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Database: PDB
Entry: 1KXQ
LinkDB: 1KXQ
Original site: 1KXQ 
HEADER    HYDROLASE, IMMUNE SYSTEM                01-FEB-02   1KXQ              
TITLE     CAMELID VHH DOMAIN IN COMPLEX WITH PORCINE PANCREATIC ALPHA-          
TITLE    2 AMYLASE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE, PANCREATIC;                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE;                        
COMPND   5 EC: 3.2.1.1;                                                         
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ANTIBODY VHH FRAGMENT CABAMD9;                             
COMPND   8 CHAIN: E, F, G, H;                                                   
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 OTHER_DETAILS: PANCREATIC ENZYME;                                    
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: CAMELUS DROMEDARIUS;                            
SOURCE   8 ORGANISM_COMMON: ARABIAN CAMEL;                                      
SOURCE   9 ORGANISM_TAXID: 9838;                                                
SOURCE  10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  12 EXPRESSION_SYSTEM_STRAIN: WK6;                                       
SOURCE  13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    ALPHA 8 BETA 8, BETA BARREL, HYDROLASE, IMMUNE SYSTEM                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.DESMYTER,S.SPINELLI,F.PAYAN,M.LAUWEREYS,L.WYNS,                     
AUTHOR   2 S.MUYLDERMANS,C.CAMBILLAU                                            
REVDAT   4   24-FEB-09 1KXQ    1       VERSN                                    
REVDAT   3   01-APR-03 1KXQ    1       JRNL                                     
REVDAT   2   14-AUG-02 1KXQ    1       JRNL                                     
REVDAT   1   19-JUN-02 1KXQ    0                                                
JRNL        AUTH   A.DESMYTER,S.SPINELLI,F.PAYAN,M.LAUWEREYS,L.WYNS,            
JRNL        AUTH 2 S.MUYLDERMANS,C.CAMBILLAU                                    
JRNL        TITL   THREE CAMELID VHH DOMAINS IN COMPLEX WITH PORCINE            
JRNL        TITL 2 PANCREATIC ALPHA-AMYLASE. INHIBITION AND                     
JRNL        TITL 3 VERSATILITY OF BINDING TOPOLOGY.                             
JRNL        REF    J.BIOL.CHEM.                  V. 277 23645 2002              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   11960990                                                     
JRNL        DOI    10.1074/JBC.M202327200                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.LAUWEREYS,M.ARBABI GHAHROUDI,A DESMYTER,J.KINNE,           
REMARK   1  AUTH 2 W.HOLZER,E.DE GENST,L.WYNS,S.MUYLDERMANS                     
REMARK   1  TITL   POTENT ENZYME INHIBITORS DERIVED FROM DROMEDARY              
REMARK   1  TITL 2 HEAVY-CHAIN ANTIBODIES.                                      
REMARK   1  REF    EMBO J.                       V.  17  3512 1998              
REMARK   1  REFN                   ISSN 0261-4189                               
REMARK   1  DOI    10.1093/EMBOJ/17.13.3512                                     
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   M.QIAN,R.HASER,F.PAYAN                                       
REMARK   1  TITL   STRUCTURE AND MOLECULAR MODEL REFINEMENT OF PIG              
REMARK   1  TITL 2 PANCREATIC ALPHA-AMYLASE AT 2.1 A RESOLUTION                 
REMARK   1  REF    J.MOL.BIOL.                   V. 231   785 1993              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  DOI    10.1006/JMBI.1993.1326                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.79                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1735909.730                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 317086                         
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 SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9426                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.002                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 29934                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580                       
REMARK   3   BIN FREE R VALUE                    : 0.2780                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 913                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.009                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 19304                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 2807                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.49000                                              
REMARK   3    B22 (A**2) : -1.66000                                             
REMARK   3    B33 (A**2) : -1.83000                                             
REMARK   3    B12 (A**2) : -2.22000                                             
REMARK   3    B13 (A**2) : -2.35000                                             
REMARK   3    B23 (A**2) : 0.85000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.19                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.16                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 10.00                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.21                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.18                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.92                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 48.68                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1KXQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB015445.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID09                               
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                  : MIRRORS                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 383526                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 70.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1JFH, PDB ENTRY 1QD0                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PHOSPHATE BUFFER 0.8 M, PH 7.0,          
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H                                  
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F                                  
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E                                  
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER E 120    OG                                                  
REMARK 470     SER F 120    OG                                                  
REMARK 470     SER G 120    OG                                                  
REMARK 470     SER H 120    OG                                                  
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   OE2  GLU A   352     OD1  ASN H    97              1.75            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A  70   CA  -  CB  -  SG  ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG A  92   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    LEU A 293   CA  -  CB  -  CG  ANGL. DEV. = -16.2 DEGREES          
REMARK 500    CYS B  70   CA  -  CB  -  SG  ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ARG C  72   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    CYS D  70   CA  -  CB  -  SG  ANGL. DEV. =   7.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  31      -57.52   -146.04                                   
REMARK 500    MET A 102     -153.47   -108.19                                   
REMARK 500    VAL A 163       51.50     36.61                                   
