GenomeNet

Database: PDB
Entry: 4D0E
LinkDB: 4D0E
Original site: 4D0E 
HEADER    TRANSCRIPTION                           25-APR-14   4D0E              
TITLE     HUMAN NOTCH1 EGF DOMAINS 11-13 MUTANT GLCNAC-FUCOSE DISACCHARIDE      
TITLE    2 MODIFIED AT T466                                                     
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: NOTCH 1, HN1, TRANSLOCATION-ASSOCIATED NOTCH PROTEIN TAN-1, 
COMPND   6 NOTCH;                                                               
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: GLCNAC, O-FUCOSE DISSACCHARIDE AT T466                
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, NOTCH     
KEYWDS   2 SIGNALING PATHWAY, DIFFERENTIATION, PHOSPHORYLATION, EGF-LIKE        
KEYWDS   3 DOMAIN, REGULATION, RECEPTOR, ACTIVATOR, ANK REPEAT, SIGNALLING,     
KEYWDS   4 GLYCOPROTEIN, EXTRACELLULAR, 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   3   07-FEB-18 4D0E    1       AUTHOR                                   
REVDAT   2   04-JUN-14 4D0E    1       JRNL                                     
REVDAT   1   21-MAY-14 4D0E    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.    1.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.07                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 16974                          
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) : 0.232                           
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 889                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.61                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.65                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1031                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4200                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 54                           
REMARK   3   BIN FREE R VALUE                    : 0.4040                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 914                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 141                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : -0.06000                                             
REMARK   3    B33 (A**2) : 0.10000                                              
REMARK   3    B12 (A**2) : -0.03000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.112         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.113         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.094         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.912         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   966 ; 0.006 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1319 ; 1.103 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   121 ; 5.625 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    48 ;40.486 ;26.667       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   146 ;12.380 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     2 ;26.665 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   147 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   739 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4D0E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-APR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290059192.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.917                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16974                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.610                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.070                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.61                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.65                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
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   (%): 44.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0                                   
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       94.13000            
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      188.26000            
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      188.26000            
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       94.13000            
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 A1535  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A2112  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     GLN A   411                                                      
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    HOH A  2013     O    HOH A  2014              2.02            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  2042     O    HOH A  2053     6655     1.86            
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    LEU A 418     -165.46   -107.70                                   
REMARK 500    SER A 435     -151.72   -152.28                                   
