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Database: PDB
Entry: 4N40
LinkDB: 4N40
Original site: 4N40 
HEADER    CELL CYCLE                              08-OCT-13   4N40              
TITLE     CRYSTAL STRUCTURE OF HUMAN EPITHELIAL CELL-TRANSFORMING SEQUENCE 2    
TITLE    2 PROTEIN                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN ECT2;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES, ISOFORM 4, 45-325;                           
COMPND   5 SYNONYM: EPITHELIAL CELL-TRANSFORMING SEQUENCE 2 ONCOGENE;           
COMPND   6 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: ECT2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    TRIPLE BRCT DOMAINS, CELL CYCLE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZOU,Z.H.SHAO,F.D.LI,D.GONG,C.WANG,Q.GONG,Y.SHI                      
REVDAT   3   15-NOV-17 4N40    1       REMARK                                   
REVDAT   2   31-DEC-14 4N40    1       JRNL                                     
REVDAT   1   27-AUG-14 4N40    0                                                
JRNL        AUTH   Y.ZOU,Z.H.SHAO,J.PENG,F.D.LI,D.GONG,C.WANG,X.ZUO,Z.ZHANG,    
JRNL        AUTH 2 J.WU,Y.SHI,Q.GONG                                            
JRNL        TITL   CRYSTAL STRUCTURE OF TRIPLE-BRCT-DOMAIN OF ECT2 AND INSIGHTS 
JRNL        TITL 2 INTO THE BINDING CHARACTERISTICS TO CYK-4                    
JRNL        REF    FEBS LETT.                    V. 588  2911 2014              
JRNL        REFN                   ISSN 0014-5793                               
JRNL        PMID   25068414                                                     
JRNL        DOI    10.1016/J.FEBSLET.2014.07.019                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.11 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.6.1_357                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.11                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.87                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.980                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 9156                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.214                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.770                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 437                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 36.8753 -  4.4783    1.00     2909   141  0.1913 0.2634        
REMARK   3     2  4.4783 -  3.5555    1.00     2899   145  0.2116 0.2620        
REMARK   3     3  3.5555 -  3.1063    1.00     2911   151  0.3120 0.3901        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.30                                          
REMARK   3   B_SOL              : 69.93                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.480            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.750           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 106.4                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 112.1                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.31770                                             
REMARK   3    B22 (A**2) : -0.31770                                             
REMARK   3    B33 (A**2) : 0.63530                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.012           2198                                  
REMARK   3   ANGLE     :  1.655           2988                                  
REMARK   3   CHIRALITY :  0.101            337                                  
REMARK   3   PLANARITY :  0.007            386                                  
REMARK   3   DIHEDRAL  : 15.811            782                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4N40 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-OCT-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000082723.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-APR-12; 06-MAY-12               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : SSRF; SSRF                         
REMARK 200  BEAMLINE                       : BL17U; BL17U                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793; 0.9793                     
REMARK 200  MONOCHROMATOR                  : PLANE GRATING; PLANE GRATING       
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R; ADSC QUANTUM    
REMARK 200                                   315R                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9161                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.95600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES, 14% MPEG 5000, PH 8.0,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 283K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
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+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        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       61.85000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       35.70911            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       29.74800            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       61.85000            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       35.70911            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       29.74800            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       61.85000            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       35.70911            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       29.74800            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       71.41823            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       59.49600            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       71.41823            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       59.49600            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       71.41823            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       59.49600            
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 42540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  45    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  64    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  73    CG   CD   CE   NZ                                   
REMARK 470     GLU A  80    CG   CD   OE1  OE2                                  
REMARK 470     VAL A  82    CG1  CG2                                            
REMARK 470     GLU A  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  86    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  89    CG   OD1  OD2                                       
REMARK 470     ASN A 108    CG   OD1  ND2                                       
REMARK 470     LYS A 129    CG   CD   CE   NZ                                   
REMARK 470     ARG A 156    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 157    CG   CD   CE   NZ                                   
REMARK 470     LYS A 158    CG   CD   CE   NZ                                   
REMARK 470     GLU A 159    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 160    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 177    CG   CD   CE   NZ                                   
REMARK 470     LYS A 182    CG   CD   CE   NZ                                   
REMARK 470     THR A 184    OG1  CG2                                            
REMARK 470     HIS A 185    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 186    CG   CD1  CD2                                       
REMARK 470     ASN A 189    CG   OD1  ND2                                       
REMARK 470     GLN A 192    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 214    CG   CD   CE   NZ                                   
REMARK 470     GLN A 222    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 234    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 252    CG   OD1  OD2                                       
REMARK 470     GLU A 253    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 260    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 275    CD   OE1  OE2                                       
REMARK 470     LYS A 288    CG   CD   CE   NZ                                   
REMARK 470     PHE A 292    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 293    CD   OE1  OE2                                       
REMARK 470     LYS A 296    CG   CD   CE   NZ                                   
REMARK 470     LYS A 297    CE   NZ                                             
REMARK 470     GLN A 303    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 322    CG   CD1  CD2                                       
REMARK 470     GLU A 324    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    THR A   184     N    LEU A   186              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASN A 189   CB  -  CA  -  C   ANGL. DEV. = -13.7 DEGREES          
REMARK 500    THR A 191   N   -  CA  -  C   ANGL. DEV. =  16.8 DEGREES          
REMARK 500    PRO A 291   C   -  N   -  CA  ANGL. DEV. =   9.7 DEGREES          
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    GLN A  48       35.99    -86.52                                   
REMARK 500    GLN A  57     -139.56     44.83                                   
REMARK 500    GLU A  58       -5.16    -53.16                                   
REMARK 500    LEU A  65      -71.16    -57.26                                   
REMARK 500    CYS A 142     -146.60   -128.95                                   
REMARK 500    THR A 143       11.60   -148.65                                   
REMARK 500    ASN A 180     -153.26   -139.67                                   
REMARK 500    HIS A 185       20.56     17.60                                   
REMARK 500    LEU A 186      115.48    175.98                                   
REMARK 500    ARG A 218       31.35    -96.93                                   
REMARK 500    GLN A 265       32.29    -93.23                                   
REMARK 500    LEU A 272      152.13    -39.95                                   
REMARK 500    ASN A 285      -76.71    -79.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU A  186     VAL A  187                  142.40                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE REFERENCE SEQUENCE OF THIS PROTEIN IS ISOFORM 4 OF Q9H8V3.       
