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Database: PDB
Entry: 2VJ2
LinkDB: 2VJ2
Original site: 2VJ2 
HEADER    PROTEIN-BINDING                         06-DEC-07   2VJ2              
TITLE     HUMAN JAGGED-1, DOMAINS DSL AND EGFS1-3                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: JAGGED-1;                                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: DSL DOMAIN AND EGFS1-3, RESIDUES 185-335;                  
COMPND   5 SYNONYM: JAGGED1, HJ1, CD339 ANTIGEN, JAGGED-1;                      
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: NM554;                                     
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PQE30                                     
KEYWDS    SIGNALLING, POLYMORPHISM, GLYCOPROTEIN, EXTRACELLULAR,                
KEYWDS   2 DEVELOPMENTAL PROTEIN, NOTCH SIGNALING PATHWAY, EGF, DSL,            
KEYWDS   3 NOTCH, JAGGED, CALCIUM, MEMBRANE, PROTEIN-BINDING,                   
KEYWDS   4 TRANSMEMBRANE, EGF-LIKE DOMAIN, DISEASE MUTATION                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.JOHNSON,J.CORDLE,J.Z.TAY,P.ROVERSI,P.A.HANDFORD,S.M.LEA             
REVDAT   3   25-AUG-10 2VJ2    1       JRNL   REMARK FORMUL                     
REVDAT   2   24-FEB-09 2VJ2    1       VERSN                                    
REVDAT   1   29-JUL-08 2VJ2    0                                                
JRNL        AUTH   J.CORDLE,S.JOHNSON,J.Z.TAY,P.ROVERSI,M.B.WILKIN,             
JRNL        AUTH 2 B.H.DE MADRID,H.SHIMIZU,S.JENSEN,P.WHITEMAN,B.JIN,           
JRNL        AUTH 3 C.REDFIELD,M.BARON,S.M.LEA,P.A.HANDFORD                      
JRNL        TITL   A CONSERVED FACE OF THE JAGGED/SERRATE DSL DOMAIN            
JRNL        TITL 2 IS INVOLVED IN NOTCH TRANS-ACTIVATION AND CIS-               
JRNL        TITL 3 INHIBITION.                                                  
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  15   849 2008              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   18660822                                                     
JRNL        DOI    10.1038/NSMB.1457                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT 5.6.1                                            
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0                              
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 11961                          
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.221                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 584                             
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.221                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.220                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.239                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5                      
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 584                    
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2299                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 9                                       
REMARK   3   SOLVENT ATOMS            : 208                                     
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : 43.800                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.007 ; 2.0   ; 2403            
REMARK   3   BOND ANGLES            (DEGREES) : 0.716 ; 2.0   ; 3244            
REMARK   3   TORSION ANGLES         (DEGREES) : 16.7  ; 0     ; 451             
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : 0.001 ; 2.0   ; 72              
REMARK   3   GENERAL PLANES               (A) : 0.03  ; 5.0   ; 356             
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : 1.289 ; 20.0  ; 2403            
REMARK   3   NON-BONDED CONTACTS          (A) : 0.116 ; 5     ; 5               
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : 0                                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : BABINET SCALING                                      
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 131                                                  
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : TNT PROTGEO                                      
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : TNT BCORREL                  
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BUSTER-TNT-GELLY 2.1.1 E. BLANC, P.       
REMARK   3  ROVERSI, C. VONRHEIN, C. FLENSBURG, S. M. LEA AND G.BRICOGNE        
REMARK   4                                                                      
REMARK   4 2VJ2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-DEC-07.                  
REMARK 100 THE PDBE ID CODE IS EBI-34691.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-APR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11962                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.50                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 57.10                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 3.7                                
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.10                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.42                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: AUTOSHARP, SHARP-SOLOMON, DM, BUSTER-TNT              
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.5                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8.5% (W/V) PEG4000, 100MM IMIDAZOLE      
REMARK 280  -MALATE, PH7.0                                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       30.50000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.15000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       30.50000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       51.15000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375      HOH A2028  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B2067  LIES ON A SPECIAL POSITION.                          
