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Database: PDB
Entry: 1KXT
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HEADER    HYDROLASE, IMMUNE SYSTEM                01-FEB-02   1KXT              
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, C, E;                                                      
COMPND   4 SYNONYM: 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE;                        
COMPND   5 EC: 3.2.1.1;                                                         
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: IMMUNOGLOBULIN VHH FRAGMENT;                               
COMPND   8 CHAIN: B, D, F;                                                      
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 GENE: IGG VHH;                                                       
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  13 EXPRESSION_SYSTEM_STRAIN: WK6;                                       
SOURCE  14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  15 EXPRESSION_SYSTEM_PLASMID: PHEN6                                     
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 1KXT    1       VERSN                                    
REVDAT   3   01-APR-03 1KXT    1       JRNL                                     
REVDAT   2   14-AUG-02 1KXT    1       JRNL                                     
REVDAT   1   19-JUN-02 1KXT    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.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2014619.790                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 50.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 65698                          
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) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1655                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 14.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3132                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2280                       
REMARK   3   BIN FREE R VALUE                    : 0.2890                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 2.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 90                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.030                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14439                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 1727                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 7.90                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.48000                                             
REMARK   3    B22 (A**2) : 0.41000                                              
REMARK   3    B33 (A**2) : 1.07000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 3.32000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.23                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.14                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.28                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.24                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.82                            
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        : 0.37                                                 
REMARK   3   BSOL        : 52.85                                                
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 1KXT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB015448.                                      
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                             : 8.0                                
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   : 65792                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 50.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 50.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.14000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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 1QDO                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000 15%, MALATE IMIDAZOLE          
REMARK 280  0.2M, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000      143.42500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 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     GLY B    26                                                      
REMARK 465     TYR B    27                                                      
REMARK 465     SER B   112                                                      
REMARK 465     SER B   113                                                      
REMARK 465     GLY D    26                                                      
REMARK 465     TYR D    27                                                      
REMARK 465     SER D   112                                                      
REMARK 465     SER D   113                                                      
REMARK 465     GLY F    26                                                      
REMARK 465     TYR F    27                                                      
REMARK 465     SER F   112                                                      
REMARK 465     SER F   113                                                      
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   O    HOH C  4009     O    HOH C  4166              2.04            
REMARK 500   N    GLU A    78     O    HOH A  4218              2.07            
REMARK 500   O    GLY A   271     O    HOH A  4270              2.15            
REMARK 500   O    ALA B    24     O    HOH B   157              2.15            
REMARK 500   O    HOH A  4012     O    HOH A  4270              2.15            
REMARK 500   O    ALA F    94     O    PRO F   100K             2.17            
REMARK 500   O    HOH B   162     O    HOH B   167              2.17            
REMARK 500   O    PHE B    29     O    HOH B   156              2.18            
REMARK 500   O    HOH E  4386     O    HOH E  4425              2.19            
REMARK 500   O    HIS A   215     O    HOH A  4341              2.19            
REMARK 500   CD1  LEU E   293     O    HOH E  4321              2.19            
