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Database: PDB
Entry: 5BO1
LinkDB: 5BO1
Original site: 5BO1 
HEADER    SIGNALING PROTEIN/IMMUNE SYSTEM         26-MAY-15   5BO1              
TITLE     CRYSTAL STRUCTURE OF A HUMAN JAG1 FRAGMENT IN COMPLEX WITH AN ANTI-   
TITLE    2 JAG1 FAB                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN JAGGED-1;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 186-335;                                      
COMPND   5 SYNONYM: HJ1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: FAB HEAVY CHAIN;                                           
COMPND   9 CHAIN: H, I;                                                         
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: FAB LIGHT CHAIN;                                           
COMPND  13 CHAIN: L, M;                                                         
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: JAG1, JAGL1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PACGP67A;                                 
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  15 EXPRESSION_SYSTEM_CELL_LINE: CHO;                                    
SOURCE  16 MOL_ID: 3;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  21 EXPRESSION_SYSTEM_CELL_LINE: CHO                                     
KEYWDS    JAG, NOTCH, ANTAGONIST, SIGNALING PROTEIN-IMMUNE SYSTEM COMPLEX       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.PAYANDEH,G.DE LEON-BOENIG                                           
REVDAT   3   16-DEC-15 5BO1    1       JRNL                                     
REVDAT   2   02-DEC-15 5BO1    1       JRNL                                     
REVDAT   1   18-NOV-15 5BO1    0                                                
JRNL        AUTH   D.LAFKAS,A.SHELTON,C.CHIU,G.DE LEON BOENIG,Y.CHEN,           
JRNL        AUTH 2 S.S.STAWICKI,C.SILTANEN,M.REICHELT,M.ZHOU,X.WU,              
JRNL        AUTH 3 J.EASTHAM-ANDERSON,H.MOORE,M.ROOSE-GIRMA,Y.CHINN,J.Q.HANG,   
JRNL        AUTH 4 S.WARMING,J.EGEN,W.P.LEE,C.AUSTIN,Y.WU,J.PAYANDEH,J.B.LOWE,  
JRNL        AUTH 5 C.W.SIEBEL                                                   
JRNL        TITL   THERAPEUTIC ANTIBODIES REVEAL NOTCH CONTROL OF               
JRNL        TITL 2 TRANSDIFFERENTIATION IN THE ADULT LUNG.                      
JRNL        REF    NATURE                        V. 528   127 2015              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   26580007                                                     
JRNL        DOI    10.1038/NATURE15715                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.56 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.5                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.56                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 71.79                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 41207                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.222                          
REMARK   3   R VALUE            (WORKING SET)  : 0.220                          
REMARK   3   FREE R VALUE                      : 0.259                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.040                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2075                           
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               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.56                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.63                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 96.36                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3066                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2302                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2911                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2275                   
REMARK   3   BIN FREE R VALUE                        : 0.2792                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.06                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 155                      