DBREF  4N40 A   45   325  UNP    Q9H8V3   ECT2_HUMAN      45    325             
SEQRES   1 A  281  GLU MSE PRO GLN ILE GLU THR ARG VAL ILE LEU VAL GLN          
SEQRES   2 A  281  GLU ALA GLY LYS GLN GLU GLU LEU ILE LYS ALA LEU LYS          
SEQRES   3 A  281  ASP ILE LYS VAL GLY PHE VAL LYS MSE GLU SER VAL GLU          
SEQRES   4 A  281  GLU PHE GLU GLY LEU ASP SER PRO GLU PHE GLU ASN VAL          
SEQRES   5 A  281  PHE VAL VAL THR ASP PHE GLN ASP SER VAL PHE ASN ASP          
SEQRES   6 A  281  LEU TYR LYS ALA ASP CYS ARG VAL ILE GLY PRO PRO VAL          
SEQRES   7 A  281  VAL LEU ASN CYS SER GLN LYS GLY GLU PRO LEU PRO PHE          
SEQRES   8 A  281  SER CYS ARG PRO LEU TYR CYS THR SER MSE MSE ASN LEU          
SEQRES   9 A  281  VAL LEU CYS PHE THR GLY PHE ARG LYS LYS GLU GLU LEU          
SEQRES  10 A  281  VAL ARG LEU VAL THR LEU VAL HIS HIS MSE GLY GLY VAL          
SEQRES  11 A  281  ILE ARG LYS ASP PHE ASN SER LYS VAL THR HIS LEU VAL          
SEQRES  12 A  281  ALA ASN CYS THR GLN GLY GLU LYS PHE ARG VAL ALA VAL          
SEQRES  13 A  281  SER LEU GLY THR PRO ILE MSE LYS PRO GLU TRP ILE TYR          
SEQRES  14 A  281  LYS ALA TRP GLU ARG ARG ASN GLU GLN ASP PHE TYR ALA          
SEQRES  15 A  281  ALA VAL ASP ASP PHE ARG ASN GLU PHE LYS VAL PRO PRO          
SEQRES  16 A  281  PHE GLN ASP CYS ILE LEU SER PHE LEU GLY PHE SER ASP          
SEQRES  17 A  281  GLU GLU LYS THR ASN MSE GLU GLU MSE THR GLU MSE GLN          
SEQRES  18 A  281  GLY GLY LYS TYR LEU PRO LEU GLY ASP GLU ARG CYS THR          
SEQRES  19 A  281  HIS LEU VAL VAL GLU GLU ASN ILE VAL LYS ASP LEU PRO          
SEQRES  20 A  281  PHE GLU PRO SER LYS LYS LEU TYR VAL VAL LYS GLN GLU          
SEQRES  21 A  281  TRP PHE TRP GLY SER ILE GLN MSE ASP ALA ARG ALA GLY          
SEQRES  22 A  281  GLU THR MSE TYR LEU TYR GLU LYS                              
MODRES 4N40 MSE A   46  MET  SELENOMETHIONINE                                   
MODRES 4N40 MSE A   79  MET  SELENOMETHIONINE                                   
MODRES 4N40 MSE A  145  MET  SELENOMETHIONINE                                   
MODRES 4N40 MSE A  146  MET  SELENOMETHIONINE                                   
MODRES 4N40 MSE A  171  MET  SELENOMETHIONINE                                   
MODRES 4N40 MSE A  207  MET  SELENOMETHIONINE                                   
MODRES 4N40 MSE A  258  MET  SELENOMETHIONINE                                   
MODRES 4N40 MSE A  261  MET  SELENOMETHIONINE                                   
MODRES 4N40 MSE A  264  MET  SELENOMETHIONINE                                   
MODRES 4N40 MSE A  312  MET  SELENOMETHIONINE                                   
MODRES 4N40 MSE A  320  MET  SELENOMETHIONINE                                   
HET    MSE  A  46       8                                                       
HET    MSE  A  79       8                                                       
HET    MSE  A 145       8                                                       
HET    MSE  A 146       8                                                       
HET    MSE  A 171       8                                                       
HET    MSE  A 207       8                                                       
HET    MSE  A 258       8                                                       
HET    MSE  A 261       8                                                       
HET    MSE  A 264       8                                                       
HET    MSE  A 312       8                                                       
HET    MSE  A 320       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    11(C5 H11 N O2 SE)                                           
HELIX    1   1 GLU A   58  GLY A   60  5                                   3    
HELIX    2   2 GLN A   62  ILE A   72  1                                  11    
HELIX    3   3 GLU A   83  ASP A   89  5                                   7    
HELIX    4   4 ASP A  104  ALA A  113  1                                  10    
HELIX    5   5 GLY A  119  LYS A  129  1                                  11    
