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Database: PDB
Entry: 1TX6
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Original site: 1TX6 
HEADER    HYDROLASE/PROTEIN BINDING               02-JUL-04   1TX6              
TITLE     TRYPSIN:BBI COMPLEX                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN;                                                   
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: BOWMAN-BIRK TYPE TRYPSIN INHIBITOR;                        
COMPND   6 CHAIN: I, J;                                                         
COMPND   7 SYNONYM: BOWMAN-BIRK INHIBITOR, BBI                                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HORDEUM VULGARE;                                
SOURCE   7 ORGANISM_TAXID: 4513                                                 
KEYWDS    ANTICARCINOGENIC ACTIVITY, DOUBLE-HEADED INHIBITOR, GENE              
KEYWDS   2 DUPLICATION, MONOCOTYLEDONOUS PLANT, INHIBITORY LOOP,                
KEYWDS   3 HYDROLASE/PROTEIN BINDING COMPLEX                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.K.SONG,E.Y.PARK,J.A.KIM,H.W.KIM,Y.S.KIM                             
REVDAT   2   24-FEB-09 1TX6    1       VERSN                                    
REVDAT   1   08-MAR-05 1TX6    0                                                
JRNL        AUTH   E.Y.PARK,J.A.KIM,H.W.KIM,Y.S.KIM,H.K.SONG                    
JRNL        TITL   CRYSTAL STRUCTURE OF THE BOWMAN-BIRK INHIBITOR               
JRNL        TITL 2 FROM BARLEY SEEDS IN TERNARY COMPLEX WITH PORCINE            
JRNL        TITL 3 TRYPSIN                                                      
JRNL        REF    J.MOL.BIOL.                   V. 343   173 2004              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   15381428                                                     
JRNL        DOI    10.1016/J.JMB.2004.08.027                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   H.K.SONG,Y.S.KIM,J.K.YANG,J.MOON,J.Y.LEE,S.W.SUH             
REMARK   1  TITL   CRYSTAL STRUCTURE OF A 16 KDA DOUBLE-HEADED                  
REMARK   1  TITL 2 BOWMAN-BIRK TRYPSIN INHIBITOR FROM BARLEY SEEDS AT           
REMARK   1  TITL 3 1.9 A RESOLUTION                                             
REMARK   1  REF    J.MOL.BIOL.                   V. 293  1133 1999              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   10547291                                                     
REMARK   1  DOI    10.1006/JMBI.1999.3239                                       
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Y.S.KIM,H.K.SONG,S.W.SUH                                     
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF            
REMARK   1  TITL 2 A COMPLEX BETWEEN THE BOWMAN-BIRK TRYPSIN                    
REMARK   1  TITL 3 INHIBITOR FROM BARLEY AND PORCINE PANCREATIC                 
REMARK   1  TITL 4 TRYPSIN                                                      
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  55  1244 1999              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  PMID   10329799                                                     
REMARK   1  DOI    10.1107/S0907444999005065                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 57380                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.274                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2912                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8273                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 492                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
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 : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1TX6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUL-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB022993.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.59                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : WEISSENBERG                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60321                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
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     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM CITRATE, DTT, PH        
REMARK 280  5.59, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       33.60400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      101.94500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.26950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      101.94500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.60400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.26950            