REMARK 500   O    HOH E  4268     O    HOH E  4370              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD1  ASN E   460     O    HOH A  4216     1655     2.14            
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. =   6.9 DEGREES          
REMARK 500    PRO B 100K  N   -  CA  -  C   ANGL. DEV. =  15.6 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    SER A   8      134.73    -39.30                                   
REMARK 500    TYR A  31      -61.92   -140.43                                   
REMARK 500    MET A 102     -159.08   -109.15                                   
REMARK 500    ASP A 138      -55.26     -2.60                                   
REMARK 500    VAL A 163       44.27     37.21                                   
REMARK 500    LEU A 166      108.00    -59.17                                   
REMARK 500    LEU A 170        3.02    -64.13                                   
REMARK 500    ALA A 224     -124.10      7.08                                   
REMARK 500    HIS A 305       41.92    -60.51                                   
REMARK 500    ASP A 317       49.96   -105.74                                   
REMARK 500    SER A 341     -163.66   -122.52                                   
REMARK 500    HIS A 386        1.63    -63.46                                   
REMARK 500    SER A 414     -110.13   -128.73                                   
REMARK 500    ASN A 460       40.97   -103.40                                   
REMARK 500    PRO A 486       32.77    -60.91                                   
REMARK 500    PHE B  29     -159.13    -84.89                                   
REMARK 500    ASN B  73      -39.57     66.31                                   
REMARK 500    ALA B  75       12.45   -166.45                                   
REMARK 500    ALA B  88      177.45    173.15                                   
REMARK 500    PRO B 100K       4.89    -63.25                                   
REMARK 500    ASN B 101      -55.39     93.93                                   
REMARK 500    SER C   8      126.54    -39.69                                   
REMARK 500    TYR C  31      -57.26   -149.50                                   
REMARK 500    SER C  66     -176.41   -173.73                                   
REMARK 500    HIS C 101     -179.57   -171.46                                   
REMARK 500    MET C 102     -165.08   -121.83                                   
REMARK 500    THR C 114      -14.30    -46.96                                   
REMARK 500    VAL C 163       41.10     35.08                                   
REMARK 500    LEU C 170        3.52    -62.14                                   
REMARK 500    ASN C 218       95.35    -49.15                                   
REMARK 500    ALA C 224      -63.52    -25.14                                   
REMARK 500    SER C 270       26.43     48.44                                   
REMARK 500    ASP C 300      -72.10    -78.38                                   
REMARK 500    ASP C 317       56.48   -108.80                                   
REMARK 500    ALA C 318      -72.42    -36.02                                   
REMARK 500    ILE C 358      129.70    -36.66                                   
REMARK 500    ASN C 364       28.67     48.91                                   
REMARK 500    ASN C 380       40.24     38.84                                   
REMARK 500    SER C 414     -110.00   -121.50                                   
REMARK 500    SER C 437      103.73   -164.72                                   
REMARK 500    PRO C 486       35.91    -70.02                                   
REMARK 500    SER D   7     -158.41   -107.35                                   
REMARK 500    ALA D  14      131.59    -24.80                                   
REMARK 500    SER D  31       29.86   -146.30                                   
REMARK 500    ASN D  73        4.45     59.41                                   
REMARK 500    ALA D  75       -1.63   -149.09                                   
REMARK 500    ASP D  86        1.61    -64.47                                   
REMARK 500    ALA D  88      174.04    175.45                                   
REMARK 500    PRO D 100K      16.51    -63.68                                   
REMARK 500    ASN D 101      -78.05     86.27                                   
REMARK 500    PHE E  17      113.19    -38.30                                   
REMARK 500    TYR E  31      -65.91   -155.91                                   
REMARK 500    SER E  55       98.96    -69.53                                   
REMARK 500    MET E 102     -166.48   -116.17                                   
REMARK 500    CYS E 103     -175.72    -57.64                                   
REMARK 500    VAL E 163       48.01     38.97                                   
REMARK 500    ALA E 224      -98.03     -7.51                                   
REMARK 500    HIS E 305       56.69    -56.04                                   
REMARK 500    THR E 376        5.02     80.97                                   
REMARK 500    ASP E 381       14.87     59.86                                   
REMARK 500    SER E 414     -103.52   -124.85                                   
REMARK 500    ASP E 433       33.67    -88.99                                   
REMARK 500    SER E 437      112.91   -161.42                                   
REMARK 500    PRO E 486       34.59    -67.55                                   
REMARK 500    PHE F  29     -159.79   -122.78                                   
REMARK 500    SER F  31       26.69   -145.35                                   
REMARK 500    ASN F  73      -46.76     66.82                                   
REMARK 500    ALA F  88      175.72    168.56                                   
REMARK 500    ASN F 101      -64.40     49.51                                   
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 D 119        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH D 120        DISTANCE =  7.16 ANGSTROMS                       
REMARK 525    HOH D 123        DISTANCE =  5.58 ANGSTROMS                       
REMARK 525    HOH F 124        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH D 125        DISTANCE =  5.72 ANGSTROMS                       
