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Database: PDB
Entry: 2UWF
LinkDB: 2UWF
Original site: 2UWF 
HEADER    HYDROLASE                               21-MAR-07   2UWF              
TITLE     CRYSTAL STRUCTURE OF FAMILY 10 XYLANASE FROM BACILLUS HALODURANS      
CAVEAT     2UWF    THE STRUCTURE FACTOR FILE ASSOCIATED WITH THIS HAS           
CAVEAT   2 2UWF    INCOMPLETE DATA.                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALKALINE ACTIVE ENDOXYLANASE;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 47-396;                                           
COMPND   5 SYNONYM: ENDOXYLANASE;                                               
COMPND   6 EC: 3.2.1.8;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: ADDITIONAL HIS-TAG PRESENT IN THIS ENTRY.             
COMPND   9 I359D360H361H362H363H364H365H366                                     
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS HALODURANS;                            
SOURCE   3 ORGANISM_TAXID: 86665;                                               
SOURCE   4 STRAIN: S7;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET22 BPLUS                               
KEYWDS    HYDROLASE, XYLAN DEGRADATION, XYLANASE STRUCTURE, GLYCOSIDASE,        
KEYWDS   2 ALKALIPHILIC, ENDOXYLANASE, BACILLUS HALODURANS, ALKALINE ADAPTATION 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.MAMO,M.THUNNISSEN,R.HATTI-KAUL,B.MATTIASSON                         
REVDAT   6   17-JAN-18 2UWF    1       REMARK                                   
REVDAT   5   18-JAN-12 2UWF    1       CAVEAT COMPND REMARK VERSN               
REVDAT   5 2                   1       DBREF  SEQADV                            
REVDAT   4   11-AUG-09 2UWF    1       JRNL                                     
REVDAT   3   14-JUL-09 2UWF    1       JRNL   REMARK                            
REVDAT   2   24-FEB-09 2UWF    1       VERSN                                    
REVDAT   1   27-MAY-08 2UWF    0                                                
JRNL        AUTH   G.MAMO,M.THUNNISSEN,R.HATTI-KAUL,B.MATTIASSON                
JRNL        TITL   AN ALKALINE ACTIVE XYLANASE: INSIGHTS INTO MECHANISMS OF     
JRNL        TITL 2 HIGH PH CATALYTIC ADAPTATION                                 
JRNL        REF    BIOCHIMIE                     V.  91  1187 2009              
JRNL        REFN                   ISSN 0300-9084                               
JRNL        PMID   19567261                                                     
JRNL        DOI    10.1016/J.BIOCHI.2009.06.017                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 64.55                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 19843                          
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) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1067                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1486                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1940                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 81                           
REMARK   3   BIN FREE R VALUE                    : 0.2820                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2953                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 210                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.65000                                              
REMARK   3    B22 (A**2) : -0.66000                                             
REMARK   3    B33 (A**2) : -1.99000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.264         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.207         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.148         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.465         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.914                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3038 ; 0.013 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2021 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4132 ; 1.337 ; 1.915       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4888 ; 0.923 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   355 ; 6.214 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   178 ;35.341 ;24.607       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   489 ;16.391 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;17.369 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   420 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3447 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   647 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   725 ; 0.222 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2211 ; 0.203 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1493 ; 0.186 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1503 ; 0.089 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   215 ; 0.185 ; 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):    38 ; 0.306 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    48 ; 0.279 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.194 ; 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):  1839 ; 0.872 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2864 ; 1.404 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1427 ; 2.171 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1268 ; 3.403 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 2UWF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-MAR-07.                  
