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Database: PDB
Entry: 3V79
LinkDB: 3V79
Original site: 3V79 
HEADER    TRANSCRIPTION/DNA                       20-DEC-11   3V79              
TITLE     STRUCTURE OF HUMAN NOTCH1 TRANSCRIPTION COMPLEX INCLUDING CSL, RAM,   
TITLE    2 ANK, AND MAML-1 ON HES-1 PROMOTER DNA SEQUENCE                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;                  
COMPND   3 CHAIN: K;                                                            
COMPND   4 SYNONYM: NOTCH 1, HN1, TRANSLOCATION-ASSOCIATED NOTCH PROTEIN TAN-1, 
COMPND   5 NOTCH 1 EXTRACELLULAR TRUNCATION, NOTCH 1 INTRACELLULAR DOMAIN, NICD;
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RECOMBINING BINDING PROTEIN SUPPRESSOR OF HAIRLESS;        
COMPND   9 CHAIN: C;                                                            
COMPND  10 SYNONYM: CBF-1, J KAPPA-RECOMBINATION SIGNAL-BINDING PROTEIN, RBP-J  
COMPND  11 KAPPA, RBP-J, RBP-JK, RENAL CARCINOMA ANTIGEN NY-REN-30;             
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: MASTERMIND-LIKE PROTEIN 1;                                 
COMPND  15 CHAIN: M;                                                            
COMPND  16 SYNONYM: MAM-1;                                                      
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: DNA 5'-                                                    
COMPND  20 D(*GP*TP*TP*AP*CP*TP*GP*TP*GP*GP*GP*AP*AP*AP*GP*AP*AP*A)-3';         
COMPND  21 CHAIN: X;                                                            
COMPND  22 ENGINEERED: YES;                                                     
COMPND  23 MOL_ID: 5;                                                           
COMPND  24 MOLECULE: DNA 5'-                                                    
COMPND  25 D(*TP*TP*TP*CP*TP*TP*TP*CP*CP*CP*AP*CP*AP*GP*TP*AP*AP*C)-3';         
COMPND  26 CHAIN: Y;                                                            
COMPND  27 ENGINEERED: YES;                                                     
COMPND  28 MOL_ID: 6;                                                           
COMPND  29 MOLECULE: RAM;                                                       
COMPND  30 CHAIN: R;                                                            
COMPND  31 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: NOTCH1, TAN1;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: IGKJRB, IGKJRB1, RBPJ, RBPJK, RBPSUH;                          
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: MAML1, KIAA0200;                                               
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 SYNTHETIC: YES;                                                      
SOURCE  24 OTHER_DETAILS: SYNTHESIZED OLIGONUCLEOTIDES;                         
SOURCE  25 MOL_ID: 5;                                                           
SOURCE  26 SYNTHETIC: YES;                                                      
SOURCE  27 OTHER_DETAILS: SYNTHESIZED OLIGONUCLEOTIDES;                         
SOURCE  28 MOL_ID: 6;                                                           
SOURCE  29 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  30 ORGANISM_TAXID: 9606;                                                
SOURCE  31 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  32 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    BETA-TREFOIL, ANKYRIN, TRANSCRIPTION ACTIVATION, DNA BINDING,         
KEYWDS   2 TRANSCRIPTION-DNA COMPLEX                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.NAM,P.SLIZ,S.BLACKLOW                                               
REVDAT   3   21-MAR-12 3V79    1       JRNL                                     
REVDAT   2   22-FEB-12 3V79    1       COMPND DBREF                             
REVDAT   1   15-FEB-12 3V79    0                                                
JRNL        AUTH   S.H.CHOI,T.E.WALES,Y.NAM,D.J.O'DONOVAN,P.SLIZ,J.R.ENGEN,     
JRNL        AUTH 2 S.C.BLACKLOW                                                 
JRNL        TITL   CONFORMATIONAL LOCKING UPON COOPERATIVE ASSEMBLY OF NOTCH    
JRNL        TITL 2 TRANSCRIPTION COMPLEXES.                                     
