GenomeNet

Database: PDB
Entry: 2EJ8
LinkDB: 2EJ8
Original site: 2EJ8 
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   15-MAR-07   2EJ8              
TITLE     CRYSTAL STRUCTURE OF APPL1 PTB DOMAIN AT 1.8A                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DCC-INTERACTING PROTEIN 13 ALPHA;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: DIP13 ALPHA, ADAPTER PROTEIN CONTAINING PH DOMAIN,          
COMPND   5 PTB DOMAIN AND LEUCINE ZIPPER MOTIF 1;                               
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: APPL1;                                                         
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 OTHER_DETAILS: E.COLI CELL-FREE EXPRESSION SYSTEM                    
KEYWDS    STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN              
KEYWDS   2 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL                 
KEYWDS   3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.TANABE,T.HOSAKA,K.MURAYAMA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,          
AUTHOR   2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)               
REVDAT   2   24-FEB-09 2EJ8    1       VERSN                                    
REVDAT   1   18-MAR-08 2EJ8    0                                                
JRNL        AUTH   H.TANABE,T.HOSAKA,K.MURAYAMA,T.TERADA,M.SHIROUZU,            
JRNL        AUTH 2 S.YOKOYAMA                                                   
JRNL        TITL   CRYSTAL STRUCTURE OF APPL1 PTB DOMAIN AT 1.8A                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.84 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 23949                          
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) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1280                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.84                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.89                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1784                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 72                           
REMARK   3   BIN FREE R VALUE                    : 0.3130                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2105                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 168                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.70000                                             
REMARK   3    B22 (A**2) : 0.16000                                              
REMARK   3    B33 (A**2) : -0.12000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.48000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.142         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.133         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.093         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.075         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2123 ; 0.018 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1923 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2878 ; 1.438 ; 1.954       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4449 ; 0.805 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   260 ; 5.684 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   346 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2328 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   426 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   449 ; 0.364 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2287 ; 0.253 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1310 ; 0.082 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   126 ; 0.165 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     9 ; 0.174 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    28 ; 0.257 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.263 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1316 ; 1.476 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2143 ; 2.797 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   807 ; 3.793 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   735 ; 6.408 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.; ANOMALOUS DATA WAS USED IN THE REFINEMENT.       
REMARK   3  THE FRIEDEL PAIRS WERE USED FOR POHASING.                           
REMARK   4                                                                      
REMARK   4 2EJ8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-APR-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB026730.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-DEC-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97900                            
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24816                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.840                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 3.565                              
REMARK 200  R MERGE                    (I) : 0.10400                            
REMARK 200  R SYM                      (I) : 0.10300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.5980                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.33100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.738                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SNB                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THE STRUCTURE FACTOR FILE CONTAINS FRIEDEL PAIRS.            
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM NA CITRATE, 10% PEG 3350, 15%      
REMARK 280  ISOPROPANOL, PH 5.0, VAPOR DIFFUSION, HANGING DROP,                 
REMARK 280  TEMPERATURE 277K                                                    
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       31.78300            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1790 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.8 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     GLY A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     GLY A   109                                                      
REMARK 465     ARG A   110                                                      
REMARK 465     SER A   111                                                      
REMARK 465     GLU A   112                                                      
REMARK 465     SER A   113                                                      
REMARK 465     ASN A   114                                                      
REMARK 465     LEU A   147                                                      
REMARK 465     ASP A   148                                                      
REMARK 465     ARG A   149                                                      
REMARK 465     ARG A   150                                                      
REMARK 465     ALA A   151                                                      
REMARK 465     SER A   152                                                      
REMARK 465     GLU A   153                                                      
REMARK 465     LYS A   154                                                      
REMARK 465     GLN A   155                                                      
REMARK 465     LYS A   156                                                      
REMARK 465     GLU A   157                                                      
REMARK 465     ILE A   158                                                      
REMARK 465     GLU A   159                                                      
REMARK 465     ARG A   160                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     GLU B     8                                                      
