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Database: PDB
Entry: 5FMA
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Original site: 5FMA 
HEADER    TRANSCRIPTION                           02-NOV-15   5FMA              
TITLE     HUMAN NOTCH 1, EGF 4-7                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: EGF DOMAINS 4-7, RESIDUES 142-294;                         
COMPND   5 SYNONYM: NOTCH 1, HN1, TRANSLOCATION-ASSOCIATED NOTCH PROTEIN TAN-1, 
COMPND   6 HUMAN NOTCH I;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 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   3   07-FEB-18 5FMA    1       AUTHOR                                   
REVDAT   2   20-APR-16 5FMA    1       JRNL                                     
REVDAT   1   13-APR-16 5FMA    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.    2.46 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) : 2.46                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.42                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 12109                          
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)  : 0.259                          
REMARK   3   R VALUE            (WORKING SET)  : 0.259                          
REMARK   3   FREE R VALUE                      : 0.263                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.770                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 578                            
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               : 6                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.46                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.69                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 93.14                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2832                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.3005                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2688                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.3019                   
REMARK   3   BIN FREE R VALUE                        : 0.2751                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.08                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 144                      
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            : 2219                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 11                                      
REMARK   3   SOLVENT ATOMS            : 18                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 74.22                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 68.95                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 11.23420                                             
REMARK   3    B22 (A**2) : -0.96950                                             
REMARK   3    B33 (A**2) : -10.26470                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.11090                                              
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) : 0.530               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.278               
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      : 0.901                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.898                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4243   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 7625   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 825    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 69     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 697    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4243   ; 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   : 292    ; 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   : 3931   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.035                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.21                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.10                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.66                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A):   31.1040   49.0097   97.1812           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1073 T22:   -0.2232                                    
REMARK   3     T33:   -0.0669 T12:   -0.0207                                    
REMARK   3     T13:   -0.0250 T23:   -0.0479                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2727 L22:    0.0000                                    
REMARK   3     L33:    1.3697 L12:   -0.0414                                    
REMARK   3     L13:   -0.9992 L23:    0.2187                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2183 S12:   -0.1032 S13:    0.1309                     
REMARK   3     S21:   -0.0340 S22:   -0.0381 S23:    0.1525                     
REMARK   3     S31:   -0.2046 S32:    0.2035 S33:   -0.1802                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A):   31.8688   31.3394   63.1594           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0798 T22:   -0.2296                                    
REMARK   3     T33:   -0.0631 T12:    0.0648                                    
REMARK   3     T13:   -0.0556 T23:   -0.0139                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.7250 L22:    0.0000                                    
