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Database: PDB
Entry: 2VJ3
LinkDB: 2VJ3
Original site: 2VJ3 
HEADER    TRANSCRIPTION                           06-DEC-07   2VJ3              
TITLE     HUMAN NOTCH-1 EGFS 11-13                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EGFS 11-13, RESIDUES 411-526;                              
COMPND   5 SYNONYM: NOTCH 1, HN1, TRANSLOCATION-ASSOCIATED NOTCH PROTEIN TAN-1, 
COMPND   6 NOTCH-1;                                                             
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: NM554;                                     
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PQE30                                     
KEYWDS    TRANSCRIPTION, METAL-BINDING, TRANSMEMBRANE, DEVELOPMENTAL PROTEIN,   
KEYWDS   2 NOTCH SIGNALING PATHWAY, DIFFERENTIATION, PHOSPHORYLATION, EGF-LIKE  
KEYWDS   3 DOMAIN, TRANSCRIPTION REGULATION, RECEPTOR, ACTIVATOR, ANK REPEAT,   
KEYWDS   4 SIGNALLING, POLYMORPHISM, GLYCOPROTEIN, EXTRACELLULAR, EGF, NOTCH,   
KEYWDS   5 JAGGED, NUCLEUS, CALCIUM, MEMBRANE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.JOHNSON,J.CORDLE,J.Z.TAY,P.ROVERSI,S.M.LEA                          
REVDAT   4   05-JUL-17 2VJ3    1       REMARK                                   
REVDAT   3   25-AUG-10 2VJ3    1       JRNL   REMARK FORMUL                     
REVDAT   2   24-FEB-09 2VJ3    1       VERSN                                    
REVDAT   1   29-JUL-08 2VJ3    0                                                
JRNL        AUTH   J.CORDLE,S.JOHNSON,J.Z.TAY,P.ROVERSI,M.B.WILKIN,             
JRNL        AUTH 2 B.H.DE MADRID,H.SHIMIZU,S.JENSEN,P.WHITEMAN,B.JIN,           
JRNL        AUTH 3 C.REDFIELD,M.BARON,S.M.LEA,P.A.HANDFORD                      
JRNL        TITL   A CONSERVED FACE OF THE JAGGED/SERRATE DSL DOMAIN IS         
JRNL        TITL 2 INVOLVED IN NOTCH TRANS-ACTIVATION AND CIS-INHIBITION.       
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  15   849 2008              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   18660822                                                     
JRNL        DOI    10.1038/NSMB.1457                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT 5.6.1                                            
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 95.40                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 4080                           
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.239                           
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 190                             
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.2390                 
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.2390                 
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.244                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.00                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 190                    
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 897                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 23                                      
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : 52.500                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.005 ; 2.000 ; 922             
REMARK   3   BOND ANGLES            (DEGREES) : 0.680 ; 2.000 ; 1250            
REMARK   3   TORSION ANGLES         (DEGREES) : 13.600; 0.000 ; 180             
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : 0.001 ; 2.000 ; 35              
REMARK   3   GENERAL PLANES               (A) : 0.020 ; 5.000 ; 132             
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : 1.066 ; 20.000; 922             
REMARK   3   NON-BONDED CONTACTS          (A) : 0.086 ; 5.000 ; 4               
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : 0                                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : BABINET SCALING                                      
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 124.0                                                
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : TNT PROTGEO                                      
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : TNT BCORREL                  
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BUSTER-TNT-GELLY 2.1.1 E. BLANC, P.       
REMARK   3  ROVERSI, C. VONRHEIN, C. FLENSBURG, S. M. LEA AND G.BRICOGNE        
REMARK   4                                                                      
REMARK   4 2VJ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-DEC-07.                  
