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Database: PDB
Entry: 3VM5
LinkDB: 3VM5
Original site: 3VM5 
HEADER    HYDROLASE                               08-DEC-11   3VM5              
TITLE     RECOMBINANT MEDAKA FISH ALPHA-AMYLASE EXPRESSED IN YEAST PICHIA       
TITLE    2 PASTORIS                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ORYZIAS LATIPES;                                
SOURCE   3 ORGANISM_TAXID: 8090;                                                
SOURCE   4 STRAIN: HD-RR;                                                       
SOURCE   5 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: KM71;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: P9KPRAHS                                  
KEYWDS    (ALPHA/BETA)8 BARREL FOLD, STARCH HYDROLYSIS, HYDROLASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.MIZUTANI,M.TOYODA,B.MIKAMI                                          
REVDAT   2   26-JUN-13 3VM5    1       JRNL                                     
REVDAT   1   06-JUN-12 3VM5    0                                                
JRNL        AUTH   K.MIZUTANI,M.TOYODA,Y.OTAKE,S.YOSHIOKA,N.TAKAHASHI,B.MIKAMI  
JRNL        TITL   STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF RECOMBINANT    
JRNL        TITL 2 MEDAKA FISH ALPHA-AMYLASE EXPRESSED IN YEAST PICHIA          
JRNL        TITL 3 PASTORIS.                                                    
JRNL        REF    BIOCHIM.BIOPHYS.ACTA          V.1824   954 2012              
JRNL        REFN                   ISSN 0006-3002                               
JRNL        PMID   22613096                                                     
JRNL        DOI    10.1016/J.BBAPAP.2012.05.005                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.73                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 15999                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 807                             
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 27.7317 -  5.1701    0.99     2808   125  0.1686 0.2198        
REMARK   3     2  5.1701 -  4.1080    0.98     2639   139  0.1430 0.1855        
REMARK   3     3  4.1080 -  3.5899    0.96     2534   138  0.1574 0.2493        
REMARK   3     4  3.5899 -  3.2623    0.95     2499   138  0.1948 0.2821        
REMARK   3     5  3.2623 -  3.0287    0.92     2411   139  0.2206 0.3082        
REMARK   3     6  3.0287 -  2.8504    0.89     2301   128  0.2517 0.3528        
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              : 0.29                                          
REMARK   3   B_SOL              : 3.95                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.470           
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) : -1.20810                                             
REMARK   3    B22 (A**2) : -1.20810                                             
REMARK   3    B33 (A**2) : 2.41610                                              
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      :  0.009           4060                                  
REMARK   3   ANGLE     :  1.155           5506                                  
REMARK   3   CHIRALITY :  0.082            539                                  
REMARK   3   PLANARITY :  0.005            740                                  
REMARK   3   DIHEDRAL  : 22.090           2436                                  
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 3VM5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-DEC-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB095217.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : RHODIUM-COATED MIRRORS             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17061                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 8.100                              
REMARK 200  R MERGE                    (I) : 0.12400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 32.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.600                              
