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Database: PDB
Entry: 3VOC
LinkDB: 3VOC
Original site: 3VOC 
HEADER    HYDROLASE                               21-JAN-12   3VOC              
TITLE     CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF BETA-AMYLASE FROM        
TITLE    2 PAENIBACILLUS POLYMYXA                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BETA/ALPHA-AMYLASE;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: BETA-AMYLASE, UNP RESIDUES 36-454;                         
COMPND   5 EC: 3.2.1.2;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PAENIBACILLUS POLYMYXA;                         
SOURCE   3 ORGANISM_TAXID: 1406;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET-21D                                   
KEYWDS    TIM BARREL, AMYLASE, CARBOHYDRATE METABOLISM, GLYCOSIDE HYDROLASE,    
KEYWDS   2 POLYSACCHARIDE DEGRADATION, HYDROLASE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.NISHIMURA,T.FUJIOKA,T.NAKANIWA,T.TADA                               
REVDAT   1   20-FEB-13 3VOC    0                                                
JRNL        AUTH   S.NISHIMURA,T.FUJIOKA,R.TAKAHASHI,T.NAKANIWA,H.FUKADA,       
JRNL        AUTH 2 T.INUI,T.TADA,T.KAWAGUCHI,J.SUMITANI                         
JRNL        TITL   STRUCTURAL ANALYSIS BY X-RAY CRYSTALLOGRAPHY AND SMALL-ANGLE 
JRNL        TITL 2 SCATTERING OF THE MULTI-DOMAIN BETA-AMYLASE FROM             
JRNL        TITL 3 PAENIBACILLUS POLYMYXA                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 27870                          
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) : 0.155                           
REMARK   3   R VALUE            (WORKING SET) : 0.153                           
REMARK   3   FREE R VALUE                     : 0.190                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1487                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2049                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.72                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1650                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 98                           
REMARK   3   BIN FREE R VALUE                    : 0.2330                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3216                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 55                                      
REMARK   3   SOLVENT ATOMS            : 282                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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): 0.158         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.136         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.084         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.870         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3415 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4630 ; 1.163 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   433 ; 5.577 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   150 ;36.590 ;25.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   535 ;12.594 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;19.606 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   472 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2623 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2098 ; 0.548 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3353 ; 1.053 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1317 ; 1.824 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1270 ; 2.897 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3VOC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-FEB-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB095296.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-FEB-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
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                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29847                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.940                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 19.0                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER_MR 2.1.4                                       
REMARK 200 STARTING MODEL: 5BCA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.1M TRIS, 25%    
REMARK 280  PEG 6000, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K   
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       30.51400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.95200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.25950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       46.95200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.51400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.25950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ASP A   417                                                      
REMARK 465     ASN A   418                                                      
REMARK 465     ASN A   419                                                      
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    THR A  80       47.90    -84.48                                   
