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Database: PDB
Entry: 3KWX
LinkDB: 3KWX
Original site: 3KWX 
HEADER    HYDROLASE                               01-DEC-09   3KWX              
TITLE     CHEMICALLY MODIFIED TAKA ALPHA-AMYLASE                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE A TYPE-1/2;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: TAKA-AMYLASE A, TAA, 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE;   
COMPND   5 EC: 3.2.1.1                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS ORYZAE;                             
SOURCE   3 ORGANISM_TAXID: 5062                                                 
KEYWDS    HYDROLASE(O-GLYCOSYL), 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE, CHEMICAL  
KEYWDS   2 MODIFICATION, ARGININEMETHYLESTER, CARBOHYDRATE METABOLISM,          
KEYWDS   3 DISULFIDE BOND, GLYCOPROTEIN, GLYCOSIDASE, HYDROLASE, METAL-BINDING  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.S.SIDDIQUI,S.J.HARROP,A.POLJAK,D.DE FRANCISCI,G.GUERRIERO,O.PILAK,  
AUTHOR   2 D.BURG,M.J.RAFTERY,D.M.PARKIN,J.TREWHELLA,R.CAVICCHIOLI              
REVDAT   2   13-JUL-11 3KWX    1       VERSN                                    
REVDAT   1   29-DEC-09 3KWX    0                                                
JRNL        AUTH   K.S.SIDDIQUI,A.POLJAK,D.DE FRANCISCI,G.GUERRIERO,O.PILAK,    
JRNL        AUTH 2 D.BURG,M.J.RAFTERY,D.M.PARKIN,J.TREWHELLA,R.CAVICCHIOLI      
JRNL        TITL   A MODIFIED ALPHA-AMYLASE WITH A MOLTEN-GLOBULE STATE HAS     
JRNL        TITL 2 ENHANCED THERMAL STABILITY                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX.REFINE                                        
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.18                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.040                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 37823                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.140                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1945                            
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 36.1809 -  5.1663    1.00     3832   194  0.1663 0.1853        
REMARK   3     2  5.1663 -  4.1025    1.00     3651   226  0.1312 0.1609        
REMARK   3     3  4.1025 -  3.5845    1.00     3683   179  0.1512 0.1828        
REMARK   3     4  3.5845 -  3.2570    1.00     3634   197  0.1806 0.2247        
REMARK   3     5  3.2570 -  3.0236    0.99     3567   200  0.2027 0.2466        
REMARK   3     6  3.0236 -  2.8454    0.99     3595   198  0.2014 0.2380        
REMARK   3     7  2.8454 -  2.7030    0.98     3526   196  0.2019 0.2413        
REMARK   3     8  2.7030 -  2.5854    0.97     3528   198  0.2062 0.2727        
REMARK   3     9  2.5854 -  2.4859    0.96     3443   178  0.2108 0.2737        
REMARK   3    10  2.4859 -  2.4001    0.94     3419   179  0.2424 0.2840        
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              : 0.33                                          
REMARK   3   B_SOL              : 44.38                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.060           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 54.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.01100                                              
REMARK   3    B22 (A**2) : 6.01100                                              
REMARK   3    B33 (A**2) : -12.02300                                            
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  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      :  0.008           3801                                  
REMARK   3   ANGLE     :  1.071           5186                                  
REMARK   3   CHIRALITY :  0.073            568                                  
REMARK   3   PLANARITY :  0.004            671                                  
REMARK   3   DIHEDRAL  : 16.783           1297                                  