REMARK 290   SMTRY3   4  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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I                               
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, J                               
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     ALA I     1                                                      
REMARK 465     GLY I     2                                                      
REMARK 465     LYS I     3                                                      
REMARK 465     LYS I     4                                                      
REMARK 465     PRO I    33                                                      
REMARK 465     LYS I    34                                                      
REMARK 465     THR I    35                                                      
REMARK 465     PRO I   100                                                      
REMARK 465     SER I   101                                                      
REMARK 465     ARG I   102                                                      
REMARK 465     SER I   103                                                      
REMARK 465     ARG I   104                                                      
REMARK 465     PRO I   105                                                      
REMARK 465     SER I   106                                                      
REMARK 465     ARG I   107                                                      
REMARK 465     ALA J     1                                                      
REMARK 465     GLY J     2                                                      
REMARK 465     LYS J     3                                                      
REMARK 465     LYS J     4                                                      
REMARK 465     PRO J    33                                                      
REMARK 465     LYS J    34                                                      
REMARK 465     ARG J   102                                                      
REMARK 465     SER J   103                                                      
REMARK 465     ARG J   104                                                      
REMARK 465     PRO J   105                                                      
REMARK 465     SER J   106                                                      
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     ARG I 125    CG   CD   NE   CZ   NH1  NH2                        
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     CYS D   22   SG                                                  
REMARK 480     CYS D   42   SG                                                  
REMARK 480     CYS D   58   SG                                                  
REMARK 480     MET D  104   SD                                                  
REMARK 480     CYS D  128   SG                                                  
REMARK 480     CYS D  136   SG                                                  
REMARK 480     CYS D  157   SG                                                  
REMARK 480     CYS D  168   SG                                                  
REMARK 480     MET D  180   SD                                                  
REMARK 480     CYS D  182   SG                                                  
REMARK 480     CYS D  191   SG                                                  
REMARK 480     CYS D  201   SG                                                  
REMARK 480     CYS D  220   SG                                                  
REMARK 480     CYS D  232   SG                                                  
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 C  22   CA  -  CB  -  SG  ANGL. DEV. =   6.7 DEGREES          
REMARK 500    CYS I  74   CA  -  CB  -  SG  ANGL. DEV. =   7.2 DEGREES          
REMARK 500    CYS J  82   CA  -  CB  -  SG  ANGL. DEV. =   6.6 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    HIS A  71      -64.10   -134.91                                   
REMARK 500    ASN A 101       39.46     70.65                                   
REMARK 500    SER A 150       88.78   -155.84                                   
REMARK 500    SER A 214      -75.31   -125.76                                   
REMARK 500    ALA B  24      118.52    -36.66                                   
REMARK 500    HIS B  71      -55.62   -138.82                                   
REMARK 500    ASN B 115     -164.57   -161.83                                   
REMARK 500    ASN B 143      153.68    -44.94                                   
REMARK 500    SER B 147      -59.08   -135.83                                   
REMARK 500    ASP B 189      171.40    174.41                                   
REMARK 500    SER B 195      136.53    -39.76                                   
