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Database: PDB
Entry: 3LGR
LinkDB: 3LGR
Original site: 3LGR 
HEADER    HYDROLASE                               21-JAN-10   3LGR              
TITLE     XYLANASE II FROM TRICHODERMA REESEI COCRYSTALLIZED WITH TRIS-         
TITLE    2 DIPICOLINATE EUROPIUM                                                
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;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HYPOCREA JECORINA;                              
SOURCE   3 ORGANISM_COMMON: HYPOCREA JECORINA;                                  
SOURCE   4 ORGANISM_TAXID: 51453;                                               
SOURCE   5 GENE: XYN2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: TRICHODERMA LONGIBRACHIATUM;                      
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 5548                                        
KEYWDS    EUROPIUM TRIS-DIPICOLINATE COMPLEX, GLYCOPROTEIN, GLYCOSIDASE,        
KEYWDS   2 HYDROLASE, XYLAN DEGRADATION                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.POMPIDOR,R.KAHN,O.MAURY                                             
REVDAT   1   19-JAN-11 3LGR    0                                                
JRNL        AUTH   G.POMPIDOR,O.MAURY,J.VICAT,R.KAHN                            
JRNL        TITL   A DIPICOLINATE LANTHANIDE COMPLEX FOR SOLVING PROTEIN        
JRNL        TITL 2 STRUCTURES USING ANOMALOUS DIFFRACTION.                      
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  66   762 2010              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   20606256                                                     
JRNL        DOI    10.1107/S0907444910010954                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.64 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.64                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.51                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 22042                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.139                           
REMARK   3   R VALUE            (WORKING SET) : 0.138                           
REMARK   3   FREE R VALUE                     : 0.168                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1182                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.64                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.68                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1487                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2600                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 74                           
REMARK   3   BIN FREE R VALUE                    : 0.3030                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1480                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 354                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 8.27                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.12000                                              
REMARK   3    B22 (A**2) : -0.16000                                             
REMARK   3    B33 (A**2) : 0.06000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.08000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.084         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.083         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1581 ; 0.025 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1004 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2164 ; 2.086 ; 1.921       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2408 ; 4.421 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   197 ; 7.396 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    78 ;40.516 ;24.103       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   205 ;10.588 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ;21.875 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   211 ; 0.144 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1866 ; 0.015 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   354 ; 0.031 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   943 ; 1.238 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   405 ; 0.000 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1518 ; 1.894 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   638 ; 2.826 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   642 ; 4.049 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):     3 ; 7.637 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3LGR COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB057258.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUL-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23239                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.630                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.510                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 0.04500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.72                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.16100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.57                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 35 % PEG 3350, PH 7.2, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       55.44500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       19.18500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       55.44500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       19.18500            
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 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 EU    EU A 201  LIES ON A SPECIAL POSITION.                          
REMARK 375 N1   PDC A 304  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 AUTHORS STATE THAT THE STRUCTURE CONTAINS A EU COMPLEXED WITH 3 PDC  
REMARK 400 LIGANDS. THE COMPLEX IS LOCATED ON A CRYSTALLOGRAPHIC 2-FOLD AXIS.   
REMARK 400 GIVEN THE SPECIAL POSITION, THE OCCUPANCY HAS BEEN SET TO 0.5        
REMARK 400 INSTEAD OF 1.0. THUS THE CLOSE CONTACTS BETWEEN THE ASYMMETRIC UNIT  
REMARK 400 AND SYMMETRY UNIT ARE NOT PHYSICAL.                                  
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    TYR A 171   CE1   TYR A 171   CZ     -0.081                       
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    ASP A 116   CB  -  CG  -  OD1 ANGL. DEV. =  -5.6 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  57       26.60   -143.48                                   
REMARK 500    ASP A 170     -141.65   -107.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             PDC A 303   O1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  EU A 201  EU                                                      
REMARK 620 2 PDC A 303   C7  128.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             PDC A 302   O4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  EU A 201  EU                                                      
REMARK 620 2 PDC A 302   C8  128.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             PDC A 302   O1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  EU A 201  EU                                                      
REMARK 620 2 PDC A 302   C7  129.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             PDC A 304   O1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  EU A 201  EU                                                      
