GenomeNet

Database: PDB
Entry: 4CC0
LinkDB: 4CC0
Original site: 4CC0 
HEADER    SIGNALING PROTEIN                       17-OCT-13   4CC0              
TITLE     NOTCH LIGAND, JAGGED-1, CONTAINS AN N-TERMINAL C2 DOMAIN              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN JAGGED-1;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 32-335;                                           
COMPND   5 SYNONYM: JAGGED1, HJ1, CD339;                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: NAG LINKAGE AT N217 IN BOTH A, B CHAINS, FUC LINKAGE  
COMPND   8 AT T311 IN A CHAIN                                                   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK 293S                                
KEYWDS    SIGNALING PROTEIN, SIGNALLING, GLYCOPROTEIN, EXTRACELLULAR,           
KEYWDS   2 DEVELOPMENTAL PROTEIN, NOTCH SIGNALING PATHWAY, EGF, DSL, LIPID,     
KEYWDS   3 MEMBRANE, PROTEIN-BINDING, TRANSMEMBRANE, EGF-LIKE DOMAIN, DISEASE   
KEYWDS   4 MUTATION                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.R.CHILAKURI,D.SHEPPARD,M.X.G.ILAGAN,L.R.HOLT,F.ABBOTT,S.LIANG,      
AUTHOR   2 R.KOPAN,P.A.HANDFORD,S.M.LEA                                         
REVDAT   4   29-JUL-20 4CC0    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE                                     
REVDAT   3   18-DEC-13 4CC0    1       JRNL                                     
REVDAT   2   11-DEC-13 4CC0    1       JRNL                                     
REVDAT   1   27-NOV-13 4CC0    0                                                
JRNL        AUTH   C.R.CHILAKURI,D.SHEPPARD,M.X.G.ILAGAN,L.R.HOLT,F.ABBOTT,     
JRNL        AUTH 2 S.LIANG,R.KOPAN,P.A.HANDFORD,S.M.LEA                         
JRNL        TITL   STRUCTURAL ANALYSIS UNCOVERS LIPID-BINDING PROPERTIES OF     
JRNL        TITL 2 NOTCH LIGANDS                                                
JRNL        REF    CELL REP.                     V.   5   861 2013              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   24239355                                                     
JRNL        DOI    10.1016/J.CELREP.2013.10.029                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.32 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.4                                        
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) : 2.32                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 31595                          
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)  : 0.219                          
REMARK   3   R VALUE            (WORKING SET)  : 0.218                          
REMARK   3   FREE R VALUE                      : 0.246                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.050                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1596                           
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               : 16                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.32                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.40                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 96.97                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2857                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2323                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2724                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2309                   
REMARK   3   BIN FREE R VALUE                        : 0.2610                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.66                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 133                      
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            : 4445                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 61                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.43                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.98                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.93950                                             
REMARK   3    B22 (A**2) : -3.33410                                             
REMARK   3    B33 (A**2) : 4.27360                                              
REMARK   3    B12 (A**2) : -7.53980                                             
REMARK   3    B13 (A**2) : -10.28410                                            
REMARK   3    B23 (A**2) : 4.06380                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.367               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.278               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.210               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.295               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.217               
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      : 0.893                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.861                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4629   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 6286   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1575   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 133    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 679    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4629   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 570    ; 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   : 4791   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.19                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.59                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.02                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.    
REMARK   3  RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=CA. NUMBER OF       
REMARK   3  ATOMS WITH PROPER CCP4 ATOM TYPE=4544. NUMBER WITH APPROX           
REMARK   3  DEFAULT CCP4 ATOM TYPE=0. NUMBER TREATED BY BAD NON-BONDED          
REMARK   3  CONTACTS=2.                                                         
REMARK   4                                                                      
REMARK   4 4CC0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-OCT-13.                  
