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Database: PDB
Entry: 5FM9
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Original site: 5FM9 
HEADER    TRANSCRIPTION                           02-NOV-15   5FM9              
TITLE     HUMAN NOTCH 1, EGF 4-7                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EGF DOMAINS 4-7, UNP RESIDUES 140-294;                     
COMPND   5 SYNONYM: NOTCH 1, HN1, TRANSLOCATION-ASSOCIATED NOTCH PROTEIN TAN-1, 
COMPND   6 NOTCH 1 EXTRACELLULAR TRUNCATION, NEXT, NOTCH 1 INTRACELLULAR DOMAIN,
COMPND   7 NICD;                                                                
COMPND   8 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: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PQE30                                     
KEYWDS    TRANSCRIPTION, TRANSMEMBRANE, DEVELOPMENTAL, PROTEIN, NOTCH SIGNALING 
KEYWDS   2 PATHWAY, DIFFERENTIATION, PHOSPHORYLATION, EGF- LIKE DOMAIN,         
KEYWDS   3 REGULATION, RECEPTOR, ACTIVATOR, ANK REPEAT, SIGNALLING,             
KEYWDS   4 GLYCOPROTEIN, EXTRACELLULAR, EGF, NOTCH, JAGGED, MEMBRANE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.C.WEISSHUHN,D.SHEPPARD,P.TAYLOR,P.WHITEMAN,S.M.LEA,P.A.HANDFORD,    
AUTHOR   2 C.REDFIELD                                                           
REVDAT   2   07-FEB-18 5FM9    1       AUTHOR                                   
REVDAT   1   20-APR-16 5FM9    0                                                
JRNL        AUTH   P.C.WEISSHUHN,D.SHEPPARD,P.TAYLOR,P.WHITEMAN,S.M.LEA,        
JRNL        AUTH 2 P.A.HANDFORD,C.REDFIELD                                      
JRNL        TITL   NON-LINEAR AND FLEXIBLE REGIONS OF THE HUMAN NOTCH1          
JRNL        TITL 2 EXTRACELLULAR DOMAIN REVEALED BY HIGH-RESOLUTION STRUCTURAL  
JRNL        TITL 3 STUDIES.                                                     
JRNL        REF    STRUCTURE                     V.  24   555 2016              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   26996961                                                     
JRNL        DOI    10.1016/J.STR.2016.02.010                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.92 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) : 2.92                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 64.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 5014                           
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)  : 0.214                          
REMARK   3   R VALUE            (WORKING SET)  : 0.213                          
REMARK   3   FREE R VALUE                      : 0.237                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.650                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 233                            
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) : 2.92                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.26                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 95.67                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 1377                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2453                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 1302                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2435                   
REMARK   3   BIN FREE R VALUE                        : 0.2754                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.45                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 75                       
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            : 1125                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 6                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.62                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -15.57360                                            
REMARK   3    B22 (A**2) : 5.41930                                              
REMARK   3    B33 (A**2) : 10.15430                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -8.46850                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.426               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 1.558               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.338               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
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      : 0.884                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.864                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2143   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3853   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 416    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 34     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 353    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2143   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 2      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 148    ; 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   : 2243   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.23                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.27                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.82                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.    
REMARK   3  RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=CA. NUMBER OF       
REMARK   3  ATOMS WITH PROPER CCP4 ATOM TYPE=2105. NUMBER WITH APPROX           
REMARK   3  DEFAULT CCP4 ATOM TYPE=0. NUMBER TREATED BY BAD NON-BONDED          
REMARK   3  CONTACTS=2.                                                         
REMARK   4                                                                      
REMARK   4 5FM9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-NOV-15.                  