REMARK 620 2 PDC A 304   C7  129.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             PDC A 304   O4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  EU A 201  EU                                                      
REMARK 620 2 PDC A 304   C8  128.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             PDC A 303   O4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  EU A 201  EU                                                      
REMARK 620 2 PDC A 303   C8  127.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             PDC A 303   N1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  EU A 201  EU                                                      
REMARK 620 2 PDC A 303   C2  117.4                                              
REMARK 620 3 PDC A 303   C6  121.0 121.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             PDC A 302   N1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  EU A 201  EU                                                      
REMARK 620 2 PDC A 302   C2  120.8                                              
REMARK 620 3 PDC A 302   C6  117.1 121.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             PDC A 304   N1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  EU A 201  EU                                                      
REMARK 620 2 PDC A 304   C2  118.2                                              
REMARK 620 3 PDC A 304   C6  118.0 123.8                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EU A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EU A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EU A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PDC A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PDC A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PDC A 304                 
DBREF  3LGR A    2   190  UNP    P36217   XYN2_TRIRE      34    222             
SEQADV 3LGR PCA A    1  UNP  P36217              EXPRESSION TAG                 
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 3LGR PCA A    1  GLU  PYROGLUTAMIC ACID                                  
HET    PCA  A   1       8                                                       
HET     EU  A 201       1                                                       
HET     EU  A 202       1                                                       
HET     EU  A 203       1                                                       
HET    PDC  A 302      12                                                       
HET    PDC  A 303      12                                                       
HET    PDC  A 304      12                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM      EU EUROPIUM ION                                                     
HETNAM     PDC PYRIDINE-2,6-DICARBOXYLIC ACID                                   
HETSYN     PDC DIPICOLINIC ACID                                                 
FORMUL   1  PCA    C5 H7 N O3                                                   
FORMUL   2   EU    3(EU 2+)                                                     
FORMUL   5  PDC    3(C7 H5 N O4)                                                
FORMUL   8  HOH   *354(H2 O)                                                    
HELIX    1   1 THR A  152  GLN A  162  1                                  11    
SHEET    1   A 6 THR A   2  ILE A   3  0                                        
SHEET    2   A 6 VAL A  25  ASN A  29 -1  O  TYR A  27   N  ILE A   3           
SHEET    3   A 6 GLN A  34  TRP A  39 -1  O  ASN A  38   N  THR A  26           
SHEET    4   A 6 SER A 182  SER A 190 -1  O  GLY A 183   N  TRP A  39           
SHEET    5   A 6 VAL A  59  ASN A  69 -1  N  ASN A  67   O  SER A 184           
SHEET    6   A 6 GLY A 148  ASN A 151 -1  O  GLY A 148   N  PHE A  62           
SHEET    1   B 9 GLY A   6  ASN A  10  0                                        
SHEET    2   B 9 TYR A  13  ASN A  19 -1  O  TYR A  15   N  GLY A   8           
SHEET    3   B 9 ASN A  44  TRP A  51 -1  O  VAL A  46   N  TRP A  18           
SHEET    4   B 9 THR A 168  TYR A 179 -1  O  GLN A 172   N  TRP A  51           
SHEET    5   B 9 SER A  72  ARG A  81 -1  N  TRP A  79   O  ASP A 170           
SHEET    6   B 9 ILE A  85  PHE A  93 -1  O  TYR A  87   N  GLY A  78           
SHEET    7   B 9 ALA A 132  ARG A 141  1  O  SER A 139   N  VAL A  90           
SHEET    8   B 9 SER A 113  GLN A 125 -1  N  ARG A 122   O  PHE A 134           
SHEET    9   B 9 THR A 103  SER A 110 -1  N  VAL A 108   O  TYR A 115           
LINK         C   PCA A   1                 N   THR A   2     1555   1555  1.29  
LINK        EU    EU A 201                 O1  PDC A 303     1555   1555  2.30  
LINK        EU    EU A 201                 O4  PDC A 302     1555   1555  2.30  
LINK        EU    EU A 201                 O1  PDC A 302     1555   1555  2.43  
LINK        EU    EU A 201                 O1  PDC A 304     1555   1555  2.44  
LINK        EU    EU A 201                 O4  PDC A 304     1555   1555  2.48  
LINK        EU    EU A 201                 O4  PDC A 303     1555   1555  2.48  
LINK        EU    EU A 203                 O   HOH A 331     1555   1555  2.49  
LINK        EU    EU A 203                 O   HOH A 544     1555   1555  2.62  
LINK        EU    EU A 201                 N1  PDC A 303     1555   1555  2.63  
LINK        EU    EU A 201                 N1  PDC A 302     1555   1555  2.64  
LINK        EU    EU A 201                 N1  PDC A 304     1555   1555  2.67  
CISPEP   1 GLN A   52    PRO A   53          0        -6.19                     
CISPEP   2 ASN A   82    PRO A   83          0         3.67                     
SITE     1 AC1  3 PDC A 302  PDC A 303  PDC A 304                               
SITE     1 AC2  1 HOH A 229                                                     
SITE     1 AC3  2 HOH A 331  HOH A 544                                          
SITE     1 AC4 12 GLN A   4  PRO A   5  ASN A  19  GLY A  21                    
SITE     2 AC4 12 HIS A  22  GLY A  23  GLY A  24   EU A 201                    
SITE     3 AC4 12 PDC A 303  PDC A 304  HOH A 383  HOH A 514                    
SITE     1 AC5 12 GLN A   4  PRO A   5  ASN A  19  GLY A  21                    
SITE     2 AC5 12 HIS A  22  GLY A  23  GLY A  24   EU A 201                    
SITE     3 AC5 12 PDC A 302  PDC A 304  HOH A 383  HOH A 514                    
SITE     1 AC6  9 ILE A   3  GLN A   4  TYR A  17  VAL A  25                    
SITE     2 AC6  9  EU A 201  PDC A 302  PDC A 303  HOH A 351                    
SITE     3 AC6  9 HOH A 395                                                     
CRYST1  110.890   38.370   47.590  90.00  99.83  90.00 C 1 2 1       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      0.009018  0.000000  0.001563        0.00000                         
SCALE2      0.000000  0.026062  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021326        0.00000                         
HETATM    1  N   PCA A   1      49.939   5.040   2.076  1.00 27.00           N  
HETATM    2  CA  PCA A   1      51.365   5.408   1.784  1.00 26.84           C  
HETATM    3  CB  PCA A   1      51.734   5.067   0.319  1.00 27.29           C  
HETATM    4  CG  PCA A   1      50.370   4.869  -0.348  1.00 31.13           C  
HETATM    5  CD  PCA A   1      49.392   4.665   0.814  1.00 29.89           C  
HETATM    6  OE  PCA A   1      48.223   4.275   0.701  1.00 29.57           O  
HETATM    7  C   PCA A   1      51.565   6.862   2.169  1.00 19.56           C  
HETATM    8  O   PCA A   1      50.541   7.533   2.358  1.00 21.73           O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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