY ASN PHE ASN PHE ALA GLY          
SEQRES   6 A  303  ALA ASP TYR LEU VAL ASN TRP ALA GLN GLN ASN GLY LYS          
SEQRES   7 A  303  LEU ILE ARG GLY HIS THR LEU VAL TRP HIS SER GLN LEU          
SEQRES   8 A  303  PRO SER TRP VAL SER SER ILE THR ASP LYS ASN THR LEU          
SEQRES   9 A  303  THR ASN VAL MET LYS ASN HIS ILE THR THR LEU MET THR          
SEQRES  10 A  303  ARG TYR LYS GLY LYS ILE ARG ALA TRP ASP VAL VAL ASN          
SEQRES  11 A  303  GLU ALA PHE ASN GLU ASP GLY SER LEU ARG GLN THR VAL          
SEQRES  12 A  303  PHE LEU ASN VAL ILE GLY GLU ASP TYR ILE PRO ILE ALA          
SEQRES  13 A  303  PHE GLN THR ALA ARG ALA ALA ASP PRO ASN ALA LYS LEU          
SEQRES  14 A  303  TYR ILE ASN ASP TYR ASN LEU ASP SER ALA SER TYR PRO          
SEQRES  15 A  303  LYS THR GLN ALA ILE VAL ASN ARG VAL LYS GLN TRP ARG          
SEQRES  16 A  303  ALA ALA GLY VAL PRO ILE ASP GLY ILE GLY SER GLN THR          
SEQRES  17 A  303  HIS LEU SER ALA GLY GLN GLY ALA GLY VAL LEU GLN ALA          
SEQRES  18 A  303  LEU PRO LEU LEU ALA SER ALA GLY THR PRO GLU VAL ALA          
SEQRES  19 A  303  ILE THR GLU LEU ASP VAL ALA GLY ALA SER PRO THR ASP          
SEQRES  20 A  303  TYR VAL ASN VAL VAL ASN ALA CYS LEU ASN VAL GLN SER          
SEQRES  21 A  303  CYS VAL GLY ILE THR VAL TRP GLY VAL ALA ASP PRO ASP          
SEQRES  22 A  303  SER TRP ARG ALA SER THR THR PRO LEU LEU PHE ASP GLY          
SEQRES  23 A  303  ASN PHE ASN PRO LYS PRO ALA TYR ASN ALA ILE VAL GLN          
SEQRES  24 A  303  ASP LEU GLN GLN                                              
FORMUL   2  HOH   *199(H2 O)                                                    
HELIX    1   1 SER A    5  ARG A   13  1                                   9    
HELIX    2   2 ASP A   23  THR A   28  1                                   6    
HELIX    3   3 LYS A   31  PHE A   40  1                                  10    
HELIX    4   4 LYS A   50  GLU A   55  1                                   6    
HELIX    5   5 PHE A   63  GLY A   77  1                                  15    
HELIX    6   6 PRO A   92  SER A   97  1                                   6    
HELIX    7   7 ASP A  100  TYR A  119  1                                  20    
HELIX    8   8 THR A  142  GLY A  149  1                                   8    
HELIX    9   9 ASP A  151  ASP A  164  1                                  14    
HELIX   10  10 TYR A  181  ALA A  197  1                                  17    
HELIX   11  11 GLN A  214  SER A  227  1                                  14    
HELIX   12  12 SER A  244  VAL A  258  1                                  15    
HELIX   13  13 ALA A  270  SER A  274  5                                   5    
HELIX   14  14 ARG A  276  THR A  280  5                                   5    
HELIX   15  15 LYS A  291  GLN A  302  1                                  12    
SHEET    1   A10 HIS A 209  LEU A 210  0                                        
SHEET    2   A10 GLU A 232  VAL A 240  1  O  ASP A 239   N  LEU A 210           
SHEET    3   A10 GLY A 203  SER A 206  1  O  ILE A 204   N  ALA A 234           
SHEET    4   A10 LYS A 168  ASP A 173  1  O  LEU A 169   N  GLY A 203           
SHEET    5   A10 ALA A 125  ASN A 130  1  O  TRP A 126   N  TYR A 170           
SHEET    6   A10 LEU A  79  VAL A  86  1  O  ILE A  80   N  ALA A 125           
SHEET    7   A10 GLN A  42  PRO A  45  1  N  VAL A  43   O  LEU A  79           
SHEET    8   A10 TYR A  17  THR A  22  1  N  VAL A  20   O  GLN A  42           
SHEET    9   A10 CYS A 261  VAL A 266  1  O  VAL A 262   N  TYR A  17           
SHEET   10   A10 GLU A 232  VAL A 240  1  O  VAL A 233   N  VAL A 262           
SSBOND   1 CYS A  255    CYS A  261                          1555   1555  2.03  
CISPEP   1 HIS A   83    THR A   84          0        -2.79                     
CRYST1   46.220   59.240   51.310  90.00 109.80  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      0.021636  0.000000  0.007789        0.00000                         
SCALE2      0.000000  0.016880  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020714        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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