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Database: PDB
Entry: 2GVY
LinkDB: 2GVY
Original site: 2GVY 
HEADER    HYDROLASE                               03-MAY-06   2GVY              
TITLE     MONOCLINIC CRYSTAL FORM OF ASPERGILLUS NIGER ALPHA-AMYLASE IN COMPLEX 
TITLE    2 WITH MALTOSE AT 1.8 A RESOLUTION                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE A;                                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: TAKA-AMYLASE A, TAA, 1,4- ALPHA-D-GLUCAN GLUCANOHYDROLASE;  
COMPND   5 EC: 3.2.1.1;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS ORYZAE;                             
SOURCE   3 ORGANISM_TAXID: 5062;                                                
SOURCE   4 GENE: AMY1;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ASPERGILLUS ORYZAE;                               
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 5062                                        
KEYWDS    (BETA-ALPHA)8 BARREL, HYDROLASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.VUJICIC-ZAGAR,B.W.DIJKSTRA                                          
REVDAT   4   13-JUL-11 2GVY    1       VERSN                                    
REVDAT   3   08-SEP-09 2GVY    1       HETATM HETNAM                            
REVDAT   2   24-FEB-09 2GVY    1       VERSN                                    
REVDAT   1   15-AUG-06 2GVY    0                                                
JRNL        AUTH   A.VUJICIC-ZAGAR,B.W.DIJKSTRA                                 
JRNL        TITL   MONOCLINIC CRYSTAL FORM OF ASPERGILLUS NIGER ALPHA-AMYLASE   
JRNL        TITL 2 IN COMPLEX WITH MALTOSE AT 1.8 ANGSTROMS RESOLUTION.         
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  62   716 2006              
JRNL        REFN                   ESSN 1744-3091                               
JRNL        PMID   16880540                                                     
JRNL        DOI    10.1107/S1744309106024729                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 84733                          
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) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4244                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5757                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2120                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 315                          
REMARK   3   BIN FREE R VALUE                    : 0.2900                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7372                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 168                                     
REMARK   3   SOLVENT ATOMS            : 751                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : 2.21000                                              
REMARK   3    B33 (A**2) : -2.30000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.32000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.126         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.125         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.087         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.792         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7745 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10596 ; 1.674 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   950 ; 6.301 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   348 ;36.408 ;25.115       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1134 ;14.648 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ; 9.206 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1196 ; 0.119 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5892 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4041 ; 0.217 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5453 ; 0.323 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1284 ; 0.184 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     7 ; 0.039 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    31 ; 0.187 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    51 ; 0.199 ; 0.500       
