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Database: PDB
Entry: 2HE7
LinkDB: 2HE7
Original site: 2HE7 
HEADER    CELL ADHESION                           21-JUN-06   2HE7              
TITLE     FERM DOMAIN OF EPB41L3 (DAL-1)                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BAND 4.1-LIKE PROTEIN 3;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: FERM DOMAIN (RESIDUES 108-390);                            
COMPND   5 SYNONYM: 4.1B, DIFFERENTIALLY EXPRESSED IN ADENOCARCINOMA OF THE LUNG
COMPND   6 PROTEIN 1, DAL-1;                                                    
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: EPB41L3;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    FERM DOMAIN, DAL-1, EPB41L3A, STRUCTURAL GENOMICS, STRUCTURAL         
KEYWDS   2 GENOMICS CONSORTIUM, SGC, CELL ADHESION                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.M.HALLBERG,R.D.BUSAM,C.ARROWSMITH,H.BERGLUND,R.COLLINS,A.EDWARDS,   
AUTHOR   2 M.EHN,S.FLODIN,A.FLORES,S.GRASLUND,M.HAMMARSTROM,L.H.SCHIAVONE,      
AUTHOR   3 I.JOHANSSON,M.HOGBOM,T.KARLBERG,T.KOTENYOVA,J.NILVEBRANDT,P.NORBERG, 
AUTHOR   4 P.STENMARK,P.NORDLUND,P.NILSSON-EHLE,T.NYMAN,D.OGG,J.SAGEMARK,       
AUTHOR   5 M.SUNDSTROM,J.UPPENBERG,S.VAN DEN BERG,J.WEIGELT,C.PERSSON,          
AUTHOR   6 A.G.THORSELL,STRUCTURAL GENOMICS CONSORTIUM (SGC)                    
REVDAT   4   16-FEB-11 2HE7    1       JRNL                                     
REVDAT   3   05-JAN-11 2HE7    1       JRNL                                     
REVDAT   2   24-FEB-09 2HE7    1       VERSN                                    
REVDAT   1   04-JUL-06 2HE7    0                                                
JRNL        AUTH   R.D.BUSAM,A.G.THORSELL,A.FLORES,M.HAMMARSTROM,C.PERSSON,     
JRNL        AUTH 2 B.OBRINK,B.M.HALLBERG                                        
JRNL        TITL   STRUCTURAL BASIS OF TUMOR SUPPRESSOR IN LUNG CANCER 1        
JRNL        TITL 2 (TSLC1) BINDING TO DIFFERENTIALLY EXPRESSED IN               
JRNL        TITL 3 ADENOCARCINOMA OF THE LUNG (DAL-1/4.1B).                     
JRNL        REF    J.BIOL.CHEM.                  V. 286  4511 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21131357                                                     
JRNL        DOI    10.1074/JBC.M110.174011                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.34                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 35521                          
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) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1779                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2479                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.96                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 114                          
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2323                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 247                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.15                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.17                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.32000                                             
REMARK   3    B22 (A**2) : -0.32000                                             
REMARK   3    B33 (A**2) : 0.48000                                              
REMARK   3    B12 (A**2) : -0.16000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.130         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.125         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.097         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.495         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2521 ; 0.021 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1791 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3416 ; 1.735 ; 1.954       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4334 ; 0.982 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   309 ; 6.241 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   129 ;36.307 ;23.101       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   459 ;15.931 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;16.261 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   352 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2861 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   561 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   466 ; 0.211 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1817 ; 0.194 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1199 ; 0.185 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1350 ; 0.091 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   178 ; 0.168 ; 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):     6 ; 0.096 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    32 ; 0.283 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    21 ; 0.197 ; 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):  1930 ; 1.678 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   597 ; 0.286 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2425 ; 1.894 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1195 ; 3.126 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   991 ; 4.325 ; 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 : 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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2HE7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB038250.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAY-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35521                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 11.000                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.1300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.800                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% ETOH  0.1 M TRIS PH 8.5, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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       33.20000            
