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Database: PDB
Entry: 2C1F
LinkDB: 2C1F
Original site: 2C1F 
HEADER    HYDROLASE                               14-SEP-05   2C1F              
TITLE     THE STRUCTURE OF THE FAMILY 11 XYLANASE FROM NEOCALLIMASTIX           
TITLE    2 PATRICIARUM                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BIFUNCTIONAL ENDO-1,4-BETA-XYLANASE A;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: DOMAIN 2, RESIDUES 275-499;                                
COMPND   5 SYNONYM: ENDO-1,4-BETA-XYLANASE A, XYLA;                             
COMPND   6 EC: 3.2.1.8;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: NEOCALLIMASTIX PATRICIARUM;                     
SOURCE   3 ORGANISM_TAXID: 4758;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HYDROLASE, GLYCOSIDASE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.W.MURRAY,R.J.LEWIS,H.J.GILBERT                                      
REVDAT   3   13-JUL-11 2C1F    1       VERSN                                    
REVDAT   2   24-FEB-09 2C1F    1       VERSN                                    
REVDAT   1   13-FEB-07 2C1F    0                                                
JRNL        AUTH   M.VARDAKOU,C.DUMON,J.W.MURRAY,P.CHRISTAKOPOULOS,D.P.WEINER,  
JRNL        AUTH 2 N.JUGE,R.J.LEWIS,H.J.GILBERT,J.E.FLINT                       
JRNL        TITL   UNDERSTANDING THE STRUCTURAL BASIS FOR SUBSTRATE AND         
JRNL        TITL 2 INHIBITOR RECOGNITION IN EUKARYOTIC GH11 XYLANASES.          
JRNL        REF    J.MOL.BIOL.                   V. 375  1293 2008              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   18078955                                                     
JRNL        DOI    10.1016/J.JMB.2007.11.007                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 83.05                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 15357                          
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) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 766                             
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) : 9.33                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 83.05                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 193                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2880                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 10                           
REMARK   3   BIN FREE R VALUE                    : 0.4320                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1718                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 173                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 26.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.186         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.159         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.106         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.951         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1762 ; 0.009 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2388 ; 1.218 ; 1.902       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   218 ; 7.212 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    90 ;39.953 ;24.667       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   272 ;14.314 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;26.111 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   243 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2030 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   285 ; 0.183 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   814 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   134 ; 0.204 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    12 ; 0.272 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.238 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1390 ; 0.789 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1698 ; 0.863 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   869 ; 1.454 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   690 ; 2.101 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   220                          
REMARK   3    RESIDUE RANGE :   A  1220        A  1221                          
REMARK   3    RESIDUE RANGE :   A  2001        A  2173                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.4620  22.2710  43.1780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0544 T22:  -0.0912                                     
REMARK   3      T33:  -0.0527 T12:   0.0303                                     
REMARK   3      T13:   0.0039 T23:   0.0086                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1426 L22:   1.3602                                     
REMARK   3      L33:   1.4684 L12:   0.4282                                     
REMARK   3      L13:   0.2065 L23:  -0.0984                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0218 S12:   0.0629 S13:  -0.0273                       
REMARK   3      S21:  -0.1349 S22:  -0.0028 S23:  -0.1490                       
REMARK   3      S31:   0.1833 S32:   0.0760 S33:   0.0246                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK BULK SOLVENT                                    
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2C1F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-SEP-05.                  