REMARK 525    HOH D 135        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH F 142        DISTANCE =  6.59 ANGSTROMS                       
REMARK 525    HOH F 145        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH B 146        DISTANCE =  5.43 ANGSTROMS                       
REMARK 525    HOH C4046        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH C4049        DISTANCE =  6.66 ANGSTROMS                       
REMARK 525    HOH D 159        DISTANCE =  7.84 ANGSTROMS                       
REMARK 525    HOH B 161        DISTANCE =  6.38 ANGSTROMS                       
REMARK 525    HOH F 168        DISTANCE =  5.46 ANGSTROMS                       
REMARK 525    HOH B 174        DISTANCE =  5.60 ANGSTROMS                       
REMARK 525    HOH D 176        DISTANCE =  6.71 ANGSTROMS                       
REMARK 525    HOH A4067        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH C4071        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH D 183        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH D 184        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH B 187        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH D 190        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH F 190        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH B 192        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH F 195        DISTANCE =  9.24 ANGSTROMS                       
REMARK 525    HOH F 196        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH D 198        DISTANCE =  7.43 ANGSTROMS                       
REMARK 525    HOH F 203        DISTANCE =  7.38 ANGSTROMS                       
REMARK 525    HOH D 204        DISTANCE =  6.19 ANGSTROMS                       
REMARK 525    HOH D 209        DISTANCE =  5.62 ANGSTROMS                       
REMARK 525    HOH E4104        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH D 212        DISTANCE =  8.57 ANGSTROMS                       
REMARK 525    HOH F 212        DISTANCE =  5.75 ANGSTROMS                       
REMARK 525    HOH B 213        DISTANCE =  7.76 ANGSTROMS                       
REMARK 525    HOH B 214        DISTANCE =  6.87 ANGSTROMS                       
REMARK 525    HOH C4106        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH D 217        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH F 218        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH B 222        DISTANCE =  9.02 ANGSTROMS                       
REMARK 525    HOH F 222        DISTANCE =  7.77 ANGSTROMS                       
REMARK 525    HOH F 223        DISTANCE =  8.01 ANGSTROMS                       
REMARK 525    HOH A4113        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH D 224        DISTANCE =  5.70 ANGSTROMS                       
REMARK 525    HOH F 224        DISTANCE =  5.74 ANGSTROMS                       
REMARK 525    HOH F 225        DISTANCE =  5.77 ANGSTROMS                       
REMARK 525    HOH A4115        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH C4119        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH D 230        DISTANCE =  8.43 ANGSTROMS                       
REMARK 525    HOH D 231        DISTANCE =  7.96 ANGSTROMS                       
REMARK 525    HOH B 235        DISTANCE =  8.67 ANGSTROMS                       
REMARK 525    HOH C4126        DISTANCE =  5.57 ANGSTROMS                       
REMARK 525    HOH E4129        DISTANCE =  5.75 ANGSTROMS                       
REMARK 525    HOH B 238        DISTANCE =  8.30 ANGSTROMS                       
REMARK 525    HOH B 242        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH A4155        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH C4160        DISTANCE =  6.37 ANGSTROMS                       
REMARK 525    HOH C4165        DISTANCE =  8.12 ANGSTROMS                       
REMARK 525    HOH C4166        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH E4168        DISTANCE =  5.58 ANGSTROMS                       
REMARK 525    HOH A4170        DISTANCE =  5.52 ANGSTROMS                       
REMARK 525    HOH C4202        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH C4207        DISTANCE =  8.09 ANGSTROMS                       
REMARK 525    HOH C4212        DISTANCE =  7.05 ANGSTROMS                       
REMARK 525    HOH C4214        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH E4221        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH E4223        DISTANCE =  6.03 ANGSTROMS                       
REMARK 525    HOH C4224        DISTANCE =  6.33 ANGSTROMS                       
REMARK 525    HOH C4233        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH C4240        DISTANCE =  7.47 ANGSTROMS                       
REMARK 525    HOH C4241        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH C4247        DISTANCE =  8.46 ANGSTROMS                       
REMARK 525    HOH C4257        DISTANCE =  5.74 ANGSTROMS                       
REMARK 525    HOH A4263        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH C4267        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH C4269        DISTANCE =  7.34 ANGSTROMS                       
REMARK 525    HOH C4277        DISTANCE =  7.87 ANGSTROMS                       
REMARK 525    HOH E4279        DISTANCE =  7.72 ANGSTROMS                       
REMARK 525    HOH A4277        DISTANCE =  6.42 ANGSTROMS                       
REMARK 525    HOH E4285        DISTANCE =  8.11 ANGSTROMS                       
REMARK 525    HOH C4289        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH C4292        DISTANCE =  6.44 ANGSTROMS                       
REMARK 525    HOH E4300        DISTANCE =  7.74 ANGSTROMS                       
REMARK 525    HOH E4301        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH C4301        DISTANCE =  6.72 ANGSTROMS                       
REMARK 525    HOH E4303        DISTANCE =  8.69 ANGSTROMS                       
REMARK 525    HOH E4305        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH E4308        DISTANCE =  7.44 ANGSTROMS                       