REMARK 100 THE DEPOSITION ID IS D_1290065332.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-FEB-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.75                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 5015                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.920                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 64.730                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.92                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
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: 2VJ3.PDB                                             
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       71.13000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       10.57500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       71.13000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       10.57500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 920 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 19210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.4 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000     -105.27620            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -74.92978            
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   138                                                      
REMARK 465     ALA A   139                                                      
REMARK 465     GLN A   140                                                      
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    ASN A 151       36.47     39.54                                   
REMARK 500    GLU A 159     -134.18     52.65                                   
REMARK 500    SER A 161     -143.43    -96.58                                   
REMARK 500    SER A 201     -163.22   -174.49                                   
REMARK 500    SER A 223      103.62   -161.88                                   
REMARK 500    PRO A 285        1.87    -60.60                                   
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 A1295  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 197   OD1                                                    
REMARK 620 2 GLU A 181   OE1  91.5                                              
REMARK 620 3 SER A 201   O    89.8  79.5                                        
REMARK 620 4 HOH A2001   O   164.1  83.7 104.2                                  
REMARK 620 5 VAL A 179   O    79.5  76.8 153.7  84.6                            
REMARK 620 6 ASP A 178   OD2  70.4 141.9 131.5 104.4  67.3                      
REMARK 620 7 GLU A 198   O    78.6 149.4  71.6 112.8 128.4  61.4                
REMARK 620 8 ASP A 178   OD1 115.5 132.5 134.7  59.5  71.2  45.4  77.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1296  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 257   OD1                                                    
REMARK 620 2 ASP A 260   OD1 147.2                                              
REMARK 620 3 ASP A 274   OD1 116.7  88.5                                        
REMARK 620 4 ASP A 274   OD2  70.5 120.9  49.9                                  
REMARK 620 5 GLY A 275   O    88.5 109.0  99.0 116.5                            
REMARK 620 6 HOH A2006   O    87.1  73.7 154.3 155.7  70.7                      
REMARK 620 7 ILE A 258   O    86.8  72.8  87.9  66.8 172.9 103.7                
REMARK 620 N                    1     2     3     4     5     6                 
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 1295                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1296                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5FMA   RELATED DB: PDB                                   
REMARK 900 HUMAN NOTCH 1, EGF 4-7                                               
DBREF  5FM9 A  140   294  UNP    P46531   NOTC1_HUMAN    140    294             
SEQADV 5FM9 SER A  138  UNP  P46531              EXPRESSION TAG                 
SEQADV 5FM9 ALA A  139  UNP  P46531              EXPRESSION TAG                 
SEQRES   1 A  157  SER ALA GLN ALA ASP PRO CYS ALA SER ASN PRO CYS ALA          
SEQRES   2 A  157  ASN GLY GLY GLN CYS LEU PRO PHE GLU ALA SER TYR ILE          
SEQRES   3 A  157  CYS HIS CYS PRO PRO SER PHE HIS GLY PRO THR CYS ARG          
SEQRES   4 A  157  GLN ASP VAL ASN GLU CYS GLY GLN LYS PRO GLY LEU CYS          
SEQRES   5 A  157  ARG HIS GLY GLY THR CYS HIS ASN GLU VAL GLY SER TYR          
SEQRES   6 A  157  ARG CYS VAL CYS ARG ALA THR HIS THR GLY PRO ASN CYS          
SEQRES   7 A  157  GLU ARG PRO TYR VAL PRO CYS SER PRO SER PRO CYS GLN          
SEQRES   8 A  157  ASN GLY GLY THR CYS ARG PRO THR GLY ASP VAL THR HIS          
SEQRES   9 A  157  GLU CYS ALA CYS LEU PRO GLY PHE THR GLY GLN ASN CYS          