REMARK 100 THE DEPOSITION ID IS D_1290034695.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-MAR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : BRUKER AXS MICROSTAR               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.542                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 4321                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.570                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.250                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY                : 8.200                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.57                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1EDM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% (W/V) PEG-5000-MME, 100MM SODIUM     
REMARK 280  ACETATE, PH5.7                                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       93.90000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      187.80000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      187.80000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       93.90000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 CA    CA A1534  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   409                                                      
REMARK 465     ALA A   410                                                      
REMARK 465     HIS A   531                                                      
REMARK 465     ILE A   532                                                      
REMARK 465     LEU A   533                                                      
REMARK 465     ASP A   534                                                      
REMARK 465     ALA A   535                                                      
REMARK 465     GLN A   536                                                      
REMARK 465     LYS A   537                                                      
REMARK 465     MET A   538                                                      
REMARK 465     VAL A   539                                                      
REMARK 465     TRP A   540                                                      
REMARK 465     ASN A   541                                                      
REMARK 465     HIS A   542                                                      
REMARK 465     ARG A   543                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLY A   481     O    HOH A  2015              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 435     -148.07   -148.70                                   
REMARK 500    LYS A 508     -157.46   -127.29                                   
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 A1531  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL A 453   O                                                      
REMARK 620 2 GLU A 455   OE1  67.9                                              
REMARK 620 3 ASP A 469   OD1  80.9  74.7                                        
REMARK 620 4 HOH A2007   O    81.9  85.2 157.3                                  
REMARK 620 5 HOH A2009   O   146.8 143.3  95.6 106.9                            
REMARK 620 6 ASP A 452   OD1  93.9 143.7 135.4  60.6  65.5                      
REMARK 620 7 GLN A 470   O   137.2  70.6  97.9  84.8  76.0 114.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1532  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 415   OE1                                                    
REMARK 620 2 HOH A2002   O    84.7                                              
REMARK 620 3 VAL A 413   O    68.3  72.2                                        
REMARK 620 4 ASN A 431   OD1  95.6 166.3  95.1                                  
REMARK 620 5 ASP A 412   OD1 135.6  53.3  83.9 121.7                            
REMARK 620 6 THR A 432   O   143.4 112.1 146.7  75.5  74.8                      
REMARK 620 7 SER A 435   O    74.9 103.7 143.2  89.5 123.9  69.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1533  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 493   OE1                                                    
REMARK 620 2 LYS A 508   O    90.5                                              
REMARK 620 3 HOH A2015   O    84.0 107.5                                        
REMARK 620 4 ASN A 490   OD1 157.2  99.9  73.5                                  
REMARK 620 5 ASP A 507   OD1  68.9  85.7 150.2 131.8                            
REMARK 620 6 ASP A 507   OD2 112.7  85.3 159.2  88.5  43.9                      
