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Database: PDB
Entry: 3LB9
LinkDB: 3LB9
Original site: 3LB9 
HEADER    HYDROLASE                               08-JAN-10   3LB9              
TITLE     CRYSTAL STRUCTURE OF THE B. CIRCULANS CPA123 CIRCULAR PERMUTANT       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDO-1,4-BETA-XYLANASE;                                    
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: RESIDUES 65-182 AND 2-63;                                  
COMPND   5 SYNONYM: XYLANASE, 1,4-BETA-D-XYLAN XYLANOHYDROLASE;                 
COMPND   6 EC: 3.2.1.8;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS CIRCULANS;                             
SOURCE   3 ORGANISM_TAXID: 1397;                                                
SOURCE   4 GENE: XLNA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21( DE3)                                 
KEYWDS    PERMUTATION, BCX, GLYCOSIDASE, XYLAN DEGRADATION, HYDROLASE           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.D'ANGELO,S.REITINGER,M.LUDWICZEK,N.STRYNADKA,S.G.WITHERS,           
AUTHOR   2 L.P.MCINTOSH                                                         
REVDAT   4   13-JUN-18 3LB9    1       KEYWDS SEQADV                            
REVDAT   3   26-JUL-17 3LB9    1       SOURCE REMARK                            
REVDAT   2   28-APR-10 3LB9    1       JRNL                                     
REVDAT   1   23-MAR-10 3LB9    0                                                
JRNL        AUTH   S.REITINGER,Y.YU,J.WICKI,M.LUDWICZEK,I.D'ANGELO,S.BATURIN,   
JRNL        AUTH 2 M.OKON,N.C.STRYNADKA,S.LUTZ,S.G.WITHERS,L.P.MCINTOSH         
JRNL        TITL   CIRCULAR PERMUTATION OF BACILLUS CIRCULANS XYLANASE: A       
JRNL        TITL 2 KINETIC AND STRUCTURAL STUDY.                                
JRNL        REF    BIOCHEMISTRY                  V.  49  2464 2010              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   20163191                                                     
JRNL        DOI    10.1021/BI100036F                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.88                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.490                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 9443                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 473                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 19.8767 -  4.3171    1.00     3011   159  0.1693 0.1993        
REMARK   3     2  4.3171 -  3.4324    1.00     2980   157  0.1790 0.2885        
REMARK   3     3  3.4324 -  3.0002    1.00     2979   157  0.2347 0.3326        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 2.52                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.490            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.680           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           4409                                  
REMARK   3   ANGLE     :  0.688           6050                                  
REMARK   3   CHIRALITY :  0.049            616                                  
REMARK   3   PLANARITY :  0.006            767                                  
REMARK   3   DIHEDRAL  : 17.601           1390                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3LB9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000057064.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-OCT-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
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 MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.514                              
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : OSMICS                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10649                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.14700                            
REMARK 200  R SYM                      (I) : 0.14800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1147.                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.41200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.41200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1HV1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13-20 % (NH4)2SO4 40 MM TRIS-HCL, PH     
REMARK 280  8, VAPOR DIFFUSION, TEMPERATURE 298K                                
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       34.90500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.48500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       34.90500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       57.48500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: B                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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 350   BIOMT1   2 -1.000000  0.000000  0.000000      -25.89942            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       59.64999            
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    PRO B 181   C   -  N   -  CD  ANGL. DEV. = -28.6 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    ALA A  44     -150.83    -89.14                                   
REMARK 500    GLN A  46      111.43   -161.55                                   
REMARK 500    ASN A  97       48.06     36.10                                   
REMARK 500    ALA A 120       88.64    -68.47                                   