REMARK 500    LYS A 153      148.12   -170.04                                   
REMARK 500    PRO A 178       40.87    -99.97                                   
REMARK 500    ASP A 227       91.85   -173.52                                   
REMARK 500    MET A 292       59.16   -141.71                                   
REMARK 500    SER A 329      -66.79   -123.55                                   
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                              CA A 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 135   OE1                                                    
REMARK 620 2 ASP A  52   OD1  99.8                                              
REMARK 620 3 GLN A 132   OE1  85.0  89.2                                        
REMARK 620 4 HOH A1046   O    93.8 165.0  85.6                                  
REMARK 620 5 GLU A  48   OE2 166.0  88.4 106.6  79.7                            
REMARK 620 6 ASN A  53   OD1  81.4  84.9 164.0 103.6  88.1                      
REMARK 620 N                    1     2     3     4     5                       
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 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 511                 
DBREF  3VOC A    1   419  UNP    P21543   AMYB_PAEPO      36    454             
SEQRES   1 A  419  ALA VAL ALA ASP ASP PHE GLN ALA SER VAL MET GLY PRO          
SEQRES   2 A  419  LEU ALA LYS ILE ASN ASP TRP GLY SER PHE LYS LYS GLN          
SEQRES   3 A  419  LEU GLN THR LEU LYS ASN ASN GLY VAL TYR ALA ILE THR          
SEQRES   4 A  419  THR ASP VAL TRP TRP GLY TYR VAL GLU SER ALA GLY ASP          
SEQRES   5 A  419  ASN GLN PHE ASP TRP SER TYR TYR LYS THR TYR ALA ASN          
SEQRES   6 A  419  ALA VAL LYS GLU ALA GLY LEU LYS TRP VAL PRO ILE ILE          
SEQRES   7 A  419  SER THR HIS LYS CYS GLY GLY ASN VAL GLY ASP ASP CYS          
SEQRES   8 A  419  ASN ILE PRO LEU PRO SER TRP LEU SER SER LYS GLY SER          
SEQRES   9 A  419  ALA ASP GLU MET GLN PHE LYS ASP GLU SER GLY TYR ALA          
SEQRES  10 A  419  ASN SER GLU ALA LEU SER PRO LEU TRP SER GLY THR GLY          
SEQRES  11 A  419  LYS GLN TYR ASP GLU LEU TYR ALA SER PHE ALA GLU ASN          
SEQRES  12 A  419  PHE ALA GLY TYR LYS SER ILE ILE PRO LYS ILE TYR LEU          
SEQRES  13 A  419  SER GLY GLY PRO SER GLY GLU LEU ARG TYR PRO SER TYR          
SEQRES  14 A  419  TYR PRO ALA ALA GLY TRP SER TYR PRO GLY ARG GLY LYS          
SEQRES  15 A  419  PHE GLN ALA TYR THR GLU THR ALA LYS ASN ALA PHE ARG          
SEQRES  16 A  419  THR ALA MET ASN ASP LYS TYR GLY SER LEU ASP LYS ILE          
SEQRES  17 A  419  ASN ALA ALA TRP GLY THR LYS LEU THR SER LEU SER GLN          
SEQRES  18 A  419  ILE ASN PRO PRO THR ASP GLY ASP GLY PHE TYR THR ASN          
SEQRES  19 A  419  GLY GLY TYR ASN SER ALA TYR GLY LYS ASP PHE LEU SER          
SEQRES  20 A  419  TRP TYR GLN SER VAL LEU GLU LYS HIS LEU GLY VAL ILE          
SEQRES  21 A  419  GLY ALA ALA ALA HIS LYS ASN PHE ASP SER VAL PHE GLY          
SEQRES  22 A  419  VAL ARG ILE GLY ALA LYS ILE SER GLY LEU HIS TRP GLN          
SEQRES  23 A  419  MET ASN ASN PRO ALA MET PRO HIS GLY THR GLU GLN ALA          
SEQRES  24 A  419  GLY GLY TYR TYR ASP TYR ASN ARG LEU ILE GLN LYS PHE          
SEQRES  25 A  419  LYS ASP ALA ASP LEU ASP LEU THR PHE THR CYS LEU GLU          
SEQRES  26 A  419  MET SER ASP SER GLY THR ALA PRO ASN TYR SER LEU PRO          
SEQRES  27 A  419  SER THR LEU VAL ASP THR VAL SER SER ILE ALA ASN ALA          
SEQRES  28 A  419  LYS GLY VAL ARG LEU ASN GLY GLU ASN ALA LEU PRO THR          
SEQRES  29 A  419  GLY GLY SER GLY PHE GLN LYS ILE GLU GLU LYS ILE THR          
SEQRES  30 A  419  LYS PHE GLY TYR HIS GLY PHE THR LEU LEU ARG ILE ASN          
SEQRES  31 A  419  ASN LEU VAL ASN ASN ASP GLY SER PRO THR GLY GLU LEU          
SEQRES  32 A  419  SER GLY PHE LYS GLN TYR ILE ILE SER LYS ALA LYS PRO          
SEQRES  33 A  419  ASP ASN ASN                                                  
HET     CA  A 501       1                                                       
HET     CL  A 502       1                                                       
HET    EDO  A 503       4                                                       
HET    EDO  A 504       4                                                       
HET    EDO  A 505       4                                                       
HET    GOL  A 506       6                                                       
HET    GOL  A 507       6                                                       
HET    GOL  A 508       6                                                       
HET    TRS  A 509       8                                                       
HET    TRS  A 510       8                                                       
HET    PEG  A 511       7                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     GOL GLYCEROL                                                         
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   2   CA    CA 2+                                                        
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  EDO    3(C2 H6 O2)                                                  
FORMUL   7  GOL    3(C3 H8 O3)                                                  