REMARK 500    SER B 214      -66.49   -126.48                                   
REMARK 500    SER C  37       35.98   -144.25                                   
REMARK 500    SER C  54     -159.02   -144.25                                   
REMARK 500    HIS C  71      -63.54   -142.95                                   
REMARK 500    ASN C  79       36.96    -95.16                                   
REMARK 500    LEU C  99       19.83     59.18                                   
REMARK 500    SER C 150       87.64   -172.43                                   
REMARK 500    SER C 214      -71.49   -123.17                                   
REMARK 500    ALA D  24      129.05    -39.17                                   
REMARK 500    ILE D  27       66.01   -115.58                                   
REMARK 500    HIS D  71      -66.48   -138.65                                   
REMARK 500    SER D 214      -66.17   -130.08                                   
REMARK 500    CYS D 232        5.02    -67.40                                   
REMARK 500    PRO I   6        6.79    -67.43                                   
REMARK 500    PRO I  93       -7.44    -59.75                                   
REMARK 500    PRO J   6       10.25    -68.47                                   
REMARK 500    PHE J  30      -72.32   -112.24                                   
REMARK 500    PRO J  93        8.10    -66.34                                   
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 J 135        DISTANCE =  9.12 ANGSTROMS                       
REMARK 525    HOH I 140        DISTANCE =  8.40 ANGSTROMS                       
REMARK 525    HOH D4318        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH I 151        DISTANCE =  6.63 ANGSTROMS                       
REMARK 525    HOH D4351        DISTANCE =  5.79 ANGSTROMS                       
REMARK 525    HOH C3357        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH A1360        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH D4363        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH D4364        DISTANCE =  5.77 ANGSTROMS                       
REMARK 525    HOH B2366        DISTANCE =  6.79 ANGSTROMS                       
REMARK 525    HOH B2378        DISTANCE =  8.05 ANGSTROMS                       
REMARK 525    HOH D4380        DISTANCE =  6.85 ANGSTROMS                       
REMARK 525    HOH B2390        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH D4407        DISTANCE =  7.53 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 A1300  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  70   OE1                                                    
REMARK 620 2 ASN A  72   O    77.9                                              
REMARK 620 3 HOH A1385   O    95.1  91.0                                        
REMARK 620 4 GLU A  80   OE2 126.8 154.7  92.0                                  
REMARK 620 5 HOH A1392   O    75.6  91.7 169.6  89.8                            
REMARK 620 6 VAL A  75   O   144.4  72.2 104.1  82.7  86.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2300  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  80   OE2                                                    
REMARK 620 2 HOH B2408   O   112.4                                              
REMARK 620 3 GLU B  70   OE2 121.3  72.2                                        
REMARK 620 4 ASN B  72   O   171.9  71.6  66.3                                  
REMARK 620 5 VAL B  75   O   103.2  84.5 134.8  69.7                            
REMARK 620 6 GLU B  77   OE1  99.4 147.7  96.7  76.2  82.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C3300  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C3355   O                                                      
REMARK 620 2 VAL C  75   O    78.9                                              
REMARK 620 3 GLU C  80   OE1  52.5  81.8                                        
REMARK 620 4 HOH C3367   O   171.9  94.5 122.3                                  
REMARK 620 5 ASN C  72   O    88.1  66.1 133.9  93.6                            
REMARK 620 6 GLU C  70   OE1  74.0 141.3 102.1 114.1  85.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D4300  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D  70   OE1                                                    
REMARK 620 2 ASN D  72   O    88.4                                              
REMARK 620 3 VAL D  75   O   155.1  70.7                                        
REMARK 620 4 GLU D  77   OE2  99.1  75.6  89.0                                  
REMARK 620 5 GLU D  80   OE1 113.7 157.8  88.1  98.0                            
REMARK 620 6 HOH A1360   O    80.3  96.0  88.3 171.6  89.9                      