JRNL        REF    STRUCTURE                     V.  20   340 2012              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   22325781                                                     
JRNL        DOI    10.1016/J.STR.2011.12.011                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 40195                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : FROM PDB CODE 2F8X              
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2049                            
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           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
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            : 5689                                    
REMARK   3   NUCLEIC ACID ATOMS       : 732                                     
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.46                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.87                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.54                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.85                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.003                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.63                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 9.144 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 14.186; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 12.798; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 18.289; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3V79 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB069683.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-DEC-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792899                          
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40195                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: 2F8X                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 81.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG 3350, 5% ETHYLENE GLYCOL, PH      
REMARK 280  7.9, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/2                                            
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        0.00000            
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        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       59.99350            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       59.99350            
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       59.99350            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       59.99350            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       59.99350            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       59.99350            
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 300 REMARK: INTRACELLULAR NOTCH, CSL, AND MAML CAN FORM A                
REMARK 300 HETEROTRIMERIC COMPLEX ON DNA DUPLEX AS SHOWN IN THE ASYMMETRIC      
REMARK 300 UNIT. IN SOME INSTANCES WHEN THE CSL BINDING SITES ARE LOCATED       
REMARK 300 CLOSE TO EACH OTHER, A HETEROTRIMER MAY INTERACT WITH ANOTHER        
REMARK 300 HETEROTRIMER.                                                        
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11370 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, C, M, R, X, Y                      
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     GLY K  1872                                                      
REMARK 465     MET K  1873                                                      
REMARK 465     ASP K  1874                                                      
REMARK 465     VAL K  1875                                                      
REMARK 465     ASN K  1876                                                      
REMARK 465     VAL K  1877                                                      
REMARK 465     ARG K  1878                                                      
REMARK 465     GLY K  1879                                                      
REMARK 465     PRO K  1880                                                      
REMARK 465     ASP K  1881                                                      
REMARK 465     GLY K  1882                                                      
REMARK 465     PHE K  1883                                                      
REMARK 465     GLY K  1893                                                      
REMARK 465     GLY K  1894                                                      
REMARK 465     GLY K  1895                                                      
REMARK 465     LEU K  1896                                                      