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            : 8746                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 158                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 59.89                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.47020                                              
REMARK   3    B22 (A**2) : 1.09910                                              
REMARK   3    B33 (A**2) : -4.56930                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.50050                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.372               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.668               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.303               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.720               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.310               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.894                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.860                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 9007   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 12261  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2929   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 200    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1320   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 9007   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1161   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 9818   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.007                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.06                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.65                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.70                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5BO1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAY-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000210255.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-JUN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : 9.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41207                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.560                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 71.790                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.13000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.56                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 2VJ2, 2R0L                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM CHES PH 9.5, 20% PEG8000, VAPOR   
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 292K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       40.48900            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5490 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I, M                               
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H, L                               
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     LYS H   132                                                      
REMARK 465     SER H   133                                                      
REMARK 465     THR H   134                                                      
REMARK 465     SER H   135                                                      
REMARK 465     GLY H   136                                                      
REMARK 465     GLY H   137                                                      
REMARK 465     SER I   131                                                      
REMARK 465     LYS I   132                                                      
REMARK 465     SER I   133                                                      
REMARK 465     THR I   134                                                      
REMARK 465     SER I   135                                                      
REMARK 465     GLY I   136                                                      
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     ARG L   24   NE   CZ   NH1  NH2                                  
REMARK 480     ARG L  142   CZ   NH1  NH2                                       
REMARK 480     ARG M   24   NE   CZ   NH1  NH2                                  