REMARK   3     L33:    1.0646 L12:    0.6133                                    
REMARK   3     L13:   -0.5965 L23:   -0.4640                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0790 S12:   -0.0366 S13:   -0.2139                     
REMARK   3     S21:   -0.1940 S22:   -0.1037 S23:    0.0852                     
REMARK   3     S31:    0.2513 S32:    0.0058 S33:    0.1827                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5FMA 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_1290065354.                                   
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                             : 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                       : 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                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PIXEL                      
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12129                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.460                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.46                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39000                            
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   (%): 55.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       43.41500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A   160                                                      
REMARK 465     GLN B   141                                                      
REMARK 465     PHE B   158                                                      
REMARK 465     GLU B   159                                                      
REMARK 465     ALA B   160                                                      
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   SG   CYS B   222     SG   CYS B   233              1.01            
REMARK 500   SG   CYS B   227     SG   CYS B   243              1.10            
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   ND2  ASN A   277     CA   ASP B   238     2859     1.74            
REMARK 500   OG1  THR A   278     O    PRO B   235     2859     2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 201     -163.90   -163.09                                   
REMARK 500    SER B 201     -163.82   -164.84                                   
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 ASP A 178   OD2                                                    
REMARK 620 2 ASP A 178   OD1  48.7                                              
REMARK 620 3 VAL A 179   O    66.6  85.8                                        
REMARK 620 4 GLU A 181   OE1 138.5 138.0  73.0                                  
REMARK 620 5 ASN A 197   OD1  81.0 127.2  88.1  88.7                            
REMARK 620 6 GLU A 198   O    73.6  66.4 140.1 146.3  87.0                      
REMARK 620 7 SER A 201   O   137.0 118.4 153.5  81.2  85.3  65.2                
REMARK 620 N                    1     2     3     4     5     6                 
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 ILE A 258   O    87.5                                              
REMARK 620 3 ASP A 260   OD2 141.4  86.2                                        
REMARK 620 4 GLY A 275   O    89.9 167.7  88.3                                  
REMARK 620 5 ASP A 274   OD2  90.0  99.3 128.6  92.7                            
REMARK 620 6 ASP A 274   OD1 142.6  89.8  75.4  99.5  53.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1295  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 201   O                                                      
REMARK 620 2 GLU B 198   O    62.6                                              
REMARK 620 3 ASN B 197   OD1  82.4  89.1                                        
REMARK 620 4 GLU B 181   OE1  74.6 137.2  87.0                                  
REMARK 620 5 VAL B 179   O   146.6 150.7  94.0  72.0                            
REMARK 620 6 ASP B 178   OD2 130.1  68.8  86.0 152.9  82.4                      
REMARK 620 7 ASP B 178   OD1 118.1  71.9 137.5 132.6  86.6  51.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1296  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 274   OD2                                                    
REMARK 620 2 ASN B 257   OD1  75.1                                              
REMARK 620 3 ILE B 258   O    83.9  83.8                                        
REMARK 620 4 ASP B 260   OD2 121.2 163.2  93.4                                  
REMARK 620 5 ASP B 274   OD1  45.6 119.9  81.1  75.7                            
REMARK 620 6 GLY B 275   O    82.3  87.4 165.1  98.5  93.0                      
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 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 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1295                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1296                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1297                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1298                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1299                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1297                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5FM9   RELATED DB: PDB                                   
REMARK 900 HUMAN NOTCH 1, EGF 4-7                                               
DBREF  5FMA A  142   294  UNP    P46531   NOTC1_HUMAN    142    294             