REMARK 620 N                    1     2     3     4     5                       
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 1300                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2300                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 3300                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 4300                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1C2A   RELATED DB: PDB                                   
REMARK 900 FREE STRUCTURE OF INHIBITOR                                          
DBREF  1TX6 I    1   125  UNP    P12940   IBB_HORVU        1    125             
DBREF  1TX6 J    1   125  UNP    P12940   IBB_HORVU        1    125             
DBREF  1TX6 A   16   245  UNP    P00761   TRYP_PIG         9    231             
DBREF  1TX6 B   16   245  UNP    P00761   TRYP_PIG         9    231             
DBREF  1TX6 C   16   245  UNP    P00761   TRYP_PIG         9    231             
DBREF  1TX6 D   16   245  UNP    P00761   TRYP_PIG         9    231             
SEQADV 1TX6 SER I   42  UNP  P12940              SEE REMARK 999                 
SEQADV 1TX6 SER J   42  UNP  P12940              SEE REMARK 999                 
SEQRES   1 A  223  ILE VAL GLY GLY TYR THR CYS ALA ALA ASN SER ILE PRO          
SEQRES   2 A  223  TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY          
SEQRES   3 A  223  GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 A  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 A  223  HIS ASN ILE ASP VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 A  223  ASN ALA ALA LYS ILE ILE THR HIS PRO ASN PHE ASN GLY          
SEQRES   7 A  223  ASN THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 A  223  SER PRO ALA THR LEU ASN SER ARG VAL ALA THR VAL SER          
SEQRES   9 A  223  LEU PRO ARG SER CYS ALA ALA ALA GLY THR GLU CYS LEU          
SEQRES  10 A  223  ILE SER GLY TRP GLY ASN THR LYS SER SER GLY SER SER          
SEQRES  11 A  223  TYR PRO SER LEU LEU GLN CYS LEU LYS ALA PRO VAL LEU          
SEQRES  12 A  223  SER ASP SER SER CYS LYS SER SER TYR PRO GLY GLN ILE          
SEQRES  13 A  223  THR GLY ASN MET ILE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 A  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 A  223  CYS ASN GLY GLN LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 A  223  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 A  223  VAL CYS ASN TYR VAL ASN TRP ILE GLN GLN THR ILE ALA          
SEQRES  18 A  223  ALA ASN                                                      
SEQRES   1 B  223  ILE VAL GLY GLY TYR THR CYS ALA ALA ASN SER ILE PRO          
SEQRES   2 B  223  TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY          
SEQRES   3 B  223  GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 B  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 B  223  HIS ASN ILE ASP VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 B  223  ASN ALA ALA LYS ILE ILE THR HIS PRO ASN PHE ASN GLY          
SEQRES   7 B  223  ASN THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 B  223  SER PRO ALA THR LEU ASN SER ARG VAL ALA THR VAL SER          
SEQRES   9 B  223  LEU PRO ARG SER CYS ALA ALA ALA GLY THR GLU CYS LEU          
SEQRES  10 B  223  ILE SER GLY TRP GLY ASN THR LYS SER SER GLY SER SER          
SEQRES  11 B  223  TYR PRO SER LEU LEU GLN CYS LEU LYS ALA PRO VAL LEU          
SEQRES  12 B  223  SER ASP SER SER CYS LYS SER SER TYR PRO GLY GLN ILE          
SEQRES  13 B  223  THR GLY ASN MET ILE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 B  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 B  223  CYS ASN GLY GLN LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 B  223  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 B  223  VAL CYS ASN TYR VAL ASN TRP ILE GLN GLN THR ILE ALA          
SEQRES  18 B  223  ALA ASN                                                      
SEQRES   1 C  223  ILE VAL GLY GLY TYR THR CYS ALA ALA ASN SER ILE PRO          
SEQRES   2 C  223  TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY          
SEQRES   3 C  223  GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 C  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 C  223  HIS ASN ILE ASP VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 C  223  ASN ALA ALA LYS ILE ILE THR HIS PRO ASN PHE ASN GLY          
SEQRES   7 C  223  ASN THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 C  223  SER PRO ALA THR LEU ASN SER ARG VAL ALA THR VAL SER          
SEQRES   9 C  223  LEU PRO ARG SER CYS ALA ALA ALA GLY THR GLU CYS LEU          
SEQRES  10 C  223  ILE SER GLY TRP GLY ASN THR LYS SER SER GLY SER SER          
SEQRES  11 C  223  TYR PRO SER LEU LEU GLN CYS LEU LYS ALA PRO VAL LEU          
SEQRES  12 C  223  SER ASP SER SER CYS LYS SER SER TYR PRO GLY GLN ILE          