REMARK 500    LYS A 508     -165.04   -125.65                                   
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 124.6                                              
REMARK 620 3 HOH A2060   O   153.2  76.0                                        
REMARK 620 4 GLN A 470   O    95.7 124.1  82.6                                  
REMARK 620 5 HOH A2066   O    80.9  74.9 123.9  75.9                            
REMARK 620 6 GLU A 455   OE1  76.1 142.0  77.4  78.3 143.2                      
REMARK 620 7 VAL A 453   O    84.9  75.8  84.5 152.2 131.3  74.9                
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 LYS A 508   O                                                      
REMARK 620 2 HOH A2095   O    90.2                                              
REMARK 620 3 ASN A 490   OD1 105.3  80.2                                        
REMARK 620 4 THR A 491   O   166.3  84.0  85.9                                  
REMARK 620 5 GLU A 493   OE1  82.5  73.5 152.6  83.9                            
REMARK 620 6 ASP A 507   OD1  92.5 143.7 133.3  85.1  71.0                      
REMARK 620 7 ASP A 507   OD2  92.6 164.8  84.6  96.3 121.8  51.1                
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 VAL A 413   O                                                      
REMARK 620 2 ASN A 431   OD1  88.6                                              
REMARK 620 3 THR A 432   O   147.1  84.2                                        
REMARK 620 4 SER A 435   O   143.8  85.6  67.5                                  
REMARK 620 5 HOH A2023   O    82.2 160.1 112.8  91.5                            
REMARK 620 6 ASP A 412   OD2  68.6  82.0  78.6 144.9 110.6                      
REMARK 620 7 ASP A 412   OD1  79.0 126.8  79.9 131.5  68.7  45.2                
REMARK 620 8 GLU A 415   OE1  70.5  82.9 139.5  73.3  77.4 136.6 136.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1535  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 523   NE2                                                    
REMARK 620 2 GLU A 511   OE2  98.1                                              
REMARK 620 3 HIS A 523   NE2 135.5  89.5                                        
REMARK 620 4 GLU A 511   OE2  89.8 158.2  99.0                                  
REMARK 620 5 GLU A 511   OE1  95.8  49.9 121.2 109.2                            
REMARK 620 6 GLU A 511   OE1 121.5 109.0  96.4  50.3  68.2                      
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 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1535                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG A    
REMARK 800  1 through FUC A1381 bound to THR A 466                              
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4D0F   RELATED DB: PDB                                   
REMARK 900 HUMAN NOTCH-1 EGFS 11-13 T466A                                       
DBREF  4D0E A  411   526  UNP    P46531   NOTC1_HUMAN    411    526             
SEQADV 4D0E SER A  409  UNP  P46531              EXPRESSION TAG                 
SEQADV 4D0E ALA A  410  UNP  P46531              EXPRESSION TAG                 
SEQADV 4D0E VAL A  527  UNP  P46531              EXPRESSION TAG                 
SEQADV 4D0E ASP A  528  UNP  P46531              EXPRESSION TAG                 
SEQADV 4D0E LEU A  529  UNP  P46531              EXPRESSION TAG                 
SEQADV 4D0E HIS A  530  UNP  P46531              EXPRESSION TAG                 
SEQADV 4D0E HIS A  531  UNP  P46531              EXPRESSION TAG                 
SEQADV 4D0E ILE A  532  UNP  P46531              EXPRESSION TAG                 
SEQADV 4D0E LEU A  533  UNP  P46531              EXPRESSION TAG                 
SEQADV 4D0E ASP A  534  UNP  P46531              EXPRESSION TAG                 
SEQADV 4D0E ALA A  535  UNP  P46531              EXPRESSION TAG                 
SEQADV 4D0E GLN A  536  UNP  P46531              EXPRESSION TAG                 
SEQADV 4D0E LYS A  537  UNP  P46531              EXPRESSION TAG                 
SEQADV 4D0E MET A  538  UNP  P46531              EXPRESSION TAG                 
SEQADV 4D0E VAL A  539  UNP  P46531              EXPRESSION TAG                 
SEQADV 4D0E TRP A  540  UNP  P46531              EXPRESSION TAG                 
SEQADV 4D0E ASN A  541  UNP  P46531              EXPRESSION TAG                 
SEQADV 4D0E HIS A  542  UNP  P46531              EXPRESSION TAG                 
SEQADV 4D0E ARG A  543  UNP  P46531              EXPRESSION TAG                 
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                                          
MODRES 4D0E THR A  466  THR  GLYCOSYLATION SITE                                 
HET    NAG  A   1      14                                                       
HET    FUC  A1381      10                                                       
HET     CA  A1531       1                                                       