REMARK 480     ARG M  142   CZ   NH1  NH2                                       
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    GLN A 236      103.68    -51.16                                   
REMARK 500    LYS A 246      -14.67   -144.37                                   
REMARK 500    VAL A 272      -95.92    -93.74                                   
REMARK 500    HIS A 273       58.05    -93.33                                   
REMARK 500    GLU A 285     -164.91   -100.13                                   
REMARK 500    GLN A 291      -62.51     75.00                                   
REMARK 500    GLN B 236       92.99    -61.15                                   
REMARK 500    CYS B 251       86.62   -153.41                                   
REMARK 500    VAL B 272      -86.96    -82.46                                   
REMARK 500    HIS B 273       59.95    -98.97                                   
REMARK 500    THR B 286      -58.08    -25.54                                   
REMARK 500    PHE H  27     -158.85   -146.30                                   
REMARK 500    SER H  30      -14.67    102.74                                   
REMARK 500    TYR H  32      -81.84   -134.45                                   
REMARK 500    ARG H  67      -46.63   -132.38                                   
REMARK 500    LEU H 127       79.50   -100.09                                   
REMARK 500    ASP H 147       78.35     50.94                                   
REMARK 500    SER H 218      -76.64    -72.23                                   
REMARK 500    TYR I  32     -104.75   -126.86                                   
REMARK 500    ASP I 147       87.33     54.69                                   
REMARK 500    SER L  30     -113.55     54.64                                   
REMARK 500    ALA L  51      -24.17     62.20                                   
REMARK 500    ALA L  84     -177.62   -172.14                                   
REMARK 500    LEU L 125       42.93    -78.40                                   
REMARK 500    ASN L 138       81.58     47.76                                   
REMARK 500    LYS L 190      -64.87   -122.04                                   
REMARK 500    PRO L 204      105.59    -59.55                                   
REMARK 500    SER M  30     -126.25     53.26                                   
REMARK 500    ALA M  51      -28.47     62.87                                   
REMARK 500    ALA M  84     -176.59   -177.66                                   
REMARK 500    ASN M 138       84.73     48.35                                   
REMARK 500    GLU M 143      109.67    -56.80                                   
REMARK 500    SER M 171       28.60     48.07                                   
REMARK 500    LYS M 190      -62.11   -106.27                                   
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 A 526        DISTANCE = 10.46 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 401                 
DBREF  5BO1 A  186   335  UNP    P78504   JAG1_HUMAN     186    335             
DBREF  5BO1 B  186   335  UNP    P78504   JAG1_HUMAN     186    335             
DBREF  5BO1 H    1   219  PDB    5BO1     5BO1             1    219             
DBREF  5BO1 I    1   219  PDB    5BO1     5BO1             1    219             
DBREF  5BO1 L    1   214  PDB    5BO1     5BO1             1    214             
DBREF  5BO1 M    1   214  PDB    5BO1     5BO1             1    214             
SEQRES   1 A  150  THR CYS ASP ASP TYR TYR TYR GLY PHE GLY CYS ASN LYS          
SEQRES   2 A  150  PHE CYS ARG PRO ARG ASP ASP PHE PHE GLY HIS TYR ALA          
SEQRES   3 A  150  CYS ASP GLN ASN GLY ASN LYS THR CYS MET GLU GLY TRP          
SEQRES   4 A  150  MET GLY PRO GLU CYS ASN ARG ALA ILE CYS ARG GLN GLY          
SEQRES   5 A  150  CYS SER PRO LYS HIS GLY SER CYS LYS LEU PRO GLY ASP          
SEQRES   6 A  150  CYS ARG CYS GLN TYR GLY TRP GLN GLY LEU TYR CYS ASP          
SEQRES   7 A  150  LYS CYS ILE PRO HIS PRO GLY CYS VAL HIS GLY ILE CYS          
SEQRES   8 A  150  ASN GLU PRO TRP GLN CYS LEU CYS GLU THR ASN TRP GLY          
SEQRES   9 A  150  GLY GLN LEU CYS ASP LYS ASP LEU ASN TYR CYS GLY THR          