REMARK 500    ASN A 126       73.66   -114.54                                   
REMARK 500    ASN A 179       33.42    106.08                                   
REMARK 500    PRO A 181     -111.42    -86.27                                   
REMARK 500    GLN B  46      113.76   -161.48                                   
REMARK 500    SER B  55     -169.78   -165.96                                   
REMARK 500    ALA B  66     -108.68   -147.09                                   
REMARK 500    SER B  67      108.13   -172.88                                   
REMARK 500    ASN B  97       48.65     38.05                                   
REMARK 500    ASN B 126       65.17   -109.31                                   
REMARK 500    SER B 182      -68.07    175.39                                   
REMARK 500    LYS C  14      118.62    -34.57                                   
REMARK 500    ALA C  44     -157.66    -95.85                                   
REMARK 500    SER C  55     -166.57   -129.91                                   
REMARK 500    SER C  56      118.49   -176.15                                   
REMARK 500    TRP C  64     -130.18   -159.30                                   
REMARK 500    ALA C  66      -74.34    123.93                                   
REMARK 500    ASN C  73       89.60   -151.92                                   
REMARK 500    TYR C 178      178.77     86.66                                   
REMARK 500    ASN C 179     -155.75   -121.11                                   
REMARK 500    ALA C 180     -153.89   -131.33                                   
REMARK 500    PRO C 181      -96.59   -120.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1HV1   RELATED DB: PDB                                   
DBREF  3LB9 A   66   183  UNP    P09850   XYNA_BACCI      29    146             
DBREF  3LB9 A    3    64  UNP    P09850   XYNA_BACCI     152    213             
DBREF  3LB9 B   66   183  UNP    P09850   XYNA_BACCI      29    146             
DBREF  3LB9 B    3    64  UNP    P09850   XYNA_BACCI     152    213             
DBREF  3LB9 C   66   183  UNP    P09850   XYNA_BACCI      29    146             
DBREF  3LB9 C    3    64  UNP    P09850   XYNA_BACCI     152    213             
SEQADV 3LB9 ALA A    2  UNP  P09850              EXPRESSION TAG                 
SEQADV 3LB9 GLY A   65  UNP  P09850              LINKER                         
SEQADV 3LB9 ALA B    2  UNP  P09850              EXPRESSION TAG                 
SEQADV 3LB9 GLY B   65  UNP  P09850              LINKER                         
SEQADV 3LB9 ALA C    2  UNP  P09850              EXPRESSION TAG                 
SEQADV 3LB9 GLY C   65  UNP  P09850              LINKER                         
SEQRES   1 A  182  ALA THR PHE THR GLN TYR TRP SER VAL ARG GLN SER LYS          
SEQRES   2 A  182  ARG PRO THR GLY SER ASN ALA THR ILE THR PHE THR ASN          
SEQRES   3 A  182  HIS VAL ASN ALA TRP LYS SER HIS GLY MET ASN LEU GLY          
SEQRES   4 A  182  SER ASN TRP ALA TYR GLN VAL MET ALA THR GLU GLY TYR          
SEQRES   5 A  182  GLN SER SER GLY SER SER ASN VAL THR VAL TRP GLY ALA          
SEQRES   6 A  182  SER THR ASP TYR TRP GLN ASN TRP THR ASP GLY GLY GLY          
SEQRES   7 A  182  ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR SER          
SEQRES   8 A  182  VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY LYS          
SEQRES   9 A  182  GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN TYR          
SEQRES  10 A  182  ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR LEU          
SEQRES  11 A  182  THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU TYR          
SEQRES  12 A  182  TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR GLY          
SEQRES  13 A  182  THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR TYR          
SEQRES  14 A  182  ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER ILE          
SEQRES   1 B  182  ALA THR PHE THR GLN TYR TRP SER VAL ARG GLN SER LYS          
SEQRES   2 B  182  ARG PRO THR GLY SER ASN ALA THR ILE THR PHE THR ASN          
SEQRES   3 B  182  HIS VAL ASN ALA TRP LYS SER HIS GLY MET ASN LEU GLY          
SEQRES   4 B  182  SER ASN TRP ALA TYR GLN VAL MET ALA THR GLU GLY TYR          
SEQRES   5 B  182  GLN SER SER GLY SER SER ASN VAL THR VAL TRP GLY ALA          
SEQRES   6 B  182  SER THR ASP TYR TRP GLN ASN TRP THR ASP GLY GLY GLY          
SEQRES   7 B  182  ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR SER          
SEQRES   8 B  182  VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY LYS          
SEQRES   9 B  182  GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN TYR          
SEQRES  10 B  182  ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR LEU          
SEQRES  11 B  182  THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU TYR          
SEQRES  12 B  182  TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR GLY          
SEQRES  13 B  182  THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR TYR          
SEQRES  14 B  182  ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER ILE          
SEQRES   1 C  182  ALA THR PHE THR GLN TYR TRP SER VAL ARG GLN SER LYS          
SEQRES   2 C  182  ARG PRO THR GLY SER ASN ALA THR ILE THR PHE THR ASN          
SEQRES   3 C  182  HIS VAL ASN ALA TRP LYS SER HIS GLY MET ASN LEU GLY          