REMARK 525    HOH E4309        DISTANCE =  7.06 ANGSTROMS                       
REMARK 525    HOH C4312        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH C4318        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH E4323        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH A4320        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH A4323        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH C4325        DISTANCE =  7.88 ANGSTROMS                       
REMARK 525    HOH E4329        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH E4331        DISTANCE =  9.98 ANGSTROMS                       
REMARK 525    HOH C4331        DISTANCE =  7.97 ANGSTROMS                       
REMARK 525    HOH A4337        DISTANCE =  5.61 ANGSTROMS                       
REMARK 525    HOH C4340        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH C4341        DISTANCE =  5.26 ANGSTROMS                       
REMARK 525    HOH A4340        DISTANCE =  9.47 ANGSTROMS                       
REMARK 525    HOH C4342        DISTANCE =  7.97 ANGSTROMS                       
REMARK 525    HOH E4348        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH C4347        DISTANCE =  8.65 ANGSTROMS                       
REMARK 525    HOH E4351        DISTANCE =  8.41 ANGSTROMS                       
REMARK 525    HOH C4361        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH A4360        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH A4361        DISTANCE =  6.62 ANGSTROMS                       
REMARK 525    HOH E4365        DISTANCE =  8.63 ANGSTROMS                       
REMARK 525    HOH A4369        DISTANCE =  9.30 ANGSTROMS                       
REMARK 525    HOH E4373        DISTANCE =  5.56 ANGSTROMS                       
REMARK 525    HOH E4375        DISTANCE =  7.48 ANGSTROMS                       
REMARK 525    HOH C4377        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH C4379        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH A4382        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH E4388        DISTANCE = 12.94 ANGSTROMS                       
REMARK 525    HOH C4390        DISTANCE = 10.44 ANGSTROMS                       
REMARK 525    HOH A4393        DISTANCE =  7.87 ANGSTROMS                       
REMARK 525    HOH C4395        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH A4396        DISTANCE =  7.62 ANGSTROMS                       
REMARK 525    HOH E4401        DISTANCE =  6.47 ANGSTROMS                       
REMARK 525    HOH E4402        DISTANCE =  6.77 ANGSTROMS                       
REMARK 525    HOH E4404        DISTANCE =  7.95 ANGSTROMS                       
REMARK 525    HOH A4405        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH A4413        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH A4417        DISTANCE =  6.44 ANGSTROMS                       
REMARK 525    HOH E4428        DISTANCE =  7.02 ANGSTROMS                       
REMARK 525    HOH E4429        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH E4431        DISTANCE =  8.80 ANGSTROMS                       
REMARK 525    HOH A4428        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH E4442        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH E4449        DISTANCE =  7.94 ANGSTROMS                       
REMARK 525    HOH E4455        DISTANCE =  9.68 ANGSTROMS                       
REMARK 525    HOH A4458        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH A4469        DISTANCE =  6.55 ANGSTROMS                       
REMARK 525    HOH E4476        DISTANCE =  7.39 ANGSTROMS                       
REMARK 525    HOH A4475        DISTANCE =  7.63 ANGSTROMS                       
REMARK 525    HOH E4485        DISTANCE =  8.44 ANGSTROMS                       
REMARK 525    HOH E4490        DISTANCE =  8.06 ANGSTROMS                       
REMARK 525    HOH E4493        DISTANCE =  5.03 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 ARG A 158   O                                                      
REMARK 620 2 ASP A 167   OD2  77.6                                              
REMARK 620 3 HIS A 201   O    82.1 159.0                                        
REMARK 620 4 HOH A4221   O    61.7  94.0  80.7                                  
REMARK 620 5 ASN A 100   OD1 157.6 120.5  80.5 101.6                            
REMARK 620 6 ASP A 167   OD1 117.0  52.1 137.4 141.7  85.4                      
REMARK 620 7 HOH A4227   O   121.6  64.0 133.3  78.3  63.9  71.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C4003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG C 158   O                                                      
REMARK 620 2 ASP C 167   OD1 108.8                                              
REMARK 620 3 ASP C 167   OD2  66.0  50.1                                        
REMARK 620 4 HOH C4141   O    76.8  66.6  80.9                                  
REMARK 620 5 ASN C 100   OD1 161.6  89.0 131.9 107.7                            
REMARK 620 6 HIS C 201   O    91.2 141.6 156.3  87.8  71.5                      
REMARK 620 7 HOH C4140   O   114.1  74.2  71.2 140.6  74.2 127.6                
REMARK 620 8 HOH C4275   O    80.4 126.0  93.5 156.8  92.8  88.7  54.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E4005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN E 100   OD1                                                    
REMARK 620 2 ARG E 158   O   160.3                                              
REMARK 620 3 ASP E 167   OD1  79.7 116.7                                        
REMARK 620 4 ASP E 167   OD2 124.9  74.5  49.1                                  
REMARK 620 5 HIS E 201   O    77.0  83.5 132.4 150.8                            
REMARK 620 6 HOH E4240   O   104.3  73.7  70.2  79.2  76.2                      
REMARK 620 7 HOH E4242   O    70.7 123.3  71.4  74.2 134.9 141.5                
REMARK 620 N                    1     2     3     4     5     6                 
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 C 4003                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 4004                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 4005                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 4006                 