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: 1PIF                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22.5% PEG 3350, 0.2M SODIUM NITRATE,     
REMARK 280  50MM TRIS-HCL, PH 8.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE   
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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      116.15200            
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       58.07600            
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       58.07600            
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      116.15200            
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     HIS A   500                                                      
REMARK 465     HIS A   501                                                      
REMARK 465     HIS A   502                                                      
REMARK 465     HIS A   503                                                      
REMARK 465     HIS A   504                                                      
REMARK 465     HIS A   505                                                      
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    PHE A  17      110.84    -37.68                                   
REMARK 500    GLU A  18       -2.42     80.98                                   
REMARK 500    PHE A  31      -57.83   -134.05                                   
REMARK 500    ILE A  99       -2.11   -140.06                                   
REMARK 500    MET A 102     -145.48   -103.24                                   
REMARK 500    VAL A 163       47.71     39.17                                   
REMARK 500    THR A 219        4.63    -67.66                                   
REMARK 500    LYS A 268       33.02     73.91                                   
REMARK 500    TRP A 280      136.89    -39.98                                   
REMARK 500    ASP A 365       -8.46    103.36                                   
REMARK 500    CYS A 385       41.96     74.39                                   
REMARK 500    ASN A 415      -98.89   -131.94                                   
REMARK 500    ASP A 438       89.81   -162.46                                   
REMARK 500    PRO A 487       42.31    -77.94                                   
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 506  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 552   O                                                      
REMARK 620 2 ARG A 158   O   125.2                                              
REMARK 620 3 HOH A 553   O   147.9  72.4                                        
REMARK 620 4 HIS A 201   O   135.1  73.5  72.3                                  
REMARK 620 5 ASP A 167   OD2  80.6  65.9  84.8 137.8                            
REMARK 620 6 ASP A 167   OD1  88.8  98.6  60.5 132.0  48.7                      
REMARK 620 7 HOH A 554   O    71.0  67.7 137.9  83.8  90.9 138.0                
REMARK 620 8 ASN A 100   OD1  79.5 146.1  75.4 106.7 100.9  55.2 146.0          
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 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 507                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 A SEQUENCE DATABASE REFERENCE FOR THIS PROTEIN DOES NOT CURRENTLY    
REMARK 999 EXIST.                                                               
DBREF  3VM5 A    1   505  PDB    3VM5     3VM5             1    505             
SEQRES   1 A  505  GLN HIS ASN PRO ASN THR ARG ASP GLY ARG THR ALA ILE          
SEQRES   2 A  505  VAL HIS LEU PHE GLU TRP ARG TRP ALA ASP ILE ALA ALA          
SEQRES   3 A  505  GLU CYS GLU ARG PHE LEU GLY PRO LYS GLY PHE ALA GLY          
SEQRES   4 A  505  VAL GLN ILE SER PRO PRO ASN GLU HIS ILE LEU VAL SER          
SEQRES   5 A  505  SER PRO TRP ARG PRO TRP TRP GLN ARG TYR GLN PRO ILE          
SEQRES   6 A  505  SER TYR ASN LEU CYS SER ARG SER GLY GLY GLU ASN GLU          
SEQRES   7 A  505  LEU ARG ASP MET ILE THR ARG CYS ASN ASN VAL GLY VAL          
SEQRES   8 A  505  ASN VAL TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY          
SEQRES   9 A  505  ALA GLY GLY GLY GLU GLY THR HIS SER SER CYS GLY SER          