REMARK 100 THE DEPOSITION ID IS D_1290058750.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-FEB-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31717                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.320                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.190                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 1.770                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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     HIS A   338                                                      
REMARK 465     HIS A   339                                                      
REMARK 465     HIS A   340                                                      
REMARK 465     HIS A   341                                                      
REMARK 465     HIS A   342                                                      
REMARK 465     HIS A   343                                                      
REMARK 465     TYR B   299                                                      
REMARK 465     CYS B   300                                                      
REMARK 465     GLY B   301                                                      
REMARK 465     THR B   302                                                      
REMARK 465     HIS B   303                                                      
REMARK 465     GLN B   304                                                      
REMARK 465     PRO B   305                                                      
REMARK 465     CYS B   306                                                      
REMARK 465     LEU B   307                                                      
REMARK 465     ASN B   308                                                      
REMARK 465     GLY B   309                                                      
REMARK 465     GLY B   310                                                      
REMARK 465     THR B   311                                                      
REMARK 465     CYS B   312                                                      
REMARK 465     SER B   313                                                      
REMARK 465     ASN B   314                                                      
REMARK 465     THR B   315                                                      
REMARK 465     GLY B   316                                                      
REMARK 465     PRO B   317                                                      
REMARK 465     ASP B   318                                                      
REMARK 465     LYS B   319                                                      
REMARK 465     TYR B   320                                                      
REMARK 465     GLN B   321                                                      
REMARK 465     CYS B   322                                                      
REMARK 465     SER B   323                                                      
REMARK 465     CYS B   324                                                      
REMARK 465     PRO B   325                                                      
REMARK 465     GLU B   326                                                      
REMARK 465     GLY B   327                                                      
REMARK 465     TYR B   328                                                      
REMARK 465     SER B   329                                                      
REMARK 465     GLY B   330                                                      
REMARK 465     PRO B   331                                                      
REMARK 465     ASN B   332                                                      
