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Database: PDB
Entry: 1KXV
LinkDB: 1KXV
Original site: 1KXV 
HEADER    HYDROLASE, IMMUNE SYSTEM                01-FEB-02   1KXV              
TITLE     CAMELID VHH DOMAINS IN COMPLEX WITH PORCINE PANCREATIC                
TITLE    2 ALPHA-AMYLASE                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE, PANCREATIC;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE;                        
COMPND   5 EC: 3.2.1.1;                                                         
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CAMELID VHH DOMAIN CAB10;                                  
COMPND   8 CHAIN: C, D;                                                         
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: PANCEATIC 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: WK;                                        
SOURCE  13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PHEN6                                     
KEYWDS    BETA 8 ALPHA 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 1KXV    1       VERSN                                    
REVDAT   3   01-APR-03 1KXV    1       JRNL                                     
REVDAT   2   14-AUG-02 1KXV    1       JRNL                                     
REVDAT   1   19-JUN-02 1KXV    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 AND HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.34                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1228117.080                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 168160                         
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) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3337                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
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) (%) : 85.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 15241                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2280                       
REMARK   3   BIN FREE R VALUE                    : 0.2430                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 1.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 165                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9574                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 1377                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.65000                                              
REMARK   3    B22 (A**2) : -2.76000                                             
REMARK   3    B33 (A**2) : -3.89000                                             
REMARK   3    B12 (A**2) : -0.47000                                             
REMARK   3    B13 (A**2) : -1.99000                                             
REMARK   3    B23 (A**2) : -3.06000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.19                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.07                            
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) : 0.22                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.13                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.020                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.53                            
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        : 0.36                                                 
REMARK   3   BSOL        : 53.06                                                
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 1KXV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB015449.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
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                  : DIAMOND                            
REMARK 200  OPTICS                         : DIAMOND                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 175069                             
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     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.6000                             
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     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.13700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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 1FJH, PDB ENTRY 1QD0                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000 32%, NA CITRATE 0.1M &           
REMARK 280  AMMONIUM ACETATE 0.2M, PH 5.0, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  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                                                    
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, C                                  
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, D                                  
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     GLN C     1                                                      
REMARK 465     SER C   121                                                      
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     LYS A 243    CG   CD   CE   NZ                                   
REMARK 470     ARG A 343    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 343    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B 465    CG1  CG2  CD1                                       