REMARK 620 7 THR A 491   O    73.9 159.6  84.3  99.3  76.6  88.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1534  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 511   OE2                                                    
REMARK 620 2 HIS A 523   NE2 101.2                                              
REMARK 620 3 HIS A 523   NE2  99.3 133.3                                        
REMARK 620 4 GLU A 511   OE2 124.1  97.3 104.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1531                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1532                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1533                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1534                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1535                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1536                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1537                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1538                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1TOZ   RELATED DB: PDB                                   
REMARK 900 NMR STRUCTURE OF THE HUMAN NOTCH-1 LIGAND BINDING REGION             
REMARK 900 RELATED ID: 2F8Y   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN NOTCH1 ANKYRIN REPEATS TO                 
REMARK 900 1.55ARESOLUTION.                                                     
REMARK 900 RELATED ID: 1YYH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN NOTCH 1 ANKYRIN DOMAIN                
REMARK 900 RELATED ID: 1PB5   RELATED DB: PDB                                   
REMARK 900 NMR STRUCTURE OF A PROTOTYPE LNR MODULE FROM HUMAN NOTCH1            
REMARK 900 RELATED ID: 2F8X   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED NOTCH, CSL AND MAML ON HES-1PROMOTER  
REMARK 900 DNA SEQUENCE                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 M477I IS A PUBLISHED CONFLICT. THE DETAILS OF WHICH CAN BE           
REMARK 999 FOUND IN HAMBLETON ET AL (2004) STRUCTURE. 12:2173-83                
DBREF  2VJ3 A  409   410  PDB    2VJ3     2VJ3           409    410             
DBREF  2VJ3 A  411   526  UNP    P46531   NOTC1_HUMAN    411    526             
DBREF  2VJ3 A  527   543  PDB    2VJ3     2VJ3           527    543             
SEQADV 2VJ3 ILE A  477  UNP  P46531    MET   477 CONFLICT                       
SEQRES   1 A  135  SER ALA GLN ASP VAL ASP GLU CYS SER LEU GLY ALA ASN          
SEQRES   2 A  135  PRO CYS GLU HIS ALA GLY LYS CYS ILE ASN THR LEU GLY          
SEQRES   3 A  135  SER PHE GLU CYS GLN CYS LEU GLN GLY TYR THR GLY PRO          
SEQRES   4 A  135  ARG CYS GLU ILE ASP VAL ASN GLU CYS VAL SER ASN PRO          
SEQRES   5 A  135  CYS GLN ASN ASP ALA THR CYS LEU ASP GLN ILE GLY GLU          
SEQRES   6 A  135  PHE GLN CYS ILE CYS MET PRO GLY TYR GLU GLY VAL HIS          
SEQRES   7 A  135  CYS GLU VAL ASN THR ASP GLU CYS ALA SER SER PRO CYS          
SEQRES   8 A  135  LEU HIS ASN GLY ARG CYS LEU ASP LYS ILE ASN GLU PHE          
SEQRES   9 A  135  GLN CYS GLU CYS PRO THR GLY PHE THR GLY HIS LEU CYS          
SEQRES  10 A  135  GLN VAL ASP LEU HIS HIS ILE LEU ASP ALA GLN LYS MET          
SEQRES  11 A  135  VAL TRP ASN HIS ARG                                          
HET     CA  A1531       1                                                       
HET     CA  A1532       1                                                       
HET     CA  A1533       1                                                       
HET     CA  A1534       1                                                       
HET     NA  A1535       1                                                       
HET     NA  A1536       1                                                       
HET     CL  A1537       1                                                       
HET     CL  A1538       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   2   CA    4(CA 2+)                                                     
FORMUL   6   NA    2(NA 1+)                                                     
FORMUL   8   CL    2(CL 1-)                                                     
FORMUL  10  HOH   *23(H2 O)                                                     
SHEET    1  AA 2 LYS A 428  ASN A 431  0                                        
SHEET    2  AA 2 PHE A 436  GLN A 439 -1  O  GLU A 437   N  ILE A 430           
SHEET    1  AB 2 TYR A 444  THR A 445  0                                        
SHEET    2  AB 2 ILE A 451  ASP A 452 -1  O  ILE A 451   N  THR A 445           
SHEET    1  AC 2 THR A 466  ASP A 469  0                                        
SHEET    2  AC 2 PHE A 474  ILE A 477 -1  O  GLN A 475   N  LEU A 468           