REMARK 500    ASP A 317       58.98   -118.55                                   
REMARK 500    SER A 414     -105.59   -132.25                                   
REMARK 500    ASP A 433       32.51    -87.52                                   
REMARK 500    ASN A 460       49.88    -97.21                                   
REMARK 500    PRO A 486       47.01    -76.66                                   
REMARK 500    TYR B  31      -57.24   -149.75                                   
REMARK 500    SER B  66     -179.57   -172.60                                   
REMARK 500    MET B 102     -156.98   -109.77                                   
REMARK 500    VAL B 163       47.48     37.66                                   
REMARK 500    SER B 414     -109.71   -132.91                                   
REMARK 500    ASP B 433       35.49    -90.50                                   
REMARK 500    ASN B 460       40.35   -105.43                                   
REMARK 500    PRO B 486       38.83    -74.71                                   
REMARK 500    TYR C  31      -56.42   -142.82                                   
REMARK 500    MET C 102     -155.88   -109.34                                   
REMARK 500    VAL C 163       49.12     37.50                                   
REMARK 500    ASP C 317       59.65   -115.43                                   
REMARK 500    THR C 376        4.74     82.03                                   
REMARK 500    SER C 414     -110.38   -133.91                                   
REMARK 500    ASP C 433       32.79    -88.13                                   
REMARK 500    PRO C 486       45.43    -79.12                                   
REMARK 500    TYR D  31      -57.48   -141.20                                   
REMARK 500    MET D 102     -145.14   -107.70                                   
REMARK 500    VAL D 163       47.82     37.12                                   
REMARK 500    SER D 414     -109.61   -129.54                                   
REMARK 500    ASP D 433       37.26    -93.16                                   
REMARK 500    PRO D 486       41.14    -77.99                                   
REMARK 500    ASN E  97       16.76   -146.64                                   
REMARK 500    ARG E 100       72.84   -104.91                                   
REMARK 500    VAL F   2       99.90   -179.95                                   
REMARK 500    PRO F  38      107.21    -35.30                                   
REMARK 500    ASN F  97       21.73   -145.81                                   
REMARK 500    ARG F 100       72.43   -119.49                                   
REMARK 500    VAL G   2      103.05   -168.87                                   
REMARK 500    ASN G  97       20.90   -144.42                                   
REMARK 500    ARG G 100       74.15   -105.28                                   
REMARK 500    ASN H  97       19.37   -146.62                                   
REMARK 500    ARG H 100       72.62   -111.15                                   
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 E 208        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH G 219        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH E 258        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH C4271        DISTANCE =  5.43 ANGSTROMS                       
REMARK 525    HOH C4273        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH C4394        DISTANCE =  7.93 ANGSTROMS                       
REMARK 525    HOH C4403        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH C4427        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH C4432        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH C4447        DISTANCE =  8.36 ANGSTROMS                       
REMARK 525    HOH B4498        DISTANCE =  6.91 ANGSTROMS                       
REMARK 525    HOH B4529        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH D4642        DISTANCE =  9.26 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 A4001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 167   OD1                                                    
REMARK 620 2 HOH A4094   O    73.5                                              
REMARK 620 3 ARG A 158   O   120.5  76.3                                        
REMARK 620 4 ASP A 167   OD2  52.6  86.5  75.8                                  
REMARK 620 5 HOH A4014   O    76.2 149.6 120.9  75.4                            
REMARK 620 6 HOH A4125   O   137.2 143.5  70.3  98.9  64.8                      
REMARK 620 7 ASN A 100   OD1  79.4 102.1 157.4 126.7  71.5 103.1                
REMARK 620 8 HIS A 201   O   138.4  80.6  82.7 157.0 123.8  81.0  74.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B4003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B4307   O                                                      
REMARK 620 2 ASN B 100   OD1  72.2                                              
REMARK 620 3 ASP B 167   OD1  74.6  82.4                                        
REMARK 620 4 HIS B 201   O   125.1  73.7 139.9                                  
REMARK 620 5 HOH B4012   O    62.0  98.6 133.5  82.5                            
REMARK 620 6 HOH B4030   O   145.9 100.2  71.4  81.5 150.7                      
REMARK 620 7 ASP B 167   OD2  71.9 128.4  53.0 157.6  95.9  89.7                
REMARK 620 8 ARG B 158   O   121.8 154.6 120.5  81.1  74.2  79.2  77.0          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C4005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C 100   OD1                                                    
REMARK 620 2 ASP C 167   OD1  80.9                                              
REMARK 620 3 ASP C 167   OD2 127.6  52.6                                        
REMARK 620 4 HOH C4047   O   103.1  73.3  86.7                                  
REMARK 620 5 HOH C4060   O    99.8 136.0  99.1 145.6                            
REMARK 620 6 HIS C 201   O    73.8 139.2 157.8  81.9  80.4                      
REMARK 620 7 ARG C 158   O   155.9 121.5  76.4  77.7  71.0  82.5                
REMARK 620 8 HOH C4022   O    70.6  74.5  74.5 147.8  64.8 123.6 121.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D4007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 201   O                                                      
REMARK 620 2 HOH D4041   O    82.3                                              
REMARK 620 3 ASP D 167   OD2 156.9  88.4                                        
REMARK 620 4 ASN D 100   OD1  75.9  99.8 126.7                                  
REMARK 620 5 ASP D 167   OD1 140.4  70.5  52.5  80.8                            
REMARK 620 6 HOH D4038   O    79.7 147.6  97.9 101.6 136.9                      
REMARK 620 7 HOH D4016   O   124.1 147.2  73.1  72.4  76.7  63.6                
REMARK 620 8 ARG D 158   O    80.7  78.4  76.8 156.5 119.6  72.3 121.2          
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 4001                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4002                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 4003                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 4004                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 4005                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 4006                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 4007                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 4008                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1KXT   RELATED DB: PDB                                   