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):  4795 ; 1.387 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7606 ; 1.981 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3411 ; 1.650 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2990 ; 2.250 ; 3.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2GVY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB037614.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97910                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : PRODC                              
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 84823                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 72.987                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.10400                            
REMARK 200  R SYM                      (I) : 0.10400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.57800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 6000, 0.1M AMMONIUM SULPHATE,    
REMARK 280  0.1M MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 296K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       50.57450            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 465     SER B   477                                                      
REMARK 465     SER B   478                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CD   LYS A   221     O    HOH A  1159              1.81            
REMARK 500   O4   GLC A   999     O    HOH A  1313              1.94            
REMARK 500   O    HOH B  1163     O    HOH B  1357              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  78       45.11    -80.14                                   
REMARK 500    SER A 141       32.19    -96.07                                   
REMARK 500    ALA A 329      122.10    -37.07                                   
REMARK 500    ASP A 340      124.46    -31.13                                   
REMARK 500    ALA A 430      130.64    -36.97                                   
REMARK 500    ALA B  78       43.39    -80.63                                   
REMARK 500    GLN B  85      -31.68   -131.32                                   
REMARK 500    ALA B 329      122.00    -33.86                                   
REMARK 500    ASP B 340      119.55    -34.41                                   
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 A1134        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH B1060        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH B1298        DISTANCE =  5.23 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 801  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 162   O                                                      
REMARK 620 2 ASP A 175   OD2  79.3                                              
REMARK 620 3 HOH A1013   O    75.0  89.6                                        
REMARK 620 4 HOH A1083   O    67.5  98.6 139.1                                  
REMARK 620 5 ASN A 121   OD1 156.0 119.9  90.0 118.7                            
REMARK 620 6 ASP A 175   OD1 115.3  50.6  67.8 144.0  74.3                      
REMARK 620 7 HIS A 210   O    82.5 160.6  79.2  80.4  76.3 135.1                
REMARK 620 8 HOH A1211   O   132.4  75.6 143.3  77.1  69.9  77.1 122.4          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 802  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 210   O                                                      
REMARK 620 2 GLU B 162   O    81.9                                              
REMARK 620 3 HOH B1023   O    82.3  72.6                                        
REMARK 620 4 ASN B 121   OD1  75.9 156.1 112.6                                  
REMARK 620 5 ASP B 175   OD1 137.5 117.0 138.2  75.6                            
REMARK 620 6 ASP B 175   OD2 159.3  77.7  95.1 123.3  52.8                      
REMARK 620 7 HOH B1252   O   121.6 131.9  70.5  69.2  75.5  76.0                
REMARK 620 8 HOH B1006   O    77.9  75.7 144.6  90.8  71.6  93.3 144.8          
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 NAG A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC B 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 802                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2TAA   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN, DIFFERENT CRYSTAL FORM.                            