SEQRES  13 C  223  THR GLY ASN MET ILE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 C  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 C  223  CYS ASN GLY GLN LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 C  223  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 C  223  VAL CYS ASN TYR VAL ASN TRP ILE GLN GLN THR ILE ALA          
SEQRES  18 C  223  ALA ASN                                                      
SEQRES   1 D  223  ILE VAL GLY GLY TYR THR CYS ALA ALA ASN SER ILE PRO          
SEQRES   2 D  223  TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY          
SEQRES   3 D  223  GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 D  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 D  223  HIS ASN ILE ASP VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 D  223  ASN ALA ALA LYS ILE ILE THR HIS PRO ASN PHE ASN GLY          
SEQRES   7 D  223  ASN THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 D  223  SER PRO ALA THR LEU ASN SER ARG VAL ALA THR VAL SER          
SEQRES   9 D  223  LEU PRO ARG SER CYS ALA ALA ALA GLY THR GLU CYS LEU          
SEQRES  10 D  223  ILE SER GLY TRP GLY ASN THR LYS SER SER GLY SER SER          
SEQRES  11 D  223  TYR PRO SER LEU LEU GLN CYS LEU LYS ALA PRO VAL LEU          
SEQRES  12 D  223  SER ASP SER SER CYS LYS SER SER TYR PRO GLY GLN ILE          
SEQRES  13 D  223  THR GLY ASN MET ILE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 D  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 D  223  CYS ASN GLY GLN LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 D  223  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 D  223  VAL CYS ASN TYR VAL ASN TRP ILE GLN GLN THR ILE ALA          
SEQRES  18 D  223  ALA ASN                                                      
SEQRES   1 I  125  ALA GLY LYS LYS ARG PRO TRP LYS CYS CYS ASP GLU ALA          
SEQRES   2 I  125  VAL CYS THR ARG SER ILE PRO PRO ILE CYS THR CYS MET          
SEQRES   3 I  125  ASP GLU VAL PHE GLU CYS PRO LYS THR CYS LYS SER CYS          
SEQRES   4 I  125  GLY PRO SER MET GLY ASP PRO SER ARG ARG ILE CYS GLN          
SEQRES   5 I  125  ASP GLN TYR VAL GLY ASP PRO GLY PRO ILE CYS ARG PRO          
SEQRES   6 I  125  TRP GLU CYS CYS ASP LYS ALA ILE CYS THR ARG SER ASN          
SEQRES   7 I  125  PRO PRO THR CYS ARG CYS VAL ASP GLU VAL LYS LYS CYS          
SEQRES   8 I  125  ALA PRO THR CYS LYS THR CYS LEU PRO SER ARG SER ARG          
SEQRES   9 I  125  PRO SER ARG ARG VAL CYS ILE ASP SER TYR PHE GLY PRO          
SEQRES  10 I  125  VAL PRO PRO ARG CYS THR PRO ARG                              
SEQRES   1 J  125  ALA GLY LYS LYS ARG PRO TRP LYS CYS CYS ASP GLU ALA          
SEQRES   2 J  125  VAL CYS THR ARG SER ILE PRO PRO ILE CYS THR CYS MET          
SEQRES   3 J  125  ASP GLU VAL PHE GLU CYS PRO LYS THR CYS LYS SER CYS          
SEQRES   4 J  125  GLY PRO SER MET GLY ASP PRO SER ARG ARG ILE CYS GLN          
SEQRES   5 J  125  ASP GLN TYR VAL GLY ASP PRO GLY PRO ILE CYS ARG PRO          
SEQRES   6 J  125  TRP GLU CYS CYS ASP LYS ALA ILE CYS THR ARG SER ASN          
SEQRES   7 J  125  PRO PRO THR CYS ARG CYS VAL ASP GLU VAL LYS LYS CYS          
SEQRES   8 J  125  ALA PRO THR CYS LYS THR CYS LEU PRO SER ARG SER ARG          
SEQRES   9 J  125  PRO SER ARG ARG VAL CYS ILE ASP SER TYR PHE GLY PRO          
SEQRES  10 J  125  VAL PRO PRO ARG CYS THR PRO ARG                              
HET     CA  A1300       1                                                       
HET     CA  B2300       1                                                       
HET     CA  C3300       1                                                       
HET     CA  D4300       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   7   CA    4(CA 2+)                                                     
FORMUL  11  HOH   *492(H2 O)                                                    
HELIX    1   1 ALA A   55  TYR A   59  5                                   5    
HELIX    2   2 SER A  164  TYR A  172  1                                   9    
HELIX    3   3 TYR A  234  ALA A  244  1                                  11    
HELIX    4   4 ALA B   55  TYR B   59  5                                   5    
HELIX    5   5 SER B  164  TYR B  172  1                                   9    
HELIX    6   6 TYR B  234  ALA B  244  1                                  11    
HELIX    7   7 ALA C   55  TYR C   59  5                                   5    
HELIX    8   8 SER C  164  TYR C  172  1                                   9    
HELIX    9   9 TYR C  234  ALA C  244  1                                  11    
HELIX   10  10 ALA D   55  TYR D   59  5                                   5    
HELIX   11  11 SER D  164  TYR D  172  1                                   9    