SEQRES  10 A  150  HIS GLN PRO CYS LEU ASN GLY GLY THR CYS SER ASN THR          
SEQRES  11 A  150  GLY PRO ASP LYS TYR GLN CYS SER CYS PRO GLU GLY TYR          
SEQRES  12 A  150  SER GLY PRO ASN CYS GLU ILE                                  
SEQRES   1 B  150  THR CYS ASP ASP TYR TYR TYR GLY PHE GLY CYS ASN LYS          
SEQRES   2 B  150  PHE CYS ARG PRO ARG ASP ASP PHE PHE GLY HIS TYR ALA          
SEQRES   3 B  150  CYS ASP GLN ASN GLY ASN LYS THR CYS MET GLU GLY TRP          
SEQRES   4 B  150  MET GLY PRO GLU CYS ASN ARG ALA ILE CYS ARG GLN GLY          
SEQRES   5 B  150  CYS SER PRO LYS HIS GLY SER CYS LYS LEU PRO GLY ASP          
SEQRES   6 B  150  CYS ARG CYS GLN TYR GLY TRP GLN GLY LEU TYR CYS ASP          
SEQRES   7 B  150  LYS CYS ILE PRO HIS PRO GLY CYS VAL HIS GLY ILE CYS          
SEQRES   8 B  150  ASN GLU PRO TRP GLN CYS LEU CYS GLU THR ASN TRP GLY          
SEQRES   9 B  150  GLY GLN LEU CYS ASP LYS ASP LEU ASN TYR CYS GLY THR          
SEQRES  10 B  150  HIS GLN PRO CYS LEU ASN GLY GLY THR CYS SER ASN THR          
SEQRES  11 B  150  GLY PRO ASP LYS TYR GLN CYS SER CYS PRO GLU GLY TYR          
SEQRES  12 B  150  SER GLY PRO ASN CYS GLU ILE                                  
SEQRES   1 H  219  GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 H  219  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 H  219  PHE THR PHE SER ASN TYR GLY ILE HIS TRP VAL ARG GLN          
SEQRES   4 H  219  ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY TRP ILE THR          
SEQRES   5 H  219  PRO ASP GLY GLY TYR THR ASP TYR ALA ASP SER VAL LYS          
SEQRES   6 H  219  GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR          
SEQRES   7 H  219  ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR          
SEQRES   8 H  219  ALA VAL TYR TYR CYS ALA ARG ALA GLY THR LEU PHE ALA          
SEQRES   9 H  219  TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA          
SEQRES  10 H  219  SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER          
SEQRES  11 H  219  SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS          
SEQRES  12 H  219  LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER          
SEQRES  13 H  219  TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE          
SEQRES  14 H  219  PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER          
SEQRES  15 H  219  SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN          
SEQRES  16 H  219  THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR          
SEQRES  17 H  219  LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS                  
SEQRES   1 I  219  GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 I  219  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 I  219  PHE THR PHE SER ASN TYR GLY ILE HIS TRP VAL ARG GLN          
SEQRES   4 I  219  ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY TRP ILE THR          
SEQRES   5 I  219  PRO ASP GLY GLY TYR THR ASP TYR ALA ASP SER VAL LYS          
SEQRES   6 I  219  GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR          
SEQRES   7 I  219  ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR          
SEQRES   8 I  219  ALA VAL TYR TYR CYS ALA ARG ALA GLY THR LEU PHE ALA          
SEQRES   9 I  219  TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA          
SEQRES  10 I  219  SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER          
SEQRES  11 I  219  SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS          
SEQRES  12 I  219  LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER          
SEQRES  13 I  219  TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE          
SEQRES  14 I  219  PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER          
SEQRES  15 I  219  SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN          
SEQRES  16 I  219  THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR          
SEQRES  17 I  219  LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS                  
SEQRES   1 L  214  ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA          
SEQRES   2 L  214  SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER          
SEQRES   3 L  214  GLN ASP VAL SER THR ALA VAL ALA TRP TYR GLN GLN LYS          