REMARK 465     GLU K  1897                                                      
REMARK 465     THR K  1898                                                      
REMARK 465     GLY K  1899                                                      
REMARK 465     ASN K  1900                                                      
REMARK 465     SER K  1901                                                      
REMARK 465     GLU K  1902                                                      
REMARK 465     GLU K  1903                                                      
REMARK 465     GLU K  1904                                                      
REMARK 465     GLU K  1905                                                      
REMARK 465     ASP K  1906                                                      
REMARK 465     ALA K  1907                                                      
REMARK 465     PRO K  1908                                                      
REMARK 465     GLN K  1917                                                      
REMARK 465     GLY K  1918                                                      
REMARK 465     ALA K  1919                                                      
REMARK 465     ARG K  2121                                                      
REMARK 465     SER K  2122                                                      
REMARK 465     PRO K  2123                                                      
REMARK 465     GLN K  2124                                                      
REMARK 465     LEU K  2125                                                      
REMARK 465     HIS K  2126                                                      
REMARK 465     GLY K  2127                                                      
REMARK 465     MET C     8                                                      
REMARK 465     GLY C     9                                                      
REMARK 465     GLU C    10                                                      
REMARK 465     GLY C   435                                                      
REMARK 465     HIS C   436                                                      
REMARK 465     HIS C   437                                                      
REMARK 465     HIS C   438                                                      
REMARK 465     HIS C   439                                                      
REMARK 465     HIS C   440                                                      
REMARK 465     HIS C   441                                                      
REMARK 465     GLY M    12                                                      
REMARK 465     LEU M    13                                                      
REMARK 465     PRO M    14                                                      
REMARK 465     ARG M    15                                                      
REMARK 465     ALA M    71                                                      
REMARK 465     GLY M    72                                                      
REMARK 465     LYS M    73                                                      
REMARK 465     HIS M    74                                                      
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 K1921      -59.39   -152.15                                   
REMARK 500    HIS K1922       53.50   -102.86                                   
REMARK 500    ARG K1941       73.46   -102.79                                   
REMARK 500    ALA K1951       24.99    -75.33                                   
REMARK 500    SER K1952       87.40     51.03                                   
REMARK 500    ASP K1959     -158.29    -83.87                                   
REMARK 500    THR K1987      126.19    -38.70                                   
REMARK 500    ASP K1990       34.18    -96.75                                   
REMARK 500    MET K1993     -170.99    -68.15                                   
REMARK 500    ARG K2005      -61.58    -93.29                                   
REMARK 500    LEU K2006       20.12    -74.55                                   
REMARK 500    ALA K2007       72.05     37.02                                   
REMARK 500    MET K2011      -34.83    -30.81                                   
REMARK 500    HIS K2019       73.94     60.97                                   
REMARK 500    ASP K2021      109.46    -49.52                                   
REMARK 500    ASN K2023       31.60    -93.42                                   
REMARK 500    ASN K2051       39.05    -96.60                                   
REMARK 500    ASN K2054       94.07    -51.61                                   
REMARK 500    HIS K2084       40.82    -81.86                                   