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 3KWX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-DEC-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB056549.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-FEB-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : YES                                
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38486                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.180                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : 0.08100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.52300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
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: PDB ENTRY 2GVY                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 0.4M AMSO4, 0.1M MES PH    
REMARK 280  7.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.55867            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       77.11733            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       77.11733            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       38.55867            
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     SER A   477                                                      
REMARK 465     SER A   478                                                      
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    CYS A  30       88.50   -154.34                                   
REMARK 500    ALA A  78       46.20    -79.74                                   
REMARK 500    GLN A  85      -34.22   -131.57                                   
REMARK 500    ASP A 168     -157.94   -151.97                                   
REMARK 500    ALA A 329      123.32    -38.89                                   
REMARK 500    ASP A 340      123.50    -26.75                                   
REMARK 500    ASN A 384      136.33    -32.31                                   
REMARK 500    TYR A 419      177.45    172.42                                   
REMARK 500    ASP A 448        1.30    -64.94                                   
REMARK 500    ASN A 450      157.89    -48.11                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 720        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH A 839        DISTANCE =  6.46 ANGSTROMS                       
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                              CA A 480  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 210   O                                                      
REMARK 620 2 ASP A 175   OD2 160.3                                              
REMARK 620 3 ASN A 121   OD1  78.1 116.8                                        
REMARK 620 4 HOH A 607   O   118.4  80.3  68.8                                  
REMARK 620 5 GLU A 162   O    81.4  81.3 157.2 130.9                            
REMARK 620 6 HOH A 605   O    80.2  87.2  88.3 144.7  78.6                      
REMARK 620 7 HOH A 606   O    78.9 103.3 116.5  72.3  68.3 142.9                
REMARK 620 8 ASP A 175   OD1 135.3  49.5  70.8  79.1 119.6  67.8 144.0          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 480                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 500                 
DBREF  3KWX A    1   478  UNP    P0C1B3   AMYA1_ASPOR     22    499             
SEQRES   1 A  478  ALA THR PRO ALA ASP TRP ARG SER GLN SER ILE TYR PHE          
SEQRES   2 A  478  LEU LEU THR ASP ARG PHE ALA ARG THR ASP GLY SER THR          
SEQRES   3 A  478  THR ALA THR CYS ASN THR ALA ASP GLN LYS TYR CYS GLY          
SEQRES   4 A  478  GLY THR TRP GLN GLY ILE ILE ASP LYS LEU ASP TYR ILE          
SEQRES   5 A  478  GLN GLY MET GLY PHE THR ALA ILE TRP ILE THR PRO VAL          
SEQRES   6 A  478  THR ALA GLN LEU PRO GLN THR THR ALA TYR GLY ASP ALA          
SEQRES   7 A  478  TYR HIS GLY TYR TRP GLN GLN ASP ILE TYR SER LEU ASN          
SEQRES   8 A  478  GLU ASN TYR GLY THR ALA ASP ASP LEU LYS ALA LEU SER          
SEQRES   9 A  478  SER ALA LEU HIS GLU ARG GLY MET TYR LEU MET VAL ASP          
SEQRES  10 A  478  VAL VAL ALA ASN HIS MET GLY TYR ASP GLY ALA GLY SER          
SEQRES  11 A  478  SER VAL ASP TYR SER VAL PHE LYS PRO PHE SER SER GLN          