SEQRES   4 C  182  SER ASN TRP ALA TYR GLN VAL MET ALA THR GLU GLY TYR          
SEQRES   5 C  182  GLN SER SER GLY SER SER ASN VAL THR VAL TRP GLY ALA          
SEQRES   6 C  182  SER THR ASP TYR TRP GLN ASN TRP THR ASP GLY GLY GLY          
SEQRES   7 C  182  ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR SER          
SEQRES   8 C  182  VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY LYS          
SEQRES   9 C  182  GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN TYR          
SEQRES  10 C  182  ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR LEU          
SEQRES  11 C  182  THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU TYR          
SEQRES  12 C  182  TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR GLY          
SEQRES  13 C  182  THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR TYR          
SEQRES  14 C  182  ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER ILE          
FORMUL   4  HOH   *40(H2 O)                                                     
HELIX    1   1 PHE A   25  SER A   34  1                                  10    
HELIX    2   2 PHE B   25  SER B   34  1                                  10    
HELIX    3   3 PHE C   25  SER C   34  1                                  10    
SHEET    1   A 5 TYR A  70  THR A  75  0                                        
SHEET    2   A 5 PHE A 101  TRP A 107 -1  O  GLY A 104   N  GLN A  72           
SHEET    3   A 5 ASN A  42  THR A  62 -1  N  THR A  50   O  VAL A 103           
SHEET    4   A 5 ASN A  90  SER A  96 -1  O  TRP A  95   N  GLY A  57           
SHEET    5   A 5 ILE A  80  ASN A  85 -1  N  ILE A  80   O  SER A  96           
SHEET    1   B 8 TYR A  70  THR A  75  0                                        
SHEET    2   B 8 PHE A 101  TRP A 107 -1  O  GLY A 104   N  GLN A  72           
SHEET    3   B 8 ASN A  42  THR A  62 -1  N  THR A  50   O  VAL A 103           
SHEET    4   B 8 VAL A 122  ARG A 138 -1  O  TYR A 134   N  VAL A  47           
SHEET    5   B 8 ILE A 142  TRP A 150 -1  O  SER A 149   N  LEU A 131           
SHEET    6   B 8 THR A   3  ARG A  11  1  N  SER A   9   O  VAL A 147           
SHEET    7   B 8 GLY A 168  TYR A 178 -1  O  THR A 175   N  GLN A   6           
SHEET    8   B 8 THR A 158  SER A 165 -1  N  GLY A 161   O  ILE A 172           
SHEET    1   C 2 ASN A  20  THR A  24  0                                        
SHEET    2   C 2 THR A 115  ASN A 119 -1  O  TYR A 118   N  ALA A  21           
SHEET    1   D 5 ASN B  20  THR B  24  0                                        
SHEET    2   D 5 THR B 115  ARG B 138 -1  O  ILE B 116   N  ILE B  23           
SHEET    3   D 5 ASN B  42  TRP B  64 -1  N  SER B  56   O  ASN B 126           
SHEET    4   D 5 ASN B  90  SER B  96 -1  O  VAL B  93   N  SER B  59           
SHEET    5   D 5 ILE B  80  ASN B  85 -1  N  VAL B  84   O  SER B  92           
SHEET    1   E 8 TYR B  70  THR B  75  0                                        
SHEET    2   E 8 ASN B 100  TRP B 107 -1  O  GLY B 104   N  GLN B  72           
SHEET    3   E 8 ASN B  42  TRP B  64 -1  N  THR B  50   O  VAL B 103           
SHEET    4   E 8 THR B 115  ARG B 138 -1  O  ASN B 126   N  SER B  56           
SHEET    5   E 8 ILE B 142  SER B 149 -1  O  ILE B 142   N  THR B 137           
SHEET    6   E 8 PHE B   4  ARG B  11  1  N  THR B   5   O  GLU B 143           
SHEET    7   E 8 GLY B 168  ARG B 177 -1  O  ARG B 177   N  PHE B   4           
SHEET    8   E 8 THR B 158  SER B 165 -1  N  GLY B 161   O  ILE B 172           
SHEET    1   F 8 TYR C  70  THR C  75  0                                        
SHEET    2   F 8 ASN C 100  TRP C 107 -1  O  GLY C 104   N  GLN C  72           
SHEET    3   F 8 ASN C  42  TYR C  53 -1  N  THR C  50   O  VAL C 103           
SHEET    4   F 8 GLY C 129  ARG C 138 -1  O  TYR C 134   N  VAL C  47           
SHEET    5   F 8 ILE C 142  TRP C 150 -1  O  SER C 149   N  LEU C 131           
SHEET    6   F 8 PHE C   4  ARG C  11  1  N  ARG C  11   O  VAL C 147           
SHEET    7   F 8 GLY C 168  ARG C 177 -1  O  TYR C 173   N  TRP C   8           
SHEET    8   F 8 THR C 158  SER C 165 -1  N  GLY C 161   O  ILE C 172           
SHEET    1   G 5 ASN C  20  THR C  24  0                                        
SHEET    2   G 5 THR C 115  ASN C 126 -1  O  TYR C 118   N  ALA C  21           
SHEET    3   G 5 SER C  56  VAL C  63 -1  N  SER C  56   O  ASN C 126           
SHEET    4   G 5 ASN C  90  SER C  96 -1  O  TYR C  91   N  VAL C  61           
SHEET    5   G 5 ILE C  80  VAL C  81 -1  N  ILE C  80   O  SER C  96           
CISPEP   1 SER A  139    PRO A  140          0        -2.77                     
CISPEP   2 SER B  139    PRO B  140          0        -1.53                     
CISPEP   3 PRO B  181    SER B  182          0       -11.39                     
CISPEP   4 SER C  139    PRO C  140          0        -2.20                     
CISPEP   5 ALA C  180    PRO C  181          0        -0.11                     
CRYST1   69.810  114.970   65.030  90.00 113.47  90.00 C 1 2 1      12          
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      0.014325  0.000000  0.006220        0.00000                         
SCALE2      0.000000  0.008698  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016764        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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