REMARK 900 RELATED ID: 6TAA   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN, DIFFERENT CRYSTAL FORM.                            
REMARK 900 RELATED ID: 7TAA   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH THE INHIBITOR ACARBOSE,             
REMARK 900 DIFFERENT CRYSTAL FORM.                                              
REMARK 900 RELATED ID: 2GUY   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH MALTOSE, DIFFERENT CRYSTAL          
REMARK 900 FORM.                                                                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 CURRENTLY THERE IS NO AMINOACID SEQUENCE DATABASE REFERENCE          
REMARK 999 AVAILABLE FOR THE PROTEIN                                            
DBREF  2GVY A    1   478  UNP    P0C1B3   AMYA1_ASPOR     22    499             
DBREF  2GVY B    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                      
SEQRES   1 B  478  ALA THR PRO ALA ASP TRP ARG SER GLN SER ILE TYR PHE          
SEQRES   2 B  478  LEU LEU THR ASP ARG PHE ALA ARG THR ASP GLY SER THR          
SEQRES   3 B  478  THR ALA THR CYS ASN THR ALA ASP GLN LYS TYR CYS GLY          
SEQRES   4 B  478  GLY THR TRP GLN GLY ILE ILE ASP LYS LEU ASP TYR ILE          
SEQRES   5 B  478  GLN GLY MET GLY PHE THR ALA ILE TRP ILE THR PRO VAL          
SEQRES   6 B  478  THR ALA GLN LEU PRO GLN THR THR ALA TYR GLY ASP ALA          
SEQRES   7 B  478  TYR HIS GLY TYR TRP GLN GLN ASP ILE TYR SER LEU ASN          
SEQRES   8 B  478  GLU ASN TYR GLY THR ALA ASP ASP LEU LYS ALA LEU SER          
SEQRES   9 B  478  SER ALA LEU HIS GLU ARG GLY MET TYR LEU MET VAL ASP          
SEQRES  10 B  478  VAL VAL ALA ASN HIS MET GLY TYR ASP GLY ALA GLY SER          
SEQRES  11 B  478  SER VAL ASP TYR SER VAL PHE LYS PRO PHE SER SER GLN          
SEQRES  12 B  478  ASP TYR PHE HIS PRO PHE CYS PHE ILE GLN ASN TYR GLU          
SEQRES  13 B  478  ASP GLN THR GLN VAL GLU ASP CYS TRP LEU GLY ASP ASN          
SEQRES  14 B  478  THR VAL SER LEU PRO ASP LEU ASP THR THR LYS ASP VAL          
SEQRES  15 B  478  VAL LYS ASN GLU TRP TYR ASP TRP VAL GLY SER LEU VAL          
SEQRES  16 B  478  SER ASN TYR SER ILE ASP GLY LEU ARG ILE ASP THR VAL          
SEQRES  17 B  478  LYS HIS VAL GLN LYS ASP PHE TRP PRO GLY TYR ASN LYS          
SEQRES  18 B  478  ALA ALA GLY VAL TYR CYS ILE GLY GLU VAL LEU ASP GLY          
SEQRES  19 B  478  ASP PRO ALA TYR THR CYS PRO TYR GLN ASN VAL MET ASP          
SEQRES  20 B  478  GLY VAL LEU ASN TYR PRO ILE TYR TYR PRO LEU LEU ASN          
SEQRES  21 B  478  ALA PHE LYS SER THR SER GLY SER MET ASP ASP LEU TYR          
SEQRES  22 B  478  ASN MET ILE ASN THR VAL LYS SER ASP CYS PRO ASP SER          
SEQRES  23 B  478  THR LEU LEU GLY THR PHE VAL GLU ASN HIS ASP ASN PRO          
SEQRES  24 B  478  ARG PHE ALA SER TYR THR ASN ASP ILE ALA LEU ALA LYS          
SEQRES  25 B  478  ASN VAL ALA ALA PHE ILE ILE LEU ASN ASP GLY ILE PRO          
SEQRES  26 B  478  ILE ILE TYR ALA GLY GLN GLU GLN HIS TYR ALA GLY GLY          
SEQRES  27 B  478  ASN ASP PRO ALA ASN ARG GLU ALA THR TRP LEU SER GLY          
SEQRES  28 B  478  TYR PRO THR ASP SER GLU LEU TYR LYS LEU ILE ALA SER          
SEQRES  29 B  478  ALA ASN ALA ILE ARG ASN TYR ALA ILE SER LYS ASP THR          
SEQRES  30 B  478  GLY PHE VAL THR TYR LYS ASN TRP PRO ILE TYR LYS ASP          
SEQRES  31 B  478  ASP THR THR ILE ALA MET ARG LYS GLY THR ASP GLY SER          
SEQRES  32 B  478  GLN ILE VAL THR ILE LEU SER ASN LYS GLY ALA SER GLY          
SEQRES  33 B  478  ASP SER TYR THR LEU SER LEU SER GLY ALA GLY TYR THR          
SEQRES  34 B  478  ALA GLY GLN GLN LEU THR GLU VAL ILE GLY CYS THR THR          
SEQRES  35 B  478  VAL THR VAL GLY SER ASP GLY ASN VAL PRO VAL PRO MET          
SEQRES  36 B  478  ALA GLY GLY LEU PRO ARG VAL LEU TYR PRO THR GLU LYS          
SEQRES  37 B  478  LEU ALA GLY SER LYS ILE CYS SER SER SER                      
MODRES 2GVY ASN A  197  ASN  GLYCOSYLATION SITE                                 
MODRES 2GVY ASN B  197  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 500      14                                                       