SEQRES  12 A  478  ASP TYR PHE HIS PRO PHE CYS PHE ILE GLN ASN TYR GLU          
SEQRES  13 A  478  ASP GLN THR GLN VAL GLU ASP CYS TRP LEU GLY ASP ASN          
SEQRES  14 A  478  THR VAL SER LEU PRO ASP LEU ASP THR THR LYS ASP VAL          
SEQRES  15 A  478  VAL LYS ASN GLU TRP TYR ASP TRP VAL GLY SER LEU VAL          
SEQRES  16 A  478  SER ASN TYR SER ILE ASP GLY LEU ARG ILE ASP THR VAL          
SEQRES  17 A  478  LYS HIS VAL GLN LYS ASP PHE TRP PRO GLY TYR ASN LYS          
SEQRES  18 A  478  ALA ALA GLY VAL TYR CYS ILE GLY GLU VAL LEU ASP GLY          
SEQRES  19 A  478  ASP PRO ALA TYR THR CYS PRO TYR GLN ASN VAL MET ASP          
SEQRES  20 A  478  GLY VAL LEU ASN TYR PRO ILE TYR TYR PRO LEU LEU ASN          
SEQRES  21 A  478  ALA PHE LYS SER THR SER GLY SER MET ASP ASP LEU TYR          
SEQRES  22 A  478  ASN MET ILE ASN THR VAL LYS SER ASP CYS PRO ASP SER          
SEQRES  23 A  478  THR LEU LEU GLY THR PHE VAL GLU ASN HIS ASP ASN PRO          
SEQRES  24 A  478  ARG PHE ALA SER TYR THR ASN ASP ILE ALA LEU ALA LYS          
SEQRES  25 A  478  ASN VAL ALA ALA PHE ILE ILE LEU ASN ASP GLY ILE PRO          
SEQRES  26 A  478  ILE ILE TYR ALA GLY GLN GLU GLN HIS TYR ALA GLY GLY          
SEQRES  27 A  478  ASN ASP PRO ALA ASN ARG GLU ALA THR TRP LEU SER GLY          
SEQRES  28 A  478  TYR PRO THR ASP SER GLU LEU TYR LYS LEU ILE ALA SER          
SEQRES  29 A  478  ALA ASN ALA ILE ARG ASN TYR ALA ILE SER LYS ASP THR          
SEQRES  30 A  478  GLY PHE VAL THR TYR LYS ASN TRP PRO ILE TYR LYS ASP          
SEQRES  31 A  478  ASP THR THR ILE ALA MET ARG LYS GLY THR ASP GLY SER          
SEQRES  32 A  478  GLN ILE VAL THR ILE LEU SER ASN LYS GLY ALA SER GLY          
SEQRES  33 A  478  ASP SER TYR THR LEU SER LEU SER GLY ALA GLY TYR THR          
SEQRES  34 A  478  ALA GLY GLN GLN LEU THR GLU VAL ILE GLY CYS THR THR          
SEQRES  35 A  478  VAL THR VAL GLY SER ASP GLY ASN VAL PRO VAL PRO MET          
SEQRES  36 A  478  ALA GLY GLY LEU PRO ARG VAL LEU TYR PRO THR GLU LYS          
SEQRES  37 A  478  LEU ALA GLY SER LYS ILE CYS SER SER SER                      
MODRES 3KWX ASN A  197  ASN  GLYCOSYLATION SITE                                 
HET     CA  A 480       1                                                       
HET    NAG  A 500      14                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   2   CA    CA 2+                                                        
FORMUL   3  NAG    C8 H15 N O6                                                  
FORMUL   4  HOH   *275(H2 O)                                                    
HELIX    1   1 THR A    2  ARG A    7  1                                   6    
HELIX    2   2 LEU A   15  ALA A   20  1                                   6    
HELIX    3   3 ASN A   31  GLN A   35  5                                   5    
HELIX    4   4 THR A   41  LYS A   48  1                                   8    
HELIX    5   5 LYS A   48  GLY A   54  1                                   7    
HELIX    6   6 GLU A   92  GLY A   95  5                                   4    
HELIX    7   7 THR A   96  GLU A  109  1                                  14    
HELIX    8   8 ASP A  133  PHE A  137  5                                   5    
HELIX    9   9 SER A  142  PHE A  146  5                                   5    
HELIX   10  10 ASP A  157  CYS A  164  1                                   8    
HELIX   11  11 LYS A  180  SER A  199  1                                  20    
HELIX   12  12 THR A  207  VAL A  211  5                                   5    
HELIX   13  13 GLN A  212  ASP A  214  5                                   3    
HELIX   14  14 PHE A  215  GLY A  224  1                                  10    
HELIX   15  15 ASP A  235  CYS A  240  1                                   6    
HELIX   16  16 PRO A  241  VAL A  245  5                                   5    
HELIX   17  17 ASN A  251  SER A  264  1                                  14    
HELIX   18  18 SER A  268  CYS A  283  1                                  16    
HELIX   19  19 ASP A  285  LEU A  288  5                                   4    
