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Database: PDB
Entry: 4CUF
LinkDB: 4CUF
Original site: 4CUF 
HEADER    TRANSCRIPTION                           18-MAR-14   4CUF              
TITLE     HUMAN NOTCH1 EGF DOMAINS 11-13 MUTANT T466S                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EGF 11-13, RESIDUES 411-526;                               
COMPND   5 SYNONYM: HUMAN NOTCH, NOTCH 1, HN1, TRANSLOCATION-ASSOCIATED NOTCH   
COMPND   6 PROTEIN TAN-1, NOTCH 1 EXTRACELLULAR TRUNCATION, NEXT, NOTCH 1       
COMPND   7 INTRACELLULAR DOMAIN, NICD;                                          
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: 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_VECTOR_TYPE: PLASMID;                              
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, REGULATION, RECEPTOR, ACTIVATOR, ANK REPEAT, SIGNALLING,     
KEYWDS   4 GLYCOPROTEIN, EXTRACELLULAR, EGF, JAGGED, NUCLEUS, MEMBRANE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.TAYLOR,H.TAKEUCHI,D.SHEPPARD,C.CHILLAKURI,S.M.LEA,R.S.HALTIWANGER,  
AUTHOR   2 P.A.HANDFORD                                                         
REVDAT   4   07-FEB-18 4CUF    1       AUTHOR                                   
REVDAT   3   22-OCT-14 4CUF    1       JRNL                                     
REVDAT   2   28-MAY-14 4CUF    1       HETATM                                   
REVDAT   1   14-MAY-14 4CUF    0                                                
JRNL        AUTH   P.TAYLOR,H.TAKEUCHI,D.SHEPPARD,C.CHILLAKURI,S.M.LEA,         
JRNL        AUTH 2 R.S.HALTIWANGER,P.A.HANDFORD                                 
JRNL        TITL   FRINGE-MEDIATED EXTENSION OF O-LINKED FUCOSE IN THE          
JRNL        TITL 2 LIGAND-BINDING REGION OF NOTCH1 INCREASES BINDING TO         
JRNL        TITL 3 MAMMALIAN NOTCH LIGANDS.                                     
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 111  7290 2014              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   24803430                                                     
JRNL        DOI    10.1073/PNAS.1319683111                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.29 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.2                                        
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) : 2.29                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 17.66                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 6676                           
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)  : 0.257                          
REMARK   3   R VALUE            (WORKING SET)  : 0.256                          
REMARK   3   FREE R VALUE                      : 0.287                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.720                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 315                            
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               : 5                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.29                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.56                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 96.49                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 1855                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2584                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 1763                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2534                   
REMARK   3   BIN FREE R VALUE                        : 0.3443                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.96                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 92                       
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            : 905                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 7                                       
REMARK   3   SOLVENT ATOMS            : 5                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 56.59                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 93.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -11.25450                                            
REMARK   3    B22 (A**2) : -11.25450                                            
REMARK   3    B33 (A**2) : 22.50910                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.810               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.358               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.253               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.325               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.243               
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      : 0.909                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.903                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 940    ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 1282   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 317    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 34     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 134    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 940    ; 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   : 121    ; 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   : 1043   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.15                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.93                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.22                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   16.9188  -17.9748    1.5113           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.2812 T22:    0.0374                                    
REMARK   3     T33:   -0.3127 T12:   -0.3967                                    
REMARK   3     T13:    0.1197 T23:   -0.0119                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.4497 L22:    0.2343                                    
REMARK   3     L33:   14.7574 L12:    0.6214                                    
REMARK   3     L13:    0.9458 L23:   -0.4972                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0657 S12:    0.0693 S13:   -0.1342                     
REMARK   3     S21:    0.1482 S22:    0.1943 S23:   -0.0062                     
REMARK   3     S31:   -1.4423 S32:    0.3212 S33:   -0.2600                     
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=920. NUMBER WITH APPROX DEFAUL     
REMARK   3  CCP4 ATOM TYPE=0. NUMBER TREATED BY BAD NON-BONDED CONTACTS=3.      
REMARK   4                                                                      
REMARK   4 4CUF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-MAR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290059349.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-APR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9797                             
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 : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6676                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.290                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 63.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2VJ3                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
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   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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       42.18667            
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       84.37333            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       63.28000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      105.46667            
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       21.09333            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       42.18667            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       84.37333            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      105.46667            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       63.28000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       21.09333            