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: 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 IMMUNOGLOBULIN VHH FRAGMENT, CHAINS                 
REMARK 999 B, D, AND F WAS NOT AVAILABLE AT THE TIME                            
REMARK 999 OF PROCESSING.                                                       
DBREF  1KXT A    1   496  UNP    P00690   AMYP_PIG         1    496             
DBREF  1KXT C    1   496  UNP    P00690   AMYP_PIG         1    496             
DBREF  1KXT E    1   496  UNP    P00690   AMYP_PIG         1    496             
DBREF  1KXT B    1   113  PDB    1KXT     1KXT             1    113             
DBREF  1KXT D    1   113  PDB    1KXT     1KXT             1    113             
DBREF  1KXT F    1   113  PDB    1KXT     1KXT             1    113             
SEQADV 1KXT LYS A  243  UNP  P00690    GLN   243 SEE REMARK 999                 
SEQADV 1KXT SER A  310  UNP  P00690    ALA   310 SEE REMARK 999                 
SEQADV 1KXT ILE A  323  UNP  P00690    VAL   323 SEE REMARK 999                 
SEQADV 1KXT GLN A  404  UNP  P00690    GLU   404 SEE REMARK 999                 
SEQADV 1KXT LYS C  243  UNP  P00690    GLN   243 SEE REMARK 999                 
SEQADV 1KXT SER C  310  UNP  P00690    ALA   310 SEE REMARK 999                 
SEQADV 1KXT ILE C  323  UNP  P00690    VAL   323 SEE REMARK 999                 
SEQADV 1KXT GLN C  404  UNP  P00690    GLU   404 SEE REMARK 999                 
SEQADV 1KXT LYS E  243  UNP  P00690    GLN   243 SEE REMARK 999                 
SEQADV 1KXT SER E  310  UNP  P00690    ALA   310 SEE REMARK 999                 
SEQADV 1KXT ILE E  323  UNP  P00690    VAL   323 SEE REMARK 999                 
SEQADV 1KXT GLN E  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  127  GLN VAL GLN LEU VAL ALA SER GLY GLY GLY SER VAL GLN          
SEQRES   2 B  127  ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 B  127  TYR THR PHE SER SER TYR PRO MET GLY TRP TYR ARG GLN          
SEQRES   4 B  127  ALA PRO GLY LYS GLU CYS GLU LEU SER ALA ARG ILE PHE          
SEQRES   5 B  127  SER ASP GLY SER ALA ASN TYR ALA ASP SER VAL LYS GLY          
SEQRES   6 B  127  ARG PHE THR ILE SER ARG ASP ASN ALA ALA ASN THR ALA          
SEQRES   7 B  127  TYR LEU GLN MET ASP SER LEU LYS PRO GLU ASP THR ALA          
SEQRES   8 B  127  VAL TYR TYR CYS ALA ALA GLY PRO GLY SER GLY LYS LEU          
SEQRES   9 B  127  VAL VAL ALA GLY ARG THR CYS TYR GLY PRO ASN TYR TRP          
SEQRES  10 B  127  GLY GLN GLY THR GLN VAL THR VAL SER SER                      
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  127  GLN VAL GLN LEU VAL ALA SER GLY GLY GLY SER VAL GLN          
SEQRES   2 D  127  ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 D  127  TYR THR PHE SER SER TYR PRO MET GLY TRP TYR ARG GLN          
SEQRES   4 D  127  ALA PRO GLY LYS GLU CYS GLU LEU SER ALA ARG ILE PHE          
SEQRES   5 D  127  SER ASP GLY SER ALA ASN TYR ALA ASP SER VAL LYS GLY          
SEQRES   6 D  127  ARG PHE THR ILE SER ARG ASP ASN ALA ALA ASN THR ALA          
SEQRES   7 D  127  TYR LEU GLN MET ASP SER LEU LYS PRO GLU ASP THR ALA          
SEQRES   8 D  127  VAL TYR TYR CYS ALA ALA GLY PRO GLY SER GLY LYS LEU          
SEQRES   9 D  127  VAL VAL ALA GLY ARG THR CYS TYR GLY PRO ASN TYR TRP          
SEQRES  10 D  127  GLY GLN GLY THR GLN VAL THR VAL SER SER                      
SEQRES   1 E  496  GLN TYR ALA PRO GLN THR GLN SER GLY ARG THR SER ILE          
SEQRES   2 E  496  VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU          
SEQRES   3 E  496  GLU CYS GLU ARG TYR LEU GLY PRO LYS GLY PHE GLY GLY          
SEQRES   4 E  496  VAL GLN VAL SER PRO PRO ASN GLU ASN ILE VAL VAL THR          
SEQRES   5 E  496  ASN PRO SER ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL          
SEQRES   6 E  496  SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASN GLU          
SEQRES   7 E  496  PHE ARG ASP MET VAL THR ARG CYS ASN ASN VAL GLY VAL          
SEQRES   8 E  496  ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY          
SEQRES   9 E  496  SER GLY ALA ALA ALA GLY THR GLY THR THR CYS GLY SER          
SEQRES  10 E  496  TYR CYS ASN PRO GLY SER ARG GLU PHE PRO ALA VAL PRO          
SEQRES  11 E  496  TYR SER ALA TRP ASP PHE ASN ASP GLY LYS CYS LYS THR          
SEQRES  12 E  496  ALA SER GLY GLY ILE GLU SER TYR ASN ASP PRO TYR GLN          
SEQRES  13 E  496  VAL ARG ASP CYS GLN LEU VAL GLY LEU LEU ASP LEU ALA          
SEQRES  14 E  496  LEU GLU LYS ASP TYR VAL ARG SER MET ILE ALA ASP TYR          
SEQRES  15 E  496  LEU ASN LYS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG          
SEQRES  16 E  496  ILE ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS          
SEQRES  17 E  496  ALA VAL LEU ASP LYS LEU HIS ASN LEU ASN THR ASN TRP          
SEQRES  18 E  496  PHE PRO ALA GLY SER ARG PRO PHE ILE PHE GLN GLU VAL          
SEQRES  19 E  496  ILE ASP LEU GLY GLY GLU ALA ILE LYS SER SER GLU TYR          
SEQRES  20 E  496  PHE GLY ASN GLY ARG VAL THR GLU PHE LYS TYR GLY ALA          
SEQRES  21 E  496  LYS LEU GLY THR VAL VAL ARG LYS TRP SER GLY GLU LYS          
SEQRES  22 E  496  MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE          
SEQRES  23 E  496  MET PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS          
SEQRES  24 E  496  ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY SER SER ILE          
SEQRES  25 E  496  LEU THR PHE TRP ASP ALA ARG LEU TYR LYS ILE ALA VAL          
SEQRES  26 E  496  GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL          
SEQRES  27 E  496  MET SER SER TYR ARG TRP ALA ARG ASN PHE VAL ASN GLY          
SEQRES  28 E  496  GLU ASP VAL ASN ASP TRP ILE GLY PRO PRO ASN ASN ASN          
SEQRES  29 E  496  GLY VAL ILE LYS GLU VAL THR ILE ASN ALA ASP THR THR          
SEQRES  30 E  496  CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLU          
SEQRES  31 E  496  ILE ARG ASN MET VAL TRP PHE ARG ASN VAL VAL ASP GLY          
SEQRES  32 E  496  GLN PRO PHE ALA ASN TRP TRP ASP ASN GLY SER ASN GLN          
SEQRES  33 E  496  VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE          