REMARK 500    PHE K2085       51.15     37.47                                   
REMARK 500    ASP K2089       42.66   -106.96                                   
REMARK 500    ASP K2092     -164.58    -70.87                                   
REMARK 500    HIS K2107       62.32   -101.91                                   
REMARK 500    HIS K2108      -37.59    -35.46                                   
REMARK 500    LEU K2114       -4.90    -57.82                                   
REMARK 500    ASN K2118       71.61     31.70                                   
REMARK 500    LEU C  17      103.72    -52.21                                   
REMARK 500    GLU C  28      -76.48    -73.47                                   
REMARK 500    ARG C  29       46.86     77.37                                   
REMARK 500    GLU C  49     -178.68    -58.61                                   
REMARK 500    LYS C  50       79.62   -161.45                                   
REMARK 500    PHE C  52      169.11    -48.57                                   
REMARK 500    ARG C  75        5.59    -65.30                                   
REMARK 500    ALA C  87      149.73   -170.13                                   
REMARK 500    ASN C  93       49.06    -94.25                                   
REMARK 500    ASP C  95       48.16    -84.69                                   
REMARK 500    TYR C 108     -159.83   -149.53                                   
REMARK 500    CYS C 109      129.34    169.53                                   
REMARK 500    LYS C 112       24.85    -70.79                                   
REMARK 500    THR C 113       11.96   -147.20                                   
REMARK 500    LYS C 121       30.99    -75.56                                   
REMARK 500    ASN C 135       44.01    -85.45                                   
REMARK 500    SER C 136       18.82     48.68                                   
REMARK 500    LYS C 152      137.10    172.55                                   
REMARK 500    SER C 154       89.71    -55.92                                   
REMARK 500    LEU C 160       30.44    -71.72                                   
REMARK 500    ALA C 163     -151.87    -72.35                                   
REMARK 500    ASP C 164      -32.83     69.22                                   
REMARK 500    ARG C 180       25.75     41.98                                   
REMARK 500    THR C 186      118.38    -17.11                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      85 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3V79 K 1873  2127  UNP    P46531   NOTC1_HUMAN   1872   2126             
DBREF  3V79 C    9   435  UNP    Q06330   SUH_HUMAN       23    449             
DBREF  3V79 M   13    74  UNP    Q92585   MAML1_HUMAN     13     74             
DBREF  3V79 X    0    17  PDB    3V79     3V79             0     17             
DBREF  3V79 Y  101   118  PDB    3V79     3V79           101    118             
DBREF  3V79 R  936   954  PDB    3V79     3V79           936    954             
SEQADV 3V79 GLY K 1872  UNP  P46531              EXPRESSION TAG                 
SEQADV 3V79 MET C    8  UNP  Q06330              EXPRESSION TAG                 
SEQADV 3V79 HIS C  436  UNP  Q06330              EXPRESSION TAG                 
SEQADV 3V79 HIS C  437  UNP  Q06330              EXPRESSION TAG                 
SEQADV 3V79 HIS C  438  UNP  Q06330              EXPRESSION TAG                 
SEQADV 3V79 HIS C  439  UNP  Q06330              EXPRESSION TAG                 
SEQADV 3V79 HIS C  440  UNP  Q06330              EXPRESSION TAG                 
SEQADV 3V79 HIS C  441  UNP  Q06330              EXPRESSION TAG                 
SEQADV 3V79 GLY M   12  UNP  Q92585              EXPRESSION TAG                 
SEQRES   1 K  256  GLY MET ASP VAL ASN VAL ARG GLY PRO ASP GLY PHE THR          
SEQRES   2 K  256  PRO LEU MET ILE ALA SER CYS SER GLY GLY GLY LEU GLU          
SEQRES   3 K  256  THR GLY ASN SER GLU GLU GLU GLU ASP ALA PRO ALA VAL          
SEQRES   4 K  256  ILE SER ASP PHE ILE TYR GLN GLY ALA SER LEU HIS ASN          
SEQRES   5 K  256  GLN THR ASP ARG THR GLY GLU THR ALA LEU HIS LEU ALA          
SEQRES   6 K  256  ALA ARG TYR SER ARG SER ASP ALA ALA LYS ARG LEU LEU          
SEQRES   7 K  256  GLU ALA SER ALA ASP ALA ASN ILE GLN ASP ASN MET GLY          
SEQRES   8 K  256  ARG THR PRO LEU HIS ALA ALA VAL SER ALA ASP ALA GLN          
SEQRES   9 K  256  GLY VAL PHE GLN ILE LEU ILE ARG ASN ARG ALA THR ASP          
SEQRES  10 K  256  LEU ASP ALA ARG MET HIS ASP GLY THR THR PRO LEU ILE          
SEQRES  11 K  256  LEU ALA ALA ARG LEU ALA VAL GLU GLY MET LEU GLU ASP          