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 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     GLN A   411                                                      
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: 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     -152.02   -162.53                                   
REMARK 500    LYS A 508     -167.33   -125.72                                   
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 ASP A 469   OD1                                                    
REMARK 620 2 ASP A 452   OD1 126.6                                              
REMARK 620 3 VAL A 453   O    81.2  79.3                                        
REMARK 620 4 GLU A 455   OE1  73.7 141.8  72.2                                  
REMARK 620 5 GLN A 470   O    94.6 126.7 146.7  75.0                            
REMARK 620 N                    1     2     3     4                             
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 493   OE1                                                    
REMARK 620 2 ASN A 490   OD1 151.7                                              
REMARK 620 3 THR A 491   O    81.2  88.3                                        
REMARK 620 4 ASP A 507   OD1  70.7 134.5  84.0                                  
REMARK 620 5 ASP A 507   OD2 122.0  85.3  97.4  51.8                            
REMARK 620 6 LYS A 508   O    81.6 104.6 162.1  95.2  96.0                      
REMARK 620 N                    1     2     3     4     5                       
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 SER A 435   O                                                      
REMARK 620 2 VAL A 413   O   153.6                                              
REMARK 620 3 HOH A2001   O   146.9  57.1                                        
REMARK 620 4 THR A 432   O    66.9 135.7  80.1                                  
REMARK 620 5 ASN A 431   OD1  85.4  86.1  86.8  80.4                            
REMARK 620 6 GLU A 415   OE1  78.2  75.9 132.4 142.1  82.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 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 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CUD   RELATED DB: PDB                                   
REMARK 900 HUMAN NOTCH-1 EGFS 11-13 FUCOSE                                      
REMARK 900 RELATED ID: 4CUE   RELATED DB: PDB                                   
REMARK 900 HUMAN NOTCH-1 EGFS 11-13                                             
DBREF  4CUF A  411   526  UNP    P46531   NOTC1_HUMAN    411    526             
SEQADV 4CUF SER A  409  UNP  P46531              EXPRESSION TAG                 
SEQADV 4CUF ALA A  410  UNP  P46531              EXPRESSION TAG                 
SEQADV 4CUF VAL A  527  UNP  P46531              EXPRESSION TAG                 
SEQADV 4CUF ASP A  528  UNP  P46531              EXPRESSION TAG                 
SEQADV 4CUF LEU A  529  UNP  P46531              EXPRESSION TAG                 
SEQADV 4CUF HIS A  530  UNP  P46531              EXPRESSION TAG                 
SEQADV 4CUF HIS A  531  UNP  P46531              EXPRESSION TAG                 
SEQADV 4CUF ILE A  532  UNP  P46531              EXPRESSION TAG                 
SEQADV 4CUF LEU A  533  UNP  P46531              EXPRESSION TAG                 
SEQADV 4CUF ASP A  534  UNP  P46531              EXPRESSION TAG                 
SEQADV 4CUF ALA A  535  UNP  P46531              EXPRESSION TAG                 
SEQADV 4CUF GLN A  536  UNP  P46531              EXPRESSION TAG                 
SEQADV 4CUF LYS A  537  UNP  P46531              EXPRESSION TAG                 
SEQADV 4CUF MET A  538  UNP  P46531              EXPRESSION TAG                 
SEQADV 4CUF VAL A  539  UNP  P46531              EXPRESSION TAG                 
SEQADV 4CUF TRP A  540  UNP  P46531              EXPRESSION TAG                 
SEQADV 4CUF ASN A  541  UNP  P46531              EXPRESSION TAG                 
SEQADV 4CUF HIS A  542  UNP  P46531              EXPRESSION TAG                 
SEQADV 4CUF ARG A  543  UNP  P46531              EXPRESSION TAG                 
SEQADV 4CUF SER A  466  UNP  P46531    THR   466 ENGINEERED MUTATION            
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 SER 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    EDO  A1534      10                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2   CA    3(CA 2+)                                                     
FORMUL   5  EDO    C2 H6 O2                                                     
FORMUL   6  HOH   *5(H2 O)                                                      
SHEET    1  AA 2 LYS A 428  THR A 432  0                                        
SHEET    2  AA 2 SER A 435  GLN A 439 -1  O  SER A 435   N  THR A 432           
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 SER A 466  GLN A 470  0                                        
SHEET    2  AC 2 GLU A 473  ILE A 477 -1  O  GLU A 473   N  GLN A 470           
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  2.05  
SSBOND   4 CYS A  456    CYS A  467                          1555   1555  2.05  
SSBOND   5 CYS A  461    CYS A  476                          1555   1555  2.01  
SSBOND   6 CYS A  478    CYS A  487                          1555   1555  2.04  
SSBOND   7 CYS A  494    CYS A  505                          1555   1555  2.07  
SSBOND   8 CYS A  499    CYS A  514                          1555   1555  2.04  
SSBOND   9 CYS A  516    CYS A  525                          1555   1555  2.06  
LINK        CA    CA A1531                 OD1 ASP A 469     1555   1555  2.48  
LINK        CA    CA A1531                 OD1 ASP A 452     1555   1555  2.33  
LINK        CA    CA A1531                 O   VAL A 453     1555   1555  2.32  
LINK        CA    CA A1531                 OE1 GLU A 455     1555   1555  2.55  
LINK        CA    CA A1531                 O   GLN A 470     1555   1555  2.30  
LINK        CA    CA A1532                 OE1 GLU A 493     1555   1555  2.37  
LINK        CA    CA A1532                 OD1 ASN A 490     1555   1555  2.25  
LINK        CA    CA A1532                 O   THR A 491     1555   1555  2.31  
LINK        CA    CA A1532                 OD1 ASP A 507     1555   1555  2.56  
LINK        CA    CA A1532                 OD2 ASP A 507     1555   1555  2.43  
LINK        CA    CA A1532                 O   LYS A 508     1555   1555  2.23  
LINK        CA    CA A1533                 O   SER A 435     1555   1555  2.34  
LINK        CA    CA A1533                 O   VAL A 413     1555   1555  2.42  
LINK        CA    CA A1533                 O   HOH A2001     1555   1555  3.02  
LINK        CA    CA A1533                 O   THR A 432     1555   1555  2.42  
LINK        CA    CA A1533                 OD1 ASN A 431     1555   1555  2.50  
LINK        CA    CA A1533                 OE1 GLU A 415     1555   1555  2.34  
SITE     1 AC1  5 ASP A 452  VAL A 453  GLU A 455  ASP A 469                    
SITE     2 AC1  5 GLN A 470                                                     
SITE     1 AC2  5 ASN A 490  THR A 491  GLU A 493  ASP A 507                    
SITE     2 AC2  5 LYS A 508                                                     
SITE     1 AC3  6 VAL A 413  GLU A 415  ASN A 431  THR A 432                    
SITE     2 AC3  6 SER A 435  HOH A2001                                          
CRYST1   61.770   61.770  126.560  90.00  90.00 120.00 P 61 2 2     12          
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      0.016189  0.009347  0.000000        0.00000                         
SCALE2      0.000000  0.018694  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007901        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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