REMARK 900 CAMELID VHH DOMAINS IN COMPLEX WITH PORCINE PANCREATIC               
REMARK 900 ALPHA-AMYLASE                                                        
REMARK 900 RELATED ID: 1KXV   RELATED DB: PDB                                   
REMARK 900 CAMELID VHH DOMAINS IN COMPLEX WITH PORCINE PANCREATIC               
REMARK 900 ALPHA-AMYLASE                                                        
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE DISCREPANCY BETWEEN THE SEQUENCE OF THIS                         
REMARK 999 ENTRY AND THE DATABASE REFERENCE IS EXPLAINED                        
REMARK 999 IN REFERENCE 2 GIVEN ABOVE.                                          
REMARK 999                                                                      
REMARK 999                                                                      
REMARK 999 AN APPROPRIATE SEQUENCE DATABASE REFERENCE                           
REMARK 999 FOR THE ANTIBODY VHH FRAGMENT CABAMD9, CHAINS                        
REMARK 999 E, F, G, AND H, WAS NOT AVAILABLE AT THE TIME                        
REMARK 999 OF PROCESSING.                                                       
DBREF  1KXQ A    1   496  UNP    P00690   AMYP_PIG         1    496             
DBREF  1KXQ B    1   496  UNP    P00690   AMYP_PIG         1    496             
DBREF  1KXQ C    1   496  UNP    P00690   AMYP_PIG         1    496             
DBREF  1KXQ D    1   496  UNP    P00690   AMYP_PIG         1    496             
DBREF  1KXQ E    1   120  PDB    1KXQ     1KXQ             1    120             
DBREF  1KXQ F    1   120  PDB    1KXQ     1KXQ             1    120             
DBREF  1KXQ G    1   120  PDB    1KXQ     1KXQ             1    120             
DBREF  1KXQ H    1   120  PDB    1KXQ     1KXQ             1    120             
SEQADV 1KXQ LYS A  243  UNP  P00690    GLN   243 SEE REMARK 999                 
SEQADV 1KXQ SER A  310  UNP  P00690    ALA   310 SEE REMARK 999                 
SEQADV 1KXQ ILE A  323  UNP  P00690    VAL   323 SEE REMARK 999                 
SEQADV 1KXQ GLN A  404  UNP  P00690    GLU   404 SEE REMARK 999                 
SEQADV 1KXQ LYS B  243  UNP  P00690    GLN   243 SEE REMARK 999                 
SEQADV 1KXQ SER B  310  UNP  P00690    ALA   310 SEE REMARK 999                 
SEQADV 1KXQ ILE B  323  UNP  P00690    VAL   323 SEE REMARK 999                 
SEQADV 1KXQ GLN B  404  UNP  P00690    GLU   404 SEE REMARK 999                 
SEQADV 1KXQ LYS C  243  UNP  P00690    GLN   243 SEE REMARK 999                 
SEQADV 1KXQ SER C  310  UNP  P00690    ALA   310 SEE REMARK 999                 
SEQADV 1KXQ ILE C  323  UNP  P00690    VAL   323 SEE REMARK 999                 
SEQADV 1KXQ GLN C  404  UNP  P00690    GLU   404 SEE REMARK 999                 
SEQADV 1KXQ LYS D  243  UNP  P00690    GLN   243 SEE REMARK 999                 
SEQADV 1KXQ SER D  310  UNP  P00690    ALA   310 SEE REMARK 999                 
SEQADV 1KXQ ILE D  323  UNP  P00690    VAL   323 SEE REMARK 999                 
SEQADV 1KXQ GLN D  404  UNP  P00690    GLU   404 SEE REMARK 999                 
SEQRES   1 A  496  GLN TYR ALA PRO GLN THR GLN SER GLY ARG THR SER ILE          
SEQRES   2 A  496  VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU          
SEQRES   3 A  496  GLU CYS GLU ARG TYR LEU GLY PRO LYS GLY PHE GLY GLY          
SEQRES   4 A  496  VAL GLN VAL SER PRO PRO ASN GLU ASN ILE VAL VAL THR          
SEQRES   5 A  496  ASN PRO SER ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL          
SEQRES   6 A  496  SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASN GLU          
SEQRES   7 A  496  PHE ARG ASP MET VAL THR ARG CYS ASN ASN VAL GLY VAL          
SEQRES   8 A  496  ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY          
SEQRES   9 A  496  SER GLY ALA ALA ALA GLY THR GLY THR THR CYS GLY SER          
SEQRES  10 A  496  TYR CYS ASN PRO GLY SER ARG GLU PHE PRO ALA VAL PRO          
SEQRES  11 A  496  TYR SER ALA TRP ASP PHE ASN ASP GLY LYS CYS LYS THR          
SEQRES  12 A  496  ALA SER GLY GLY ILE GLU SER TYR ASN ASP PRO TYR GLN          
SEQRES  13 A  496  VAL ARG ASP CYS GLN LEU VAL GLY LEU LEU ASP LEU ALA          
SEQRES  14 A  496  LEU GLU LYS ASP TYR VAL ARG SER MET ILE ALA ASP TYR          
SEQRES  15 A  496  LEU ASN LYS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG          
SEQRES  16 A  496  ILE ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS          
SEQRES  17 A  496  ALA VAL LEU ASP LYS LEU HIS ASN LEU ASN THR ASN TRP          
SEQRES  18 A  496  PHE PRO ALA GLY SER ARG PRO PHE ILE PHE GLN GLU VAL          
SEQRES  19 A  496  ILE ASP LEU GLY GLY GLU ALA ILE LYS SER SER GLU TYR          
SEQRES  20 A  496  PHE GLY ASN GLY ARG VAL THR GLU PHE LYS TYR GLY ALA          
SEQRES  21 A  496  LYS LEU GLY THR VAL VAL ARG LYS TRP SER GLY GLU LYS          
SEQRES  22 A  496  MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE          
SEQRES  23 A  496  MET PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS          
SEQRES  24 A  496  ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY SER SER ILE          
SEQRES  25 A  496  LEU THR PHE TRP ASP ALA ARG LEU TYR LYS ILE ALA VAL          
SEQRES  26 A  496  GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL          
SEQRES  27 A  496  MET SER SER TYR ARG TRP ALA ARG ASN PHE VAL ASN GLY          
SEQRES  28 A  496  GLU ASP VAL ASN ASP TRP ILE GLY PRO PRO ASN ASN ASN          
SEQRES  29 A  496  GLY VAL ILE LYS GLU VAL THR ILE ASN ALA ASP THR THR          
SEQRES  30 A  496  CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLU          
SEQRES  31 A  496  ILE ARG ASN MET VAL TRP PHE ARG ASN VAL VAL ASP GLY          
SEQRES  32 A  496  GLN PRO PHE ALA ASN TRP TRP ASP ASN GLY SER ASN GLN          
SEQRES  33 A  496  VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE          
SEQRES  34 A  496  ASN ASN ASP ASP TRP GLN LEU SER SER THR LEU GLN THR          
SEQRES  35 A  496  GLY LEU PRO GLY GLY THR TYR CYS ASP VAL ILE SER GLY          
SEQRES  36 A  496  ASP LYS VAL GLY ASN SER CYS THR GLY ILE LYS VAL TYR          
SEQRES  37 A  496  VAL SER SER ASP GLY THR ALA GLN PHE SER ILE SER ASN          
SEQRES  38 A  496  SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER          
SEQRES  39 A  496  LYS LEU                                                      
SEQRES   1 B  496  GLN TYR ALA PRO GLN THR GLN SER GLY ARG THR SER ILE          
SEQRES   2 B  496  VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU          
SEQRES   3 B  496  GLU CYS GLU ARG TYR LEU GLY PRO LYS GLY PHE GLY GLY          
SEQRES   4 B  496  VAL GLN VAL SER PRO PRO ASN GLU ASN ILE VAL VAL THR          
SEQRES   5 B  496  ASN PRO SER ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL          
SEQRES   6 B  496  SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASN GLU          
SEQRES   7 B  496  PHE ARG ASP MET VAL THR ARG CYS ASN ASN VAL GLY VAL          
SEQRES   8 B  496  ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY          
SEQRES   9 B  496  SER GLY ALA ALA ALA GLY THR GLY THR THR CYS GLY SER          
SEQRES  10 B  496  TYR CYS ASN PRO GLY SER ARG GLU PHE PRO ALA VAL PRO          
SEQRES  11 B  496  TYR SER ALA TRP ASP PHE ASN ASP GLY LYS CYS LYS THR          
SEQRES  12 B  496  ALA SER GLY GLY ILE GLU SER TYR ASN ASP PRO TYR GLN          
SEQRES  13 B  496  VAL ARG ASP CYS GLN LEU VAL GLY LEU LEU ASP LEU ALA          
SEQRES  14 B  496  LEU GLU LYS ASP TYR VAL ARG SER MET ILE ALA ASP TYR          
SEQRES  15 B  496  LEU ASN LYS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG          