REMARK 100 THE DEPOSITION ID IS D_1290031975.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-FEB-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I711                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9707                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21002                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 65.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.9000                             
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     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1HIZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30 % (V/V) 2-METHYL-2, 4-PENTANEDIOL,    
REMARK 280  20 MM CACL2 AND 100 MM SODIUM ACETATE BUFFER (PH 4.6)               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.80100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.78250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.79300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       63.78250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.80100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.79300            
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: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: 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   OE2  GLU A   159     O    HOH A  2104              2.09            
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    GLU A  27       -1.04     76.49                                   
REMARK 500    LEU A  40       35.77    -91.99                                   
REMARK 500    GLU A 169       48.91    -87.44                                   
REMARK 500    GLU A 265       46.52   -143.40                                   
REMARK 500    HIS A 363       46.27   -147.15                                   
REMARK 500    HIS A 365      169.82     66.17                                   
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                              CU A1367  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 298   OD2                                                    
REMARK 620 2 HIS A 362   NE2 124.0                                              
REMARK 620 3 HIS A 366   NE2 105.8  94.6                                        
REMARK 620 4 GLU A 302   OE1 114.3 105.6 110.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1368  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 298   OD1                                                    
REMARK 620 2 HOH A2206   O    68.3                                              
REMARK 620 3 HOH A2208   O    82.3  90.2                                        
REMARK 620 4 ARG A 357   O    93.4  86.2 175.2                                  
REMARK 620 5 ASP A 360   OD1 136.6  68.3  95.3  86.2                            
REMARK 620 6 HOH A2204   O   146.1 144.9  89.9  94.9  76.8                      
REMARK 620 7 HOH A2169   O    80.0 147.5  92.7  88.7 143.3  67.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1369  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2180   O                                                      
REMARK 620 2 HOH A2015   O    87.7                                              
REMARK 620 3 HOH A2013   O    73.2  88.9                                        
REMARK 620 4 GLN A  28   O   153.0  90.5  79.8                                  
REMARK 620 5 SER A 308   O    96.0  90.9 169.2 111.0                            
REMARK 620 6 ILE A 311   O    88.0 174.1  93.7  95.2  85.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1370  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2077   O                                                      
REMARK 620 2 HIS A 365   ND1 114.4                                              
REMARK 620 3 ASP A  30   OD2  98.5 101.9                                        
REMARK 620 4 ASP A  30   OD1 128.2 114.1  54.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1371  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 340   O                                                      
REMARK 620 2 ASP A 327   OD1  80.8                                              
REMARK 620 3 ASP A 321   O   115.3 145.7                                        
REMARK 620 4 TYR A 282   OH  108.5 111.7  92.3                                  
REMARK 620 5 ASP A 327   OD2 130.4  49.8 105.9  95.7                            
REMARK 620 N                    1     2     3     4                             
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 CU A 1367                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1368                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1369                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1370                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1371                 