REMARK 465     CYS B   333                                                      
REMARK 465     GLU B   334                                                      
REMARK 465     ILE B   335                                                      
REMARK 465     VAL B   336                                                      
REMARK 465     ASP B   337                                                      
REMARK 465     HIS B   338                                                      
REMARK 465     HIS B   339                                                      
REMARK 465     HIS B   340                                                      
REMARK 465     HIS B   341                                                      
REMARK 465     HIS B   342                                                      
REMARK 465     HIS B   343                                                      
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    ARG A 130      -51.77     74.29                                   
REMARK 500    ASP A 144        0.80   -152.34                                   
REMARK 500    SER A 164      140.94    179.96                                   
REMARK 500    ASP A 204       73.86   -151.57                                   
REMARK 500    ARG A 235      128.31    -38.95                                   
REMARK 500    LYS A 246      -46.40   -134.17                                   
REMARK 500    VAL A 272      -82.77   -105.87                                   
REMARK 500    HIS A 273       58.53    -97.29                                   
REMARK 500    ARG B  68      -75.39     80.60                                   
REMARK 500    ARG B 130      -52.02     74.97                                   
REMARK 500    SER B 142       75.05   -113.61                                   
REMARK 500    SER B 164      141.72   -173.97                                   
REMARK 500    ASP B 204       71.43   -153.85                                   
REMARK 500    VAL B 272      -79.49   -107.19                                   
REMARK 500    HIS B 273       58.74    -97.63                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 A1338  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  72   OD2                                                    
REMARK 620 2 ASP A 140   OD2 138.6                                              
REMARK 620 3 ASP A 140   OD1  93.1  48.2                                        
REMARK 620 4 SER A 141   O    81.4  86.3  93.3                                  
REMARK 620 5 HOH A2005   O    84.6 104.3  87.3 165.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1299  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  72   OD2                                                    
REMARK 620 2 ASP B 140   OD2 140.3                                              
REMARK 620 3 ASP B 140   OD1  97.3  48.0                                        
REMARK 620 4 SER B 141   O    72.0  89.8  94.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CBZ   RELATED DB: PDB                                   
REMARK 900 NOTCH LIGAND, JAGGED-1, CONTAINS AN N-TERMINAL C2 DOMAIN             
REMARK 900 RELATED ID: 4CC1   RELATED DB: PDB                                   
REMARK 900 NOTCH LIGAND, JAGGED-1, CONTAINS AN N-TERMINAL C2 DOMAIN             
DBREF  4CC0 A   32   335  UNP    P78504   JAG1_HUMAN      32    335             
DBREF  4CC0 B   32   335  UNP    P78504   JAG1_HUMAN      32    335             
SEQADV 4CC0 VAL A  336  UNP  P78504              EXPRESSION TAG                 
SEQADV 4CC0 ASP A  337  UNP  P78504              EXPRESSION TAG                 
SEQADV 4CC0 HIS A  338  UNP  P78504              EXPRESSION TAG                 
SEQADV 4CC0 HIS A  339  UNP  P78504              EXPRESSION TAG                 