REMARK 470     TYR B 468    CG   CD1  CD2  CE1  CE2  CZ   OH                    
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   OE1  GLU B   282     O    HOH B   626              1.66            
REMARK 500   OD2  ASP D    61     O    HOH D   159              1.87            
REMARK 500   O    HOH B   690     O    HOH B   799              2.02            
REMARK 500   N    GLN A     1     O    PRO A   228              2.03            
REMARK 500   O    HOH B   742     O    HOH B   805              2.13            
REMARK 500   ND2  ASN B   355     O    HOH B   805              2.15            
REMARK 500   O    LEU B   170     CD   ARG B   176              2.15            
REMARK 500   O    ASN B   355     O    HOH B   826              2.15            
REMARK 500   OD1  ASN A   347     O    HOH A   838              2.16            
REMARK 500   O    HOH B   579     O    HOH B   826              2.17            
REMARK 500   OD1  ASP D    33     O    HOH D   128              2.18            
REMARK 500   O    LEU A   170     CD   ARG A   176              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLN D   1   C     VAL D   2   N      -0.154                       
REMARK 500    GLY D   8   C     GLY D   9   N      -0.434                       
REMARK 500    SER D 121   C     SER D 121   OXT     0.634                       
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    ARG A  10   NE  -  CZ  -  NH1 ANGL. DEV. =  -8.4 DEGREES          
REMARK 500    ARG A  10   NE  -  CZ  -  NH2 ANGL. DEV. =   7.8 DEGREES          
REMARK 500    CYS A  70   CA  -  CB  -  SG  ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ARG A  72   CD  -  NE  -  CZ  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    ARG A  72   NE  -  CZ  -  NH1 ANGL. DEV. =  -8.3 DEGREES          
REMARK 500    ARG A  72   NE  -  CZ  -  NH2 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    ARG A  92   CB  -  CG  -  CD  ANGL. DEV. =  18.7 DEGREES          
REMARK 500    ARG A  92   CD  -  NE  -  CZ  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ARG A  92   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    ARG A  92   NE  -  CZ  -  NH2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG A 176   CB  -  CG  -  CD  ANGL. DEV. =  21.0 DEGREES          
REMARK 500    ARG A 176   NE  -  CZ  -  NH1 ANGL. DEV. =  -8.5 DEGREES          
REMARK 500    ARG A 176   NE  -  CZ  -  NH2 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    ARG A 195   CD  -  NE  -  CZ  ANGL. DEV. =  10.4 DEGREES          
REMARK 500    ARG A 195   NE  -  CZ  -  NH1 ANGL. DEV. = -10.5 DEGREES          
REMARK 500    ARG A 195   NE  -  CZ  -  NH2 ANGL. DEV. =  10.3 DEGREES          
REMARK 500    GLY A 225   C   -  N   -  CA  ANGL. DEV. = -18.2 DEGREES          
REMARK 500    ARG A 252   CB  -  CG  -  CD  ANGL. DEV. =  20.4 DEGREES          
REMARK 500    ARG A 252   CD  -  NE  -  CZ  ANGL. DEV. =  13.7 DEGREES          
REMARK 500    ARG A 252   NE  -  CZ  -  NH1 ANGL. DEV. =  -9.6 DEGREES          
REMARK 500    ARG A 252   NE  -  CZ  -  NH2 ANGL. DEV. =   9.9 DEGREES          
REMARK 500    LEU A 293   CA  -  CB  -  CG  ANGL. DEV. = -21.1 DEGREES          
REMARK 500    ARG A 389   CG  -  CD  -  NE  ANGL. DEV. = -15.7 DEGREES          
REMARK 500    ARG A 389   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    ARG A 389   NE  -  CZ  -  NH2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    VAL A 395   CG1 -  CB  -  CG2 ANGL. DEV. =  10.6 DEGREES          
REMARK 500    ARG A 421   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG A 421   NE  -  CZ  -  NH2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG B  10   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG B  10   NE  -  CZ  -  NH2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    CYS B  70   CA  -  CB  -  SG  ANGL. DEV. =  11.6 DEGREES          
REMARK 500    ARG B  72   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    ARG B  72   NE  -  CZ  -  NH2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ARG B 176   CB  -  CG  -  CD  ANGL. DEV. =  17.3 DEGREES          
REMARK 500    ARG B 176   CD  -  NE  -  CZ  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    ARG B 176   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    ARG B 176   NE  -  CZ  -  NH2 ANGL. DEV. =   9.4 DEGREES          
REMARK 500    ARG B 195   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG B 195   NE  -  CZ  -  NH2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG B 252   CB  -  CG  -  CD  ANGL. DEV. =  18.8 DEGREES          
REMARK 500    ARG B 252   CD  -  NE  -  CZ  ANGL. DEV. =  11.9 DEGREES          
REMARK 500    ARG B 252   NE  -  CZ  -  NH1 ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    ARG B 252   NE  -  CZ  -  NH2 ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ASP B 290   CB  -  CG  -  OD1 ANGL. DEV. =  -9.4 DEGREES          
REMARK 500    ASP B 290   CB  -  CG  -  OD2 ANGL. DEV. =  11.3 DEGREES          
REMARK 500    LEU B 293   CA  -  CB  -  CG  ANGL. DEV. = -20.1 DEGREES          
REMARK 500    ARG B 389   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG B 389   NE  -  CZ  -  NH2 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG C  39   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG C  45   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      61 ANGLE DEVIATIONS.                             