SEQRES  12 K  256  LEU ILE ASN SER HIS ALA ASP VAL ASN ALA VAL ASP ASP          
SEQRES  13 K  256  LEU GLY LYS SER ALA LEU HIS TRP ALA ALA ALA VAL ASN          
SEQRES  14 K  256  ASN VAL ASP ALA ALA VAL VAL LEU LEU LYS ASN GLY ALA          
SEQRES  15 K  256  ASN LYS ASP MET GLN ASN ASN ARG GLU GLU THR PRO LEU          
SEQRES  16 K  256  PHE LEU ALA ALA ARG GLU GLY SER TYR GLU THR ALA LYS          
SEQRES  17 K  256  VAL LEU LEU ASP HIS PHE ALA ASN ARG ASP ILE THR ASP          
SEQRES  18 K  256  HIS MET ASP ARG LEU PRO ARG ASP ILE ALA GLN GLU ARG          
SEQRES  19 K  256  MET HIS HIS ASP ILE VAL ARG LEU LEU ASP GLU TYR ASN          
SEQRES  20 K  256  LEU VAL ARG SER PRO GLN LEU HIS GLY                          
SEQRES   1 C  434  MET GLY GLU ARG PRO PRO PRO LYS ARG LEU THR ARG GLU          
SEQRES   2 C  434  ALA MET ARG ASN TYR LEU LYS GLU ARG GLY ASP GLN THR          
SEQRES   3 C  434  VAL LEU ILE LEU HIS ALA LYS VAL ALA GLN LYS SER TYR          
SEQRES   4 C  434  GLY ASN GLU LYS ARG PHE PHE CYS PRO PRO PRO CYS VAL          
SEQRES   5 C  434  TYR LEU MET GLY SER GLY TRP LYS LYS LYS LYS GLU GLN          
SEQRES   6 C  434  MET GLU ARG ASP GLY CYS SER GLU GLN GLU SER GLN PRO          
SEQRES   7 C  434  CYS ALA PHE ILE GLY ILE GLY ASN SER ASP GLN GLU MET          
SEQRES   8 C  434  GLN GLN LEU ASN LEU GLU GLY LYS ASN TYR CYS THR ALA          
SEQRES   9 C  434  LYS THR LEU TYR ILE SER ASP SER ASP LYS ARG LYS HIS          
SEQRES  10 C  434  PHE MET LEU SER VAL LYS MET PHE TYR GLY ASN SER ASP          
SEQRES  11 C  434  ASP ILE GLY VAL PHE LEU SER LYS ARG ILE LYS VAL ILE          
SEQRES  12 C  434  SER LYS PRO SER LYS LYS LYS GLN SER LEU LYS ASN ALA          
SEQRES  13 C  434  ASP LEU CYS ILE ALA SER GLY THR LYS VAL ALA LEU PHE          
SEQRES  14 C  434  ASN ARG LEU ARG SER GLN THR VAL SER THR ARG TYR LEU          
SEQRES  15 C  434  HIS VAL GLU GLY GLY ASN PHE HIS ALA SER SER GLN GLN          
SEQRES  16 C  434  TRP GLY ALA PHE PHE ILE HIS LEU LEU ASP ASP ASP GLU          
SEQRES  17 C  434  SER GLU GLY GLU GLU PHE THR VAL ARG ASP GLY TYR ILE          
SEQRES  18 C  434  HIS TYR GLY GLN THR VAL LYS LEU VAL CYS SER VAL THR          
SEQRES  19 C  434  GLY MET ALA LEU PRO ARG LEU ILE ILE ARG LYS VAL ASP          
SEQRES  20 C  434  LYS GLN THR ALA LEU LEU ASP ALA ASP ASP PRO VAL SER          
SEQRES  21 C  434  GLN LEU HIS LYS CYS ALA PHE TYR LEU LYS ASP THR GLU          
SEQRES  22 C  434  ARG MET TYR LEU CYS LEU SER GLN GLU ARG ILE ILE GLN          
SEQRES  23 C  434  PHE GLN ALA THR PRO CYS PRO LYS GLU PRO ASN LYS GLU          
SEQRES  24 C  434  MET ILE ASN ASP GLY ALA SER TRP THR ILE ILE SER THR          
SEQRES  25 C  434  ASP LYS ALA GLU TYR THR PHE TYR GLU GLY MET GLY PRO          
SEQRES  26 C  434  VAL LEU ALA PRO VAL THR PRO VAL PRO VAL VAL GLU SER          
SEQRES  27 C  434  LEU GLN LEU ASN GLY GLY GLY ASP VAL ALA MET LEU GLU          
SEQRES  28 C  434  LEU THR GLY GLN ASN PHE THR PRO ASN LEU ARG VAL TRP          
SEQRES  29 C  434  PHE GLY ASP VAL GLU ALA GLU THR MET TYR ARG CYS GLY          
SEQRES  30 C  434  GLU SER MET LEU CYS VAL VAL PRO ASP ILE SER ALA PHE          
SEQRES  31 C  434  ARG GLU GLY TRP ARG TRP VAL ARG GLN PRO VAL GLN VAL          
SEQRES  32 C  434  PRO VAL THR LEU VAL ARG ASN ASP GLY ILE ILE TYR SER          
SEQRES  33 C  434  THR SER LEU THR PHE THR TYR THR PRO GLU PRO GLY HIS          
SEQRES  34 C  434  HIS HIS HIS HIS HIS                                          
SEQRES   1 M   63  GLY LEU PRO ARG HIS SER ALA VAL MET GLU ARG LEU ARG          
SEQRES   2 M   63  ARG ARG ILE GLU LEU CYS ARG ARG HIS HIS SER THR CYS          
SEQRES   3 M   63  GLU ALA ARG TYR GLU ALA VAL SER PRO GLU ARG LEU GLU          
SEQRES   4 M   63  LEU GLU ARG GLN HIS THR PHE ALA LEU HIS GLN ARG CYS          
SEQRES   5 M   63  ILE GLN ALA LYS ALA LYS ARG ALA GLY LYS HIS                  
SEQRES   1 X   18   DG  DT  DT  DA  DC  DT  DG  DT  DG  DG  DG  DA  DA          
SEQRES   2 X   18   DA  DG  DA  DA  DA                                          
SEQRES   1 Y   18   DT  DT  DT  DC  DT  DT  DT  DC  DC  DC  DA  DC  DA          
SEQRES   2 Y   18   DG  DT  DA  DA  DC                                          
SEQRES   1 R   19  LYS ARG ARG ARG GLN HIS GLY GLN LEU TRP PHE PRO GLU          
SEQRES   2 R   19  GLY PHE LYS VAL SER GLU                                      
HELIX    1   1 ILE K 1911  TYR K 1916  1                                   6    
HELIX    2   2 THR K 1931  TYR K 1939  1                                   9    
HELIX    3   3 ARG K 1941  ALA K 1951  1                                  11    
HELIX    4   4 THR K 1964  ALA K 1972  1                                   9    
HELIX    5   5 ALA K 1974  ARG K 1983  1                                  10    