SEQRES  34 E  496  ASN ASN ASP ASP TRP GLN LEU SER SER THR LEU GLN THR          
SEQRES  35 E  496  GLY LEU PRO GLY GLY THR TYR CYS ASP VAL ILE SER GLY          
SEQRES  36 E  496  ASP LYS VAL GLY ASN SER CYS THR GLY ILE LYS VAL TYR          
SEQRES  37 E  496  VAL SER SER ASP GLY THR ALA GLN PHE SER ILE SER ASN          
SEQRES  38 E  496  SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER          
SEQRES  39 E  496  LYS LEU                                                      
SEQRES   1 F  127  GLN VAL GLN LEU VAL ALA SER GLY GLY GLY SER VAL GLN          
SEQRES   2 F  127  ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 F  127  TYR THR PHE SER SER TYR PRO MET GLY TRP TYR ARG GLN          
SEQRES   4 F  127  ALA PRO GLY LYS GLU CYS GLU LEU SER ALA ARG ILE PHE          
SEQRES   5 F  127  SER ASP GLY SER ALA ASN TYR ALA ASP SER VAL LYS GLY          
SEQRES   6 F  127  ARG PHE THR ILE SER ARG ASP ASN ALA ALA ASN THR ALA          
SEQRES   7 F  127  TYR LEU GLN MET ASP SER LEU LYS PRO GLU ASP THR ALA          
SEQRES   8 F  127  VAL TYR TYR CYS ALA ALA GLY PRO GLY SER GLY LYS LEU          
SEQRES   9 F  127  VAL VAL ALA GLY ARG THR CYS TYR GLY PRO ASN TYR TRP          
SEQRES  10 F  127  GLY GLN GLY THR GLN VAL THR VAL SER SER                      
HET     CA  A4001       1                                                       
HET     CL  A4002       1                                                       
HET     CA  C4003       1                                                       
HET     CL  C4004       1                                                       
HET     CA  E4005       1                                                       
HET     CL  E4006       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   7   CA    3(CA 2+)                                                     
FORMUL   8   CL    3(CL 1-)                                                     
FORMUL  13  HOH   *1727(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 GLN A  161  VAL A  163  5                                   3    
HELIX    8   8 LYS A  172  GLY A  190  1                                  19    
HELIX    9   9 ALA A  198  MET A  202  5                                   5    
HELIX   10  10 TRP A  203  ASP A  212  1                                  10    
HELIX   11  11 LYS A  243  TYR A  247  5                                   5    
HELIX   12  12 GLU A  255  LYS A  268  1                                  14    
HELIX   13  13 LYS A  273  TRP A  280  5                                   8    
HELIX   14  14 GLY A  281  GLY A  285  5                                   5    
HELIX   15  15 PRO A  288  ASP A  290  5                                   3    
HELIX   16  16 ASP A  300  GLY A  304  5                                   5    
HELIX   17  17 GLY A  308  ILE A  312  5                                   5    
HELIX   18  18 THR A  314  TRP A  316  5                                   3    
HELIX   19  19 ASP A  317  HIS A  331  1                                  15    
HELIX   20  20 CYS A  384  ARG A  387  5                                   4    
HELIX   21  21 TRP A  388  VAL A  401  1                                  14    
HELIX   22  22 GLU A  493  LYS A  495  5                                   3    
HELIX   23  23 LYS B   83  THR B   87  5                                   5    
HELIX   24  24 ARG C   20  TYR C   31  1                                  12    
HELIX   25  25 PRO C   57  GLN C   63  5                                   7    
HELIX   26  26 GLU C   76  ASN C   88  1                                  13    
HELIX   27  27 ASN C  120  ARG C  124  5                                   5    
HELIX   28  28 SER C  132  PHE C  136  5                                   5    
HELIX   29  29 ASP C  153  CYS C  160  1                                   8    
HELIX   30  30 LYS C  172  GLY C  190  1                                  19    
HELIX   31  31 ALA C  198  MET C  202  5                                   5    
HELIX   32  32 TRP C  203  ASP C  212  1                                  10    
HELIX   33  33 LYS C  243  PHE C  248  5                                   6    
HELIX   34  34 GLU C  255  ARG C  267  1                                  13    
HELIX   35  35 LYS C  273  TRP C  280  5                                   8    
HELIX   36  36 GLY C  281  GLY C  285  5                                   5    
HELIX   37  37 PRO C  288  ASP C  290  5                                   3    
HELIX   38  38 ASP C  300  GLY C  304  5                                   5    
HELIX   39  39 GLY C  308  ILE C  312  5                                   5    
HELIX   40  40 THR C  314  TRP C  316  5                                   3    
HELIX   41  41 ASP C  317  HIS C  331  1                                  15    
HELIX   42  42 CYS C  384  ARG C  387  5                                   4    
HELIX   43  43 TRP C  388  VAL C  401  1                                  14    
HELIX   44  44 LYS D   83  THR D   87  5                                   5    
HELIX   45  45 ARG E   20  TYR E   31  1                                  12    
HELIX   46  46 PRO E   57  GLN E   63  5                                   7    
HELIX   47  47 ASN E   75  VAL E   89  1                                  15    
HELIX   48  48 SER E  132  PHE E  136  5                                   5    
HELIX   49  49 ASP E  153  CYS E  160  1                                   8    
HELIX   50  50 LYS E  172  GLY E  190  1                                  19    
HELIX   51  51 TRP E  203  ASP E  212  1                                  10    
HELIX   52  52 LYS E  243  GLY E  251  5                                   9    
HELIX   53  53 GLU E  255  LYS E  268  1                                  14    
HELIX   54  54 TRP E  269  GLU E  272  5                                   4    
HELIX   55  55 LYS E  273  TRP E  280  5                                   8    
HELIX   56  56 GLY E  281  GLY E  285  5                                   5    
HELIX   57  57 PRO E  288  ASP E  290  5                                   3    
HELIX   58  58 ASP E  300  GLY E  304  5                                   5    
HELIX   59  59 GLY E  308  ILE E  312  5                                   5    