SEQADV 4CC0 HIS A  340  UNP  P78504              EXPRESSION TAG                 
SEQADV 4CC0 HIS A  341  UNP  P78504              EXPRESSION TAG                 
SEQADV 4CC0 HIS A  342  UNP  P78504              EXPRESSION TAG                 
SEQADV 4CC0 HIS A  343  UNP  P78504              EXPRESSION TAG                 
SEQADV 4CC0 VAL B  336  UNP  P78504              EXPRESSION TAG                 
SEQADV 4CC0 ASP B  337  UNP  P78504              EXPRESSION TAG                 
SEQADV 4CC0 HIS B  338  UNP  P78504              EXPRESSION TAG                 
SEQADV 4CC0 HIS B  339  UNP  P78504              EXPRESSION TAG                 
SEQADV 4CC0 HIS B  340  UNP  P78504              EXPRESSION TAG                 
SEQADV 4CC0 HIS B  341  UNP  P78504              EXPRESSION TAG                 
SEQADV 4CC0 HIS B  342  UNP  P78504              EXPRESSION TAG                 
SEQADV 4CC0 HIS B  343  UNP  P78504              EXPRESSION TAG                 
SEQRES   1 A  312  SER GLY GLN PHE GLU LEU GLU ILE LEU SER MET GLN ASN          
SEQRES   2 A  312  VAL ASN GLY GLU LEU GLN ASN GLY ASN CYS CYS GLY GLY          
SEQRES   3 A  312  ALA ARG ASN PRO GLY ASP ARG LYS CYS THR ARG ASP GLU          
SEQRES   4 A  312  CYS ASP THR TYR PHE LYS VAL CYS LEU LYS GLU TYR GLN          
SEQRES   5 A  312  SER ARG VAL THR ALA GLY GLY PRO CYS SER PHE GLY SER          
SEQRES   6 A  312  GLY SER THR PRO VAL ILE GLY GLY ASN THR PHE ASN LEU          
SEQRES   7 A  312  LYS ALA SER ARG GLY ASN ASP ARG ASN ARG ILE VAL LEU          
SEQRES   8 A  312  PRO PHE SER PHE ALA TRP PRO ARG SER TYR THR LEU LEU          
SEQRES   9 A  312  VAL GLU ALA TRP ASP SER SER ASN ASP THR VAL GLN PRO          
SEQRES  10 A  312  ASP SER ILE ILE GLU LYS ALA SER HIS SER GLY MET ILE          
SEQRES  11 A  312  ASN PRO SER ARG GLN TRP GLN THR LEU LYS GLN ASN THR          
SEQRES  12 A  312  GLY VAL ALA HIS PHE GLU TYR GLN ILE ARG VAL THR CYS          
SEQRES  13 A  312  ASP ASP TYR TYR TYR GLY PHE GLY CYS ASN LYS PHE CYS          
SEQRES  14 A  312  ARG PRO ARG ASP ASP PHE PHE GLY HIS TYR ALA CYS ASP          
SEQRES  15 A  312  GLN ASN GLY ASN LYS THR CYS MET GLU GLY TRP MET GLY          
SEQRES  16 A  312  PRO GLU CYS ASN ARG ALA ILE CYS ARG GLN GLY CYS SER          
SEQRES  17 A  312  PRO LYS HIS GLY SER CYS LYS LEU PRO GLY ASP CYS ARG          
SEQRES  18 A  312  CYS GLN TYR GLY TRP GLN GLY LEU TYR CYS ASP LYS CYS          
SEQRES  19 A  312  ILE PRO HIS PRO GLY CYS VAL HIS GLY ILE CYS ASN GLU          
SEQRES  20 A  312  PRO TRP GLN CYS LEU CYS GLU THR ASN TRP GLY GLY GLN          
SEQRES  21 A  312  LEU CYS ASP LYS ASP LEU ASN TYR CYS GLY THR HIS GLN          
SEQRES  22 A  312  PRO CYS LEU ASN GLY GLY THR CYS SER ASN THR GLY PRO          
SEQRES  23 A  312  ASP LYS TYR GLN CYS SER CYS PRO GLU GLY TYR SER GLY          
SEQRES  24 A  312  PRO ASN CYS GLU ILE VAL ASP HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  312  SER GLY GLN PHE GLU LEU GLU ILE LEU SER MET GLN ASN          
SEQRES   2 B  312  VAL ASN GLY GLU LEU GLN ASN GLY ASN CYS CYS GLY GLY          
SEQRES   3 B  312  ALA ARG ASN PRO GLY ASP ARG LYS CYS THR ARG ASP GLU          
SEQRES   4 B  312  CYS ASP THR TYR PHE LYS VAL CYS LEU LYS GLU TYR GLN          
SEQRES   5 B  312  SER ARG VAL THR ALA GLY GLY PRO CYS SER PHE GLY SER          
SEQRES   6 B  312  GLY SER THR PRO VAL ILE GLY GLY ASN THR PHE ASN LEU          
SEQRES   7 B  312  LYS ALA SER ARG GLY ASN ASP ARG ASN ARG ILE VAL LEU          
SEQRES   8 B  312  PRO PHE SER PHE ALA TRP PRO ARG SER TYR THR LEU LEU          
SEQRES   9 B  312  VAL GLU ALA TRP ASP SER SER ASN ASP THR VAL GLN PRO          
SEQRES  10 B  312  ASP SER ILE ILE GLU LYS ALA SER HIS SER GLY MET ILE          