SEQRES  10 A  505  TRP PHE ASN ALA ASN ASN LYS ASP PHE PRO SER VAL PRO          
SEQRES  11 A  505  TYR SER ASN LEU ASP PHE ASN ASP GLY LYS CYS LYS THR          
SEQRES  12 A  505  GLY SER GLY ASN ILE GLU ASN TYR GLY ASP PRO TYR GLN          
SEQRES  13 A  505  VAL ARG ASP CYS ARG LEU VAL GLY LEU LEU ASP LEU ALA          
SEQRES  14 A  505  LEU GLU LYS ASP TYR VAL ARG GLY LYS VAL ALA ASP PHE          
SEQRES  15 A  505  MET ASN LYS LEU ILE ASP MET GLY VAL ALA GLY PHE ARG          
SEQRES  16 A  505  VAL ASP ALA CYS LYS HIS MET TRP PRO GLY ASP LEU ASP          
SEQRES  17 A  505  ASN VAL TYR ARG ARG LEU ASN ASN LEU ASN THR LYS TRP          
SEQRES  18 A  505  PHE PRO GLY GLY SER ARG PRO PHE ILE PHE GLN GLU VAL          
SEQRES  19 A  505  ILE ASP LEU GLY GLY GLU PRO ILE THR THR GLY GLU TYR          
SEQRES  20 A  505  VAL GLY LEU GLY ARG VAL THR GLU PHE LYS TYR GLY ALA          
SEQRES  21 A  505  ARG LEU GLY GLU LEU PHE ARG LYS TRP ASN GLY GLN LYS          
SEQRES  22 A  505  LEU SER TYR THR LYS ASN TRP GLY GLU GLY TRP GLY PHE          
SEQRES  23 A  505  MET ALA ASP GLY ASN ALA VAL VAL PHE THR ASP ASN HIS          
SEQRES  24 A  505  ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY ALA SER ILE          
SEQRES  25 A  505  LEU THR PHE TRP ASP PRO ARG LEU TYR LYS MET ALA VAL          
SEQRES  26 A  505  GLY TYR MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL          
SEQRES  27 A  505  MET SER SER TYR SER TRP ASP ARG ASN PHE VAL ASN GLY          
SEQRES  28 A  505  LYS ASP GLU ASN ASP TRP ILE GLY PRO PRO SER ASN GLY          
SEQRES  29 A  505  ASP GLY SER THR LYS PRO VAL PRO ILE ASN PRO ASP GLN          
SEQRES  30 A  505  THR CYS GLY ASP GLY TRP VAL CYS GLU HIS ARG TRP ARG          
SEQRES  31 A  505  GLN ILE MET ASN MET VAL GLN PHE ARG ASN VAL VAL ASN          
SEQRES  32 A  505  GLY GLN PRO HIS ALA ASN TRP TRP ASP ASN GLY ASN ASN          
SEQRES  33 A  505  GLN VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL          
SEQRES  34 A  505  PHE ASN ASN ASP ASP TRP ALA LEU ASP VAL THR LEU ASN          
SEQRES  35 A  505  THR GLY LEU PRO GLY GLY THR TYR CYS ASP VAL ILE SER          
SEQRES  36 A  505  GLY ASN LYS ASP GLY GLY SER CYS THR GLY LYS GLN ILE          
SEQRES  37 A  505  THR VAL GLY GLY ASP GLY ARG ALA HIS PHE TYR ILE ASN          
SEQRES  38 A  505  ASN SER GLU GLU ASP PRO PHE ILE ALA ILE HIS ALA ASP          
SEQRES  39 A  505  SER LYS LEU HIS HIS HIS HIS HIS HIS HIS HIS                  
HET     CA  A 506       1                                                       
HET     CL  A 507       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   2   CA    CA 2+                                                        
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  HOH   *47(H2 O)                                                     
HELIX    1   1 ARG A   20  PHE A   31  1                                  12    
HELIX    2   2 PRO A   57  GLN A   63  5                                   7    
HELIX    3   3 GLY A   75  VAL A   89  1                                  15    
HELIX    4   4 SER A  132  PHE A  136  5                                   5    
HELIX    5   5 ASN A  137  CYS A  141  5                                   5    
HELIX    6   6 ASP A  153  CYS A  160  1                                   8    
HELIX    7   7 LYS A  172  GLY A  190  1                                  19    
HELIX    8   8 ALA A  198  MET A  202  5                                   5    
HELIX    9   9 TRP A  203  ARG A  212  1                                  10    
HELIX   10  10 THR A  243  TYR A  247  5                                   5    
HELIX   11  11 GLU A  255  LYS A  268  1                                  14    
HELIX   12  12 TRP A  269  GLN A  272  5                                   4    
HELIX   13  13 LYS A  273  TRP A  280  5                                   8    
HELIX   14  14 GLY A  281  GLY A  285  5                                   5    
HELIX   15  15 ALA A  288  GLY A  290  5                                   3    
HELIX   16  16 ASP A  300  GLY A  304  5                                   5    