HELIX   60  60 THR E  314  TRP E  316  5                                   3    
HELIX   61  61 ASP E  317  HIS E  331  1                                  15    
HELIX   62  62 CYS E  384  ARG E  387  5                                   4    
HELIX   63  63 TRP E  388  VAL E  401  1                                  14    
HELIX   64  64 LYS F   83  THR F   87  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  N  ARG A 252   O  ILE A 230           
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  O  VAL A 467   N  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 4 LEU B   4  SER B   7  0                                        
SHEET    2   I 4 LEU B  18  ALA B  24 -1  O  SER B  21   N  SER B   7           
SHEET    3   I 4 THR B  77  MET B  82 -1  N  ALA B  78   O  CYS B  22           
SHEET    4   I 4 PHE B  67  ARG B  71 -1  O  THR B  68   N  GLN B  81           
SHEET    1   J 8 GLY B  10  SER B  11  0                                        
SHEET    2   J 8 THR B 107  THR B 110  1  O  GLN B 108   N  GLY B  10           
SHEET    3   J 8 ALA B  88  ALA B  94 -1  O  ALA B  88   N  VAL B 109           
SHEET    4   J 8 TYR B 102  TRP B 103 -1  O  TYR B 102   N  ALA B  94           
SHEET    5   J 8 ALA B  88  ALA B  94 -1  N  ALA B  94   O  TYR B 102           
SHEET    6   J 8 MET B  34  GLN B  39 -1  N  GLY B  35   O  ALA B  93           
SHEET    7   J 8 CYS B  45  ILE B  51 -1  N  GLU B  46   O  ARG B  38           
SHEET    8   J 8 ALA B  57  TYR B  59 -1  N  ASN B  58   O  ARG B  50           
SHEET    1   K 2 GLY B  99  VAL B 100C 0                                        
SHEET    2   K 2 ARG B 100F GLY B 100J-1  O  ARG B 100F  N  VAL B 100C          
SHEET    1   L 9 SER C  12  LEU C  16  0                                        
SHEET    2   L 9 GLY C  39  VAL C  42  1  O  GLY C  39   N  VAL C  14           
SHEET    3   L 9 ARG C  92  ALA C  97  1  O  ARG C  92   N  VAL C  40           
SHEET    4   L 9 GLY C 193  ILE C 196  1  O  GLY C 193   N  VAL C  95           
SHEET    5   L 9 PHE C 229  GLN C 232  1  O  PHE C 229   N  PHE C 194           
SHEET    6   L 9 ARG C 252  THR C 254  1  O  ARG C 252   N  GLN C 232           
SHEET    7   L 9 ALA C 292  VAL C 294  1  N  LEU C 293   O  VAL C 253           
SHEET    8   L 9 PHE C 335  SER C 340  1  N  PHE C 335   O  ALA C 292           
SHEET    9   L 9 SER C  12  LEU C  16  1  O  ILE C  13   N  VAL C 338           
SHEET    1   M 2 CYS C  70  THR C  71  0                                        
SHEET    2   M 2 GLY C  74  ASN C  75 -1  O  GLY C  74   N  THR C  71           
SHEET    1   N 2 HIS C 101  GLY C 104  0                                        
SHEET    2   N 2 LEU C 165  ASP C 167 -1  N  LEU C 166   O  CYS C 103           
SHEET    1   O 2 PHE C 348  VAL C 349  0                                        
SHEET    2   O 2 GLU C 352  ASP C 353 -1  O  GLU C 352   N  VAL C 349           
SHEET    1   P 2 ASN C 362  ASN C 363  0                                        
SHEET    2   P 2 VAL C 366  ILE C 367 -1  N  VAL C 366   O  ASN C 363           
SHEET    1   Q 4 PHE C 406  ASP C 411  0                                        
SHEET    2   Q 4 GLN C 416  ARG C 421 -1  N  ALA C 418   O  TRP C 410           
SHEET    3   Q 4 GLY C 425  ASN C 430 -1  O  GLY C 425   N  ARG C 421           
SHEET    4   Q 4 PHE C 487  HIS C 491 -1  O  ILE C 488   N  VAL C 428           
SHEET    1   R 2 LEU C 436  GLN C 441  0                                        
SHEET    2   R 2 THR C 474  ILE C 479 -1  O  ALA C 475   N  LEU C 440           
SHEET    1   S 2 GLY C 447  CYS C 450  0                                        
SHEET    2   S 2 LYS C 466  VAL C 469 -1  O  VAL C 467   N  TYR C 449           
SHEET    1   T 2 LYS C 457  VAL C 458  0                                        
SHEET    2   T 2 SER C 461  CYS C 462 -1  N  SER C 461   O  VAL C 458           
SHEET    1   U 4 GLN D   3  ALA D   6  0                                        
SHEET    2   U 4 LEU D  18  SER D  25 -1  N  ALA D  23   O  VAL D   5           
SHEET    3   U 4 ALA D  78  MET D  82 -1  N  ALA D  78   O  CYS D  22           
SHEET    4   U 4 PHE D  67  ARG D  71 -1  O  THR D  68   N  GLN D  81           
SHEET    1   V 7 THR D 107  VAL D 109  0                                        
SHEET    2   V 7 ALA D  88  ALA D  94 -1  O  ALA D  88   N  VAL D 109           
SHEET    3   V 7 TYR D 102  TRP D 103 -1  O  TYR D 102   N  ALA D  94           
SHEET    4   V 7 ALA D  88  ALA D  94 -1  N  ALA D  94   O  TYR D 102           
SHEET    5   V 7 MET D  34  GLN D  39 -1  N  GLY D  35   O  ALA D  93           
SHEET    6   V 7 CYS D  45  ILE D  51 -1  O  GLU D  46   N  ARG D  38           
SHEET    7   V 7 ALA D  57  TYR D  59 -1  O  ASN D  58   N  ARG D  50           
SHEET    1   W 2 GLY D  99  VAL D 100C 0                                        
SHEET    2   W 2 ARG D 100F GLY D 100J-1  O  ARG D 100F  N  VAL D 100C          
SHEET    1   X 9 SER E  12  LEU E  16  0                                        
SHEET    2   X 9 GLY E  39  VAL E  42  1  O  GLY E  39   N  VAL E  14           
SHEET    3   X 9 ARG E  92  ALA E  97  1  O  ARG E  92   N  VAL E  40           
SHEET    4   X 9 GLY E 193  ILE E 196  1  O  GLY E 193   N  VAL E  95           
SHEET    5   X 9 PHE E 229  GLN E 232  1  O  PHE E 229   N  PHE E 194           
SHEET    6   X 9 ARG E 252  THR E 254  1  O  ARG E 252   N  GLN E 232           
SHEET    7   X 9 ALA E 292  VAL E 294  1  N  LEU E 293   O  VAL E 253           
SHEET    8   X 9 PHE E 335  SER E 340  1  O  PHE E 335   N  VAL E 294           
SHEET    9   X 9 SER E  12  LEU E  16  1  O  ILE E  13   N  VAL E 338           
SHEET    1   Y 2 HIS E 101  GLY E 104  0                                        
SHEET    2   Y 2 LEU E 165  ASP E 167 -1  N  LEU E 166   O  CYS E 103           
SHEET    1   Z 2 PHE E 348  VAL E 349  0                                        
SHEET    2   Z 2 GLU E 352  ASP E 353 -1  O  GLU E 352   N  VAL E 349           
SHEET    1  AA 2 ASN E 362  ASN E 363  0                                        
SHEET    2  AA 2 VAL E 366  ILE E 367 -1  N  VAL E 366   O  ASN E 363           
SHEET    1  AB 4 PHE E 406  ASP E 411  0                                        