SEQRES  11 B  312  ASN PRO SER ARG GLN TRP GLN THR LEU LYS GLN ASN THR          
SEQRES  12 B  312  GLY VAL ALA HIS PHE GLU TYR GLN ILE ARG VAL THR CYS          
SEQRES  13 B  312  ASP ASP TYR TYR TYR GLY PHE GLY CYS ASN LYS PHE CYS          
SEQRES  14 B  312  ARG PRO ARG ASP ASP PHE PHE GLY HIS TYR ALA CYS ASP          
SEQRES  15 B  312  GLN ASN GLY ASN LYS THR CYS MET GLU GLY TRP MET GLY          
SEQRES  16 B  312  PRO GLU CYS ASN ARG ALA ILE CYS ARG GLN GLY CYS SER          
SEQRES  17 B  312  PRO LYS HIS GLY SER CYS LYS LEU PRO GLY ASP CYS ARG          
SEQRES  18 B  312  CYS GLN TYR GLY TRP GLN GLY LEU TYR CYS ASP LYS CYS          
SEQRES  19 B  312  ILE PRO HIS PRO GLY CYS VAL HIS GLY ILE CYS ASN GLU          
SEQRES  20 B  312  PRO TRP GLN CYS LEU CYS GLU THR ASN TRP GLY GLY GLN          
SEQRES  21 B  312  LEU CYS ASP LYS ASP LEU ASN TYR CYS GLY THR HIS GLN          
SEQRES  22 B  312  PRO CYS LEU ASN GLY GLY THR CYS SER ASN THR GLY PRO          
SEQRES  23 B  312  ASP LYS TYR GLN CYS SER CYS PRO GLU GLY TYR SER GLY          
SEQRES  24 B  312  PRO ASN CYS GLU ILE VAL ASP HIS HIS HIS HIS HIS HIS          
MODRES 4CC0 ASN A  217  ASN  GLYCOSYLATION SITE                                 
MODRES 4CC0 THR A  311  THR  GLYCOSYLATION SITE                                 
MODRES 4CC0 ASN B  217  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A   1      14                                                       
HET    FUC  A   2      10                                                       
HET     CA  A1338       1                                                       
HET    NAG  B   1      14                                                       
HET     CA  B1299       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   4  FUC    C6 H12 O5                                                    
FORMUL   5   CA    2(CA 2+)                                                     
FORMUL   8  HOH   *61(H2 O)                                                     
HELIX    1   1 ASN A  298  GLN A  304  1                                   7    
SHEET    1  AA 2 PHE A 107  ASN A 108  0                                        
SHEET    2  AA 2 GLY A  33  GLN A  43 -1  O  MET A  42   N  PHE A 107           
SHEET    1  AB 2 ARG A 119  PHE A 124  0                                        
SHEET    2  AB 2 GLY A  33  GLN A  43 -1  O  GLY A  33   N  PHE A 124           
SHEET    1  AC 4 SER A 164  GLN A 172  0                                        
SHEET    2  AC 4 HIS A 178  CYS A 187 -1  O  PHE A 179   N  GLN A 172           
SHEET    3  AC 4 GLY A  33  GLN A  43 -1  O  GLN A  34   N  THR A 186           
SHEET    4  AC 4 PHE A 107  ASN A 108 -1  O  PHE A 107   N  MET A  42           
SHEET    1  AD 4 SER A 164  GLN A 172  0                                        
SHEET    2  AD 4 HIS A 178  CYS A 187 -1  O  PHE A 179   N  GLN A 172           
SHEET    3  AD 4 GLY A  33  GLN A  43 -1  O  GLN A  34   N  THR A 186           
SHEET    4  AD 4 ARG A 119  PHE A 124 -1  O  ILE A 120   N  LEU A  37           
SHEET    1  AE 4 GLY A  95  SER A  98  0                                        
SHEET    2  AE 4 THR A  73  LYS A  80 -1  O  VAL A  77   N  GLY A  97           
SHEET    3  AE 4 SER A 131  ASP A 140 -1  O  THR A 133   N  LYS A  80           
SHEET    4  AE 4 SER A 150  MET A 160 -1  O  SER A 150   N  ASP A 140           
SHEET    1  AF 2 TYR A 191  TYR A 192  0                                        
SHEET    2  AF 2 LYS A 198  PHE A 199 -1  O  LYS A 198   N  TYR A 192           
SHEET    1  AG 3 ARG A 203  ASP A 205  0                                        
SHEET    2  AG 3 GLY A 208  CYS A 212 -1  O  GLY A 208   N  ASP A 205           
SHEET    3  AG 3 LYS A 218  CYS A 220 -1  O  THR A 219   N  ALA A 211           