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     MET A   167                                                      
REMARK 465     ARG A   168                                                      
REMARK 465     GLY A   169                                                      
REMARK 465     SER A   170                                                      
REMARK 465     HIS A   171                                                      
REMARK 465     HIS A   172                                                      
REMARK 465     HIS A   173                                                      
REMARK 465     HIS A   174                                                      
REMARK 465     HIS A   175                                                      
REMARK 465     HIS A   176                                                      
REMARK 465     GLY A   177                                                      
REMARK 465     SER A   178                                                      
REMARK 465     ILE A   179                                                      
REMARK 465     GLU A   180                                                      
REMARK 465     GLY A   181                                                      
REMARK 465     ARG A   182                                                      
REMARK 465     SER A   183                                                      
REMARK 465     ALA A   184                                                      
REMARK 465     VAL A   185                                                      
REMARK 465     THR A   186                                                      
REMARK 465     MET B   167                                                      
REMARK 465     ARG B   168                                                      
REMARK 465     GLY B   169                                                      
REMARK 465     SER B   170                                                      
REMARK 465     HIS B   171                                                      
REMARK 465     HIS B   172                                                      
REMARK 465     HIS B   173                                                      
REMARK 465     HIS B   174                                                      
REMARK 465     HIS B   175                                                      
REMARK 465     HIS B   176                                                      
REMARK 465     GLY B   177                                                      
REMARK 465     SER B   178                                                      
REMARK 465     ILE B   179                                                      
REMARK 465     GLU B   180                                                      
REMARK 465     GLY B   181                                                      
REMARK 465     ARG B   182                                                      
REMARK 465     SER B   183                                                      
REMARK 465     ALA B   184                                                      
REMARK 465     VAL B   185                                                      
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 B  2022     O    HOH B  2028              2.09            
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    HIS B 273   CB  -  CG  -  ND1 ANGL. DEV. =   9.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A 190       -6.27     76.89                                   
REMARK 500    LYS A 246      -31.60   -131.66                                   
REMARK 500    VAL A 272      -78.68    -88.69                                   
REMARK 500    HIS A 273       59.24    -99.92                                   
REMARK 500    GLN A 304       72.54     51.06                                   
REMARK 500    GLN B 236      106.78    -58.55                                   
REMARK 500    VAL B 272      -81.25    -86.38                                   
REMARK 500    HIS B 273       58.47   -101.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLT B1336                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2CAO   RELATED DB: PDB                                   
REMARK 900  HUMAN JAGGED1 DOMAINS DSL AND EGFS1-3                               
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 FIRST 18 RESIDUES ARE FROM THE N-TERMINAL HIS-TAG ENCODED            