HET     CA  A1532       1                                                       
HET     CA  A1533       1                                                       
HET     CA  A1535       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM      CA CALCIUM ION                                                      
FORMUL   2  NAG    C8 H15 N O6                                                  
FORMUL   2  FUC    C6 H12 O5                                                    
FORMUL   3   CA    4(CA 2+)                                                     
FORMUL   7  HOH   *141(H2 O)                                                    
HELIX    1   1 ASP A  414  LEU A  418  5                                   5    
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 THR 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  2.04  
SSBOND   2 CYS A  423    CYS A  438                          1555   1555  2.04  
SSBOND   3 CYS A  440    CYS A  449                          1555   1555  2.05  
SSBOND   4 CYS A  456    CYS A  467                          1555   1555  2.04  
SSBOND   5 CYS A  461    CYS A  476                          1555   1555  2.02  
SSBOND   6 CYS A  478    CYS A  487                          1555   1555  2.04  
SSBOND   7 CYS A  494    CYS A  505                          1555   1555  2.05  
SSBOND   8 CYS A  499    CYS A  514                          1555   1555  2.03  
SSBOND   9 CYS A  516    CYS A  525                          1555   1555  2.04  
LINK         C1  NAG A   1                 O3  FUC A1381     1555   1555  1.44  
LINK         OG1 THR A 466                 C1  FUC A1381     1555   1555  1.44  
LINK        CA    CA A1531                 OD1 ASP A 469     1555   1555  2.42  
LINK        CA    CA A1531                 OD1 ASP A 452     1555   1555  2.43  
LINK        CA    CA A1531                 O   HOH A2060     1555   1555  2.42  
LINK        CA    CA A1531                 O   GLN A 470     1555   1555  2.31  
LINK        CA    CA A1531                 O   HOH A2066     1555   1555  2.38  
LINK        CA    CA A1531                 OE1 GLU A 455     1555   1555  2.43  
LINK        CA    CA A1531                 O   VAL A 453     1555   1555  2.29  
LINK        CA    CA A1532                 O   LYS A 508     1555   1555  2.31  
LINK        CA    CA A1532                 O   HOH A2095     1555   1555  2.48  
LINK        CA    CA A1532                 OD1 ASN A 490     1555   1555  2.33  
LINK        CA    CA A1532                 O   THR A 491     1555   1555  2.28  
LINK        CA    CA A1532                 OE1 GLU A 493     1555   1555  2.29  
LINK        CA    CA A1532                 OD1 ASP A 507     1555   1555  2.59  
LINK        CA    CA A1532                 OD2 ASP A 507     1555   1555  2.48  
LINK        CA    CA A1533                 O   VAL A 413     1555   1555  2.43  
LINK        CA    CA A1533                 OD1 ASN A 431     1555   1555  2.40  
LINK        CA    CA A1533                 O   THR A 432     1555   1555  2.35  
LINK        CA    CA A1533                 O   SER A 435     1555   1555  2.41  
LINK        CA    CA A1533                 O   HOH A2023     1555   1555  2.53  
LINK        CA    CA A1533                 OD2 ASP A 412     1555   1555  3.05  
LINK        CA    CA A1533                 OD1 ASP A 412     1555   1555  2.50  
LINK        CA    CA A1533                 OE1 GLU A 415     1555   1555  2.47  
LINK        CA    CA A1535                 NE2 HIS A 523     1555   1555  2.43  
LINK        CA    CA A1535                 OE2 GLU A 511     1555   4645  2.29  
LINK        CA    CA A1535                 NE2 HIS A 523     1555   4645  2.42  
LINK        CA    CA A1535                 OE2 GLU A 511     1555   1555  2.26  
LINK        CA    CA A1535                 OE1 GLU A 511     1555   4645  2.78  
LINK        CA    CA A1535                 OE1 GLU A 511     1555   1555  2.76  
SITE     1 AC1  7 ASP A 452  VAL A 453  GLU A 455  ASP A 469                    
SITE     2 AC1  7 GLN A 470  HOH A2060  HOH A2066                               
SITE     1 AC2  6 ASN A 490  THR A 491  GLU A 493  ASP A 507                    
SITE     2 AC2  6 LYS A 508  HOH A2095                                          
SITE     1 AC3  7 ASP A 412  VAL A 413  GLU A 415  ASN A 431                    
SITE     2 AC3  7 THR A 432  SER A 435  HOH A2023                               
SITE     1 AC4  2 GLU A 511  HIS A 523                                          
SITE     1 AC5  8 ASP A 464  THR A 466  ILE A 477  CYS A 478                    
SITE     2 AC5  8 MET A 479  ASP A 528  HOH A2018  HOH A2141                    
CRYST1   28.440   28.440  282.390  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      0.035162  0.020301  0.000000        0.00000                         
SCALE2      0.000000  0.040601  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003541        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system