HET    BGC  A1002      12                                                       
HET    GLC  A1001      11                                                       
HET    GLC  A1000      12                                                       
HET    GLC  A 999      11                                                       
HET    BGC  A1003      12                                                       
HET    GLC  A1004      11                                                       
HET    GLC  A1011      12                                                       
HET    GLC  A1012      11                                                       
HET     CA  A 801       1                                                       
HET    NDG  B 500      14                                                       
HET    GLC  B1000      12                                                       
HET    GLC  B 999      11                                                       
HET    BGC  B1002      12                                                       
HET    GLC  B1001      11                                                       
HET     CA  B 802       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM      CA CALCIUM ION                                                      
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
FORMUL   3  NAG    C8 H15 N O6                                                  
FORMUL   4  BGC    3(C6 H12 O6)                                                 
FORMUL   4  GLC    9(C6 H12 O6)                                                 
FORMUL   8   CA    2(CA 2+)                                                     
FORMUL   9  NDG    C8 H15 N O6                                                  
FORMUL  13  HOH   *751(H2 O)                                                    
HELIX    1   1 THR A    2  SER A    8  1                                   7    
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  MET A   55  1                                   8    
HELIX    6   6 THR A   96  ARG A  110  1                                  15    
HELIX    7   7 ALA A  128  VAL A  132  5                                   5    
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  LYS A  263  1                                  13    
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    
HELIX   26  26 THR B    2  ARG B    7  1                                   6    
HELIX   27  27 LEU B   15  ALA B   20  1                                   6    
HELIX   28  28 ASN B   31  GLN B   35  5                                   5    
HELIX   29  29 THR B   41  LYS B   48  1                                   8    
HELIX   30  30 LYS B   48  GLY B   54  1                                   7    
HELIX   31  31 GLU B   92  GLY B   95  5                                   4    
HELIX   32  32 THR B   96  ARG B  110  1                                  15    
HELIX   33  33 ALA B  128  VAL B  132  5                                   5    
HELIX   34  34 ASP B  133  PHE B  137  5                                   5    
HELIX   35  35 SER B  142  PHE B  146  5                                   5    
HELIX   36  36 ASP B  157  CYS B  164  1                                   8    
HELIX   37  37 LYS B  180  SER B  199  1                                  20    
HELIX   38  38 THR B  207  VAL B  211  5                                   5    
HELIX   39  39 GLN B  212  ASP B  214  5                                   3    
HELIX   40  40 PHE B  215  GLY B  224  1                                  10    
HELIX   41  41 ASP B  235  CYS B  240  1                                   6    
HELIX   42  42 PRO B  241  VAL B  245  5                                   5    
HELIX   43  43 ASN B  251  LYS B  263  1                                  13    
HELIX   44  44 SER B  268  CYS B  283  1                                  16    
HELIX   45  45 ASP B  285  LEU B  288  5                                   4    
HELIX   46  46 ARG B  300  THR B  305  1                                   6    
HELIX   47  47 ASP B  307  ASN B  321  1                                  15    
HELIX   48  48 GLY B  330  HIS B  334  5                                   5    