REMARK 100 THE PDBE ID CODE IS EBI-25647.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-APR-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : NULL                               
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                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15357                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.040                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 7.490                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.3700                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.87                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.070                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1F5J                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.8                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CDCL2, 0.1M SODIUM ACETATE          
REMARK 280  AND 30% V/V PEG400                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3                            
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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z,-X,-Y                                                 
REMARK 290       7555   -Z,-X,Y                                                 
REMARK 290       8555   -Z,X,-Y                                                 
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z,-X                                                 
REMARK 290      11555   Y,-Z,-X                                                 
REMARK 290      12555   -Y,-Z,X                                                 
REMARK 290      13555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      14555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      15555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      16555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      17555   Z+1/2,X+1/2,Y+1/2                                       
REMARK 290      18555   Z+1/2,-X+1/2,-Y+1/2                                     
REMARK 290      19555   -Z+1/2,-X+1/2,Y+1/2                                     
REMARK 290      20555   -Z+1/2,X+1/2,-Y+1/2                                     
REMARK 290      21555   Y+1/2,Z+1/2,X+1/2                                       
REMARK 290      22555   -Y+1/2,Z+1/2,-X+1/2                                     
REMARK 290      23555   Y+1/2,-Z+1/2,-X+1/2                                     
REMARK 290      24555   -Y+1/2,-Z+1/2,X+1/2                                     
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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       58.66800            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       58.66800            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       58.66800            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       58.66800            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       58.66800            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       58.66800            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       58.66800            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       58.66800            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       58.66800            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       58.66800            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       58.66800            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       58.66800            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       58.66800            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       58.66800            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       58.66800            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000       58.66800            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       58.66800            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       58.66800            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000       58.66800            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       58.66800            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       58.66800            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       58.66800            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       58.66800            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       58.66800            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       58.66800            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       58.66800            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       58.66800            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       58.66800            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       58.66800            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       58.66800            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000       58.66800            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       58.66800            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       58.66800            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000       58.66800            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       58.66800            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       58.66800            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A   220                                                      
REMARK 465     LYS A   221                                                      
REMARK 465     GLY A   222                                                      
REMARK 465     SER A   223                                                      
REMARK 465     SER A   224                                                      
REMARK 465     PRO A   225                                                      
REMARK 465     ALA A   226                                                      
REMARK 465     LEU A   227                                                      
REMARK 465     GLU A   228                                                      
REMARK 465     HIS A   229                                                      
REMARK 465     HIS A   230                                                      
REMARK 465     HIS A   231                                                      
REMARK 465     HIS A   232                                                      
REMARK 465     HIS A   233                                                      
REMARK 465     HIS A   234                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   N    MET A     1     O    HOH A  2001              1.79            
REMARK 500   OE2  GLU A   201     O    HOH A  2158              2.11            