DBREF  5FMA B  142   294  UNP    P46531   NOTC1_HUMAN    142    294             
SEQADV 5FMA GLN A  141  UNP  P46531              EXPRESSION TAG                 
SEQADV 5FMA GLU A  184  UNP  P46531    GLN   184 CONFLICT                       
SEQADV 5FMA GLN B  141  UNP  P46531              EXPRESSION TAG                 
SEQADV 5FMA GLU B  184  UNP  P46531    GLN   184 CONFLICT                       
SEQRES   1 A  154  GLN ASP PRO CYS ALA SER ASN PRO CYS ALA ASN GLY GLY          
SEQRES   2 A  154  GLN CYS LEU PRO PHE GLU ALA SER TYR ILE CYS HIS CYS          
SEQRES   3 A  154  PRO PRO SER PHE HIS GLY PRO THR CYS ARG GLN ASP VAL          
SEQRES   4 A  154  ASN GLU CYS GLY GLU LYS PRO GLY LEU CYS ARG HIS GLY          
SEQRES   5 A  154  GLY THR CYS HIS ASN GLU VAL GLY SER TYR ARG CYS VAL          
SEQRES   6 A  154  CYS ARG ALA THR HIS THR GLY PRO ASN CYS GLU ARG PRO          
SEQRES   7 A  154  TYR VAL PRO CYS SER PRO SER PRO CYS GLN ASN GLY GLY          
SEQRES   8 A  154  THR CYS ARG PRO THR GLY ASP VAL THR HIS GLU CYS ALA          
SEQRES   9 A  154  CYS LEU PRO GLY PHE THR GLY GLN ASN CYS GLU GLU ASN          
SEQRES  10 A  154  ILE ASP ASP CYS PRO GLY ASN ASN CYS LYS ASN GLY GLY          
SEQRES  11 A  154  ALA CYS VAL ASP GLY VAL ASN THR TYR ASN CYS ARG CYS          
SEQRES  12 A  154  PRO PRO GLU TRP THR GLY GLN TYR CYS THR GLU                  
SEQRES   1 B  154  GLN ASP PRO CYS ALA SER ASN PRO CYS ALA ASN GLY GLY          
SEQRES   2 B  154  GLN CYS LEU PRO PHE GLU ALA SER TYR ILE CYS HIS CYS          
SEQRES   3 B  154  PRO PRO SER PHE HIS GLY PRO THR CYS ARG GLN ASP VAL          
SEQRES   4 B  154  ASN GLU CYS GLY GLU LYS PRO GLY LEU CYS ARG HIS GLY          
SEQRES   5 B  154  GLY THR CYS HIS ASN GLU VAL GLY SER TYR ARG CYS VAL          
SEQRES   6 B  154  CYS ARG ALA THR HIS THR GLY PRO ASN CYS GLU ARG PRO          
SEQRES   7 B  154  TYR VAL PRO CYS SER PRO SER PRO CYS GLN ASN GLY GLY          
SEQRES   8 B  154  THR CYS ARG PRO THR GLY ASP VAL THR HIS GLU CYS ALA          
SEQRES   9 B  154  CYS LEU PRO GLY PHE THR GLY GLN ASN CYS GLU GLU ASN          
SEQRES  10 B  154  ILE ASP ASP CYS PRO GLY ASN ASN CYS LYS ASN GLY GLY          
SEQRES  11 B  154  ALA CYS VAL ASP GLY VAL ASN THR TYR ASN CYS ARG CYS          
SEQRES  12 B  154  PRO PRO GLU TRP THR GLY GLN TYR CYS THR GLU                  
HET     CA  A1295       1                                                       
HET     CA  A1296       1                                                       
HET     CA  A1297       1                                                       
HET     CA  B1295       1                                                       
HET     CA  B1296       1                                                       
HET     CL  B1297       1                                                       
HET    EDO  B1298       4                                                       
HET     CL  B1299       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3   CA    5(CA 2+)                                                     
FORMUL   8   CL    2(CL 1-)                                                     
FORMUL   9  EDO    C2 H6 O2                                                     
FORMUL  11  HOH   *18(H2 O)                                                     
HELIX    1   1 ASP A  142  ASN A  147  5                                   6    
HELIX    2   2 ASN A  180  LYS A  185  1                                   6    
HELIX    3   3 ASP B  142  ASN B  147  5                                   6    
HELIX    4   4 ASN B  180  LYS B  185  1                                   6    
SHEET    1  AA 2 GLN A 154  PRO A 157  0                                        
SHEET    2  AA 2 TYR A 162  HIS A 165 -1  O  ILE A 163   N  LEU A 156           
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  PRO A 235  0                                        
SHEET    2  AE 2 HIS A 241  ALA A 244 -1  O  GLU A 242   N  ARG A 234           
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           
SHEET    1  BA 2 GLN B 154  LEU B 156  0                                        
SHEET    2  BA 2 ILE B 163  HIS B 165 -1  O  ILE B 163   N  LEU B 156           
SHEET    1  BB 2 PHE B 170  HIS B 171  0                                        
SHEET    2  BB 2 GLN B 177  ASP B 178 -1  O  GLN B 177   N  HIS B 171           
SHEET    1  BC 2 THR B 194  GLU B 198  0                                        
SHEET    2  BC 2 SER B 201  VAL B 205 -1  O  SER B 201   N  GLU B 198           
SHEET    1  BD 2 HIS B 210  THR B 211  0                                        
SHEET    2  BD 2 ARG B 217  PRO B 218 -1  O  ARG B 217   N  THR B 211           
SHEET    1  BE 2 THR B 232  PRO B 235  0                                        
SHEET    2  BE 2 HIS B 241  ALA B 244 -1  O  GLU B 242   N  ARG B 234           
SHEET    1  BF 2 PHE B 249  THR B 250  0                                        
SHEET    2  BF 2 GLU B 256  ASN B 257 -1  O  GLU B 256   N  THR B 250           
SHEET    1  BG 2 ALA B 271  ASP B 274  0                                        
SHEET    2  BG 2 TYR B 279  ARG B 282 -1  O  ASN B 280   N  VAL B 273           
SSBOND   1 CYS A  144    CYS A  155                          1555   1555  2.04  
SSBOND   2 CYS A  149    CYS A  164                          1555   1555  2.03  
SSBOND   3 CYS A  166    CYS A  175                          1555   1555  2.04  