SHEET    2  AB 4 GLN E 416  ARG E 421 -1  O  ALA E 418   N  TRP E 410           
SHEET    3  AB 4 GLY E 425  ASN E 430 -1  O  GLY E 425   N  ARG E 421           
SHEET    4  AB 4 PHE E 487  HIS E 491 -1  O  ILE E 488   N  VAL E 428           
SHEET    1  AC 2 LEU E 436  GLN E 441  0                                        
SHEET    2  AC 2 THR E 474  ILE E 479 -1  O  ALA E 475   N  LEU E 440           
SHEET    1  AD 2 GLY E 447  CYS E 450  0                                        
SHEET    2  AD 2 LYS E 466  VAL E 469 -1  N  VAL E 467   O  TYR E 449           
SHEET    1  AE 2 LYS E 457  VAL E 458  0                                        
SHEET    2  AE 2 SER E 461  CYS E 462 -1  O  SER E 461   N  VAL E 458           
SHEET    1  AF 4 LEU F   4  SER F   7  0                                        
SHEET    2  AF 4 LEU F  18  ALA F  24 -1  O  SER F  21   N  SER F   7           
SHEET    3  AF 4 ALA F  78  MET F  82 -1  N  ALA F  78   O  CYS F  22           
SHEET    4  AF 4 PHE F  67  ARG F  71 -1  O  THR F  68   N  GLN F  81           
SHEET    1  AG 6 GLY F  10  SER F  11  0                                        
SHEET    2  AG 6 THR F 107  THR F 110  1  O  GLN F 108   N  GLY F  10           
SHEET    3  AG 6 ALA F  88  ALA F  94 -1  N  ALA F  88   O  VAL F 109           
SHEET    4  AG 6 MET F  34  GLN F  39 -1  N  GLY F  35   O  ALA F  93           
SHEET    5  AG 6 GLU F  46  ILE F  51 -1  O  GLU F  46   N  ARG F  38           
SHEET    6  AG 6 ALA F  57  TYR F  59 -1  N  ASN F  58   O  ARG F  50           
SHEET    1  AH 2 GLY F  99  VAL F 100C 0                                        
SHEET    2  AH 2 ARG F 100F GLY F 100J-1  N  ARG F 100F  O  VAL F 100C          
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  2.04  
SSBOND   5 CYS A  450    CYS A  462                          1555   1555  2.03  
SSBOND   6 CYS B   22    CYS B   92                          1555   1555  2.04  
SSBOND   7 CYS C   28    CYS C   86                          1555   1555  2.03  
SSBOND   8 CYS C   70    CYS C  115                          1555   1555  2.05  
SSBOND   9 CYS C  141    CYS C  160                          1555   1555  2.04  
SSBOND  10 CYS C  378    CYS C  384                          1555   1555  2.03  
SSBOND  11 CYS C  450    CYS C  462                          1555   1555  2.03  
SSBOND  12 CYS D   22    CYS D   92                          1555   1555  2.03  
SSBOND  13 CYS E   28    CYS E   86                          1555   1555  2.04  
SSBOND  14 CYS E   70    CYS E  115                          1555   1555  2.04  
SSBOND  15 CYS E  141    CYS E  160                          1555   1555  2.04  
SSBOND  16 CYS E  378    CYS E  384                          1555   1555  2.04  
SSBOND  17 CYS E  450    CYS E  462                          1555   1555  2.03  
SSBOND  18 CYS F   22    CYS F   92                          1555   1555  2.04  
LINK        CA    CA A4001                 O   ARG A 158     1555   1555  2.58  
LINK        CA    CA A4001                 OD2 ASP A 167     1555   1555  2.59  
LINK        CA    CA A4001                 O   HIS A 201     1555   1555  2.40  
LINK        CA    CA A4001                 O   HOH A4221     1555   1555  2.62  
LINK        CA    CA A4001                 OD1 ASN A 100     1555   1555  2.24  
LINK        CA    CA A4001                 OD1 ASP A 167     1555   1555  2.38  
LINK        CA    CA A4001                 O   HOH A4227     1555   1555  2.76  
LINK        CA    CA C4003                 O   ARG C 158     1555   1555  2.25  
LINK        CA    CA C4003                 OD1 ASP C 167     1555   1555  2.38  
LINK        CA    CA C4003                 OD2 ASP C 167     1555   1555  2.69  
LINK        CA    CA C4003                 O   HOH C4141     1555   1555  2.29  
LINK        CA    CA C4003                 OD1 ASN C 100     1555   1555  2.33  
LINK        CA    CA C4003                 O   HIS C 201     1555   1555  2.30  
LINK        CA    CA C4003                 O   HOH C4140     1555   1555  2.59  
LINK        CA    CA C4003                 O   HOH C4275     1555   1555  2.32  
LINK        CA    CA E4005                 OD1 ASN E 100     1555   1555  2.50  
LINK        CA    CA E4005                 O   ARG E 158     1555   1555  2.55  
LINK        CA    CA E4005                 OD1 ASP E 167     1555   1555  2.54  
LINK        CA    CA E4005                 OD2 ASP E 167     1555   1555  2.77  
LINK        CA    CA E4005                 O   HIS E 201     1555   1555  2.33  
LINK        CA    CA E4005                 O   HOH E4240     1555   1555  2.45  
LINK        CA    CA E4005                 O   HOH E4242     1555   1555  2.34  
CISPEP   1 ASN A   53    PRO A   54          0         0.08                     
CISPEP   2 VAL A  129    PRO A  130          0         0.52                     
CISPEP   3 ASN C   53    PRO C   54          0        -0.16                     
CISPEP   4 VAL C  129    PRO C  130          0        -0.36                     
CISPEP   5 ASN E   53    PRO E   54          0        -0.77                     
CISPEP   6 VAL E  129    PRO E  130          0         0.22                     
SITE     1 AC1  6 ASN A 100  ARG A 158  ASP A 167  HIS A 201                    
SITE     2 AC1  6 HOH A4221  HOH A4227                                          
SITE     1 AC2  3 ARG A 195  GLU A 233  ARG A 337                               
SITE     1 AC3  7 ASN C 100  ARG C 158  ASP C 167  HIS C 201                    
SITE     2 AC3  7 HOH C4140  HOH C4141  HOH C4275                               
SITE     1 AC4  4 ARG C 195  ASN C 298  ARG C 337  HOH C4293                    
SITE     1 AC5  6 ASN E 100  ARG E 158  ASP E 167  HIS E 201                    
SITE     2 AC5  6 HOH E4240  HOH E4242                                          
SITE     1 AC6  4 ARG E 195  GLU E 233  ARG E 337  HOH E4011                    
CRYST1   52.780  286.850   65.980  90.00  93.73  90.00 P 1 21 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018947  0.000000  0.001235        0.00000                         
SCALE2      0.000000  0.003486  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015188        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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