SEQRES  16 B  496  ILE ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS          
SEQRES  17 B  496  ALA VAL LEU ASP LYS LEU HIS ASN LEU ASN THR ASN TRP          
SEQRES  18 B  496  PHE PRO ALA GLY SER ARG PRO PHE ILE PHE GLN GLU VAL          
SEQRES  19 B  496  ILE ASP LEU GLY GLY GLU ALA ILE LYS SER SER GLU TYR          
SEQRES  20 B  496  PHE GLY ASN GLY ARG VAL THR GLU PHE LYS TYR GLY ALA          
SEQRES  21 B  496  LYS LEU GLY THR VAL VAL ARG LYS TRP SER GLY GLU LYS          
SEQRES  22 B  496  MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE          
SEQRES  23 B  496  MET PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS          
SEQRES  24 B  496  ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY SER SER ILE          
SEQRES  25 B  496  LEU THR PHE TRP ASP ALA ARG LEU TYR LYS ILE ALA VAL          
SEQRES  26 B  496  GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL          
SEQRES  27 B  496  MET SER SER TYR ARG TRP ALA ARG ASN PHE VAL ASN GLY          
SEQRES  28 B  496  GLU ASP VAL ASN ASP TRP ILE GLY PRO PRO ASN ASN ASN          
SEQRES  29 B  496  GLY VAL ILE LYS GLU VAL THR ILE ASN ALA ASP THR THR          
SEQRES  30 B  496  CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLU          
SEQRES  31 B  496  ILE ARG ASN MET VAL TRP PHE ARG ASN VAL VAL ASP GLY          
SEQRES  32 B  496  GLN PRO PHE ALA ASN TRP TRP ASP ASN GLY SER ASN GLN          
SEQRES  33 B  496  VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE          
SEQRES  34 B  496  ASN ASN ASP ASP TRP GLN LEU SER SER THR LEU GLN THR          
SEQRES  35 B  496  GLY LEU PRO GLY GLY THR TYR CYS ASP VAL ILE SER GLY          
SEQRES  36 B  496  ASP LYS VAL GLY ASN SER CYS THR GLY ILE LYS VAL TYR          
SEQRES  37 B  496  VAL SER SER ASP GLY THR ALA GLN PHE SER ILE SER ASN          
SEQRES  38 B  496  SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER          
SEQRES  39 B  496  LYS LEU                                                      
SEQRES   1 C  496  GLN TYR ALA PRO GLN THR GLN SER GLY ARG THR SER ILE          
SEQRES   2 C  496  VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU          
SEQRES   3 C  496  GLU CYS GLU ARG TYR LEU GLY PRO LYS GLY PHE GLY GLY          
SEQRES   4 C  496  VAL GLN VAL SER PRO PRO ASN GLU ASN ILE VAL VAL THR          
SEQRES   5 C  496  ASN PRO SER ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL          
SEQRES   6 C  496  SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASN GLU          
SEQRES   7 C  496  PHE ARG ASP MET VAL THR ARG CYS ASN ASN VAL GLY VAL          
SEQRES   8 C  496  ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY          
SEQRES   9 C  496  SER GLY ALA ALA ALA GLY THR GLY THR THR CYS GLY SER          
SEQRES  10 C  496  TYR CYS ASN PRO GLY SER ARG GLU PHE PRO ALA VAL PRO          
SEQRES  11 C  496  TYR SER ALA TRP ASP PHE ASN ASP GLY LYS CYS LYS THR          
SEQRES  12 C  496  ALA SER GLY GLY ILE GLU SER TYR ASN ASP PRO TYR GLN          
SEQRES  13 C  496  VAL ARG ASP CYS GLN LEU VAL GLY LEU LEU ASP LEU ALA          
SEQRES  14 C  496  LEU GLU LYS ASP TYR VAL ARG SER MET ILE ALA ASP TYR          
SEQRES  15 C  496  LEU ASN LYS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG          
SEQRES  16 C  496  ILE ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS          
SEQRES  17 C  496  ALA VAL LEU ASP LYS LEU HIS ASN LEU ASN THR ASN TRP          
SEQRES  18 C  496  PHE PRO ALA GLY SER ARG PRO PHE ILE PHE GLN GLU VAL          
SEQRES  19 C  496  ILE ASP LEU GLY GLY GLU ALA ILE LYS SER SER GLU TYR          
SEQRES  20 C  496  PHE GLY ASN GLY ARG VAL THR GLU PHE LYS TYR GLY ALA          
SEQRES  21 C  496  LYS LEU GLY THR VAL VAL ARG LYS TRP SER GLY GLU LYS          
SEQRES  22 C  496  MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE          
SEQRES  23 C  496  MET PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS          
SEQRES  24 C  496  ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY SER SER ILE          
SEQRES  25 C  496  LEU THR PHE TRP ASP ALA ARG LEU TYR LYS ILE ALA VAL          
SEQRES  26 C  496  GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL          
SEQRES  27 C  496  MET SER SER TYR ARG TRP ALA ARG ASN PHE VAL ASN GLY          
SEQRES  28 C  496  GLU ASP VAL ASN ASP TRP ILE GLY PRO PRO ASN ASN ASN          
SEQRES  29 C  496  GLY VAL ILE LYS GLU VAL THR ILE ASN ALA ASP THR THR          
SEQRES  30 C  496  CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLU          
SEQRES  31 C  496  ILE ARG ASN MET VAL TRP PHE ARG ASN VAL VAL ASP GLY          
SEQRES  32 C  496  GLN PRO PHE ALA ASN TRP TRP ASP ASN GLY SER ASN GLN          
SEQRES  33 C  496  VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE          
SEQRES  34 C  496  ASN ASN ASP ASP TRP GLN LEU SER SER THR LEU GLN THR          
SEQRES  35 C  496  GLY LEU PRO GLY GLY THR TYR CYS ASP VAL ILE SER GLY          
SEQRES  36 C  496  ASP LYS VAL GLY ASN SER CYS THR GLY ILE LYS VAL TYR          
SEQRES  37 C  496  VAL SER SER ASP GLY THR ALA GLN PHE SER ILE SER ASN          
SEQRES  38 C  496  SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER          
SEQRES  39 C  496  LYS LEU                                                      
SEQRES   1 D  496  GLN TYR ALA PRO GLN THR GLN SER GLY ARG THR SER ILE          
SEQRES   2 D  496  VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU          
SEQRES   3 D  496  GLU CYS GLU ARG TYR LEU GLY PRO LYS GLY PHE GLY GLY          
SEQRES   4 D  496  VAL GLN VAL SER PRO PRO ASN GLU ASN ILE VAL VAL THR          
SEQRES   5 D  496  ASN PRO SER ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL          
SEQRES   6 D  496  SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASN GLU          
SEQRES   7 D  496  PHE ARG ASP MET VAL THR ARG CYS ASN ASN VAL GLY VAL          
SEQRES   8 D  496  ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY          
SEQRES   9 D  496  SER GLY ALA ALA ALA GLY THR GLY THR THR CYS GLY SER          
SEQRES  10 D  496  TYR CYS ASN PRO GLY SER ARG GLU PHE PRO ALA VAL PRO          
SEQRES  11 D  496  TYR SER ALA TRP ASP PHE ASN ASP GLY LYS CYS LYS THR          
SEQRES  12 D  496  ALA SER GLY GLY ILE GLU SER TYR ASN ASP PRO TYR GLN          
SEQRES  13 D  496  VAL ARG ASP CYS GLN LEU VAL GLY LEU LEU ASP LEU ALA          
SEQRES  14 D  496  LEU GLU LYS ASP TYR VAL ARG SER MET ILE ALA ASP TYR          
SEQRES  15 D  496  LEU ASN LYS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG          
SEQRES  16 D  496  ILE ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS          
SEQRES  17 D  496  ALA VAL LEU ASP LYS LEU HIS ASN LEU ASN THR ASN TRP          
SEQRES  18 D  496  PHE PRO ALA GLY SER ARG PRO PHE ILE PHE GLN GLU VAL          
SEQRES  19 D  496  ILE ASP LEU GLY GLY GLU ALA ILE LYS SER SER GLU TYR          
SEQRES  20 D  496  PHE GLY ASN GLY ARG VAL THR GLU PHE LYS TYR GLY ALA          
SEQRES  21 D  496  LYS LEU GLY THR VAL VAL ARG LYS TRP SER GLY GLU LYS          
SEQRES  22 D  496  MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE          
SEQRES  23 D  496  MET PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS          
SEQRES  24 D  496  ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY SER SER ILE          
SEQRES  25 D  496  LEU THR PHE TRP ASP ALA ARG LEU TYR LYS ILE ALA VAL          
SEQRES  26 D  496  GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL          
SEQRES  27 D  496  MET SER SER TYR ARG TRP ALA ARG ASN PHE VAL ASN GLY          
SEQRES  28 D  496  GLU ASP VAL ASN ASP TRP ILE GLY PRO PRO ASN ASN ASN          
SEQRES  29 D  496  GLY VAL ILE LYS GLU VAL THR ILE ASN ALA ASP THR THR          
SEQRES  30 D  496  CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLU          