SEQRES   4 L  214  PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER          
SEQRES   5 L  214  PHE LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU          
SEQRES   7 L  214  GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR          
SEQRES   8 L  214  TYR THR THR ALA THR THR PHE GLY GLN GLY THR LYS VAL          
SEQRES   9 L  214  GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE          
SEQRES  10 L  214  PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA          
SEQRES  11 L  214  SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU          
SEQRES  12 L  214  ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER          
SEQRES  13 L  214  GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER          
SEQRES  15 L  214  LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU          
SEQRES  16 L  214  VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER          
SEQRES  17 L  214  PHE ASN ARG GLY GLU CYS                                      
SEQRES   1 M  214  ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA          
SEQRES   2 M  214  SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER          
SEQRES   3 M  214  GLN ASP VAL SER THR ALA VAL ALA TRP TYR GLN GLN LYS          
SEQRES   4 M  214  PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER          
SEQRES   5 M  214  PHE LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 M  214  GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU          
SEQRES   7 M  214  GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR          
SEQRES   8 M  214  TYR THR THR ALA THR THR PHE GLY GLN GLY THR LYS VAL          
SEQRES   9 M  214  GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE          
SEQRES  10 M  214  PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA          
SEQRES  11 M  214  SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU          
SEQRES  12 M  214  ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER          
SEQRES  13 M  214  GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS          
SEQRES  14 M  214  ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER          
SEQRES  15 M  214  LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU          
SEQRES  16 M  214  VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER          
SEQRES  17 M  214  PHE ASN ARG GLY GLU CYS                                      
HET    GOL  A 401       6                                                       
HET    GOL  B 401       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   7  GOL    2(C3 H8 O3)                                                  
FORMUL   9  HOH   *158(H2 O)                                                    
HELIX    1 AA1 ASN A  298  GLN A  304  1                                   7    
HELIX    2 AA2 ASN B  298  GLN B  304  1                                   7    
HELIX    3 AA3 ARG H   87  THR H   91  5                                   5    
HELIX    4 AA4 SER H  159  ALA H  161  5                                   3    
HELIX    5 AA5 THR I   28  TYR I   32  5                                   5    
HELIX    6 AA6 ARG I   87  THR I   91  5                                   5    
HELIX    7 AA7 LYS I  204  ASN I  207  5                                   4    
HELIX    8 AA8 GLN L   79  PHE L   83  5                                   5    
HELIX    9 AA9 LYS L  183  LYS L  188  1                                   6    
HELIX   10 AB1 GLN M   79  PHE M   83  5                                   5    
HELIX   11 AB2 SER M  121  SER M  127  1                                   7    
HELIX   12 AB3 LYS M  183  LYS M  188  1                                   6    
SHEET    1 AA1 2 TYR A 191  TYR A 192  0                                        
SHEET    2 AA1 2 LYS A 198  PHE A 199 -1  O  LYS A 198   N  TYR A 192           
SHEET    1 AA2 3 ARG A 203  ASP A 205  0                                        
SHEET    2 AA2 3 GLY A 208  CYS A 212 -1  O  GLY A 208   N  ASP A 205           
SHEET    3 AA2 3 LYS A 218  CYS A 220 -1  O  THR A 219   N  ALA A 211           
SHEET    1 AA3 2 TRP A 224  MET A 225  0                                        