FORMUL  10  TRS    2(C4 H12 N O3 1+)                                            
FORMUL  12  PEG    C4 H10 O3                                                    
FORMUL  13  HOH   *282(H2 O)                                                    
HELIX    1   1 ASP A   19  ASN A   33  1                                  15    
HELIX    2   2 TRP A   44  GLU A   48  1                                   5    
HELIX    3   3 TRP A   57  ALA A   70  1                                  14    
HELIX    4   4 PRO A   96  LYS A  102  5                                   7    
HELIX    5   5 SER A  104  GLN A  109  1                                   6    
HELIX    6   6 SER A  127  ALA A  145  1                                  19    
HELIX    7   7 GLY A  146  ILE A  151  5                                   6    
HELIX    8   8 GLY A  159  GLU A  163  5                                   5    
HELIX    9   9 TYR A  170  GLY A  174  5                                   5    
HELIX   10  10 THR A  187  GLY A  203  1                                  17    
HELIX   11  11 SER A  204  GLY A  213  1                                  10    
HELIX   12  12 SER A  218  ILE A  222  5                                   5    
HELIX   13  13 SER A  239  ASP A  269  1                                  31    
HELIX   14  14 HIS A  294  GLY A  301  1                                   8    
HELIX   15  15 ASP A  304  ASP A  316  1                                  13    
HELIX   16  16 LEU A  337  GLY A  353  1                                  17    
HELIX   17  17 GLY A  366  PHE A  379  1                                  14    
HELIX   18  18 ARG A  388  LEU A  392  5                                   5    
HELIX   19  19 GLU A  402  ILE A  410  1                                   9    
HELIX   20  20 ILE A  411  ALA A  414  5                                   4    
SHEET    1   A 9 GLN A   7  MET A  11  0                                        
SHEET    2   A 9 ALA A  37  TRP A  43  1  O  THR A  39   N  VAL A  10           
SHEET    3   A 9 LYS A  73  SER A  79  1  O  VAL A  75   N  ILE A  38           
SHEET    4   A 9 LYS A 153  LEU A 156  1  O  TYR A 155   N  PRO A  76           
SHEET    5   A 9 ARG A 275  LYS A 279  1  O  GLY A 277   N  LEU A 156           
SHEET    6   A 9 ASP A 318  PHE A 321  1  O  ASP A 318   N  ILE A 276           
SHEET    7   A 9 LEU A 356  GLU A 359  1  O  ASN A 357   N  LEU A 319           
SHEET    8   A 9 GLY A 383  LEU A 386  1  O  THR A 385   N  GLY A 358           
SHEET    9   A 9 GLN A   7  MET A  11  1  N  SER A   9   O  PHE A 384           
SHEET    1   B 2 CYS A  83  GLY A  84  0                                        
SHEET    2   B 2 ASN A  92  ILE A  93 -1  O  ILE A  93   N  CYS A  83           
SHEET    1   C 2 PHE A 110  LYS A 111  0                                        
SHEET    2   C 2 ALA A 117  ASN A 118 -1  O  ASN A 118   N  PHE A 110           
SSBOND   1 CYS A   83    CYS A   91                          1555   1555  2.03  
LINK         OE1 GLU A 135                CA    CA A 501     1555   1555  2.25  
LINK         OD1 ASP A  52                CA    CA A 501     1555   1555  2.28  
LINK         OE1 GLN A 132                CA    CA A 501     1555   1555  2.33  
LINK        CA    CA A 501                 O   HOH A1046     1555   1555  2.34  
LINK         OE2 GLU A  48                CA    CA A 501     1555   1555  2.35  
LINK         OD1 ASN A  53                CA    CA A 501     1555   1555  2.38  
CISPEP   1 TYR A  177    PRO A  178          0         2.02                     
CISPEP   2 ALA A  332    PRO A  333          0         1.13                     
CISPEP   3 LEU A  387    ARG A  388          0        -9.47                     
SITE     1 AC1  6 GLU A  48  ASP A  52  ASN A  53  GLN A 132                    
SITE     2 AC1  6 GLU A 135  HOH A1046                                          
SITE     1 AC2  4 CYS A  91  ASN A  92  HOH A1034  HOH A1189                    
SITE     1 AC3  1 LYS A  16                                                     
SITE     1 AC4  3 GLN A 298  TYR A 302  TYR A 305                               
SITE     1 AC5  2 ASP A 314  HOH A1012                                          
SITE     1 AC6  6 LEU A 205  ASP A 206  THR A 217  ASP A 343                    
SITE     2 AC6  6 SER A 347  HOH A1254                                          
SITE     1 AC7  2 THR A 233  GLY A 235                                          
SITE     1 AC8  6 VAL A  87  ASP A 328  SER A 339  ASP A 343                    
SITE     2 AC8  6 LYS A 375  HOH A1275                                          
SITE     1 AC9  6 ASN A  18  ASP A  19  SER A  22  GLN A  26                    
SITE     2 AC9  6 ASN A 395  HOH A1258                                          
SITE     1 BC1  3 GLY A  88  PRO A 293  HIS A 294                               
CRYST1   61.028   68.519   93.904  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      0.016386  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014594  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010649        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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