HELIX   12  12 TYR D  234  ASN D  245  1                                  12    
SHEET    1   A 7 TYR A  20  THR A  21  0                                        
SHEET    2   A 7 GLN A 156  PRO A 161 -1  O  CYS A 157   N  TYR A  20           
SHEET    3   A 7 GLU A 135  GLY A 140 -1  N  CYS A 136   O  ALA A 160           
SHEET    4   A 7 PRO A 198  CYS A 201 -1  O  VAL A 200   N  LEU A 137           
SHEET    5   A 7 GLN A 204  GLY A 216 -1  O  GLN A 204   N  CYS A 201           
SHEET    6   A 7 GLY A 226  LYS A 230 -1  O  VAL A 227   N  TRP A 215           
SHEET    7   A 7 MET A 180  VAL A 183 -1  N  ILE A 181   O  TYR A 228           
SHEET    1   B 8 TYR A  20  THR A  21  0                                        
SHEET    2   B 8 GLN A 156  PRO A 161 -1  O  CYS A 157   N  TYR A  20           
SHEET    3   B 8 GLU A 135  GLY A 140 -1  N  CYS A 136   O  ALA A 160           
SHEET    4   B 8 PRO A 198  CYS A 201 -1  O  VAL A 200   N  LEU A 137           
SHEET    5   B 8 GLN A 204  GLY A 216 -1  O  GLN A 204   N  CYS A 201           
SHEET    6   B 8 ALA I  13  THR I  16 -1  O  CYS I  15   N  GLY A 216           
SHEET    7   B 8 ILE I  22  CYS I  25 -1  O  THR I  24   N  VAL I  14           
SHEET    8   B 8 GLN I  54  VAL I  56 -1  O  TYR I  55   N  CYS I  23           
SHEET    1   C 7 GLN A  30  ASN A  34  0                                        
SHEET    2   C 7 HIS A  40  LEU A  46 -1  O  CYS A  42   N  LEU A  33           
SHEET    3   C 7 TRP A  51  SER A  54 -1  O  VAL A  53   N  SER A  45           
SHEET    4   C 7 MET A 104  LEU A 108 -1  O  ILE A 106   N  VAL A  52           
SHEET    5   C 7 GLN A  81  THR A  90 -1  N  ALA A  86   O  LYS A 107           
SHEET    6   C 7 GLN A  64  LEU A  67 -1  N  VAL A  65   O  ILE A  83           
SHEET    7   C 7 GLN A  30  ASN A  34 -1  N  ASN A  34   O  GLN A  64           
SHEET    1   D 7 TYR B  20  THR B  21  0                                        
SHEET    2   D 7 GLN B 156  PRO B 161 -1  O  CYS B 157   N  TYR B  20           
SHEET    3   D 7 GLU B 135  GLY B 140 -1  N  CYS B 136   O  ALA B 160           
SHEET    4   D 7 PRO B 198  CYS B 201 -1  O  VAL B 200   N  LEU B 137           
SHEET    5   D 7 GLN B 204  TYR B 217 -1  O  GLN B 210   N  VAL B 199           
SHEET    6   D 7 GLY B 226  LYS B 230 -1  O  VAL B 227   N  TRP B 215           
SHEET    7   D 7 MET B 180  VAL B 183 -1  N  ILE B 181   O  TYR B 228           
SHEET    1   E 8 TYR B  20  THR B  21  0                                        
SHEET    2   E 8 GLN B 156  PRO B 161 -1  O  CYS B 157   N  TYR B  20           
SHEET    3   E 8 GLU B 135  GLY B 140 -1  N  CYS B 136   O  ALA B 160           
SHEET    4   E 8 PRO B 198  CYS B 201 -1  O  VAL B 200   N  LEU B 137           
SHEET    5   E 8 GLN B 204  TYR B 217 -1  O  GLN B 210   N  VAL B 199           
SHEET    6   E 8 ALA I  72  THR I  75 -1  O  CYS I  74   N  GLY B 216           
SHEET    7   E 8 THR I  81  CYS I  84 -1  O  ARG I  83   N  ILE I  73           
SHEET    8   E 8 TYR I 114  PHE I 115 -1  O  TYR I 114   N  CYS I  82           
SHEET    1   F 7 GLN B  30  ASN B  34  0                                        
SHEET    2   F 7 HIS B  40  LEU B  46 -1  O  CYS B  42   N  LEU B  33           
SHEET    3   F 7 TRP B  51  SER B  54 -1  O  VAL B  53   N  SER B  45           
SHEET    4   F 7 MET B 104  LEU B 108 -1  O  ILE B 106   N  VAL B  52           
SHEET    5   F 7 GLN B  81  THR B  90 -1  N  ALA B  86   O  LYS B 107           
SHEET    6   F 7 GLN B  64  LEU B  67 -1  N  VAL B  65   O  ILE B  83           
SHEET    7   F 7 GLN B  30  ASN B  34 -1  N  ASN B  34   O  GLN B  64           
SHEET    1   G 7 TYR C  20  THR C  21  0                                        
SHEET    2   G 7 GLN C 156  PRO C 161 -1  O  CYS C 157   N  TYR C  20           
SHEET    3   G 7 GLU C 135  GLY C 140 -1  N  ILE C 138   O  LEU C 158           
SHEET    4   G 7 PRO C 198  CYS C 201 -1  O  VAL C 200   N  LEU C 137           
SHEET    5   G 7 GLN C 204  GLY C 216 -1  O  GLN C 204   N  CYS C 201           
SHEET    6   G 7 GLY C 226  LYS C 230 -1  O  VAL C 227   N  TRP C 215           
SHEET    7   G 7 MET C 180  VAL C 183 -1  N  ILE C 181   O  TYR C 228           
SHEET    1   H 8 TYR C  20  THR C  21  0                                        
SHEET    2   H 8 GLN C 156  PRO C 161 -1  O  CYS C 157   N  TYR C  20           
SHEET    3   H 8 GLU C 135  GLY C 140 -1  N  ILE C 138   O  LEU C 158           
SHEET    4   H 8 PRO C 198  CYS C 201 -1  O  VAL C 200   N  LEU C 137           
SHEET    5   H 8 GLN C 204  GLY C 216 -1  O  GLN C 204   N  CYS C 201           
SHEET    6   H 8 ALA J  13  THR J  16 -1  O  CYS J  15   N  GLY C 216           
SHEET    7   H 8 ILE J  22  CYS J  25 -1  O  THR J  24   N  VAL J  14           