SHEET    2 AA3 2 ARG A 231  ALA A 232 -1  O  ARG A 231   N  MET A 225           
SHEET    1 AA4 2 GLY A 243  SER A 244  0                                        
SHEET    2 AA4 2 ARG A 252  CYS A 253 -1  O  ARG A 252   N  SER A 244           
SHEET    1 AA5 2 TRP A 257  GLN A 258  0                                        
SHEET    2 AA5 2 LYS A 264  CYS A 265 -1  O  LYS A 264   N  GLN A 258           
SHEET    1 AA6 2 GLY A 274  ILE A 275  0                                        
SHEET    2 AA6 2 LEU A 283  CYS A 284 -1  O  LEU A 283   N  ILE A 275           
SHEET    1 AA7 2 TRP A 288  GLY A 289  0                                        
SHEET    2 AA7 2 LYS A 295  ASP A 296 -1  O  LYS A 295   N  GLY A 289           
SHEET    1 AA8 2 THR A 311  GLY A 316  0                                        
SHEET    2 AA8 2 LYS A 319  SER A 323 -1  O  SER A 323   N  THR A 311           
SHEET    1 AA9 2 TYR B 191  TYR B 192  0                                        
SHEET    2 AA9 2 LYS B 198  PHE B 199 -1  O  LYS B 198   N  TYR B 192           
SHEET    1 AB1 3 ARG B 203  ASP B 205  0                                        
SHEET    2 AB1 3 GLY B 208  CYS B 212 -1  O  GLY B 208   N  ASP B 205           
SHEET    3 AB1 3 LYS B 218  CYS B 220 -1  O  THR B 219   N  ALA B 211           
SHEET    1 AB2 2 TRP B 224  MET B 225  0                                        
SHEET    2 AB2 2 ARG B 231  ALA B 232 -1  O  ARG B 231   N  MET B 225           
SHEET    1 AB3 2 GLY B 243  SER B 244  0                                        
SHEET    2 AB3 2 ARG B 252  CYS B 253 -1  O  ARG B 252   N  SER B 244           
SHEET    1 AB4 2 TRP B 257  GLN B 258  0                                        
SHEET    2 AB4 2 LYS B 264  CYS B 265 -1  O  LYS B 264   N  GLN B 258           
SHEET    1 AB5 2 GLY B 274  ILE B 275  0                                        
SHEET    2 AB5 2 LEU B 283  CYS B 284 -1  O  LEU B 283   N  ILE B 275           
SHEET    1 AB6 2 TRP B 288  GLY B 289  0                                        
SHEET    2 AB6 2 LYS B 295  ASP B 296 -1  O  LYS B 295   N  GLY B 289           
SHEET    1 AB7 2 THR B 311  GLY B 316  0                                        
SHEET    2 AB7 2 LYS B 319  SER B 323 -1  O  SER B 323   N  THR B 311           
SHEET    1 AB8 4 GLN H   3  SER H   7  0                                        
SHEET    2 AB8 4 LEU H  18  SER H  25 -1  O  ALA H  23   N  VAL H   5           
SHEET    3 AB8 4 THR H  78  MET H  83 -1  O  MET H  83   N  LEU H  18           
SHEET    4 AB8 4 THR H  69  ASP H  73 -1  N  SER H  71   O  TYR H  80           
SHEET    1 AB9 6 LEU H  11  VAL H  12  0                                        
SHEET    2 AB9 6 THR H 110  VAL H 114  1  O  THR H 113   N  VAL H  12           
SHEET    3 AB9 6 ALA H  92  ARG H  98 -1  N  TYR H  94   O  THR H 110           
SHEET    4 AB9 6 ILE H  34  GLN H  39 -1  N  VAL H  37   O  TYR H  95           
SHEET    5 AB9 6 LEU H  45  THR H  52 -1  O  GLU H  46   N  ARG H  38           
SHEET    6 AB9 6 TYR H  57  TYR H  60 -1  O  ASP H  59   N  TRP H  50           
SHEET    1 AC1 4 SER H 123  LEU H 127  0                                        
SHEET    2 AC1 4 ALA H 139  TYR H 148 -1  O  LEU H 144   N  PHE H 125           
SHEET    3 AC1 4 TYR H 179  VAL H 187 -1  O  LEU H 181   N  VAL H 145           
SHEET    4 AC1 4 VAL H 166  THR H 168 -1  N  HIS H 167   O  VAL H 184           
SHEET    1 AC2 4 SER H 123  LEU H 127  0                                        
SHEET    2 AC2 4 ALA H 139  TYR H 148 -1  O  LEU H 144   N  PHE H 125           
SHEET    3 AC2 4 TYR H 179  VAL H 187 -1  O  LEU H 181   N  VAL H 145           
SHEET    4 AC2 4 VAL H 172  LEU H 173 -1  N  VAL H 172   O  SER H 180           
SHEET    1 AC3 3 THR H 154  TRP H 157  0                                        
SHEET    2 AC3 3 TYR H 197  HIS H 203 -1  O  ASN H 200   N  SER H 156           
SHEET    3 AC3 3 THR H 208  VAL H 214 -1  O  VAL H 214   N  TYR H 197           
SHEET    1 AC4 4 GLN I   3  SER I   7  0                                        
SHEET    2 AC4 4 LEU I  18  SER I  25 -1  O  ALA I  23   N  VAL I   5           
SHEET    3 AC4 4 THR I  78  MET I  83 -1  O  MET I  83   N  LEU I  18           
SHEET    4 AC4 4 PHE I  68  ASP I  73 -1  N  THR I  69   O  GLN I  82           