DBREF  2UWF A   11   360  UNP    Q17TM8   Q17TM8_BACHD    47    396             
SEQADV 2UWF ASN A   11  UNP  Q17TM8    ASP    47 CONFLICT                       
SEQADV 2UWF HIS A  361  UNP  Q17TM8              EXPRESSION TAG                 
SEQADV 2UWF HIS A  362  UNP  Q17TM8              EXPRESSION TAG                 
SEQADV 2UWF HIS A  363  UNP  Q17TM8              EXPRESSION TAG                 
SEQADV 2UWF HIS A  364  UNP  Q17TM8              EXPRESSION TAG                 
SEQADV 2UWF HIS A  365  UNP  Q17TM8              EXPRESSION TAG                 
SEQADV 2UWF HIS A  366  UNP  Q17TM8              EXPRESSION TAG                 
SEQADV 2UWF ASP A  164  UNP  Q17TM8    GLY   200 CONFLICT                       
SEQRES   1 A  356  ASN GLN PRO PHE ALA TRP GLN VAL ALA SER LEU SER GLU          
SEQRES   2 A  356  ARG TYR GLN GLU GLN PHE ASP ILE GLY ALA ALA VAL GLU          
SEQRES   3 A  356  PRO TYR GLN LEU GLU GLY ARG GLN ALA GLN ILE LEU LYS          
SEQRES   4 A  356  HIS HIS TYR ASN SER LEU VAL ALA GLU ASN ALA MET LYS          
SEQRES   5 A  356  PRO VAL SER LEU GLN PRO ARG GLU GLY GLU TRP ASN TRP          
SEQRES   6 A  356  GLU GLY ALA ASP LYS ILE VAL GLU PHE ALA ARG LYS HIS          
SEQRES   7 A  356  ASN MET GLU LEU ARG PHE HIS THR LEU VAL TRP HIS SER          
SEQRES   8 A  356  GLN VAL PRO GLU TRP PHE PHE ILE ASP GLU ASN GLY ASN          
SEQRES   9 A  356  ARG MET VAL ASP GLU THR ASP PRO GLU LYS ARG LYS ALA          
SEQRES  10 A  356  ASN LYS GLN LEU LEU LEU GLU ARG MET GLU ASN HIS ILE          
SEQRES  11 A  356  LYS THR VAL VAL GLU ARG TYR LYS ASP ASP VAL THR SER          
SEQRES  12 A  356  TRP ASP VAL VAL ASN GLU VAL ILE ASP ASP ASP GLY GLY          
SEQRES  13 A  356  LEU ARG GLU SER GLU TRP TYR GLN ILE THR GLY THR ASP          
SEQRES  14 A  356  TYR ILE LYS VAL ALA PHE GLU THR ALA ARG LYS TYR GLY          
SEQRES  15 A  356  GLY GLU GLU ALA LYS LEU TYR ILE ASN ASP TYR ASN THR          
SEQRES  16 A  356  GLU VAL PRO SER LYS ARG ASP ASP LEU TYR ASN LEU VAL          
SEQRES  17 A  356  LYS ASP LEU LEU GLU GLN GLY VAL PRO ILE ASP GLY VAL          
SEQRES  18 A  356  GLY HIS GLN SER HIS ILE GLN ILE GLY TRP PRO SER ILE          
SEQRES  19 A  356  GLU ASP THR ARG ALA SER PHE GLU LYS PHE THR SER LEU          
SEQRES  20 A  356  GLY LEU ASP ASN GLN VAL THR GLU LEU ASP MET SER LEU          
SEQRES  21 A  356  TYR GLY TRP PRO PRO THR GLY ALA TYR THR SER TYR ASP          
SEQRES  22 A  356  ASP ILE PRO GLU GLU LEU PHE GLN ALA GLN ALA ASP ARG          
SEQRES  23 A  356  TYR ASP GLN LEU PHE GLU LEU TYR GLU GLU LEU SER ALA          
SEQRES  24 A  356  THR ILE SER SER VAL THR PHE TRP GLY ILE ALA ASP ASN          
SEQRES  25 A  356  HIS THR TRP LEU ASP ASP ARG ALA ARG GLU TYR ASN ASN          
SEQRES  26 A  356  GLY VAL GLY VAL ASP ALA PRO PHE VAL PHE ASP HIS ASN          
SEQRES  27 A  356  TYR ARG VAL LYS PRO ALA TYR TRP ARG ILE ILE ASP HIS          
SEQRES  28 A  356  HIS HIS HIS HIS HIS                                          
HET     CU  A1367       1                                                       
HET     CA  A1368       1                                                       
HET     CA  A1369       1                                                       
HET     CA  A1370       1                                                       
HET     CA  A1371       1                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM      CA CALCIUM ION                                                      
FORMUL   2   CU    CU 2+                                                        
FORMUL   3   CA    4(CA 2+)                                                     
FORMUL   7  HOH   *210(H2 O)                                                    
HELIX    1   1 ALA A   15  VAL A   18  5                                   4    
HELIX    2   2 SER A   20  TYR A   25  1                                   6    
HELIX    3   3 GLU A   36  LEU A   40  5                                   5    
HELIX    4   4 GLU A   41  TYR A   52  1                                  12    
HELIX    5   5 LYS A   62  GLN A   67  1                                   6    
HELIX    6   6 TRP A   75  ASN A   89  1                                  15    
HELIX    7   7 PRO A  104  PHE A  108  5                                   5    
HELIX    8   8 MET A  116  GLU A  119  5                                   4    
HELIX    9   9 ASP A  121  LYS A  148  1                                  28    
HELIX   10  10 SER A  170  GLY A  177  1                                   8    
HELIX   11  11 THR A  178  GLY A  193  1                                  16    