HELIX   49  49 ALA B  346  GLY B  351  5                                   6    
HELIX   50  50 SER B  356  ASP B  376  1                                  21    
HELIX   51  51 GLU B  467  ALA B  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  ILE A 228           
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  ILE A 327   N  PHE A  13           
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  GLN A  85   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  ALA A 395   N  TYR A 388           
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  LEU A 463   N  VAL A 406           
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           
SHEET    1   F 8 GLY B 248  VAL B 249  0                                        
SHEET    2   F 8 TYR B 226  GLY B 229  1  N  GLY B 229   O  GLY B 248           
SHEET    3   F 8 GLY B 202  ILE B 205  1  N  LEU B 203   O  ILE B 228           
SHEET    4   F 8 TYR B 113  VAL B 118  1  N  VAL B 118   O  ARG B 204           
SHEET    5   F 8 ALA B  59  ILE B  62  1  N  ILE B  60   O  MET B 115           
SHEET    6   F 8 ILE B  11  LEU B  14  1  N  LEU B  14   O  TRP B  61           
SHEET    7   F 8 ILE B 324  TYR B 328  1  O  PRO B 325   N  ILE B  11           
SHEET    8   F 8 GLY B 290  THR B 291  1  N  THR B 291   O  ILE B 326           
SHEET    1   G 2 THR B  66  GLN B  68  0                                        
SHEET    2   G 2 GLN B  84  LEU B  90 -1  O  GLN B  85   N  ALA B  67           
SHEET    1   H 3 TYR B 125  ASP B 126  0                                        
SHEET    2   H 3 VAL B 171  LEU B 173 -1  O  SER B 172   N  TYR B 125           
SHEET    3   H 3 LEU B 166  GLY B 167 -1  N  LEU B 166   O  LEU B 173           
SHEET    1   I 6 TRP B 385  ASP B 390  0                                        
SHEET    2   I 6 THR B 393  LYS B 398 -1  O  ARG B 397   N  TRP B 385           
SHEET    3   I 6 ILE B 405  SER B 410 -1  O  LEU B 409   N  ILE B 394           
SHEET    4   I 6 ARG B 461  PRO B 465 -1  O  ARG B 461   N  ILE B 408           
SHEET    5   I 6 GLN B 433  GLU B 436 -1  N  THR B 435   O  TYR B 464           
SHEET    6   I 6 THR B 441  THR B 444 -1  O  VAL B 443   N  LEU B 434           
SHEET    1   J 2 TYR B 419  LEU B 423  0                                        
SHEET    2   J 2 VAL B 451  MET B 455 -1  O  MET B 455   N  TYR B 419           
SSBOND   1 CYS A   30    CYS A   38                          1555   1555  2.07  
SSBOND   2 CYS A  150    CYS A  164                          1555   1555  2.52  
SSBOND   3 CYS A  240    CYS A  283                          1555   1555  2.01  
SSBOND   4 CYS A  440    CYS A  475                          1555   1555  2.07  
SSBOND   5 CYS B   30    CYS B   38                          1555   1555  2.08  
SSBOND   6 CYS B  150    CYS B  164                          1555   1555  2.09  
SSBOND   7 CYS B  240    CYS B  283                          1555   1555  2.00  
SSBOND   8 CYS B  440    CYS B  475                          1555   1555  2.08  
LINK         ND2 ASN A 197                 C1  NAG A 500     1555   1555  1.44  
LINK         ND2 ASN B 197                 C1  NDG B 500     1555   1555  1.46  
LINK         O4  GLC A1000                 C1  GLC A 999     1555   1555  1.42  
LINK         O4  GLC A1011                 C1  GLC A1012     1555   1555  1.43  
LINK         O4  GLC B1000                 C1  GLC B 999     1555   1555  1.44  
LINK        CA    CA A 801                 O   GLU A 162     1555   1555  2.48  
LINK        CA    CA A 801                 OD2 ASP A 175     1555   1555  2.47  
LINK        CA    CA A 801                 O   HOH A1013     1555   1555  2.65  
LINK        CA    CA A 801                 O   HOH A1083     1555   1555  2.41  
LINK        CA    CA A 801                 OD1 ASN A 121     1555   1555  2.41  
LINK        CA    CA A 801                 OD1 ASP A 175     1555   1555  2.72  
LINK        CA    CA A 801                 O   HIS A 210     1555   1555  2.38  
LINK        CA    CA A 801                 O   HOH A1211     1555   1555  2.35  
LINK        CA    CA B 802                 O   HIS B 210     1555   1555  2.39  
LINK        CA    CA B 802                 O   GLU B 162     1555   1555  2.39  