SEQRES  10 A  157  GLU GLU ASN ILE ASP ASP CYS PRO GLY ASN ASN CYS LYS          
SEQRES  11 A  157  ASN GLY GLY ALA CYS VAL ASP GLY VAL ASN THR TYR ASN          
SEQRES  12 A  157  CYS ARG CYS PRO PRO GLU TRP THR GLY GLN TYR CYS THR          
SEQRES  13 A  157  GLU                                                          
HET     CA  A1295       1                                                       
HET     CA  A1296       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   2   CA    2(CA 2+)                                                     
FORMUL   4  HOH   *6(H2 O)                                                      
HELIX    1   1 ASP A  142  ASN A  147  5                                   6    
HELIX    2   2 ASN A  180  LYS A  185  1                                   6    
SHEET    1  AA 2 GLN A 154  PHE A 158  0                                        
SHEET    2  AA 2 SER A 161  HIS A 165 -1  O  SER A 161   N  PHE A 158           
SHEET    1  AB 2 PHE A 170  HIS A 171  0                                        
SHEET    2  AB 2 GLN A 177  ASP A 178 -1  O  GLN A 177   N  HIS A 171           
SHEET    1  AC 2 THR A 194  GLU A 198  0                                        
SHEET    2  AC 2 SER A 201  VAL A 205 -1  O  SER A 201   N  GLU A 198           
SHEET    1  AD 2 HIS A 210  THR A 211  0                                        
SHEET    2  AD 2 ARG A 217  PRO A 218 -1  O  ARG A 217   N  THR A 211           
SHEET    1  AE 2 THR A 232  CYS A 233  0                                        
SHEET    2  AE 2 CYS A 243  ALA A 244 -1  O  ALA A 244   N  THR A 232           
SHEET    1  AF 2 PHE A 249  THR A 250  0                                        
SHEET    2  AF 2 GLU A 256  ASN A 257 -1  O  GLU A 256   N  THR A 250           
SHEET    1  AG 2 ALA A 271  ASP A 274  0                                        
SHEET    2  AG 2 TYR A 279  ARG A 282 -1  O  ASN A 280   N  VAL A 273           
SSBOND   1 CYS A  144    CYS A  155                          1555   1555  2.08  
SSBOND   2 CYS A  149    CYS A  164                          1555   1555  2.02  
SSBOND   3 CYS A  166    CYS A  175                          1555   1555  2.05  
SSBOND   4 CYS A  182    CYS A  195                          1555   1555  2.05  
SSBOND   5 CYS A  189    CYS A  204                          1555   1555  2.04  
SSBOND   6 CYS A  206    CYS A  215                          1555   1555  2.06  
SSBOND   7 CYS A  222    CYS A  233                          1555   1555  2.05  
SSBOND   8 CYS A  227    CYS A  243                          1555   1555  2.03  
SSBOND   9 CYS A  245    CYS A  254                          1555   1555  2.05  
SSBOND  10 CYS A  261    CYS A  272                          1555   1555  2.07  
SSBOND  11 CYS A  266    CYS A  281                          1555   1555  2.04  
SSBOND  12 CYS A  283    CYS A  292                          1555   1555  2.04  
LINK        CA    CA A1295                 OD1 ASN A 197     1555   1555  2.32  
LINK        CA    CA A1295                 OE1 GLU A 181     1555   1555  2.14  
LINK        CA    CA A1295                 O   SER A 201     1555   1555  2.45  
LINK        CA    CA A1295                 O   HOH A2001     1555   1555  2.55  
LINK        CA    CA A1295                 O   VAL A 179     1555   1555  2.69  
LINK        CA    CA A1295                 OD2 ASP A 178     1555   1555  3.01  
LINK        CA    CA A1295                 O   GLU A 198     1555   1555  2.39  
LINK        CA    CA A1295                 OD1 ASP A 178     1555   1555  2.57  
LINK        CA    CA A1296                 OD1 ASN A 257     1555   1555  2.32  
LINK        CA    CA A1296                 OD1 ASP A 260     1555   1555  2.17  
LINK        CA    CA A1296                 OD1 ASP A 274     1555   1555  2.08  
LINK        CA    CA A1296                 OD2 ASP A 274     1555   1555  2.86  
LINK        CA    CA A1296                 O   GLY A 275     1555   1555  2.42  
LINK        CA    CA A1296                 O   HOH A2006     1555   1555  2.31  
LINK        CA    CA A1296                 O   ILE A 258     1555   1555  2.50  
CISPEP   1 SER A  223    PRO A  224          0        -0.62                     
SITE     1 AC1  7 ASP A 178  VAL A 179  GLU A 181  ASN A 197                    
SITE     2 AC1  7 GLU A 198  SER A 201  HOH A2001                               
SITE     1 AC2  6 ASN A 257  ILE A 258  ASP A 260  ASP A 274                    
SITE     2 AC2  6 GLY A 275  HOH A2006                                          
CRYST1  142.260   21.150   83.560  90.00 116.27  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007029  0.000000  0.003470        0.00000                         
SCALE2      0.000000  0.047281  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013346        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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