SHEET    8   H 8 GLN J  54  VAL J  56 -1  O  TYR J  55   N  CYS J  23           
SHEET    1   I 7 GLN C  30  ASN C  34  0                                        
SHEET    2   I 7 HIS C  40  ASN C  48 -1  O  CYS C  42   N  LEU C  33           
SHEET    3   I 7 TRP C  51  SER C  54 -1  O  VAL C  53   N  SER C  45           
SHEET    4   I 7 MET C 104  LEU C 108 -1  O  ILE C 106   N  VAL C  52           
SHEET    5   I 7 GLN C  81  THR C  90 -1  N  ALA C  86   O  LYS C 107           
SHEET    6   I 7 GLN C  64  LEU C  67 -1  N  VAL C  65   O  ILE C  83           
SHEET    7   I 7 GLN C  30  ASN C  34 -1  N  ASN C  34   O  GLN C  64           
SHEET    1   J 7 TYR D  20  THR D  21  0                                        
SHEET    2   J 7 GLN D 156  PRO D 161 -1  O  CYS D 157   N  TYR D  20           
SHEET    3   J 7 GLU D 135  GLY D 140 -1  N  ILE D 138   O  LEU D 158           
SHEET    4   J 7 PRO D 198  CYS D 201 -1  O  VAL D 200   N  LEU D 137           
SHEET    5   J 7 GLN D 204  TYR D 217 -1  O  GLN D 204   N  CYS D 201           
SHEET    6   J 7 GLY D 226  LYS D 230 -1  O  THR D 229   N  ILE D 212           
SHEET    7   J 7 MET D 180  VAL D 183 -1  N  ILE D 181   O  TYR D 228           
SHEET    1   K 8 TYR D  20  THR D  21  0                                        
SHEET    2   K 8 GLN D 156  PRO D 161 -1  O  CYS D 157   N  TYR D  20           
SHEET    3   K 8 GLU D 135  GLY D 140 -1  N  ILE D 138   O  LEU D 158           
SHEET    4   K 8 PRO D 198  CYS D 201 -1  O  VAL D 200   N  LEU D 137           
SHEET    5   K 8 GLN D 204  TYR D 217 -1  O  GLN D 204   N  CYS D 201           
SHEET    6   K 8 ALA J  72  THR J  75 -1  O  CYS J  74   N  GLY D 216           
SHEET    7   K 8 THR J  81  CYS J  84 -1  O  ARG J  83   N  ILE J  73           
SHEET    8   K 8 TYR J 114  PHE J 115 -1  O  TYR J 114   N  CYS J  82           
SHEET    1   L 7 GLN D  30  ASN D  34  0                                        
SHEET    2   L 7 HIS D  40  ASN D  48 -1  O  CYS D  42   N  LEU D  33           
SHEET    3   L 7 TRP D  51  SER D  54 -1  O  VAL D  53   N  SER D  45           
SHEET    4   L 7 MET D 104  LEU D 108 -1  O  ILE D 106   N  VAL D  52           
SHEET    5   L 7 GLN D  81  THR D  90 -1  N  ALA D  86   O  LYS D 107           
SHEET    6   L 7 GLN D  64  LEU D  67 -1  N  VAL D  65   O  ILE D  83           
SHEET    7   L 7 GLN D  30  ASN D  34 -1  N  ASN D  34   O  GLN D  64           
SHEET    1   M 2 CYS I  39  PRO I  41  0                                        
SHEET    2   M 2 ARG I  49  CYS I  51 -1  O  ILE I  50   N  GLY I  40           
SHEET    1   N 2 CYS J  39  GLY J  40  0                                        
SHEET    2   N 2 ILE J  50  CYS J  51 -1  O  ILE J  50   N  GLY J  40           
SHEET    1   O 2 CYS J  98  LEU J  99  0                                        
SHEET    2   O 2 VAL J 109  CYS J 110 -1  O  VAL J 109   N  LEU J  99           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.04  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.04  
SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.03  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  2.03  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.02  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.03  
SSBOND   7 CYS B   22    CYS B  157                          1555   1555  2.04  
SSBOND   8 CYS B   42    CYS B   58                          1555   1555  2.04  
SSBOND   9 CYS B  128    CYS B  232                          1555   1555  2.03  
SSBOND  10 CYS B  136    CYS B  201                          1555   1555  2.03  
SSBOND  11 CYS B  168    CYS B  182                          1555   1555  2.03  
SSBOND  12 CYS B  191    CYS B  220                          1555   1555  2.03  
SSBOND  13 CYS C   22    CYS C  157                          1555   1555  2.04  
SSBOND  14 CYS C   42    CYS C   58                          1555   1555  2.03  
SSBOND  15 CYS C  128    CYS C  232                          1555   1555  2.03  
SSBOND  16 CYS C  136    CYS C  201                          1555   1555  2.03  
SSBOND  17 CYS C  168    CYS C  182                          1555   1555  2.03  
SSBOND  18 CYS C  191    CYS C  220                          1555   1555  2.03  
SSBOND  19 CYS D   22    CYS D  157                          1555   1555  2.03  
SSBOND  20 CYS D   42    CYS D   58                          1555   1555  2.03  
SSBOND  21 CYS D  128    CYS D  232                          1555   1555  2.03  
SSBOND  22 CYS D  136    CYS D  201                          1555   1555  2.03  
SSBOND  23 CYS D  168    CYS D  182                          1555   1555  2.03  
SSBOND  24 CYS D  191    CYS D  220                          1555   1555  2.03  
SSBOND  25 CYS I    9    CYS I   63                          1555   1555  2.04  