HELIX    6   6 LYS A  157  HIS A  170  1                                  14    
HELIX    7   7 GLY A  193  GLY A  203  1                                  11    
HELIX    8   8 PRO A  209  GLU A  217  1                                   9    
HELIX    9   9 VAL A  228  LYS A  236  1                                   9    
HELIX   10  10 SER A  251  GLU A  263  1                                  13    
HELIX   11  11 GLN A  303  MSE A  312  1                                  10    
HELIX   12  12 GLY A  317  LEU A  322  5                                   6    
SHEET    1   A 4 PHE A  76  MSE A  79  0                                        
SHEET    2   A 4 THR A  51  VAL A  56  1  N  LEU A  55   O  VAL A  77           
SHEET    3   A 4 GLU A  94  VAL A  98  1  O  VAL A  98   N  ILE A  54           
SHEET    4   A 4 ARG A 116  ILE A 118  1  O  ARG A 116   N  PHE A  97           
SHEET    1   B 2 VAL A 149  LEU A 150  0                                        
SHEET    2   B 2 VAL A 174  ILE A 175  1  O  VAL A 174   N  LEU A 150           
SHEET    1   C 3 PHE A 152  THR A 153  0                                        
SHEET    2   C 3 VAL A 187  ASN A 189  1  O  ALA A 188   N  THR A 153           
SHEET    3   C 3 ILE A 206  MSE A 207  1  O  MSE A 207   N  VAL A 187           
SHEET    1   D 2 ILE A 244  LEU A 245  0                                        
SHEET    2   D 2 LYS A 268  TYR A 269  1  O  LYS A 268   N  LEU A 245           
SHEET    1   E 3 PHE A 247  LEU A 248  0                                        
SHEET    2   E 3 HIS A 279  VAL A 282  1  O  VAL A 281   N  LEU A 248           
SHEET    3   E 3 TYR A 299  LYS A 302  1  O  TYR A 299   N  LEU A 280           
LINK         C   GLU A  45                 N   MSE A  46     1555   1555  1.33  
LINK         C   MSE A  46                 N   PRO A  47     1555   1555  1.35  
LINK         C   LYS A  78                 N   MSE A  79     1555   1555  1.33  
LINK         C   MSE A  79                 N   GLU A  80     1555   1555  1.34  
LINK         C   SER A 144                 N   MSE A 145     1555   1555  1.33  
LINK         C   MSE A 145                 N   MSE A 146     1555   1555  1.32  
LINK         C   MSE A 146                 N   ASN A 147     1555   1555  1.33  
LINK         C   HIS A 170                 N   MSE A 171     1555   1555  1.33  
LINK         C   MSE A 171                 N   GLY A 172     1555   1555  1.33  
LINK         C   ILE A 206                 N   MSE A 207     1555   1555  1.33  
LINK         C   MSE A 207                 N   LYS A 208     1555   1555  1.33  
LINK         C   ASN A 257                 N   MSE A 258     1555   1555  1.33  
LINK         C   MSE A 258                 N   GLU A 259     1555   1555  1.33  
LINK         C   GLU A 260                 N   MSE A 261     1555   1555  1.33  
LINK         C   MSE A 261                 N   THR A 262     1555   1555  1.33  
LINK         C   GLU A 263                 N   MSE A 264     1555   1555  1.32  
LINK         C   MSE A 264                 N   GLN A 265     1555   1555  1.32  
LINK         C   GLN A 311                 N   MSE A 312     1555   1555  1.34  
LINK         C   MSE A 312                 N   ASP A 313     1555   1555  1.33  
LINK         C   THR A 319                 N   MSE A 320     1555   1555  1.33  
LINK         C   MSE A 320                 N   TYR A 321     1555   1555  1.33  
CISPEP   1 PHE A  102    GLN A  103          0        -0.26                     
CISPEP   2 MSE A  146    ASN A  147          0         1.46                     
CISPEP   3 MSE A  171    GLY A  172          0        -2.88                     
CRYST1  123.700  123.700   89.244  90.00  90.00 120.00 H 3           9          
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      0.008084  0.004667  0.000000        0.00000                         
SCALE2      0.000000  0.009335  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011205        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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