HELIX   20  20 ARG A  300  THR A  305  1                                   6    
HELIX   21  21 ASP A  307  ASN A  321  1                                  15    
HELIX   22  22 GLY A  330  HIS A  334  5                                   5    
HELIX   23  23 ALA A  346  GLY A  351  5                                   6    
HELIX   24  24 SER A  356  ASP A  376  1                                  21    
HELIX   25  25 GLU A  467  ALA A  470  5                                   4    
SHEET    1   A 8 GLY A 248  VAL A 249  0                                        
SHEET    2   A 8 TYR A 226  GLY A 229  1  N  GLY A 229   O  GLY A 248           
SHEET    3   A 8 GLY A 202  ILE A 205  1  N  LEU A 203   O  TYR A 226           
SHEET    4   A 8 TYR A 113  VAL A 118  1  N  VAL A 118   O  ARG A 204           
SHEET    5   A 8 ALA A  59  ILE A  62  1  N  ILE A  60   O  MET A 115           
SHEET    6   A 8 ILE A  11  LEU A  14  1  N  LEU A  14   O  TRP A  61           
SHEET    7   A 8 ILE A 324  TYR A 328  1  O  PRO A 325   N  ILE A  11           
SHEET    8   A 8 GLY A 290  THR A 291  1  N  THR A 291   O  ILE A 326           
SHEET    1   B 2 THR A  66  GLN A  68  0                                        
SHEET    2   B 2 GLN A  84  LEU A  90 -1  O  SER A  89   N  ALA A  67           
SHEET    1   C 3 TYR A 125  ASP A 126  0                                        
SHEET    2   C 3 VAL A 171  LEU A 173 -1  O  SER A 172   N  TYR A 125           
SHEET    3   C 3 LEU A 166  GLY A 167 -1  N  LEU A 166   O  LEU A 173           
SHEET    1   D 6 TRP A 385  ASP A 390  0                                        
SHEET    2   D 6 THR A 393  LYS A 398 -1  O  ARG A 397   N  TRP A 385           
SHEET    3   D 6 ILE A 405  SER A 410 -1  O  LEU A 409   N  ILE A 394           
SHEET    4   D 6 ARG A 461  PRO A 465 -1  O  ARG A 461   N  ILE A 408           
SHEET    5   D 6 GLN A 433  GLU A 436 -1  N  THR A 435   O  TYR A 464           
SHEET    6   D 6 THR A 441  THR A 444 -1  O  VAL A 443   N  LEU A 434           
SHEET    1   E 2 TYR A 419  LEU A 423  0                                        
SHEET    2   E 2 VAL A 451  MET A 455 -1  O  VAL A 453   N  LEU A 421           
SSBOND   1 CYS A   30    CYS A   38                          1555   1555  2.12  
SSBOND   2 CYS A  150    CYS A  164                          1555   1555  2.10  
SSBOND   3 CYS A  240    CYS A  283                          1555   1555  2.04  
SSBOND   4 CYS A  440    CYS A  475                          1555   1555  2.05  
LINK         ND2 ASN A 197                 C1  NAG A 500     1555   1555  1.44  
LINK         O   HIS A 210                CA    CA A 480     1555   1555  2.47  
LINK         OD2 ASP A 175                CA    CA A 480     1555   1555  2.50  
LINK         OD1 ASN A 121                CA    CA A 480     1555   1555  2.51  
LINK        CA    CA A 480                 O   HOH A 607     1555   1555  2.51  
LINK         O   GLU A 162                CA    CA A 480     1555   1555  2.51  
LINK        CA    CA A 480                 O   HOH A 605     1555   1555  2.62  
LINK        CA    CA A 480                 O   HOH A 606     1555   1555  2.64  
LINK         OD1 ASP A 175                CA    CA A 480     1555   1555  2.72  
CISPEP   1 LYS A  138    PRO A  139          0         7.59                     
CISPEP   2 ASP A  340    PRO A  341          0         7.08                     
SITE     1 AC1  7 ASN A 121  GLU A 162  ASP A 175  HIS A 210                    
SITE     2 AC1  7 HOH A 605  HOH A 606  HOH A 607                               
SITE     1 AC2  5 TYR A  88  SER A 193  LEU A 194  ASN A 197                    
SITE     2 AC2  5 HOH A 644                                                     
CRYST1  120.727  120.727  115.676  90.00  90.00 120.00 P 31 2 1      6          
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      0.008283  0.004782  0.000000        0.00000                         
SCALE2      0.000000  0.009565  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008645        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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