REMARK 999 BY THE VECTOR                                                        
DBREF  2VJ2 A  167   184  PDB    2VJ2     2VJ2           167    184             
DBREF  2VJ2 A  185   335  UNP    P78504   JAG1_HUMAN     185    335             
DBREF  2VJ2 B  167   184  PDB    2VJ2     2VJ2           167    184             
DBREF  2VJ2 B  185   335  UNP    P78504   JAG1_HUMAN     185    335             
SEQRES   1 A  169  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE          
SEQRES   2 A  169  GLU GLY ARG SER ALA VAL THR CYS ASP ASP TYR TYR TYR          
SEQRES   3 A  169  GLY PHE GLY CYS ASN LYS PHE CYS ARG PRO ARG ASP ASP          
SEQRES   4 A  169  PHE PHE GLY HIS TYR ALA CYS ASP GLN ASN GLY ASN LYS          
SEQRES   5 A  169  THR CYS MET GLU GLY TRP MET GLY PRO GLU CYS ASN ARG          
SEQRES   6 A  169  ALA ILE CYS ARG GLN GLY CYS SER PRO LYS HIS GLY SER          
SEQRES   7 A  169  CYS LYS LEU PRO GLY ASP CYS ARG CYS GLN TYR GLY TRP          
SEQRES   8 A  169  GLN GLY LEU TYR CYS ASP LYS CYS ILE PRO HIS PRO GLY          
SEQRES   9 A  169  CYS VAL HIS GLY ILE CYS ASN GLU PRO TRP GLN CYS LEU          
SEQRES  10 A  169  CYS GLU THR ASN TRP GLY GLY GLN LEU CYS ASP LYS ASP          
SEQRES  11 A  169  LEU ASN TYR CYS GLY THR HIS GLN PRO CYS LEU ASN GLY          
SEQRES  12 A  169  GLY THR CYS SER ASN THR GLY PRO ASP LYS TYR GLN CYS          
SEQRES  13 A  169  SER CYS PRO GLU GLY TYR SER GLY PRO ASN CYS GLU ILE          
SEQRES   1 B  169  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE          
SEQRES   2 B  169  GLU GLY ARG SER ALA VAL THR CYS ASP ASP TYR TYR TYR          
SEQRES   3 B  169  GLY PHE GLY CYS ASN LYS PHE CYS ARG PRO ARG ASP ASP          
SEQRES   4 B  169  PHE PHE GLY HIS TYR ALA CYS ASP GLN ASN GLY ASN LYS          
SEQRES   5 B  169  THR CYS MET GLU GLY TRP MET GLY PRO GLU CYS ASN ARG          
SEQRES   6 B  169  ALA ILE CYS ARG GLN GLY CYS SER PRO LYS HIS GLY SER          
SEQRES   7 B  169  CYS LYS LEU PRO GLY ASP CYS ARG CYS GLN TYR GLY TRP          
SEQRES   8 B  169  GLN GLY LEU TYR CYS ASP LYS CYS ILE PRO HIS PRO GLY          
SEQRES   9 B  169  CYS VAL HIS GLY ILE CYS ASN GLU PRO TRP GLN CYS LEU          
SEQRES  10 B  169  CYS GLU THR ASN TRP GLY GLY GLN LEU CYS ASP LYS ASP          
SEQRES  11 B  169  LEU ASN TYR CYS GLY THR HIS GLN PRO CYS LEU ASN GLY          
SEQRES  12 B  169  GLY THR CYS SER ASN THR GLY PRO ASP LYS TYR GLN CYS          
SEQRES  13 B  169  SER CYS PRO GLU GLY TYR SER GLY PRO ASN CYS GLU ILE          
HET    MLT  B1336       9                                                       
HETNAM     MLT MALATE ION                                                       
FORMUL   3  MLT    C4 H5 O5 1-                                                  
FORMUL   4  HOH   *208(H2 O)                                                    
HELIX    1   1 ASN A  298  HIS A  303  1                                   6    
HELIX    2   2 ASN B  298  HIS B  303  1                                   6    
SHEET    1  AA 2 TYR A 191  TYR A 192  0                                        
SHEET    2  AA 2 LYS A 198  PHE A 199 -1  O  LYS A 198   N  TYR A 192           
SHEET    1  AB 3 ARG A 203  ASP A 205  0                                        
SHEET    2  AB 3 GLY A 208  CYS A 212 -1  O  GLY A 208   N  ASP A 205           
SHEET    3  AB 3 LYS A 218  CYS A 220 -1  O  THR A 219   N  ALA A 211           
SHEET    1  AC 2 TRP A 224  MET A 225  0                                        
SHEET    2  AC 2 ARG A 231  ALA A 232 -1  O  ARG A 231   N  MET A 225           
SHEET    1  AD 2 GLY A 243  SER A 244  0                                        
SHEET    2  AD 2 ARG A 252  CYS A 253 -1  O  ARG A 252   N  SER A 244           
SHEET    1  AE 2 TRP A 257  GLN A 258  0                                        
SHEET    2  AE 2 LYS A 264  CYS A 265 -1  O  LYS A 264   N  GLN A 258           
SHEET    1  AF 2 GLY A 274  ILE A 275  0                                        
SHEET    2  AF 2 LEU A 283  CYS A 284 -1  O  LEU A 283   N  ILE A 275           
SHEET    1  AG 2 TRP A 288  GLY A 289  0                                        
SHEET    2  AG 2 LYS A 295  ASP A 296 -1  O  LYS A 295   N  GLY A 289           
SHEET    1  AH 2 THR A 311  ASN A 314  0                                        
SHEET    2  AH 2 TYR A 320  SER A 323 -1  O  GLN A 321   N  SER A 313           