SSBOND  26 CYS I   10    CYS I   25                          1555   1555  2.03  
SSBOND  27 CYS I   15    CYS I   23                          1555   1555  2.03  
SSBOND  28 CYS I   32    CYS I   39                          1555   1555  2.03  
SSBOND  29 CYS I   36    CYS I   51                          1555   1555  2.03  
SSBOND  30 CYS I   68    CYS I  122                          1555   1555  2.03  
SSBOND  31 CYS I   69    CYS I   84                          1555   1555  2.03  
SSBOND  32 CYS I   74    CYS I   82                          1555   1555  2.03  
SSBOND  33 CYS I   91    CYS I   98                          1555   1555  2.03  
SSBOND  34 CYS I   95    CYS I  110                          1555   1555  2.03  
SSBOND  35 CYS J    9    CYS J   63                          1555   1555  2.04  
SSBOND  36 CYS J   10    CYS J   25                          1555   1555  2.03  
SSBOND  37 CYS J   15    CYS J   23                          1555   1555  2.03  
SSBOND  38 CYS J   32    CYS J   39                          1555   1555  2.03  
SSBOND  39 CYS J   36    CYS J   51                          1555   1555  2.04  
SSBOND  40 CYS J   68    CYS J  122                          1555   1555  2.03  
SSBOND  41 CYS J   69    CYS J   84                          1555   1555  2.04  
SSBOND  42 CYS J   74    CYS J   82                          1555   1555  2.02  
SSBOND  43 CYS J   91    CYS J   98                          1555   1555  2.03  
SSBOND  44 CYS J   95    CYS J  110                          1555   1555  2.04  
LINK        CA    CA A1300                 OE1 GLU A  70     1555   1555  2.81  
LINK        CA    CA A1300                 O   ASN A  72     1555   1555  2.73  
LINK        CA    CA A1300                 O   HOH A1385     1555   1555  2.80  
LINK        CA    CA A1300                 OE2 GLU A  80     1555   1555  2.66  
LINK        CA    CA A1300                 O   HOH A1392     1555   1555  2.85  
LINK        CA    CA A1300                 O   VAL A  75     1555   1555  2.76  
LINK        CA    CA B2300                 OE2 GLU B  80     1555   1555  2.75  
LINK        CA    CA B2300                 O   HOH B2408     1555   1555  2.93  
LINK        CA    CA B2300                 OE2 GLU B  70     1555   1555  2.88  
LINK        CA    CA B2300                 O   ASN B  72     1555   1555  2.85  
LINK        CA    CA B2300                 O   VAL B  75     1555   1555  2.78  
LINK        CA    CA B2300                 OE1 GLU B  77     1555   1555  3.19  
LINK        CA    CA C3300                 O   HOH C3355     1555   1555  3.25  
LINK        CA    CA C3300                 O   VAL C  75     1555   1555  2.84  
LINK        CA    CA C3300                 OE1 GLU C  80     1555   1555  3.16  
LINK        CA    CA C3300                 O   HOH C3367     1555   1555  2.80  
LINK        CA    CA C3300                 O   ASN C  72     1555   1555  2.74  
LINK        CA    CA C3300                 OE1 GLU C  70     1555   1555  2.72  
LINK        CA    CA D4300                 OE1 GLU D  70     1555   1555  2.57  
LINK        CA    CA D4300                 O   ASN D  72     1555   1555  2.66  
LINK        CA    CA D4300                 O   VAL D  75     1555   1555  2.61  
LINK        CA    CA D4300                 OE2 GLU D  77     1555   1555  3.10  
LINK        CA    CA D4300                 OE1 GLU D  80     1555   1555  2.68  
LINK        CA    CA D4300                 O   HOH A1360     1555   1455  2.82  
CISPEP   1 ILE I   19    PRO I   20          0         0.11                     
CISPEP   2 ASN I   78    PRO I   79          0        -0.11                     
CISPEP   3 ILE J   19    PRO J   20          0         0.01                     
CISPEP   4 ASN J   78    PRO J   79          0        -0.16                     
SITE     1 AC1  6 GLU A  70  ASN A  72  VAL A  75  GLU A  80                    
SITE     2 AC1  6 HOH A1385  HOH A1392                                          
SITE     1 AC2  6 GLU B  70  ASN B  72  VAL B  75  GLU B  77                    
SITE     2 AC2  6 GLU B  80  HOH B2408                                          
SITE     1 AC3  5 GLU C  70  ASN C  72  VAL C  75  GLU C  80                    
SITE     2 AC3  5 HOH C3367                                                     
SITE     1 AC4  6 HOH A1360  GLU D  70  ASN D  72  VAL D  75                    
SITE     2 AC4  6 GLU D  77  GLU D  80                                          
CRYST1   67.208   88.539  203.890  90.00  90.00  90.00 P 21 21 21   16          
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      0.014879  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011294  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004905        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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