SEQRES  31 D  496  ILE ARG ASN MET VAL TRP PHE ARG ASN VAL VAL ASP GLY          
SEQRES  32 D  496  GLN PRO PHE ALA ASN TRP TRP ASP ASN GLY SER ASN GLN          
SEQRES  33 D  496  VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE          
SEQRES  34 D  496  ASN ASN ASP ASP TRP GLN LEU SER SER THR LEU GLN THR          
SEQRES  35 D  496  GLY LEU PRO GLY GLY THR TYR CYS ASP VAL ILE SER GLY          
SEQRES  36 D  496  ASP LYS VAL GLY ASN SER CYS THR GLY ILE LYS VAL TYR          
SEQRES  37 D  496  VAL SER SER ASP GLY THR ALA GLN PHE SER ILE SER ASN          
SEQRES  38 D  496  SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER          
SEQRES  39 D  496  LYS LEU                                                      
SEQRES   1 E  120  GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER VAL GLN          
SEQRES   2 E  120  ALA GLY GLY SER LEU SER LEU SER CYS ALA ALA SER THR          
SEQRES   3 E  120  TYR THR ASP THR VAL GLY TRP PHE ARG GLN ALA PRO GLY          
SEQRES   4 E  120  LYS GLU ARG GLU GLY VAL ALA ALA ILE TYR ARG ARG THR          
SEQRES   5 E  120  GLY TYR THR TYR SER ALA ASP SER VAL LYS GLY ARG PHE          
SEQRES   6 E  120  THR LEU SER GLN ASP ASN ASN LYS ASN THR VAL TYR LEU          
SEQRES   7 E  120  GLN MET ASN SER LEU LYS PRO GLU ASP THR GLY ILE TYR          
SEQRES   8 E  120  TYR CYS ALA THR GLY ASN SER VAL ARG LEU ALA SER TRP          
SEQRES   9 E  120  GLU GLY TYR PHE TYR TRP GLY GLN GLY THR GLN VAL THR          
SEQRES  10 E  120  VAL SER SER                                                  
SEQRES   1 F  120  GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER VAL GLN          
SEQRES   2 F  120  ALA GLY GLY SER LEU SER LEU SER CYS ALA ALA SER THR          
SEQRES   3 F  120  TYR THR ASP THR VAL GLY TRP PHE ARG GLN ALA PRO GLY          
SEQRES   4 F  120  LYS GLU ARG GLU GLY VAL ALA ALA ILE TYR ARG ARG THR          
SEQRES   5 F  120  GLY TYR THR TYR SER ALA ASP SER VAL LYS GLY ARG PHE          
SEQRES   6 F  120  THR LEU SER GLN ASP ASN ASN LYS ASN THR VAL TYR LEU          
SEQRES   7 F  120  GLN MET ASN SER LEU LYS PRO GLU ASP THR GLY ILE TYR          
SEQRES   8 F  120  TYR CYS ALA THR GLY ASN SER VAL ARG LEU ALA SER TRP          
SEQRES   9 F  120  GLU GLY TYR PHE TYR TRP GLY GLN GLY THR GLN VAL THR          
SEQRES  10 F  120  VAL SER SER                                                  
SEQRES   1 G  120  GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER VAL GLN          
SEQRES   2 G  120  ALA GLY GLY SER LEU SER LEU SER CYS ALA ALA SER THR          
SEQRES   3 G  120  TYR THR ASP THR VAL GLY TRP PHE ARG GLN ALA PRO GLY          
SEQRES   4 G  120  LYS GLU ARG GLU GLY VAL ALA ALA ILE TYR ARG ARG THR          
SEQRES   5 G  120  GLY TYR THR TYR SER ALA ASP SER VAL LYS GLY ARG PHE          
SEQRES   6 G  120  THR LEU SER GLN ASP ASN ASN LYS ASN THR VAL TYR LEU          
SEQRES   7 G  120  GLN MET ASN SER LEU LYS PRO GLU ASP THR GLY ILE TYR          
SEQRES   8 G  120  TYR CYS ALA THR GLY ASN SER VAL ARG LEU ALA SER TRP          
SEQRES   9 G  120  GLU GLY TYR PHE TYR TRP GLY GLN GLY THR GLN VAL THR          
SEQRES  10 G  120  VAL SER SER                                                  
SEQRES   1 H  120  GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER VAL GLN          
SEQRES   2 H  120  ALA GLY GLY SER LEU SER LEU SER CYS ALA ALA SER THR          
SEQRES   3 H  120  TYR THR ASP THR VAL GLY TRP PHE ARG GLN ALA PRO GLY          
SEQRES   4 H  120  LYS GLU ARG GLU GLY VAL ALA ALA ILE TYR ARG ARG THR          
SEQRES   5 H  120  GLY TYR THR TYR SER ALA ASP SER VAL LYS GLY ARG PHE          
SEQRES   6 H  120  THR LEU SER GLN ASP ASN ASN LYS ASN THR VAL TYR LEU          
SEQRES   7 H  120  GLN MET ASN SER LEU LYS PRO GLU ASP THR GLY ILE TYR          
SEQRES   8 H  120  TYR CYS ALA THR GLY ASN SER VAL ARG LEU ALA SER TRP          
SEQRES   9 H  120  GLU GLY TYR PHE TYR TRP GLY GLN GLY THR GLN VAL THR          
SEQRES  10 H  120  VAL SER SER                                                  
HET     CA  A4001       1                                                       
HET     CL  A4002       1                                                       
HET     CA  B4003       1                                                       
HET     CL  B4004       1                                                       
HET     CA  C4005       1                                                       
HET     CL  C4006       1                                                       
HET     CA  D4007       1                                                       
HET     CL  D4008       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   9   CA    4(CA 2+)                                                     
FORMUL  10   CL    4(CL 1-)                                                     
FORMUL  17  HOH   *2807(H2 O)                                                   
HELIX    1   1 ARG A   20  TYR A   31  1                                  12    
HELIX    2   2 PRO A   57  GLN A   63  5                                   7    
HELIX    3   3 ASN A   75  VAL A   89  1                                  15    
HELIX    4   4 ASN A  120  ARG A  124  5                                   5    
HELIX    5   5 SER A  132  LYS A  140  5                                   9    
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  ASP A  212  1                                  10    
HELIX   10  10 LYS A  243  PHE A  248  5                                   6    
HELIX   11  11 PHE A  256  ARG A  267  1                                  12    
HELIX   12  12 LYS A  273  TRP A  280  5                                   8    
HELIX   13  13 GLY A  281  GLY A  285  5                                   5    
HELIX   14  14 PRO A  288  ASP A  290  5                                   3    
HELIX   15  15 ASP A  300  GLY A  304  5                                   5    
HELIX   16  16 GLY A  308  ILE A  312  5                                   5    
HELIX   17  17 THR A  314  TRP A  316  5                                   3    
HELIX   18  18 ASP A  317  HIS A  331  1                                  15    
HELIX   19  19 CYS A  384  ARG A  387  5                                   4    
HELIX   20  20 TRP A  388  ASP A  402  1                                  15    
HELIX   21  21 ARG B   20  TYR B   31  1                                  12    
HELIX   22  22 PRO B   57  GLN B   63  5                                   7    
HELIX   23  23 ASN B   75  ASN B   88  1                                  14    
HELIX   24  24 ASN B  120  ARG B  124  5                                   5    
HELIX   25  25 SER B  132  PHE B  136  5                                   5    
HELIX   26  26 ASN B  137  CYS B  141  5                                   5    
HELIX   27  27 ASP B  153  CYS B  160  1                                   8    
HELIX   28  28 LYS B  172  GLY B  190  1                                  19    
HELIX   29  29 ALA B  198  MET B  202  5                                   5    
HELIX   30  30 TRP B  203  ASP B  212  1                                  10    
HELIX   31  31 LYS B  243  PHE B  248  5                                   6    
HELIX   32  32 PHE B  256  ARG B  267  1                                  12    
HELIX   33  33 LYS B  273  TRP B  280  5                                   8    
HELIX   34  34 GLY B  281  GLY B  285  5                                   5    
HELIX   35  35 PRO B  288  ASP B  290  5                                   3    
HELIX   36  36 ASP B  300  GLY B  304  5                                   5    