SHEET    1 AC5 6 LEU I  11  VAL I  12  0                                        
SHEET    2 AC5 6 THR I 110  VAL I 114  1  O  THR I 113   N  VAL I  12           
SHEET    3 AC5 6 ALA I  92  ARG I  98 -1  N  TYR I  94   O  THR I 110           
SHEET    4 AC5 6 ILE I  34  GLN I  39 -1  N  VAL I  37   O  TYR I  95           
SHEET    5 AC5 6 LEU I  45  ILE I  51 -1  O  GLU I  46   N  ARG I  38           
SHEET    6 AC5 6 THR I  58  TYR I  60 -1  O  ASP I  59   N  TRP I  50           
SHEET    1 AC6 4 SER I 123  LEU I 127  0                                        
SHEET    2 AC6 4 THR I 138  TYR I 148 -1  O  LEU I 144   N  PHE I 125           
SHEET    3 AC6 4 TYR I 179  PRO I 188 -1  O  VAL I 187   N  ALA I 139           
SHEET    4 AC6 4 VAL I 166  THR I 168 -1  N  HIS I 167   O  VAL I 184           
SHEET    1 AC7 4 SER I 123  LEU I 127  0                                        
SHEET    2 AC7 4 THR I 138  TYR I 148 -1  O  LEU I 144   N  PHE I 125           
SHEET    3 AC7 4 TYR I 179  PRO I 188 -1  O  VAL I 187   N  ALA I 139           
SHEET    4 AC7 4 VAL I 172  LEU I 173 -1  N  VAL I 172   O  SER I 180           
SHEET    1 AC8 3 THR I 154  TRP I 157  0                                        
SHEET    2 AC8 3 TYR I 197  HIS I 203 -1  O  ASN I 200   N  SER I 156           
SHEET    3 AC8 3 THR I 208  VAL I 214 -1  O  LYS I 212   N  CYS I 199           
SHEET    1 AC9 4 MET L   4  SER L   7  0                                        
SHEET    2 AC9 4 VAL L  19  ALA L  25 -1  O  THR L  22   N  SER L   7           
SHEET    3 AC9 4 ASP L  70  ILE L  75 -1  O  LEU L  73   N  ILE L  21           
SHEET    4 AC9 4 PHE L  62  SER L  67 -1  N  SER L  65   O  THR L  72           
SHEET    1 AD1 6 SER L  10  SER L  14  0                                        
SHEET    2 AD1 6 THR L 102  LYS L 107  1  O  GLU L 105   N  LEU L  11           
SHEET    3 AD1 6 ALA L  84  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4 AD1 6 VAL L  33  GLN L  38 -1  N  ALA L  34   O  GLN L  89           
SHEET    5 AD1 6 LYS L  45  TYR L  49 -1  O  LEU L  47   N  TRP L  35           
SHEET    6 AD1 6 PHE L  53  LEU L  54 -1  O  PHE L  53   N  TYR L  49           
SHEET    1 AD2 4 SER L  10  SER L  14  0                                        
SHEET    2 AD2 4 THR L 102  LYS L 107  1  O  GLU L 105   N  LEU L  11           
SHEET    3 AD2 4 ALA L  84  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4 AD2 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1 AD3 4 SER L 114  PHE L 118  0                                        
SHEET    2 AD3 4 THR L 129  PHE L 139 -1  O  LEU L 135   N  PHE L 116           
SHEET    3 AD3 4 TYR L 173  SER L 182 -1  O  LEU L 181   N  ALA L 130           
SHEET    4 AD3 4 SER L 159  VAL L 163 -1  N  SER L 162   O  SER L 176           
SHEET    1 AD4 4 ALA L 153  LEU L 154  0                                        
SHEET    2 AD4 4 LYS L 145  VAL L 150 -1  N  VAL L 150   O  ALA L 153           
SHEET    3 AD4 4 VAL L 191  THR L 197 -1  O  GLU L 195   N  GLN L 147           
SHEET    4 AD4 4 VAL L 205  ASN L 210 -1  O  VAL L 205   N  VAL L 196           
SHEET    1 AD5 4 MET M   4  SER M   7  0                                        
SHEET    2 AD5 4 VAL M  19  ALA M  25 -1  O  THR M  22   N  SER M   7           
SHEET    3 AD5 4 ASP M  70  ILE M  75 -1  O  LEU M  73   N  ILE M  21           
SHEET    4 AD5 4 PHE M  62  GLY M  66 -1  N  SER M  65   O  THR M  72           
SHEET    1 AD6 6 SER M  10  ALA M  13  0                                        
SHEET    2 AD6 6 THR M 102  ILE M 106  1  O  GLU M 105   N  LEU M  11           
SHEET    3 AD6 6 ALA M  84  GLN M  90 -1  N  TYR M  86   O  THR M 102           
SHEET    4 AD6 6 VAL M  33  GLN M  38 -1  N  ALA M  34   O  GLN M  89           
SHEET    5 AD6 6 LYS M  45  TYR M  49 -1  O  LEU M  47   N  TRP M  35           
SHEET    6 AD6 6 PHE M  53  LEU M  54 -1  O  PHE M  53   N  TYR M  49           
SHEET    1 AD7 4 SER M  10  ALA M  13  0                                        
SHEET    2 AD7 4 THR M 102  ILE M 106  1  O  GLU M 105   N  LEU M  11           
SHEET    3 AD7 4 ALA M  84  GLN M  90 -1  N  TYR M  86   O  THR M 102           
SHEET    4 AD7 4 THR M  97  PHE M  98 -1  O  THR M  97   N  GLN M  90           