SHEET    1  AH 2 TRP A 224  MET A 225  0                                        
SHEET    2  AH 2 ARG A 231  ALA A 232 -1  O  ARG A 231   N  MET A 225           
SHEET    1  AI 2 GLY A 243  SER A 244  0                                        
SHEET    2  AI 2 ARG A 252  CYS A 253 -1  O  ARG A 252   N  SER A 244           
SHEET    1  AJ 2 TRP A 257  GLN A 258  0                                        
SHEET    2  AJ 2 LYS A 264  CYS A 265 -1  O  LYS A 264   N  GLN A 258           
SHEET    1  AK 2 GLY A 274  ILE A 275  0                                        
SHEET    2  AK 2 LEU A 283  CYS A 284 -1  O  LEU A 283   N  ILE A 275           
SHEET    1  AL 2 TRP A 288  GLY A 289  0                                        
SHEET    2  AL 2 LYS A 295  ASP A 296 -1  O  LYS A 295   N  GLY A 289           
SHEET    1  AM 2 THR A 311  GLY A 316  0                                        
SHEET    2  AM 2 LYS A 319  SER A 323 -1  O  LYS A 319   N  THR A 315           
SHEET    1  AN 2 TYR A 328  SER A 329  0                                        
SHEET    2  AN 2 ILE A 335  VAL A 336 -1  O  ILE A 335   N  SER A 329           
SHEET    1  BA 2 PHE B 107  ASN B 108  0                                        
SHEET    2  BA 2 GLY B  33  GLN B  43 -1  O  MET B  42   N  PHE B 107           
SHEET    1  BB 2 ARG B 119  PHE B 124  0                                        
SHEET    2  BB 2 GLY B  33  GLN B  43 -1  O  GLY B  33   N  PHE B 124           
SHEET    1  BC 4 SER B 164  GLN B 172  0                                        
SHEET    2  BC 4 HIS B 178  CYS B 187 -1  O  PHE B 179   N  GLN B 172           
SHEET    3  BC 4 GLY B  33  GLN B  43 -1  O  GLN B  34   N  THR B 186           
SHEET    4  BC 4 PHE B 107  ASN B 108 -1  O  PHE B 107   N  MET B  42           
SHEET    1  BD 4 SER B 164  GLN B 172  0                                        
SHEET    2  BD 4 HIS B 178  CYS B 187 -1  O  PHE B 179   N  GLN B 172           
SHEET    3  BD 4 GLY B  33  GLN B  43 -1  O  GLN B  34   N  THR B 186           
SHEET    4  BD 4 ARG B 119  PHE B 124 -1  O  ILE B 120   N  LEU B  37           
SHEET    1  BE 4 GLY B  95  SER B  98  0                                        
SHEET    2  BE 4 THR B  73  LYS B  80 -1  O  VAL B  77   N  GLY B  97           
SHEET    3  BE 4 SER B 131  ASP B 140 -1  O  THR B 133   N  LYS B  80           
SHEET    4  BE 4 SER B 150  MET B 160 -1  O  SER B 150   N  ASP B 140           
SHEET    1  BF 2 TYR B 191  TYR B 192  0                                        
SHEET    2  BF 2 LYS B 198  PHE B 199 -1  O  LYS B 198   N  TYR B 192           
SHEET    1  BG 3 ARG B 203  ASP B 205  0                                        
SHEET    2  BG 3 GLY B 208  CYS B 212 -1  O  GLY B 208   N  ASP B 205           
SHEET    3  BG 3 LYS B 218  CYS B 220 -1  O  THR B 219   N  ALA B 211           
SHEET    1  BH 2 TRP B 224  MET B 225  0                                        
SHEET    2  BH 2 ARG B 231  ALA B 232 -1  O  ARG B 231   N  MET B 225           
SHEET    1  BI 2 GLY B 243  SER B 244  0                                        
SHEET    2  BI 2 ARG B 252  CYS B 253 -1  O  ARG B 252   N  SER B 244           
SHEET    1  BJ 2 TRP B 257  GLN B 258  0                                        
SHEET    2  BJ 2 LYS B 264  CYS B 265 -1  O  LYS B 264   N  GLN B 258           
SHEET    1  BK 2 GLY B 274  ILE B 275  0                                        
SHEET    2  BK 2 LEU B 283  CYS B 284 -1  O  LEU B 283   N  ILE B 275           
SHEET    1  BL 2 TRP B 288  GLY B 289  0                                        
SHEET    2  BL 2 LYS B 295  ASP B 296 -1  O  LYS B 295   N  GLY B 289           
SSBOND   1 CYS A   54    CYS A   66                          1555   1555  2.04  