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 122      -42.47     77.89                                   
REMARK 500    SER A 155      107.31    -15.50                                   
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                              CD A1220  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  17   OD1                                                    
REMARK 620 2 ASP A  17   OD2  54.0                                              
REMARK 620 3 HOH A2075   O    83.8 118.8                                        
REMARK 620 4 HOH A2091   O   149.8  97.3 106.2                                  
REMARK 620 5 ASP A 122   OD1  88.7  91.4 134.3 102.6                            
REMARK 620 6 ASP A 122   OD2 119.8 144.9  92.1  88.8  53.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A1221  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  71   OD2                                                    
REMARK 620 2 HOH A2057   O   114.3                                              
REMARK 620 3 ASP A  71   OD1  96.7  99.8                                        
REMARK 620 4 HOH A2057   O   133.5  95.6 113.0                                  
REMARK 620 5 ASP A  71   OD1  52.1 134.2 123.6  81.4                            
REMARK 620 6 ASP A  71   OD2  91.4 143.5  49.6  82.8  81.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CD A1220                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CD A1221                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 CONSTRUCT CORRESPONDS TO RESIDUES 275-495 IN THE                     
REMARK 999 NATIVE FULL-LENGTH PROTEIN                                           
DBREF  2C1F A    2   226  UNP    P29127   XYNA_NEOPA     275    499             
SEQADV 2C1F MET A    1  UNP  P29127              EXPRESSION TAG                 
SEQADV 2C1F LEU A  227  UNP  P29127              EXPRESSION TAG                 
SEQADV 2C1F GLU A  228  UNP  P29127              EXPRESSION TAG                 
SEQADV 2C1F HIS A  229  UNP  P29127              EXPRESSION TAG                 
SEQADV 2C1F HIS A  230  UNP  P29127              EXPRESSION TAG                 
SEQADV 2C1F HIS A  231  UNP  P29127              EXPRESSION TAG                 
SEQADV 2C1F HIS A  232  UNP  P29127              EXPRESSION TAG                 
SEQADV 2C1F HIS A  233  UNP  P29127              EXPRESSION TAG                 
SEQADV 2C1F HIS A  234  UNP  P29127              EXPRESSION TAG                 
SEQRES   1 A  234  MET LYS PHE THR VAL GLY ASN GLY GLN ASN GLN HIS LYS          
SEQRES   2 A  234  GLY VAL ASN ASP GLY PHE SER TYR GLU ILE TRP LEU ASP          
SEQRES   3 A  234  ASN THR GLY GLY ASN GLY SER MET THR LEU GLY SER GLY          
SEQRES   4 A  234  ALA THR PHE LYS ALA GLU TRP ASN ALA ALA VAL ASN ARG          
SEQRES   5 A  234  GLY ASN PHE LEU ALA ARG ARG GLY LEU ASP PHE GLY SER          
SEQRES   6 A  234  GLN LYS LYS ALA THR ASP TYR ASP TYR ILE GLY LEU ASP          
SEQRES   7 A  234  TYR ALA ALA THR TYR LYS GLN THR ALA SER ALA SER GLY          
SEQRES   8 A  234  ASN SER ARG LEU CYS VAL TYR GLY TRP PHE GLN ASN ARG          
SEQRES   9 A  234  GLY LEU ASN GLY VAL PRO LEU VAL GLU TYR TYR ILE ILE          
SEQRES  10 A  234  GLU ASP TRP VAL ASP TRP VAL PRO ASP ALA GLN GLY LYS          
SEQRES  11 A  234  MET VAL THR ILE ASP GLY ALA GLN TYR LYS ILE PHE GLN          
SEQRES  12 A  234  MET ASP HIS THR GLY PRO THR ILE ASN GLY GLY SER GLU          
SEQRES  13 A  234  THR PHE LYS GLN TYR PHE SER VAL ARG GLN GLN LYS ARG          
SEQRES  14 A  234  THR SER GLY HIS ILE THR VAL SER ASP HIS PHE LYS GLU          
SEQRES  15 A  234  TRP ALA LYS GLN GLY TRP GLY ILE GLY ASN LEU TYR GLU          
SEQRES  16 A  234  VAL ALA LEU ASN ALA GLU GLY TRP GLN SER SER GLY VAL          
SEQRES  17 A  234  ALA ASP VAL THR LEU LEU ASP VAL TYR THR THR PRO LYS          
SEQRES  18 A  234  GLY SER SER PRO ALA LEU GLU HIS HIS HIS HIS HIS HIS          
HET     CD  A1220       1                                                       
HET     CD  A1221       1                                                       
HETNAM      CD CADMIUM ION                                                      
FORMUL   2   CD    2(CD 2+)                                                     
FORMUL   4  HOH   *173(H2 O)                                                    
HELIX    1   1 ALA A   69  TYR A   72  5                                   4    
HELIX    2   2 VAL A  176  GLN A  186  1                                  11    
SHEET    1  AA 7 LYS A   2  VAL A   5  0                                        
SHEET    2  AA 7 ASN A  31  LEU A  36 -1  O  GLY A  32   N  VAL A   5           
SHEET    3  AA 7 PHE A  42  ASN A  47 -1  O  LYS A  43   N  THR A  35           
SHEET    4  AA 7 GLU A 195  THR A 219 -1  O  GLY A 207   N  TRP A  46           
SHEET    5  AA 7 ASN A  54  ASP A  62 -1  O  PHE A  55   N  GLY A 202           
SHEET    6  AA 7 PHE A  19  LEU A  25 -1  O  SER A  20   N  GLY A  60           
SHEET    7  AA 7 GLN A  11  ASN A  16 -1  O  HIS A  12   N  ILE A  23           
SHEET    1  AB 5 LYS A   2  VAL A   5  0                                        
SHEET    2  AB 5 ASN A  31  LEU A  36 -1  O  GLY A  32   N  VAL A   5           
SHEET    3  AB 5 PHE A  42  ASN A  47 -1  O  LYS A  43   N  THR A  35           
SHEET    4  AB 5 GLU A 195  THR A 219 -1  O  GLY A 207   N  TRP A  46           
SHEET    5  AB 5 TYR A  74  GLN A 102 -1  O  TYR A  74   N  THR A 219           
LINK        CD    CD A1220                 OD1 ASP A  17     1555   1555  2.57  
LINK        CD    CD A1220                 OD2 ASP A  17     1555   1555  2.14  
LINK        CD    CD A1220                 O   HOH A2075     1555  24555  2.39  
LINK        CD    CD A1220                 O   HOH A2091     1555  24555  2.57  
LINK        CD    CD A1220                 OD1 ASP A 122     1555  24555  2.40  
LINK        CD    CD A1220                 OD2 ASP A 122     1555  24555  2.49  
LINK        CD    CD A1221                 O   HOH A2057     1555   1555  2.36  
LINK        CD    CD A1221                 OD1 ASP A  71     1555   1555  2.55  
LINK        CD    CD A1221                 O   HOH A2057     1555   2555  3.04  
LINK        CD    CD A1221                 OD1 ASP A  71     1555   2555  2.71  
LINK        CD    CD A1221                 OD2 ASP A  71     1555   1555  2.67  
LINK        CD    CD A1221                 OD2 ASP A  71     1555   2555  2.14  
SITE     1 AC1  4 ASP A  17  ASP A 122  HOH A2075  HOH A2091                    
SITE     1 AC2  2 ASP A  71  HOH A2057                                          
CRYST1  117.336  117.336  117.336  90.00  90.00  90.00 I 2 3        24          
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      0.008523  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008523  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008523        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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