SHEET    1  BA 2 TYR B 191  TYR B 192  0                                        
SHEET    2  BA 2 LYS B 198  PHE B 199 -1  O  LYS B 198   N  TYR B 192           
SHEET    1  BB 3 ARG B 203  ASP B 205  0                                        
SHEET    2  BB 3 GLY B 208  CYS B 212 -1  O  GLY B 208   N  ASP B 205           
SHEET    3  BB 3 LYS B 218  CYS B 220 -1  O  THR B 219   N  ALA B 211           
SHEET    1  BC 2 TRP B 224  MET B 225  0                                        
SHEET    2  BC 2 ARG B 231  ALA B 232 -1  O  ARG B 231   N  MET B 225           
SHEET    1  BD 2 GLY B 243  SER B 244  0                                        
SHEET    2  BD 2 ARG B 252  CYS B 253 -1  O  ARG B 252   N  SER B 244           
SHEET    1  BE 2 TRP B 257  GLN B 258  0                                        
SHEET    2  BE 2 LYS B 264  CYS B 265 -1  O  LYS B 264   N  GLN B 258           
SHEET    1  BF 2 GLY B 274  ILE B 275  0                                        
SHEET    2  BF 2 LEU B 283  CYS B 284 -1  O  LEU B 283   N  ILE B 275           
SHEET    1  BG 2 TRP B 288  GLY B 289  0                                        
SHEET    2  BG 2 LYS B 295  ASP B 296 -1  O  LYS B 295   N  GLY B 289           
SHEET    1  BH 2 THR B 311  GLY B 316  0                                        
SHEET    2  BH 2 LYS B 319  SER B 323 -1  O  LYS B 319   N  THR B 315           
SSBOND   1 CYS A  187    CYS A  196                          1555   1555  2.03  
SSBOND   2 CYS A  200    CYS A  212                          1555   1555  2.03  
SSBOND   3 CYS A  220    CYS A  229                          1555   1555  2.03  
SSBOND   4 CYS A  234    CYS A  245                          1555   1555  2.03  
SSBOND   5 CYS A  238    CYS A  251                          1555   1555  2.03  
SSBOND   6 CYS A  253    CYS A  262                          1555   1555  2.03  
SSBOND   7 CYS A  265    CYS A  276                          1555   1555  2.04  
SSBOND   8 CYS A  271    CYS A  282                          1555   1555  2.03  
SSBOND   9 CYS A  284    CYS A  293                          1555   1555  2.03  
SSBOND  10 CYS A  300    CYS A  312                          1555   1555  2.03  
SSBOND  11 CYS A  306    CYS A  322                          1555   1555  2.03  
SSBOND  12 CYS A  324    CYS A  333                          1555   1555  2.03  
SSBOND  13 CYS B  187    CYS B  196                          1555   1555  2.03  
SSBOND  14 CYS B  200    CYS B  212                          1555   1555  2.03  
SSBOND  15 CYS B  220    CYS B  229                          1555   1555  2.03  
SSBOND  16 CYS B  234    CYS B  245                          1555   1555  2.03  
SSBOND  17 CYS B  238    CYS B  251                          1555   1555  2.03  
SSBOND  18 CYS B  253    CYS B  262                          1555   1555  2.03  
SSBOND  19 CYS B  265    CYS B  276                          1555   1555  2.04  
SSBOND  20 CYS B  271    CYS B  282                          1555   1555  2.03  
SSBOND  21 CYS B  284    CYS B  293                          1555   1555  2.03  
SSBOND  22 CYS B  300    CYS B  312                          1555   1555  2.03  
SSBOND  23 CYS B  306    CYS B  322                          1555   1555  2.03  
SSBOND  24 CYS B  324    CYS B  333                          1555   1555  2.03  
CISPEP   1 PRO A  248    GLY A  249          0        -4.13                     
CISPEP   2 PRO A  269    GLY A  270          0        -1.43                     
CISPEP   3 THR A  286    ASN A  287          0        -0.54                     
CISPEP   4 GLY A  289    GLY A  290          0        -4.93                     
CISPEP   5 PRO B  269    GLY B  270          0        -3.09                     
SITE     1 AC1  4 THR B 186  ASP B 188  GLY B 195  HOH B2111                    
CRYST1   61.000  102.300   62.700  90.00 114.30  90.00 C 1 2 1       8          
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      0.016393  0.000000  0.007402        0.00000                         
SCALE2      0.000000  0.009775  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017499        0.00000                         
MTRIX1   1  0.449000 -0.006000 -0.893000       28.04469    1                    
MTRIX2   1 -0.065000 -0.998000 -0.026000      134.20255    1                    
MTRIX3   1 -0.891000  0.070000 -0.449000       37.42754    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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