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       16.60000            
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       24.90000            
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        8.30000            
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       41.50000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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     LYS A 108    CG   CD   CE   NZ                                   
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    GLU A 121   CG    GLU A 121   CD      0.092                       
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    ARG A 344     -126.03     57.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2HE7 A  108   390  UNP    Q9Y2J2   E41L3_HUMAN    108    390             
SEQRES   1 A  283  LYS SER MET GLN CYS LYS VAL ILE LEU LEU ASP GLY SER          
SEQRES   2 A  283  GLU TYR THR CYS ASP VAL GLU LYS ARG SER ARG GLY GLN          
SEQRES   3 A  283  VAL LEU PHE ASP LYS VAL CYS GLU HIS LEU ASN LEU LEU          
SEQRES   4 A  283  GLU LYS ASP TYR PHE GLY LEU THR TYR ARG ASP ALA GLU          
SEQRES   5 A  283  ASN GLN LYS ASN TRP LEU ASP PRO ALA LYS GLU ILE LYS          
SEQRES   6 A  283  LYS GLN VAL ARG SER GLY ALA TRP HIS PHE SER PHE ASN          
SEQRES   7 A  283  VAL LYS PHE TYR PRO PRO ASP PRO ALA GLN LEU SER GLU          
SEQRES   8 A  283  ASP ILE THR ARG TYR TYR LEU CYS LEU GLN LEU ARG ASP          
SEQRES   9 A  283  ASP ILE VAL SER GLY ARG LEU PRO CYS SER PHE VAL THR          
SEQRES  10 A  283  LEU ALA LEU LEU GLY SER TYR THR VAL GLN SER GLU LEU          
SEQRES  11 A  283  GLY ASP TYR ASP PRO ASP GLU CYS GLY SER ASP TYR ILE          
SEQRES  12 A  283  SER GLU PHE ARG PHE ALA PRO ASN HIS THR LYS GLU LEU          
SEQRES  13 A  283  GLU ASP LYS VAL ILE GLU LEU HIS LYS SER HIS ARG GLY          
SEQRES  14 A  283  MET THR PRO ALA GLU ALA GLU MET HIS PHE LEU GLU ASN          
SEQRES  15 A  283  ALA LYS LYS LEU SER MET TYR GLY VAL ASP LEU HIS HIS          
SEQRES  16 A  283  ALA LYS ASP SER GLU GLY VAL GLU ILE MET LEU GLY VAL          
SEQRES  17 A  283  CYS ALA SER GLY LEU LEU ILE TYR ARG ASP ARG LEU ARG          
SEQRES  18 A  283  ILE ASN ARG PHE ALA TRP PRO LYS VAL LEU LYS ILE SER          
SEQRES  19 A  283  TYR LYS ARG ASN ASN PHE TYR ILE LYS ILE ARG PRO GLY          
SEQRES  20 A  283  GLU PHE GLU GLN PHE GLU SER THR ILE GLY PHE LYS LEU          
SEQRES  21 A  283  PRO ASN HIS ARG ALA ALA LYS ARG LEU TRP LYS VAL CYS          
SEQRES  22 A  283  VAL GLU HIS HIS THR PHE PHE ARG LEU LEU                      
FORMUL   2  HOH   *247(H2 O)                                                    
HELIX    1   1 ARG A  131  LEU A  143  1                                  13    
HELIX    2   2 GLU A  147  ASP A  149  5                                   3    
HELIX    3   3 GLU A  170  VAL A  175  1                                   6    
HELIX    4   4 ASP A  192  LEU A  196  5                                   5    
HELIX    5   5 GLU A  198  SER A  215  1                                  18    
HELIX    6   6 SER A  221  GLY A  238  1                                  18    
HELIX    7   7 THR A  260  HIS A  274  1                                  15    
HELIX    8   8 THR A  278  LYS A  291  1                                  14    
HELIX    9   9 PRO A  335  VAL A  337  5                                   3    
HELIX   10  10 ASN A  369  LEU A  389  1                                  21    
SHEET    1   A 5 GLU A 121  GLU A 127  0                                        
SHEET    2   A 5 SER A 109  ILE A 115 -1  N  CYS A 112   O  CYS A 124           
SHEET    3   A 5 TRP A 180  VAL A 186  1  O  PHE A 182   N  ILE A 115           
SHEET    4   A 5 PHE A 151  ARG A 156 -1  N  GLY A 152   O  ASN A 185           
SHEET    5   A 5 LYS A 162  TRP A 164 -1  O  ASN A 163   N  TYR A 155           
SHEET    1   B 4 ASP A 299  LYS A 304  0                                        
SHEET    2   B 4 GLU A 310  VAL A 315 -1  O  LEU A 313   N  HIS A 301           
SHEET    3   B 4 GLY A 319  ARG A 324 -1  O  LEU A 321   N  GLY A 314           
SHEET    4   B 4 LEU A 327  ALA A 333 -1  O  ILE A 329   N  ILE A 322           
SHEET    1   C 3 LYS A 339  LYS A 343  0                                        
SHEET    2   C 3 ASN A 346  ILE A 351 -1  O  TYR A 348   N  SER A 341           
SHEET    3   C 3 SER A 361  LYS A 366 -1  O  ILE A 363   N  ILE A 349           
CRYST1  135.500  135.500   49.800  90.00  90.00 120.00 P 65          6          
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      0.007380  0.004261  0.000000        0.00000                         
SCALE2      0.000000  0.008522  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020080        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system