HELIX   12  12 VAL A  207  GLN A  224  1                                  18    
HELIX   13  13 SER A  243  SER A  256  1                                  14    
HELIX   14  14 SER A  281  ILE A  285  5                                   5    
HELIX   15  15 PRO A  286  LEU A  307  1                                  22    
HELIX   16  16 THR A  324  ASN A  334  1                                  11    
HELIX   17  17 LYS A  352  ASP A  360  1                                   9    
SHEET    1  AA 7 VAL A  98  TRP A  99  0                                        
SHEET    2  AA 7 SER A 153  ASN A 158  1  O  VAL A 156   N  VAL A  98           
SHEET    3  AA 7 GLU A  91  PHE A  94  1  O  PHE A  94   N  ASP A 155           
SHEET    4  AA 7 SER A  54  ALA A  57  1  O  LEU A  55   N  ARG A  93           
SHEET    5  AA 7 ASP A  30  VAL A  35  1  O  ALA A  33   N  VAL A  56           
SHEET    6  AA 7 ILE A 311  PHE A 316  1  O  SER A 312   N  ASP A  30           
SHEET    7  AA 7 ASP A 260  SER A 269  1  O  ASN A 261   N  SER A 312           
SHEET    1  AB 5 VAL A  98  TRP A  99  0                                        
SHEET    2  AB 5 SER A 153  ASN A 158  1  O  VAL A 156   N  VAL A  98           
SHEET    3  AB 5 LEU A 198  ASP A 202  1  O  TYR A 199   N  VAL A 156           
SHEET    4  AB 5 GLY A 230  HIS A 233  1  O  GLY A 230   N  ILE A 200           
SHEET    5  AB 5 ASP A 260  SER A 269  1  O  ASP A 260   N  VAL A 231           
LINK        CU    CU A1367                 OD2 ASP A 298     1555   1555  2.09  
LINK        CU    CU A1367                 NE2 HIS A 362     1555   1555  1.79  
LINK        CU    CU A1367                 NE2 HIS A 366     1555   1555  2.06  
LINK        CU    CU A1367                 OE1 GLU A 302     1555   1555  1.99  
LINK        CA    CA A1368                 OD1 ASP A 298     1555   1555  2.30  
LINK        CA    CA A1368                 O   HOH A2206     1555   1555  2.33  
LINK        CA    CA A1368                 O   HOH A2208     1555   1555  2.56  
LINK        CA    CA A1368                 O   ARG A 357     1555   1555  2.25  
LINK        CA    CA A1368                 OD1 ASP A 360     1555   1555  2.49  
LINK        CA    CA A1368                 O   HOH A2204     1555   1555  2.40  
LINK        CA    CA A1368                 O   HOH A2169     1555   1555  2.34  
LINK        CA    CA A1369                 O   HOH A2180     1555   1555  2.29  
LINK        CA    CA A1369                 O   HOH A2015     1555   1555  2.37  
LINK        CA    CA A1369                 O   HOH A2013     1555   1555  2.33  
LINK        CA    CA A1369                 O   GLN A  28     1555   1555  2.10  
LINK        CA    CA A1369                 O   SER A 308     1555   1555  2.21  
LINK        CA    CA A1369                 O   ILE A 311     1555   1555  2.34  
LINK        CA    CA A1370                 O   HOH A2077     1555   1555  2.93  
LINK        CA    CA A1370                 ND1 HIS A 365     1555   4456  2.16  
LINK        CA    CA A1370                 OD2 ASP A  30     1555   1555  2.60  
LINK        CA    CA A1370                 OD1 ASP A  30     1555   1555  2.00  
LINK        CA    CA A1371                 O   ASP A 340     1555   1555  2.37  
LINK        CA    CA A1371                 OD1 ASP A 327     1555   1555  2.61  
LINK        CA    CA A1371                 O   ASP A 321     1555   1555  2.33  
LINK        CA    CA A1371                 OH  TYR A 282     1555   1555  2.19  
LINK        CA    CA A1371                 OD2 ASP A 327     1555   1555  2.59  
CISPEP   1 HIS A   95    THR A   96          0        -2.67                     
CISPEP   2 TRP A  241    PRO A  242          0        -5.73                     
CISPEP   3 TRP A  273    PRO A  274          0        -7.92                     
CISPEP   4 THR A  276    GLY A  277          0       -28.01                     
SITE     1 AC1  4 ASP A 298  GLU A 302  HIS A 362  HIS A 366                    
SITE     1 AC2  7 ASP A 298  ARG A 357  ASP A 360  HOH A2169                    
SITE     2 AC2  7 HOH A2204  HOH A2206  HOH A2208                               
SITE     1 AC3  6 GLN A  28  SER A 308  ILE A 311  HOH A2013                    
SITE     2 AC3  6 HOH A2015  HOH A2180                                          
SITE     1 AC4  4 ASP A  30  GLU A  91  HIS A 365  HOH A2077                    
SITE     1 AC5  4 TYR A 282  ASP A 321  ASP A 327  ASP A 340                    
CRYST1   51.602   53.586  127.565  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019379  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018662  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007839        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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