HELIX   37  37 GLY B  308  ILE B  312  5                                   5    
HELIX   38  38 THR B  314  TRP B  316  5                                   3    
HELIX   39  39 ASP B  317  HIS B  331  1                                  15    
HELIX   40  40 CYS B  384  ARG B  387  5                                   4    
HELIX   41  41 TRP B  388  VAL B  401  1                                  14    
HELIX   42  42 GLU B  493  LYS B  495  5                                   3    
HELIX   43  43 ARG C   20  TYR C   31  1                                  12    
HELIX   44  44 PRO C   57  GLN C   63  5                                   7    
HELIX   45  45 ASN C   75  VAL C   89  1                                  15    
HELIX   46  46 ASN C  120  ARG C  124  5                                   5    
HELIX   47  47 SER C  132  LYS C  140  5                                   9    
HELIX   48  48 ASP C  153  CYS C  160  1                                   8    
HELIX   49  49 LYS C  172  GLY C  190  1                                  19    
HELIX   50  50 ALA C  198  MET C  202  5                                   5    
HELIX   51  51 TRP C  203  ASP C  212  1                                  10    
HELIX   52  52 LYS C  243  PHE C  248  5                                   6    
HELIX   53  53 PHE C  256  LYS C  268  1                                  13    
HELIX   54  54 LYS C  273  TRP C  280  5                                   8    
HELIX   55  55 GLY C  281  GLY C  285  5                                   5    
HELIX   56  56 PRO C  288  ASP C  290  5                                   3    
HELIX   57  57 ASP C  300  GLY C  304  5                                   5    
HELIX   58  58 GLY C  308  ILE C  312  5                                   5    
HELIX   59  59 THR C  314  TRP C  316  5                                   3    
HELIX   60  60 ASP C  317  HIS C  331  1                                  15    
HELIX   61  61 CYS C  384  ARG C  387  5                                   4    
HELIX   62  62 TRP C  388  VAL C  401  1                                  14    
HELIX   63  63 GLU C  493  LYS C  495  5                                   3    
HELIX   64  64 ARG D   20  TYR D   31  1                                  12    
HELIX   65  65 PRO D   57  GLN D   63  5                                   7    
HELIX   66  66 ASN D   75  VAL D   89  1                                  15    
HELIX   67  67 ASN D  120  ARG D  124  5                                   5    
HELIX   68  68 SER D  132  PHE D  136  5                                   5    
HELIX   69  69 ASP D  153  CYS D  160  1                                   8    
HELIX   70  70 LYS D  172  GLY D  190  1                                  19    
HELIX   71  71 ALA D  198  MET D  202  5                                   5    
HELIX   72  72 TRP D  203  ASP D  212  1                                  10    
HELIX   73  73 LYS D  243  PHE D  248  5                                   6    
HELIX   74  74 PHE D  256  ARG D  267  1                                  12    
HELIX   75  75 LYS D  273  TRP D  280  5                                   8    
HELIX   76  76 GLY D  281  GLY D  285  5                                   5    
HELIX   77  77 PRO D  288  ASP D  290  5                                   3    
HELIX   78  78 ASP D  300  GLY D  304  5                                   5    
HELIX   79  79 GLY D  308  ILE D  312  5                                   5    
HELIX   80  80 THR D  314  TRP D  316  5                                   3    
HELIX   81  81 ASP D  317  HIS D  331  1                                  15    
HELIX   82  82 CYS D  384  ARG D  387  5                                   4    
HELIX   83  83 TRP D  388  VAL D  401  1                                  14    
HELIX   84  84 GLU D  493  LYS D  495  5                                   3    
HELIX   85  85 LYS E   84  THR E   88  5                                   5    
HELIX   86  86 ARG E  100  TRP E  104  5                                   5    
HELIX   87  87 LYS F   84  THR F   88  5                                   5    
HELIX   88  88 ARG F  100  TRP F  104  5                                   5    
HELIX   89  89 LYS G   84  THR G   88  5                                   5    
HELIX   90  90 ARG G  100  TRP G  104  5                                   5    
HELIX   91  91 ASP H   59  LYS H   62  5                                   4    
HELIX   92  92 LYS H   84  THR H   88  5                                   5    
HELIX   93  93 ARG H  100  TRP H  104  5                                   5    
SHEET    1   A 9 SER A  12  LEU A  16  0                                        
SHEET    2   A 9 GLY A  39  VAL A  42  1  O  GLY A  39   N  VAL A  14           
SHEET    3   A 9 ARG A  92  ALA A  97  1  O  ARG A  92   N  VAL A  40           
SHEET    4   A 9 GLY A 193  ILE A 196  1  O  GLY A 193   N  VAL A  95           
SHEET    5   A 9 PHE A 229  GLN A 232  1  O  PHE A 229   N  PHE A 194           
SHEET    6   A 9 ARG A 252  THR A 254  1  O  ARG A 252   N  GLN A 232           
SHEET    7   A 9 ALA A 292  VAL A 294  1  N  LEU A 293   O  VAL A 253           
SHEET    8   A 9 PHE A 335  SER A 340  1  O  PHE A 335   N  VAL A 294           
SHEET    9   A 9 SER A  12  LEU A  16  1  O  ILE A  13   N  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  N  LEU A 166   O  CYS A 103           
SHEET    1   C 2 PHE A 348  VAL A 349  0                                        
SHEET    2   C 2 GLU A 352  ASP A 353 -1  O  GLU A 352   N  VAL A 349           
SHEET    1   D 2 ASN A 362  ASN A 363  0                                        
SHEET    2   D 2 VAL A 366  ILE A 367 -1  O  VAL A 366   N  ASN A 363           
SHEET    1   E 4 PHE A 406  ASP A 411  0                                        
SHEET    2   E 4 GLN A 416  ARG A 421 -1  N  ALA A 418   O  TRP A 410           
SHEET    3   E 4 GLY A 425  ASN A 430 -1  O  GLY A 425   N  ARG A 421           
SHEET    4   E 4 PHE A 487  HIS A 491 -1  O  ILE A 488   N  VAL A 428           
SHEET    1   F 2 LEU A 436  GLN A 441  0                                        
SHEET    2   F 2 THR A 474  ILE A 479 -1  O  ALA A 475   N  LEU A 440           
SHEET    1   G 2 GLY A 447  CYS A 450  0                                        
SHEET    2   G 2 LYS A 466  VAL A 469 -1  N  VAL A 467   O  TYR A 449           
SHEET    1   H 2 LYS A 457  VAL A 458  0                                        
SHEET    2   H 2 SER A 461  CYS A 462 -1  O  SER A 461   N  VAL A 458           
SHEET    1   I 9 SER B  12  LEU B  16  0                                        
SHEET    2   I 9 GLY B  39  VAL B  42  1  O  GLY B  39   N  VAL B  14           
SHEET    3   I 9 ARG B  92  ALA B  97  1  O  ARG B  92   N  VAL B  40           
SHEET    4   I 9 GLY B 193  ILE B 196  1  O  GLY B 193   N  VAL B  95           
SHEET    5   I 9 PHE B 229  GLN B 232  1  O  PHE B 229   N  PHE B 194           
SHEET    6   I 9 ARG B 252  THR B 254  1  O  ARG B 252   N  GLN B 232           
SHEET    7   I 9 ALA B 292  VAL B 294  1  N  LEU B 293   O  VAL B 253           
SHEET    8   I 9 PHE B 335  SER B 340  1  O  PHE B 335   N  VAL B 294           
SHEET    9   I 9 SER B  12  LEU B  16  1  O  ILE B  13   N  VAL B 338           
SHEET    1   J 2 HIS B 101  GLY B 104  0                                        
SHEET    2   J 2 LEU B 165  ASP B 167 -1  N  LEU B 166   O  CYS B 103           
SHEET    1   K 2 PHE B 348  VAL B 349  0                                        
SHEET    2   K 2 GLU B 352  ASP B 353 -1  O  GLU B 352   N  VAL B 349           
SHEET    1   L 2 ASN B 362  ASN B 363  0                                        