SHEET    1 AD8 4 SER M 114  PHE M 118  0                                        
SHEET    2 AD8 4 THR M 129  PHE M 139 -1  O  VAL M 133   N  PHE M 118           
SHEET    3 AD8 4 TYR M 173  SER M 182 -1  O  LEU M 179   N  VAL M 132           
SHEET    4 AD8 4 SER M 159  VAL M 163 -1  N  SER M 162   O  SER M 176           
SHEET    1 AD9 4 ALA M 153  LEU M 154  0                                        
SHEET    2 AD9 4 LYS M 145  VAL M 150 -1  N  VAL M 150   O  ALA M 153           
SHEET    3 AD9 4 VAL M 191  THR M 197 -1  O  GLU M 195   N  GLN M 147           
SHEET    4 AD9 4 VAL M 205  ASN M 210 -1  O  VAL M 205   N  VAL M 196           
SSBOND   1 CYS A  187    CYS A  196                          1555   1555  2.03  
SSBOND   2 CYS A  200    CYS A  212                          1555   1555  2.04  
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  2.04  
SSBOND   9 CYS A  284    CYS A  293                          1555   1555  2.07  
SSBOND  10 CYS A  300    CYS A  312                          1555   1555  2.04  
SSBOND  11 CYS A  306    CYS A  322                          1555   1555  2.03  
SSBOND  12 CYS A  324    CYS A  333                          1555   1555  2.04  
SSBOND  13 CYS B  187    CYS B  196                          1555   1555  2.04  
SSBOND  14 CYS B  200    CYS B  212                          1555   1555  2.04  
SSBOND  15 CYS B  220    CYS B  229                          1555   1555  2.03  
SSBOND  16 CYS B  234    CYS B  245                          1555   1555  2.04  
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  2.04  
SSBOND  25 CYS H   22    CYS H   96                          1555   1555  2.03  
SSBOND  26 CYS H  143    CYS H  199                          1555   1555  2.03  
SSBOND  27 CYS H  219    CYS L  214                          1555   1555  2.03  
SSBOND  28 CYS I   22    CYS I   96                          1555   1555  2.13  
SSBOND  29 CYS I  143    CYS I  199                          1555   1555  2.13  
SSBOND  30 CYS I  219    CYS M  214                          1555   1555  2.13  
SSBOND  31 CYS L   23    CYS L   88                          1555   1555  2.03  
SSBOND  32 CYS L  134    CYS L  194                          1555   1555  2.04  
SSBOND  33 CYS M   23    CYS M   88                          1555   1555  2.13  
SSBOND  34 CYS M  134    CYS M  194                          1555   1555  2.11  
CISPEP   1 PRO A  248    GLY A  249          0        -2.58                     
CISPEP   2 PRO A  269    GLY A  270          0         0.20                     
CISPEP   3 THR A  286    ASN A  287          0        -0.19                     
CISPEP   4 GLY A  289    GLY A  290          0       -18.43                     
CISPEP   5 PHE B  194    GLY B  195          0        -8.49                     
CISPEP   6 PRO B  248    GLY B  249          0        -4.42                     
CISPEP   7 PRO B  269    GLY B  270          0        -0.58                     
CISPEP   8 GLY B  289    GLY B  290          0        -1.99                     
CISPEP   9 PHE H  149    PRO H  150          0        -0.95                     
CISPEP  10 GLU H  151    PRO H  152          0         5.80                     
CISPEP  11 PHE I  149    PRO I  150          0        -3.29                     
CISPEP  12 GLU I  151    PRO I  152          0         6.44                     
CISPEP  13 SER L    7    PRO L    8          0         0.20                     
CISPEP  14 TYR L  140    PRO L  141          0         2.20                     
CISPEP  15 SER M    7    PRO M    8          0        -0.09                     
CISPEP  16 TYR M  140    PRO M  141          0         2.85                     
SITE     1 AC1  2 GLY A 309  THR A 311                                          
SITE     1 AC2  3 GLY B 309  THR B 311  SER B 323                               
CRYST1   53.258   80.978  155.616  90.00  94.39  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018777  0.000000  0.001441        0.00000                         
SCALE2      0.000000  0.012349  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006445        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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