HELIX   17  17 GLY A  308  ILE A  312  5                                   5    
HELIX   18  18 ASP A  317  HIS A  331  1                                  15    
HELIX   19  19 CYS A  385  ARG A  388  5                                   4    
HELIX   20  20 TRP A  389  ASN A  403  1                                  15    
HELIX   21  21 ASP A  494  LYS A  496  5                                   3    
SHEET    1   A 9 ALA A  12  HIS A  15  0                                        
SHEET    2   A 9 GLY A  39  ILE A  42  1  O  GLN A  41   N  VAL A  14           
SHEET    3   A 9 ASN A  92  ALA A  97  1  O  TYR A  94   N  VAL A  40           
SHEET    4   A 9 GLY A 193  VAL A 196  1  O  ARG A 195   N  ALA A  97           
SHEET    5   A 9 PHE A 229  GLN A 232  1  O  PHE A 231   N  VAL A 196           
SHEET    6   A 9 ARG A 252  THR A 254  1  O  THR A 254   N  GLN A 232           
SHEET    7   A 9 ALA A 292  VAL A 294  1  O  VAL A 293   N  VAL A 253           
SHEET    8   A 9 PHE A 335  MET A 339  1  O  ARG A 337   N  VAL A 294           
SHEET    9   A 9 ALA A  12  HIS A  15  1  N  HIS A  15   O  VAL A 338           
SHEET    1   B 2 HIS A 101  GLY A 104  0                                        
SHEET    2   B 2 LEU A 165  ASP A 167 -1  O  LEU A 166   N  CYS A 103           
SHEET    1   C 2 GLU A 109  GLY A 110  0                                        
SHEET    2   C 2 PHE A 119  ASN A 120 -1  O  PHE A 119   N  GLY A 110           
SHEET    1   D 4 HIS A 407  ASP A 412  0                                        
SHEET    2   D 4 GLN A 417  ARG A 422 -1  O  GLY A 421   N  ALA A 408           
SHEET    3   D 4 GLY A 426  ASN A 431 -1  O  PHE A 430   N  VAL A 418           
SHEET    4   D 4 PHE A 488  HIS A 492 -1  O  ILE A 489   N  VAL A 429           
SHEET    1   E 2 LEU A 437  ASN A 442  0                                        
SHEET    2   E 2 ARG A 475  ILE A 480 -1  O  PHE A 478   N  VAL A 439           
SHEET    1   F 2 GLY A 448  CYS A 451  0                                        
SHEET    2   F 2 GLN A 467  VAL A 470 -1  O  VAL A 470   N  GLY A 448           
SHEET    1   G 2 LYS A 458  ASP A 459  0                                        
SHEET    2   G 2 SER A 462  CYS A 463 -1  O  SER A 462   N  ASP A 459           
SSBOND   1 CYS A   28    CYS A   86                          1555   1555  2.04  
SSBOND   2 CYS A   70    CYS A  115                          1555   1555  2.04  
SSBOND   3 CYS A  141    CYS A  160                          1555   1555  2.07  
SSBOND   4 CYS A  379    CYS A  385                          1555   1555  2.05  
SSBOND   5 CYS A  451    CYS A  463                          1555   1555  2.05  
LINK        CA    CA A 506                 O   HOH A 552     1555   1555  2.40  
LINK         O   ARG A 158                CA    CA A 506     1555   1555  2.48  
LINK        CA    CA A 506                 O   HOH A 553     1555   1555  2.55  
LINK         O   HIS A 201                CA    CA A 506     1555   1555  2.56  
LINK         OD2 ASP A 167                CA    CA A 506     1555   1555  2.60  
LINK         OD1 ASP A 167                CA    CA A 506     1555   1555  2.75  
LINK        CA    CA A 506                 O   HOH A 554     1555   1555  2.89  
LINK         OD1 ASN A 100                CA    CA A 506     1555   1555  3.06  
CISPEP   1 SER A   53    PRO A   54          0        -0.18                     
CISPEP   2 VAL A  129    PRO A  130          0        -4.15                     
SITE     1 AC1  7 ASN A 100  ARG A 158  ASP A 167  HIS A 201                    
SITE     2 AC1  7 HOH A 552  HOH A 553  HOH A 554                               
SITE     1 AC2  3 ARG A 195  ASN A 298  ARG A 337                               
CRYST1   83.045   83.045  174.228  90.00  90.00 120.00 P 32 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      0.012042  0.006952  0.000000        0.00000                         
SCALE2      0.000000  0.013905  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005740        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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