HELIX    6   6 THR K 1998  LEU K 2006  1                                   9    
HELIX    7   7 GLY K 2010  SER K 2018  1                                   9    
HELIX    8   8 SER K 2031  VAL K 2039  1                                   9    
HELIX    9   9 ASN K 2041  ASN K 2051  1                                  11    
HELIX   10  10 THR K 2064  GLY K 2073  1                                  10    
HELIX   11  11 SER K 2074  HIS K 2084  1                                  11    
HELIX   12  12 LEU K 2097  MET K 2106  1                                  10    
HELIX   13  13 HIS K 2107  TYR K 2117  1                                  11    
HELIX   14  14 THR C   18  GLU C   28  1                                  11    
HELIX   15  15 SER C   64  ARG C   75  1                                  12    
HELIX   16  16 GLY C  351  VAL C  354  5                                   4    
HELIX   17  17 ASP C  393  PHE C  397  5                                   5    
HELIX   18  18 SER M   17  LYS M   69  1                                  53    
HELIX   19  19 PHE R  950  GLU R  954  5                                   5    
SHEET    1   A 2 GLN C  32  ALA C  39  0                                        
SHEET    2   A 2 THR C 319  PHE C 326 -1  O  ASP C 320   N  HIS C  38           
SHEET    1   B 3 VAL C  41  GLN C  43  0                                        
SHEET    2   B 3 ILE C 147  ILE C 150  1  O  ILE C 150   N  ALA C  42           
SHEET    3   B 3 HIS C 124  PHE C 125 -1  N  PHE C 125   O  ILE C 147           
SHEET    1   C 4 GLN C  99  GLN C 100  0                                        
SHEET    2   C 4 CYS C  86  ILE C  91 -1  N  ILE C  89   O  GLN C  99           
SHEET    3   C 4 LEU C 127  PHE C 132 -1  O  SER C 128   N  GLY C  90           
SHEET    4   C 4 ASP C 138  LEU C 143 -1  O  PHE C 142   N  VAL C 129           
SHEET    1   D 5 LYS C 172  VAL C 173  0                                        
SHEET    2   D 5 PHE C 206  LEU C 211 -1  O  PHE C 206   N  VAL C 173           
SHEET    3   D 5 THR C 233  CYS C 238 -1  O  THR C 233   N  LEU C 211           
SHEET    4   D 5 LEU C 248  ASP C 254 -1  O  LEU C 248   N  VAL C 234           
SHEET    5   D 5 CYS C 272  TYR C 275 -1  O  TYR C 275   N  ILE C 249           
SHEET    1   E 6 LYS C 172  VAL C 173  0                                        
SHEET    2   E 6 PHE C 206  LEU C 211 -1  O  PHE C 206   N  VAL C 173           
SHEET    3   E 6 THR C 233  CYS C 238 -1  O  THR C 233   N  LEU C 211           
SHEET    4   E 6 LEU C 248  ASP C 254 -1  O  LEU C 248   N  VAL C 234           
SHEET    5   E 6 THR C 257  LEU C 259 -1  O  LEU C 259   N  LYS C 252           
SHEET    6   E 6 LYS C 305  MET C 307 -1  O  GLU C 306   N  ALA C 258           
SHEET    1   F 2 PHE C 176  ASN C 177  0                                        
SHEET    2   F 2 ARG C 187  TYR C 188 -1  O  ARG C 187   N  ASN C 177           
SHEET    1   G 2 VAL C 191  GLU C 192  0                                        
SHEET    2   G 2 ASN C 195  PHE C 196 -1  O  ASN C 195   N  GLU C 192           
SHEET    1   H 2 MET C 243  ALA C 244  0                                        
SHEET    2   H 2 GLN R 943  LEU R 944  1  O  GLN R 943   N  ALA C 244           
SHEET    1   I 2 LEU C 284  LEU C 286  0                                        
SHEET    2   I 2 ILE C 291  GLN C 293 -1  O  ILE C 292   N  CYS C 285           
SHEET    1   J 4 VAL C 342  ASN C 349  0                                        
SHEET    2   J 4 MET C 356  GLN C 362 -1  O  MET C 356   N  ASN C 349           
SHEET    3   J 4 SER C 386  VAL C 390 -1  O  MET C 387   N  LEU C 359           
SHEET    4   J 4 THR C 379  CYS C 383 -1  N  MET C 380   O  LEU C 388           
SHEET    1   K 4 VAL C 375  ALA C 377  0                                        
SHEET    2   K 4 LEU C 368  PHE C 372 -1  N  PHE C 372   O  VAL C 375           
SHEET    3   K 4 THR C 413  ARG C 416 -1  O  VAL C 415   N  ARG C 369           
SHEET    4   K 4 ILE C 421  SER C 423 -1  O  TYR C 422   N  LEU C 414           
SHEET    1   L 2 VAL C 408  GLN C 409  0                                        
SHEET    2   L 2 THR C 429  TYR C 430 -1  O  TYR C 430   N  VAL C 408           
CISPEP   1 CYS C   54    PRO C   55          0         0.04                     
CISPEP   2 THR C  338    PRO C  339          0        -0.10                     
CRYST1  272.646  272.646  119.987  90.00  90.00 120.00 P 63 2 2     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.003668  0.002118  0.000000        0.00000                         
SCALE2      0.000000  0.004235  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008334        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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