SHEET    2   L 2 VAL B 366  ILE B 367 -1  N  VAL B 366   O  ASN B 363           
SHEET    1   M 4 PHE B 406  ASP B 411  0                                        
SHEET    2   M 4 GLN B 416  ARG B 421 -1  O  ALA B 418   N  TRP B 410           
SHEET    3   M 4 GLY B 425  ASN B 430 -1  O  GLY B 425   N  ARG B 421           
SHEET    4   M 4 PHE B 487  HIS B 491 -1  O  ILE B 488   N  VAL B 428           
SHEET    1   N 2 LEU B 436  GLN B 441  0                                        
SHEET    2   N 2 THR B 474  ILE B 479 -1  O  ALA B 475   N  LEU B 440           
SHEET    1   O 2 GLY B 447  CYS B 450  0                                        
SHEET    2   O 2 LYS B 466  VAL B 469 -1  O  VAL B 467   N  TYR B 449           
SHEET    1   P 2 LYS B 457  VAL B 458  0                                        
SHEET    2   P 2 SER B 461  CYS B 462 -1  O  SER B 461   N  VAL B 458           
SHEET    1   Q 9 SER C  12  LEU C  16  0                                        
SHEET    2   Q 9 GLY C  39  VAL C  42  1  O  GLY C  39   N  VAL C  14           
SHEET    3   Q 9 ARG C  92  ALA C  97  1  O  ARG C  92   N  VAL C  40           
SHEET    4   Q 9 GLY C 193  ILE C 196  1  O  GLY C 193   N  VAL C  95           
SHEET    5   Q 9 PHE C 229  GLN C 232  1  O  PHE C 229   N  PHE C 194           
SHEET    6   Q 9 ARG C 252  THR C 254  1  O  ARG C 252   N  GLN C 232           
SHEET    7   Q 9 ALA C 292  VAL C 294  1  N  LEU C 293   O  VAL C 253           
SHEET    8   Q 9 PHE C 335  SER C 340  1  O  PHE C 335   N  VAL C 294           
SHEET    9   Q 9 SER C  12  LEU C  16  1  O  ILE C  13   N  VAL C 338           
SHEET    1   R 2 HIS C 101  GLY C 104  0                                        
SHEET    2   R 2 LEU C 165  ASP C 167 -1  N  LEU C 166   O  CYS C 103           
SHEET    1   S 2 PHE C 348  VAL C 349  0                                        
SHEET    2   S 2 GLU C 352  ASP C 353 -1  N  GLU C 352   O  VAL C 349           
SHEET    1   T 2 ASN C 362  ASN C 363  0                                        
SHEET    2   T 2 VAL C 366  ILE C 367 -1  O  VAL C 366   N  ASN C 363           
SHEET    1   U 4 PHE C 406  ASP C 411  0                                        
SHEET    2   U 4 GLN C 416  ARG C 421 -1  O  ALA C 418   N  TRP C 410           
SHEET    3   U 4 GLY C 425  ASN C 430 -1  O  GLY C 425   N  ARG C 421           
SHEET    4   U 4 PHE C 487  HIS C 491 -1  O  ILE C 488   N  VAL C 428           
SHEET    1   V 2 LEU C 436  GLN C 441  0                                        
SHEET    2   V 2 THR C 474  ILE C 479 -1  O  ALA C 475   N  LEU C 440           
SHEET    1   W 2 GLY C 447  CYS C 450  0                                        
SHEET    2   W 2 LYS C 466  VAL C 469 -1  N  VAL C 467   O  TYR C 449           
SHEET    1   X 2 LYS C 457  VAL C 458  0                                        
SHEET    2   X 2 SER C 461  CYS C 462 -1  O  SER C 461   N  VAL C 458           
SHEET    1   Y 9 SER D  12  LEU D  16  0                                        
SHEET    2   Y 9 GLY D  39  VAL D  42  1  O  GLY D  39   N  VAL D  14           
SHEET    3   Y 9 ARG D  92  ALA D  97  1  O  ARG D  92   N  VAL D  40           
SHEET    4   Y 9 GLY D 193  ILE D 196  1  O  GLY D 193   N  VAL D  95           
SHEET    5   Y 9 PHE D 229  GLN D 232  1  O  PHE D 229   N  PHE D 194           
SHEET    6   Y 9 ARG D 252  THR D 254  1  O  ARG D 252   N  GLN D 232           
SHEET    7   Y 9 ALA D 292  VAL D 294  1  N  LEU D 293   O  VAL D 253           
SHEET    8   Y 9 PHE D 335  SER D 340  1  O  PHE D 335   N  VAL D 294           
SHEET    9   Y 9 SER D  12  LEU D  16  1  O  ILE D  13   N  VAL D 338           
SHEET    1   Z 2 HIS D 101  GLY D 104  0                                        
SHEET    2   Z 2 LEU D 165  ASP D 167 -1  N  LEU D 166   O  CYS D 103           
SHEET    1  AA 2 PHE D 348  VAL D 349  0                                        
SHEET    2  AA 2 GLU D 352  ASP D 353 -1  N  GLU D 352   O  VAL D 349           
SHEET    1  AB 2 ASN D 362  ASN D 363  0                                        
SHEET    2  AB 2 VAL D 366  ILE D 367 -1  O  VAL D 366   N  ASN D 363           
SHEET    1  AC 4 PHE D 406  ASP D 411  0                                        
SHEET    2  AC 4 GLN D 416  ARG D 421 -1  O  ALA D 418   N  TRP D 410           
SHEET    3  AC 4 PHE D 348  VAL D 349  0                                        
SHEET    4  AC 4 PHE D 487  HIS D 491  0                                        
SHEET    1  AD 2 LEU D 436  GLN D 441  0                                        
SHEET    2  AD 2 THR D 474  ILE D 479 -1  O  ALA D 475   N  LEU D 440           
SHEET    1  AE 2 GLY D 447  CYS D 450  0                                        
SHEET    2  AE 2 LYS D 466  VAL D 469 -1  O  VAL D 467   N  TYR D 449           
SHEET    1  AF 2 LYS D 457  VAL D 458  0                                        
SHEET    2  AF 2 SER D 461  CYS D 462 -1  O  SER D 461   N  VAL D 458           
SHEET    1  AG 4 LEU E   4  SER E   7  0                                        
SHEET    2  AG 4 LEU E  18  ALA E  24 -1  N  SER E  21   O  SER E   7           
SHEET    3  AG 4 THR E  75  MET E  80 -1  O  VAL E  76   N  CYS E  22           
SHEET    4  AG 4 PHE E  65  GLN E  69 -1  O  THR E  66   N  GLN E  79           
SHEET    1  AH 8 SER E  11  VAL E  12  0                                        
SHEET    2  AH 8 THR E 114  VAL E 118  1  O  THR E 117   N  VAL E  12           
SHEET    3  AH 8 GLY E  89  GLY E  96 -1  N  GLY E  89   O  VAL E 116           
SHEET    4  AH 8 TYR E 107  TRP E 110 -1  N  PHE E 108   O  THR E  95           
SHEET    5  AH 8 GLY E  89  GLY E  96 -1  O  THR E  95   N  PHE E 108           
SHEET    6  AH 8 THR E  30  GLN E  36 -1  O  THR E  30   N  GLY E  96           
SHEET    7  AH 8 GLU E  43  TYR E  49 -1  N  GLU E  43   O  ARG E  35           
SHEET    8  AH 8 THR E  55  SER E  57 -1  O  TYR E  56   N  ALA E  47           
SHEET    1  AI 4 LEU F   4  GLY F   8  0                                        
SHEET    2  AI 4 LEU F  18  ALA F  24 -1  N  SER F  21   O  SER F   7           
SHEET    3  AI 4 THR F  75  MET F  80 -1  O  VAL F  76   N  CYS F  22           
SHEET    4  AI 4 PHE F  65  GLN F  69 -1  O  THR F  66   N  GLN F  79           
SHEET    1  AJ 8 GLY F  10  GLN F  13  0                                        
SHEET    2  AJ 8 THR F 114  SER F 119  1  O  GLN F 115   N  GLY F  10           
SHEET    3  AJ 8 GLY F  89  GLY F  96 -1  N  GLY F  89   O  VAL F 116           
SHEET    4  AJ 8 TYR F 107  TRP F 110 -1  N  PHE F 108   O  THR F  95           
SHEET    5  AJ 8 GLY F  89  GLY F  96 -1  O  THR F  95   N  PHE F 108           
SHEET    6  AJ 8 THR F  30  GLN F  36 -1  O  THR F  30   N  GLY F  96           
SHEET    7  AJ 8 GLU F  43  TYR F  49 -1  O  GLU F  43   N  ARG F  35           
SHEET    8  AJ 8 THR F  55  SER F  57 -1  O  TYR F  56   N  ALA F  47           
SHEET    1  AK 4 LEU G   4  SER G   7  0                                        
SHEET    2  AK 4 LEU G  18  ALA G  24 -1  N  SER G  21   O  SER G   7           
SHEET    3  AK 4 THR G  75  MET G  80 -1  N  VAL G  76   O  CYS G  22           
SHEET    4  AK 4 PHE G  65  GLN G  69 -1  O  THR G  66   N  GLN G  79           
SHEET    1  AL 8 GLY G  10  GLN G  13  0                                        
SHEET    2  AL 8 THR G 114  SER G 119  1  O  GLN G 115   N  GLY G  10           
SHEET    3  AL 8 GLY G  89  GLY G  96 -1  N  GLY G  89   O  VAL G 116           
SHEET    4  AL 8 TYR G 107  TRP G 110 -1  N  PHE G 108   O  THR G  95           
SHEET    5  AL 8 GLY G  89  GLY G  96 -1  O  THR G  95   N  PHE G 108           
SHEET    6  AL 8 THR G  30  GLN G  36 -1  O  THR G  30   N  GLY G  96           