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      -59.66   -143.57                                   
REMARK 500    MET A 102     -150.89   -107.26                                   
REMARK 500    ASP A 402      121.15    -39.33                                   
REMARK 500    SER A 414     -106.91   -135.67                                   
REMARK 500    ASP A 433       41.48    -91.55                                   
REMARK 500    ASN A 460       40.87    -96.80                                   
REMARK 500    PRO A 486       41.25    -82.01                                   
REMARK 500    TYR B  31      -58.66   -143.60                                   
REMARK 500    MET B 102     -148.28   -110.17                                   
REMARK 500    VAL B 129      -60.86    -90.32                                   
REMARK 500    ALA B 224     -104.28    -20.27                                   
REMARK 500    SER B 414     -106.18   -134.36                                   
REMARK 500    ASP B 433       42.48    -92.07                                   
REMARK 500    ASN B 460       56.71   -101.29                                   
REMARK 500    PRO B 486       38.32    -82.55                                   
REMARK 500    ASN C  27       93.89   -161.40                                   
REMARK 500    LYS C  75      151.53    -49.79                                   
REMARK 500    ALA C  91      172.92    175.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 468         0.07    SIDE_CHAIN                              
REMARK 500    ARG C  39         0.11    SIDE_CHAIN                              
REMARK 500    ARG C  45         0.08    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1KXQ   RELATED DB: PDB                                   
REMARK 900 CAMELID VHH DOMAIN IN COMPLEX WITH PORCINE PANCREATIC ALPHA          
REMARK 900 -AMYLASE                                                             
REMARK 900 RELATED ID: 1KXT   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 CAMELID VHH DOMAIN CAB10 , CHAINS                   
REMARK 999 C AND D, WAS NOT AVAILABLE AT THE TIME                               
REMARK 999 OF PROCESSING.                                                       
DBREF  1KXV A    1   496  UNP    P00690   AMYP_PIG         1    496             
DBREF  1KXV B    1   496  UNP    P00690   AMYP_PIG         1    496             
DBREF  1KXV C    1   121  PDB    1KXV     1KXV             1    121             
DBREF  1KXV D    1   121  PDB    1KXV     1KXV             1    121             
SEQADV 1KXV LYS A  243  UNP  P00690    GLN   243 SEE REMARK 999                 
SEQADV 1KXV SER A  310  UNP  P00690    ALA   310 SEE REMARK 999                 
SEQADV 1KXV ILE A  323  UNP  P00690    VAL   323 SEE REMARK 999                 
SEQADV 1KXV GLN A  404  UNP  P00690    GLU   404 SEE REMARK 999                 
SEQADV 1KXV LYS B  243  UNP  P00690    GLN   243 SEE REMARK 999                 
SEQADV 1KXV SER B  310  UNP  P00690    ALA   310 SEE REMARK 999                 
SEQADV 1KXV ILE B  323  UNP  P00690    VAL   323 SEE REMARK 999                 
SEQADV 1KXV GLN B  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  121  GLN VAL GLN LEU VAL GLU SER GLY GLY GLY THR VAL PRO          
SEQRES   2 C  121  ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 C  121  ASN THR LEU CYS THR TYR ASP MET SER TRP TYR ARG ARG          
SEQRES   4 C  121  ALA PRO GLY LYS GLY ARG ASP PHE VAL SER GLY ILE ASP          
SEQRES   5 C  121  ASN ASP GLY THR THR THR TYR VAL ASP SER VAL ALA GLY          
SEQRES   6 C  121  ARG PHE THR ILE SER GLN GLY ASN ALA LYS ASN THR ALA          
SEQRES   7 C  121  TYR LEU GLN MET ASP SER LEU LYS PRO ASP ASP THR ALA          
SEQRES   8 C  121  MET TYR TYR CYS LYS PRO SER LEU ARG TYR GLY LEU PRO          
SEQRES   9 C  121  GLY CYS PRO ILE ILE PRO TRP GLY GLN GLY THR GLN VAL          
SEQRES  10 C  121  THR VAL SER SER                                              
SEQRES   1 D  121  GLN VAL GLN LEU VAL GLU SER GLY GLY GLY THR VAL PRO          
SEQRES   2 D  121  ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 D  121  ASN THR LEU CYS THR TYR ASP MET SER TRP TYR ARG ARG          
SEQRES   4 D  121  ALA PRO GLY LYS GLY ARG ASP PHE VAL SER GLY ILE ASP          
SEQRES   5 D  121  ASN ASP GLY THR THR THR TYR VAL ASP SER VAL ALA GLY          
SEQRES   6 D  121  ARG PHE THR ILE SER GLN GLY ASN ALA LYS ASN THR ALA          
SEQRES   7 D  121  TYR LEU GLN MET ASP SER LEU LYS PRO ASP ASP THR ALA          
SEQRES   8 D  121  MET TYR TYR CYS LYS PRO SER LEU ARG TYR GLY LEU PRO          
SEQRES   9 D  121  GLY CYS PRO ILE ILE PRO TRP GLY GLN GLY THR GLN VAL          
SEQRES  10 D  121  THR VAL SER SER                                              
FORMUL   5  HOH   *1377(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  ASN A   88  1                                  14    
HELIX    4   4 ASN A  120  ARG A  124  5                                   5    
HELIX    5   5 SER A  132  PHE A  136  5                                   5    
HELIX    6   6 ASP A  153  CYS A  160  1                                   8    
HELIX    7   7 LYS A  172  GLY A  190  1                                  19    