REMARK 465     THR B     9                                                      
REMARK 465     GLU B    10                                                      
REMARK 465     SER B   108                                                      
REMARK 465     GLY B   109                                                      
REMARK 465     ARG B   110                                                      
REMARK 465     SER B   111                                                      
REMARK 465     GLU B   112                                                      
REMARK 465     SER B   113                                                      
REMARK 465     ASN B   114                                                      
REMARK 465     ARG B   149                                                      
REMARK 465     ARG B   150                                                      
REMARK 465     ALA B   151                                                      
REMARK 465     SER B   152                                                      
REMARK 465     GLU B   153                                                      
REMARK 465     LYS B   154                                                      
REMARK 465     GLN B   155                                                      
REMARK 465     LYS B   156                                                      
REMARK 465     GLU B   157                                                      
REMARK 465     ILE B   158                                                      
REMARK 465     GLU B   159                                                      
REMARK 465     ARG B   160                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    MET B  26   SD    MET B  26   CE     -0.354                       
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    ASP A  11   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A  66   CB  -  CG  -  OD2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ASP B  31   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP B  72   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 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    HIS A  15       74.90   -159.38                                   
REMARK 500    GLN A  76       17.29     56.89                                   
REMARK 500    ASN A  96       94.50   -161.98                                   
REMARK 500    HIS B  15       75.45   -153.77                                   
REMARK 500    HIS B  33      107.08    -40.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: HSK002201400.1   RELATED DB: TARGETDB                    
DBREF  2EJ8 A    8   160  UNP    Q9UKG1   DP13A_HUMAN    492    644             
DBREF  2EJ8 B    8   160  UNP    Q9UKG1   DP13A_HUMAN    492    644             
SEQADV 2EJ8 GLY A    1  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2EJ8 SER A    2  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2EJ8 SER A    3  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2EJ8 GLY A    4  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2EJ8 SER A    5  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2EJ8 SER A    6  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2EJ8 GLY A    7  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2EJ8 GLY B    1  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2EJ8 SER B    2  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2EJ8 SER B    3  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2EJ8 GLY B    4  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2EJ8 SER B    5  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2EJ8 SER B    6  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2EJ8 GLY B    7  UNP  Q9UKG1              EXPRESSION TAG                 
SEQRES   1 A  160  GLY SER SER GLY SER SER GLY GLU THR GLU ASP SER ILE          
SEQRES   2 A  160  LEU HIS GLN LEU PHE ILE VAL ARG PHE LEU GLY SER MET          
SEQRES   3 A  160  GLU VAL LYS SER ASP ASP HIS PRO ASP VAL VAL TYR GLU          
SEQRES   4 A  160  THR MET ARG GLN ILE LEU ALA ALA ARG ALA ILE HIS ASN          
SEQRES   5 A  160  ILE PHE ARG MET THR GLU SER HIS LEU LEU VAL THR CYS          
SEQRES   6 A  160  ASP CYS LEU LYS LEU ILE ASP PRO GLN THR GLN VAL THR          
SEQRES   7 A  160  ARG LEU THR PHE PRO LEU PRO CYS VAL VAL LEU TYR ALA          
SEQRES   8 A  160  THR HIS GLN GLU ASN LYS ARG LEU PHE GLY PHE VAL LEU          
SEQRES   9 A  160  ARG THR SER SER GLY ARG SER GLU SER ASN LEU SER SER          
SEQRES  10 A  160  VAL CYS TYR ILE PHE GLU SER ASN ASN GLU GLY GLU LYS          
SEQRES  11 A  160  ILE CYS ASP SER VAL GLY LEU ALA LYS GLN ILE ALA LEU          
SEQRES  12 A  160  HIS ALA GLU LEU ASP ARG ARG ALA SER GLU LYS GLN LYS          
SEQRES  13 A  160  GLU ILE GLU ARG                                              
SEQRES   1 B  160  GLY SER SER GLY SER SER GLY GLU THR GLU ASP SER ILE          
SEQRES   2 B  160  LEU HIS GLN LEU PHE ILE VAL ARG PHE LEU GLY SER MET          
SEQRES   3 B  160  GLU VAL LYS SER ASP ASP HIS PRO ASP VAL VAL TYR GLU          
SEQRES   4 B  160  THR MET ARG GLN ILE LEU ALA ALA ARG ALA ILE HIS ASN          
SEQRES   5 B  160  ILE PHE ARG MET THR GLU SER HIS LEU LEU VAL THR CYS          
SEQRES   6 B  160  ASP CYS LEU LYS LEU ILE ASP PRO GLN THR GLN VAL THR          
SEQRES   7 B  160  ARG LEU THR PHE PRO LEU PRO CYS VAL VAL LEU TYR ALA          
SEQRES   8 B  160  THR HIS GLN GLU ASN LYS ARG LEU PHE GLY PHE VAL LEU          
SEQRES   9 B  160  ARG THR SER SER GLY ARG SER GLU SER ASN LEU SER SER          
SEQRES  10 B  160  VAL CYS TYR ILE PHE GLU SER ASN ASN GLU GLY GLU LYS          
SEQRES  11 B  160  ILE CYS ASP SER VAL GLY LEU ALA LYS GLN ILE ALA LEU          
SEQRES  12 B  160  HIS ALA GLU LEU ASP ARG ARG ALA SER GLU LYS GLN LYS          
SEQRES  13 B  160  GLU ILE GLU ARG                                              
FORMUL   3  HOH   *168(H2 O)                                                    
HELIX    1   1 PRO A   34  HIS A   51  1                                  18    
HELIX    2   2 GLU A  127  GLU A  146  1                                  20    
HELIX    3   3 ASP B   35  HIS B   51  1                                  17    
HELIX    4   4 GLU B  127  ASP B  148  1                                  22    
SHEET    1   A 7 THR A  78  PRO A  83  0                                        
SHEET    2   A 7 CYS A  67  ILE A  71 -1  N  LEU A  68   O  PHE A  82           
SHEET    3   A 7 GLU A  58  THR A  64 -1  N  LEU A  62   O  LYS A  69           
SHEET    4   A 7 HIS A  15  VAL A  28 -1  N  VAL A  20   O  SER A  59           
SHEET    5   A 7 SER A 116  SER A 124 -1  O  ILE A 121   N  GLY A  24           
SHEET    6   A 7 ASN A  96  THR A 106 -1  N  PHE A 100   O  PHE A 122           
SHEET    7   A 7 VAL A  87  HIS A  93 -1  N  LEU A  89   O  VAL A 103           
SHEET    1   B 7 THR B  78  PRO B  83  0                                        
SHEET    2   B 7 CYS B  67  ILE B  71 -1  N  LEU B  68   O  PHE B  82           
SHEET    3   B 7 GLU B  58  VAL B  63 -1  N  LEU B  62   O  LYS B  69           
SHEET    4   B 7 GLN B  16  VAL B  28 -1  N  PHE B  18   O  LEU B  61           
SHEET    5   B 7 SER B 116  SER B 124 -1  O  ILE B 121   N  GLY B  24           
SHEET    6   B 7 ASN B  96  THR B 106 -1  N  LEU B 104   O  VAL B 118           
SHEET    7   B 7 VAL B  87  HIS B  93 -1  N  LEU B  89   O  VAL B 103           
CRYST1   45.230   63.566   52.449  90.00 102.67  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      0.022109  0.000000  0.004969        0.00000                         
SCALE2      0.000000  0.015732  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019542        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system