SHEET    1  AD 2 TYR A 482  GLU A 483  0                                        
SHEET    2  AD 2 VAL A 489  ASN A 490 -1  O  VAL A 489   N  GLU A 483           
SHEET    1  AE 2 ARG A 504  ASP A 507  0                                        
SHEET    2  AE 2 PHE A 512  GLU A 515 -1  O  GLN A 513   N  LEU A 506           
SHEET    1  AF 2 PHE A 520  THR A 521  0                                        
SHEET    2  AF 2 VAL A 527  ASP A 528 -1  O  VAL A 527   N  THR A 521           
SSBOND   1 CYS A  416    CYS A  429                          1555   1555  2.03  
SSBOND   2 CYS A  423    CYS A  438                          1555   1555  2.03  
SSBOND   3 CYS A  440    CYS A  449                          1555   1555  2.03  
SSBOND   4 CYS A  456    CYS A  467                          1555   1555  2.02  
SSBOND   5 CYS A  461    CYS A  476                          1555   1555  2.03  
SSBOND   6 CYS A  478    CYS A  487                          1555   1555  2.03  
SSBOND   7 CYS A  494    CYS A  505                          1555   1555  2.03  
SSBOND   8 CYS A  499    CYS A  514                          1555   1555  2.03  
SSBOND   9 CYS A  516    CYS A  525                          1555   1555  2.03  
LINK        CA    CA A1531                 O   VAL A 453     1555   1555  2.33  
LINK        CA    CA A1531                 OE1 GLU A 455     1555   1555  2.64  
LINK        CA    CA A1531                 OD1 ASP A 469     1555   1555  2.68  
LINK        CA    CA A1531                 O   HOH A2007     1555   1555  2.40  
LINK        CA    CA A1531                 O   HOH A2009     1555   1555  2.43  
LINK        CA    CA A1531                 OD1 ASP A 452     1555   1555  2.95  
LINK        CA    CA A1531                 O   GLN A 470     1555   1555  2.40  
LINK        CA    CA A1532                 OE1 GLU A 415     1555   1555  2.56  
LINK        CA    CA A1532                 O   HOH A2002     1555   1555  2.53  
LINK        CA    CA A1532                 O   VAL A 413     1555   1555  2.59  
LINK        CA    CA A1532                 OD1 ASN A 431     1555   1555  2.44  
LINK        CA    CA A1532                 OD1 ASP A 412     1555   1555  2.82  
LINK        CA    CA A1532                 O   THR A 432     1555   1555  2.60  
LINK        CA    CA A1532                 O   SER A 435     1555   1555  2.40  
LINK        CA    CA A1533                 OE1 GLU A 493     1555   1555  2.59  
LINK        CA    CA A1533                 O   LYS A 508     1555   1555  2.18  
LINK        CA    CA A1533                 O   HOH A2015     1555   1555  2.51  
LINK        CA    CA A1533                 OD1 ASN A 490     1555   1555  2.55  
LINK        CA    CA A1533                 OD1 ASP A 507     1555   1555  2.79  
LINK        CA    CA A1533                 OD2 ASP A 507     1555   1555  3.05  
LINK        CA    CA A1533                 O   THR A 491     1555   1555  2.23  
LINK        CA    CA A1534                 OE2 GLU A 511     1555   5554  2.37  
LINK        CA    CA A1534                 NE2 HIS A 523     1555   1555  2.53  
LINK        CA    CA A1534                 NE2 HIS A 523     1555   5554  2.44  
LINK        CA    CA A1534                 OE2 GLU A 511     1555   1555  2.34  
CISPEP   1 THR A  518    GLY A  519          0        -2.42                     
CISPEP   2 THR A  521    GLY A  522          0        -3.77                     
SITE     1 AC1  7 ASP A 452  VAL A 453  GLU A 455  ASP A 469                    
SITE     2 AC1  7 GLN A 470  HOH A2007  HOH A2009                               
SITE     1 AC2  7 ASP A 412  VAL A 413  GLU A 415  ASN A 431                    
SITE     2 AC2  7 THR A 432  SER A 435  HOH A2002                               
SITE     1 AC3  6 ASN A 490  THR A 491  GLU A 493  ASP A 507                    
SITE     2 AC3  6 LYS A 508  HOH A2015                                          
SITE     1 AC4  2 GLU A 511  HIS A 523                                          
SITE     1 AC5  4 LEU A 524  CYS A 525  GLN A 526   CL A1537                    
SITE     1 AC6  2 GLU A 483  ASP A 528                                          
SITE     1 AC7  3 GLU A 493  ASN A 510   NA A1535                               
SITE     1 AC8  3 GLN A 475  CYS A 476  VAL A 485                               
CRYST1   28.000   28.000  281.700  90.00  90.00 120.00 P 31 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.035733  0.020630  0.000000        0.00000                         
SCALE2      0.000000  0.041260  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003549        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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