SHEET    7  AL 8 GLU G  43  TYR G  49 -1  N  GLU G  43   O  ARG G  35           
SHEET    8  AL 8 THR G  55  SER G  57 -1  O  TYR G  56   N  ALA G  47           
SHEET    1  AM 4 LEU H   4  SER H   7  0                                        
SHEET    2  AM 4 LEU H  18  ALA H  24 -1  N  SER H  21   O  SER H   7           
SHEET    3  AM 4 THR H  75  MET H  80 -1  O  VAL H  76   N  CYS H  22           
SHEET    4  AM 4 PHE H  65  GLN H  69 -1  O  THR H  66   N  GLN H  79           
SHEET    1  AN 8 GLY H  10  GLN H  13  0                                        
SHEET    2  AN 8 THR H 114  SER H 119  1  O  GLN H 115   N  GLY H  10           
SHEET    3  AN 8 GLY H  89  GLY H  96 -1  N  GLY H  89   O  VAL H 116           
SHEET    4  AN 8 TYR H 107  TRP H 110 -1  N  PHE H 108   O  THR H  95           
SHEET    5  AN 8 GLY H  89  GLY H  96 -1  O  THR H  95   N  PHE H 108           
SHEET    6  AN 8 THR H  30  GLN H  36 -1  O  THR H  30   N  GLY H  96           
SHEET    7  AN 8 GLU H  43  TYR H  49 -1  N  GLU H  43   O  ARG H  35           
SHEET    8  AN 8 THR H  55  SER H  57 -1  N  TYR H  56   O  ALA H  47           
SSBOND   1 CYS A   28    CYS A   86                          1555   1555  2.04  
SSBOND   2 CYS A   70    CYS A  115                          1555   1555  2.05  
SSBOND   3 CYS A  141    CYS A  160                          1555   1555  2.04  
SSBOND   4 CYS A  378    CYS A  384                          1555   1555  2.05  
SSBOND   5 CYS A  450    CYS A  462                          1555   1555  2.03  
SSBOND   6 CYS B   28    CYS B   86                          1555   1555  2.04  
SSBOND   7 CYS B   70    CYS B  115                          1555   1555  2.05  
SSBOND   8 CYS B  141    CYS B  160                          1555   1555  2.07  
SSBOND   9 CYS B  378    CYS B  384                          1555   1555  2.04  
SSBOND  10 CYS B  450    CYS B  462                          1555   1555  2.03  
SSBOND  11 CYS C   28    CYS C   86                          1555   1555  2.04  
SSBOND  12 CYS C   70    CYS C  115                          1555   1555  2.05  
SSBOND  13 CYS C  141    CYS C  160                          1555   1555  2.07  
SSBOND  14 CYS C  378    CYS C  384                          1555   1555  2.04  
SSBOND  15 CYS C  450    CYS C  462                          1555   1555  2.03  
SSBOND  16 CYS D   28    CYS D   86                          1555   1555  2.04  
SSBOND  17 CYS D   70    CYS D  115                          1555   1555  2.05  
SSBOND  18 CYS D  141    CYS D  160                          1555   1555  2.07  
SSBOND  19 CYS D  378    CYS D  384                          1555   1555  2.03  
SSBOND  20 CYS D  450    CYS D  462                          1555   1555  2.03  
SSBOND  21 CYS E   22    CYS E   93                          1555   1555  2.02  
SSBOND  22 CYS F   22    CYS F   93                          1555   1555  2.03  
SSBOND  23 CYS G   22    CYS G   93                          1555   1555  2.03  
SSBOND  24 CYS H   22    CYS H   93                          1555   1555  2.02  
LINK        CA    CA A4001                 OD1 ASP A 167     1555   1555  2.50  
LINK        CA    CA A4001                 O   HOH A4094     1555   1555  2.45  
LINK        CA    CA A4001                 O   ARG A 158     1555   1555  2.42  
LINK        CA    CA A4001                 OD2 ASP A 167     1555   1555  2.49  
LINK        CA    CA A4001                 O   HOH A4014     1555   1555  2.49  
LINK        CA    CA A4001                 O   HOH A4125     1555   1555  2.58  
LINK        CA    CA A4001                 OD1 ASN A 100     1555   1555  2.42  
LINK        CA    CA A4001                 O   HIS A 201     1555   1555  2.41  
LINK        CA    CA B4003                 O   HOH B4307     1555   1555  2.50  
LINK        CA    CA B4003                 OD1 ASN B 100     1555   1555  2.42  
LINK        CA    CA B4003                 OD1 ASP B 167     1555   1555  2.48  
LINK        CA    CA B4003                 O   HIS B 201     1555   1555  2.42  
LINK        CA    CA B4003                 O   HOH B4012     1555   1555  2.55  
LINK        CA    CA B4003                 O   HOH B4030     1555   1555  2.42  
LINK        CA    CA B4003                 OD2 ASP B 167     1555   1555  2.47  
LINK        CA    CA B4003                 O   ARG B 158     1555   1555  2.40  
LINK        CA    CA C4005                 OD1 ASN C 100     1555   1555  2.40  
LINK        CA    CA C4005                 OD1 ASP C 167     1555   1555  2.50  
LINK        CA    CA C4005                 OD2 ASP C 167     1555   1555  2.47  
LINK        CA    CA C4005                 O   HOH C4047     1555   1555  2.44  
LINK        CA    CA C4005                 O   HOH C4060     1555   1555  2.53  
LINK        CA    CA C4005                 O   HIS C 201     1555   1555  2.39  
LINK        CA    CA C4005                 O   ARG C 158     1555   1555  2.41  
LINK        CA    CA C4005                 O   HOH C4022     1555   1555  2.53  
LINK        CA    CA D4007                 O   HIS D 201     1555   1555  2.41  
LINK        CA    CA D4007                 O   HOH D4041     1555   1555  2.51  
LINK        CA    CA D4007                 OD2 ASP D 167     1555   1555  2.51  
LINK        CA    CA D4007                 OD1 ASN D 100     1555   1555  2.41  
LINK        CA    CA D4007                 OD1 ASP D 167     1555   1555  2.46  
LINK        CA    CA D4007                 O   HOH D4038     1555   1555  2.56  
LINK        CA    CA D4007                 O   HOH D4016     1555   1555  2.52  
LINK        CA    CA D4007                 O   ARG D 158     1555   1555  2.40  
CISPEP   1 ASN A   53    PRO A   54          0         0.25                     
CISPEP   2 VAL A  129    PRO A  130          0         0.00                     
CISPEP   3 ASN B   53    PRO B   54          0         0.31                     
CISPEP   4 VAL B  129    PRO B  130          0        -0.24                     
CISPEP   5 ASN C   53    PRO C   54          0         0.31                     
CISPEP   6 VAL C  129    PRO C  130          0        -0.31                     
CISPEP   7 ASN D   53    PRO D   54          0        -0.07                     
CISPEP   8 VAL D  129    PRO D  130          0         0.45                     
SITE     1 AC1  7 ASN A 100  ARG A 158  ASP A 167  HIS A 201                    
SITE     2 AC1  7 HOH A4014  HOH A4094  HOH A4125                               
SITE     1 AC2  3 ARG A 195  ASN A 298  ARG A 337                               
SITE     1 AC3  7 ASN B 100  ARG B 158  ASP B 167  HIS B 201                    
SITE     2 AC3  7 HOH B4012  HOH B4030  HOH B4307                               
SITE     1 AC4  3 ARG B 195  ASN B 298  ARG B 337                               
SITE     1 AC5  7 ASN C 100  ARG C 158  ASP C 167  HIS C 201                    
SITE     2 AC5  7 HOH C4022  HOH C4047  HOH C4060                               
SITE     1 AC6  3 ARG C 195  ASN C 298  ARG C 337                               
SITE     1 AC7  7 ASN D 100  ARG D 158  ASP D 167  HIS D 201                    
SITE     2 AC7  7 HOH D4016  HOH D4038  HOH D4041                               
SITE     1 AC8  3 ARG D 195  ASN D 298  ARG D 337                               
CRYST1   65.170  100.920  103.740  79.31  72.63  86.11 P 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      0.015344 -0.001043 -0.004690        0.00000                         
SCALE2      0.000000  0.009932 -0.001750        0.00000                         
SCALE3      0.000000  0.000000  0.010256        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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