HELIX    8   8 ALA A  198  MET A  202  5                                   5    
HELIX    9   9 TRP A  203  ASP A  212  1                                  10    
HELIX   10  10 LYS A  243  PHE A  248  5                                   6    
HELIX   11  11 PHE A  256  LYS A  268  1                                  13    
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 GLU A  493  LYS A  495  5                                   3    
HELIX   22  22 ARG B   20  TYR B   31  1                                  12    
HELIX   23  23 PRO B   57  GLN B   63  5                                   7    
HELIX   24  24 ASN B   75  VAL B   89  1                                  15    
HELIX   25  25 ASN B  120  ARG B  124  5                                   5    
HELIX   26  26 SER B  132  PHE B  136  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  LYS B  213  1                                  11    
HELIX   31  31 LYS B  243  PHE B  248  5                                   6    
HELIX   32  32 PHE B  256  LYS B  268  1                                  13    
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  ASP B  402  1                                  15    
HELIX   42  42 GLU B  493  LYS B  495  5                                   3    
HELIX   43  43 ASP C   61  ALA C   64  5                                   4    
HELIX   44  44 LYS C   86  THR C   90  5                                   5    
HELIX   45  45 ASP D   61  ALA D   64  5                                   4    
HELIX   46  46 LYS D   86  THR D   90  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  O  ALA A 418   N  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  O  VAL B 366   N  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  N  VAL B 467   O  TYR B 449           
SHEET    1   P 4 GLN C   3  SER C   7  0                                        
SHEET    2   P 4 LEU C  18  SER C  25 -1  N  SER C  21   O  SER C   7           
SHEET    3   P 4 THR C  77  MET C  82 -1  O  ALA C  78   N  CYS C  22           
SHEET    4   P 4 PHE C  67  GLN C  71 -1  O  THR C  68   N  GLN C  81           
SHEET    1   Q 6 GLY C  10  VAL C  12  0                                        
SHEET    2   Q 6 THR C 115  VAL C 119  1  O  GLN C 116   N  GLY C  10           
SHEET    3   Q 6 ALA C  91  LEU C  99 -1  O  ALA C  91   N  VAL C 117           
SHEET    4   Q 6 TYR C  32  ARG C  39 -1  N  ASP C  33   O  SER C  98           
SHEET    5   Q 6 ARG C  45  ILE C  51 -1  N  ASP C  46   O  ARG C  38           
SHEET    6   Q 6 THR C  57  TYR C  59 -1  O  THR C  58   N  GLY C  50           
SHEET    1   R 4 GLN D   3  SER D   7  0                                        
SHEET    2   R 4 LEU D  18  SER D  25 -1  N  SER D  21   O  SER D   7           
SHEET    3   R 4 THR D  77  MET D  82 -1  N  ALA D  78   O  CYS D  22           
SHEET    4   R 4 PHE D  67  GLN D  71 -1  O  THR D  68   N  GLN D  81           
SHEET    1   S 6 GLY D  10  PRO D  13  0                                        
SHEET    2   S 6 THR D 115  SER D 120  1  O  GLN D 116   N  GLY D  10           
SHEET    3   S 6 ALA D  91  LEU D  99 -1  O  ALA D  91   N  VAL D 117           
SHEET    4   S 6 TYR D  32  ARG D  39 -1  N  ASP D  33   O  SER D  98           
SHEET    5   S 6 ARG D  45  ILE D  51 -1  N  ASP D  46   O  ARG D  38           
SHEET    6   S 6 THR D  57  TYR D  59 -1  N  THR D  58   O  GLY D  50           
SSBOND   1 CYS A   28    CYS A   86                          1555   1555  2.08  
SSBOND   2 CYS A   70    CYS A  115                          1555   1555  2.08  
SSBOND   3 CYS A  141    CYS A  160                          1555   1555  2.07  
SSBOND   4 CYS A  378    CYS A  384                          1555   1555  2.06  
SSBOND   5 CYS A  450    CYS A  462                          1555   1555  2.03  
SSBOND   6 CYS B   28    CYS B   86                          1555   1555  2.07  
SSBOND   7 CYS B   70    CYS B  115                          1555   1555  2.07  
SSBOND   8 CYS B  141    CYS B  160                          1555   1555  2.08  
SSBOND   9 CYS B  378    CYS B  384                          1555   1555  2.05  
SSBOND  10 CYS B  450    CYS B  462                          1555   1555  2.05  
SSBOND  11 CYS C   22    CYS C   95                          1555   1555  2.03  
SSBOND  12 CYS C   30    CYS C  106                          1555   1555  2.07  
SSBOND  13 CYS D   22    CYS D   95                          1555   1555  2.03  
SSBOND  14 CYS D   30    CYS D  106                          1555   1555  2.07  
CISPEP   1 ASN A   53    PRO A   54          0         0.00                     
CISPEP   2 VAL A  129    PRO A  130          0        -0.48                     
CISPEP   3 ASN B   53    PRO B   54          0         0.05                     
CISPEP   4 VAL B  129    PRO B  130          0         0.61                     
CRYST1   57.568   60.990  107.333  98.78 100.88 101.14 P 1           2          
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      0.017371  0.003421  0.004090        0.00000                         
SCALE2      0.000000  0.016711  0.003345        0.00000                         
SCALE3      0.000000  0.000000  0.009676        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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