SSBOND   4 CYS A  182    CYS A  195                          1555   1555  2.03  
SSBOND   5 CYS A  189    CYS A  204                          1555   1555  2.03  
SSBOND   6 CYS A  206    CYS A  215                          1555   1555  2.04  
SSBOND   7 CYS A  222    CYS A  233                          1555   1555  2.04  
SSBOND   8 CYS A  227    CYS A  243                          1555   1555  2.03  
SSBOND   9 CYS A  245    CYS A  254                          1555   1555  2.03  
SSBOND  10 CYS A  261    CYS A  272                          1555   1555  2.04  
SSBOND  11 CYS A  266    CYS A  281                          1555   1555  2.04  
SSBOND  12 CYS A  283    CYS A  292                          1555   1555  2.03  
SSBOND  13 CYS B  144    CYS B  155                          1555   1555  2.04  
SSBOND  14 CYS B  149    CYS B  164                          1555   1555  2.03  
SSBOND  15 CYS B  166    CYS B  175                          1555   1555  2.03  
SSBOND  16 CYS B  182    CYS B  195                          1555   1555  2.04  
SSBOND  17 CYS B  189    CYS B  204                          1555   1555  2.03  
SSBOND  18 CYS B  206    CYS B  215                          1555   1555  2.04  
SSBOND  19 CYS B  245    CYS B  254                          1555   1555  2.04  
SSBOND  20 CYS B  261    CYS B  272                          1555   1555  2.03  
SSBOND  21 CYS B  266    CYS B  281                          1555   1555  2.03  
SSBOND  22 CYS B  283    CYS B  292                          1555   1555  2.03  
LINK        CA    CA A1295                 OD2 ASP A 178     1555   1555  2.51  
LINK        CA    CA A1295                 OD1 ASP A 178     1555   1555  2.75  
LINK        CA    CA A1295                 O   VAL A 179     1555   1555  2.62  
LINK        CA    CA A1295                 OE1 GLU A 181     1555   1555  2.38  
LINK        CA    CA A1295                 OD1 ASN A 197     1555   1555  2.34  
LINK        CA    CA A1295                 O   GLU A 198     1555   1555  2.60  
LINK        CA    CA A1295                 O   SER A 201     1555   1555  2.57  
LINK        CA    CA A1296                 OD1 ASN A 257     1555   1555  2.17  
LINK        CA    CA A1296                 O   ILE A 258     1555   1555  2.22  
LINK        CA    CA A1296                 OD2 ASP A 260     1555   1555  2.74  
LINK        CA    CA A1296                 O   GLY A 275     1555   1555  2.35  
LINK        CA    CA A1296                 OD2 ASP A 274     1555   1555  2.19  
LINK        CA    CA A1296                 OD1 ASP A 274     1555   1555  2.62  
LINK        CA    CA B1295                 O   SER B 201     1555   1555  2.77  
LINK        CA    CA B1295                 O   GLU B 198     1555   1555  2.62  
LINK        CA    CA B1295                 OD1 ASN B 197     1555   1555  2.25  
LINK        CA    CA B1295                 OE1 GLU B 181     1555   1555  2.54  
LINK        CA    CA B1295                 O   VAL B 179     1555   1555  2.46  
LINK        CA    CA B1295                 OD2 ASP B 178     1555   1555  2.39  
LINK        CA    CA B1295                 OD1 ASP B 178     1555   1555  2.60  
LINK        CA    CA B1296                 OD2 ASP B 274     1555   1555  2.69  
LINK        CA    CA B1296                 OD1 ASN B 257     1555   1555  2.30  
LINK        CA    CA B1296                 O   ILE B 258     1555   1555  2.28  
LINK        CA    CA B1296                 OD2 ASP B 260     1555   1555  2.39  
LINK        CA    CA B1296                 OD1 ASP B 274     1555   1555  2.92  
LINK        CA    CA B1296                 O   GLY B 275     1555   1555  2.30  
CISPEP   1 SER A  223    PRO A  224          0         2.58                     
CISPEP   2 SER B  223    PRO B  224          0        27.27                     
SITE     1 AC1  6 ASP A 178  VAL A 179  GLU A 181  ASN A 197                    
SITE     2 AC1  6 GLU A 198  SER A 201                                          
SITE     1 AC2  5 ASN A 257  ILE A 258  ASP A 260  ASP A 274                    
SITE     2 AC2  5 GLY A 275                                                     
SITE     1 AC3  6 ASP B 178  VAL B 179  GLU B 181  ASN B 197                    
SITE     2 AC3  6 GLU B 198  SER B 201                                          
SITE     1 AC4  5 ASN B 257  ILE B 258  ASP B 260  ASP B 274                    
SITE     2 AC4  5 GLY B 275                                                     
SITE     1 AC5  1 ARG B 282                                                     
SITE     1 AC6  6 ASN A 268  GLY A 269  PRO A 284  GLU A 286                    
SITE     2 AC6  6 CYS B 195  HIS B 196                                          
SITE     1 AC7  1 GLN A 252                                                     
SITE     1 AC8  1 GLN A 177                                                     
CRYST1   40.940   86.830   53.450  90.00 107.58  90.00 P 1 21 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      0.024426  0.000000  0.007739        0.00000                         
SCALE2      0.000000  0.011517  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019626        0.00000                         
MTRIX1   1 -0.118000  0.127000  0.098500      -67.54100    1                    
MTRIX2   1  0.130000 -0.981000  0.142000       61.99300    1                    
MTRIX3   1  0.985000  0.144000  0.099000       15.55700    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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