LINK        CA    CA B 802                 O   HOH B1023     1555   1555  2.59  
LINK        CA    CA B 802                 OD1 ASN B 121     1555   1555  2.39  
LINK        CA    CA B 802                 OD1 ASP B 175     1555   1555  2.58  
LINK        CA    CA B 802                 OD2 ASP B 175     1555   1555  2.49  
LINK        CA    CA B 802                 O   HOH B1252     1555   1555  2.53  
LINK        CA    CA B 802                 O   HOH B1006     1555   1555  2.51  
LINK         O4  BGC A1002                 C1  GLC A1001     1555   1555  1.42  
LINK         O4  BGC A1003                 C1  GLC A1004     1555   1555  1.45  
LINK         O4  BGC B1002                 C1  GLC B1001     1555   1555  1.44  
CISPEP   1 LYS A  138    PRO A  139          0         3.16                     
CISPEP   2 ASP A  340    PRO A  341          0         8.05                     
CISPEP   3 LYS B  138    PRO B  139          0         4.74                     
CISPEP   4 ASP B  340    PRO B  341          0        14.28                     
SITE     1 AC1  6 TYR A  88  TRP A 190  SER A 193  LEU A 194                    
SITE     2 AC1  6 ASN A 197  HOH A1180                                          
SITE     1 AC2  4 TYR A 155  LYS A 209  GLC A1001  HOH A1309                    
SITE     1 AC3 11 TYR A 155  LEU A 166  HIS A 210  GLC A1000                    
SITE     2 AC3 11 BGC A1002  HOH A1066  HOH A1069  HOH A1168                    
SITE     3 AC3 11 HOH A1312  HOH A1327  HOH A1372                               
SITE     1 AC4 13 TYR A  82  HIS A 122  ARG A 204  ASP A 206                    
SITE     2 AC4 13 THR A 207  GLU A 230  HIS A 296  ASP A 297                    
SITE     3 AC4 13 ARG A 344  GLC A 999  GLC A1001  HOH A1069                    
SITE     4 AC4 13 HOH A1372                                                     
SITE     1 AC5 13 HIS A  80  TYR A  82  TRP A  83  LEU A 173                    
SITE     2 AC5 13 ASP A 340  ARG A 344  GLC A1000  HOH A1030                    
SITE     3 AC5 13 HOH A1069  HOH A1310  HOH A1311  HOH A1312                    
SITE     4 AC5 13 HOH A1313                                                     
SITE     1 AC6  7 GLY A 234  ASP A 235  PRO A 236  GLC A1004                    
SITE     2 AC6  7 HOH A1141  HOH A1194  HOH A1376                               
SITE     1 AC7  6 ASP A 233  GLY A 234  ASP A 235  TYR A 256                    
SITE     2 AC7  6 BGC A1003  HOH A1374                                          
SITE     1 AC8  3 LYS A 280  GLC A1012  HOH A1333                               
SITE     1 AC9  5 TYR A 382  LYS A 383  GLC A1011  HOH A1146                    
SITE     2 AC9  5 HOH A1344                                                     
SITE     1 BC1  7 ASN A 121  GLU A 162  ASP A 175  HIS A 210                    
SITE     2 BC1  7 HOH A1013  HOH A1083  HOH A1211                               
SITE     1 BC2  6 TYR B  88  TRP B 190  SER B 193  ASN B 197                    
SITE     2 BC2  6 HOH B1159  HOH B1342                                          
SITE     1 BC3 11 TYR B  82  HIS B 122  ARG B 204  ASP B 206                    
SITE     2 BC3 11 THR B 207  GLU B 230  HIS B 296  ASP B 297                    
SITE     3 BC3 11 ARG B 344  GLC B 999  GLC B1001                               
SITE     1 BC4  8 TYR B  82  TRP B  83  ASP B 340  ARG B 344                    
SITE     2 BC4  8 GLC B1000  HOH B1163  HOH B1178  HOH B1357                    
SITE     1 BC5  4 TYR B 155  LYS B 209  GLC B1001  HOH B1358                    
SITE     1 BC6  6 TYR B 155  LEU B 166  HIS B 210  GLC B1000                    
SITE     2 BC6  6 BGC B1002  HOH B1040                                          
SITE     1 BC7  7 ASN B 121  GLU B 162  ASP B 175  HIS B 210                    
SITE     2 BC7  7 HOH B1006  HOH B1023  HOH B1252                               
CRYST1   65.451  101.149   75.185  90.00 103.89  90.00 P 1 21 1      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      0.015279  0.000000  0.003778        0.00000                         
SCALE2      0.000000  0.009886  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013701        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system