SSBOND   2 CYS A   55    CYS A   71                          1555   1555  2.04  
SSBOND   3 CYS A   78    CYS A   92                          1555   1555  2.06  
SSBOND   4 CYS A  187    CYS A  196                          1555   1555  2.09  
SSBOND   5 CYS A  200    CYS A  212                          1555   1555  2.06  
SSBOND   6 CYS A  220    CYS A  229                          1555   1555  2.06  
SSBOND   7 CYS A  234    CYS A  245                          1555   1555  2.05  
SSBOND   8 CYS A  238    CYS A  251                          1555   1555  2.06  
SSBOND   9 CYS A  253    CYS A  262                          1555   1555  2.04  
SSBOND  10 CYS A  265    CYS A  276                          1555   1555  2.09  
SSBOND  11 CYS A  271    CYS A  282                          1555   1555  2.05  
SSBOND  12 CYS A  284    CYS A  293                          1555   1555  2.06  
SSBOND  13 CYS A  300    CYS A  312                          1555   1555  2.04  
SSBOND  14 CYS A  306    CYS A  322                          1555   1555  2.03  
SSBOND  15 CYS A  324    CYS A  333                          1555   1555  2.05  
SSBOND  16 CYS B   54    CYS B   66                          1555   1555  2.03  
SSBOND  17 CYS B   55    CYS B   71                          1555   1555  2.05  
SSBOND  18 CYS B   78    CYS B   92                          1555   1555  2.06  
SSBOND  19 CYS B  187    CYS B  196                          1555   1555  2.08  
SSBOND  20 CYS B  200    CYS B  212                          1555   1555  2.04  
SSBOND  21 CYS B  220    CYS B  229                          1555   1555  2.05  
SSBOND  22 CYS B  234    CYS B  245                          1555   1555  2.05  
SSBOND  23 CYS B  238    CYS B  251                          1555   1555  2.06  
SSBOND  24 CYS B  253    CYS B  262                          1555   1555  2.05  
SSBOND  25 CYS B  265    CYS B  276                          1555   1555  2.08  
SSBOND  26 CYS B  271    CYS B  282                          1555   1555  2.04  
SSBOND  27 CYS B  284    CYS B  293                          1555   1555  2.06  
LINK         C1  NAG A   1                 ND2 ASN A 217     1555   1555  1.44  
LINK         C1  FUC A   2                 OG1 THR A 311     1555   1555  1.42  
LINK         C1  NAG B   1                 ND2 ASN B 217     1555   1555  1.44  
LINK         OD2 ASP A  72                CA    CA A1338     1555   1555  2.41  
LINK         OD2 ASP A 140                CA    CA A1338     1555   1555  2.74  
LINK         OD1 ASP A 140                CA    CA A1338     1555   1555  2.69  
LINK         O   SER A 141                CA    CA A1338     1555   1555  2.40  
LINK        CA    CA A1338                 O   HOH A2005     1555   1555  2.37  
LINK         OD2 ASP B  72                CA    CA B1299     1555   1555  2.30  
LINK         OD2 ASP B 140                CA    CA B1299     1555   1555  2.80  
LINK         OD1 ASP B 140                CA    CA B1299     1555   1555  2.63  
LINK         O   SER B 141                CA    CA B1299     1555   1555  2.78  
CRYST1   55.980   60.250   62.650  92.59 104.44 106.67 P 1           2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017864  0.005349  0.005315        0.00000                         
SCALE2      0.000000  0.017326  0.002197        0.00000                         
SCALE3      0.000000  0.000000  0.016614        0.00000                         
MTRIX1   1 -0.300000 -0.588000  0.751000      -25.87424    1                    
MTRIX2   1 -0.592000 -0.502000 -0.630000       13.52499    1                    
MTRIX3   1  0.748000 -0.634000 -0.198000      -16.70453    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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