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Database: PDB
Entry: 6IBE
LinkDB: 6IBE
Original site: 6IBE 
HEADER    CELL ADHESION                           29-NOV-18   6IBE              
TITLE     THE FERM DOMAIN OF HUMAN EPB41L3                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BAND 4.1-LIKE PROTEIN 3;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: 4.1B,DIFFERENTIALLY EXPRESSED IN ADENOCARCINOMA OF THE LUNG 
COMPND   5 PROTEIN 1,DAL-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: EPB41L3, DAL1, KIAA0987;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    FERM DOMAIN, ALZHEIMER'S DISEASE, CELL ADHESION                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.J.BRADSHAW,V.L.KATIS,J.A.NEWMAN,A.FERNANDEZ-CID,N.BURGESS-BROWN,    
AUTHOR   2 F.VON DELFT,C.H.ARROWSMITH,A.EDWARDS,C.BOUNTRA,O.GILEADI             
REVDAT   1   19-DEC-18 6IBE    0                                                
JRNL        AUTH   W.J.BRADSHAW,V.L.KATIS,J.A.NEWMAN,A.FERNANDEZ-CID,           
JRNL        AUTH 2 N.BURGESS-BROWN,F.VON DELFT,C.H.ARROWSMITH,A.EDWARDS,        
JRNL        AUTH 3 C.BOUNTRA,O.GILEADI                                          
JRNL        TITL   THE FERM DOMAIN OF HUMAN EPB41L3                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0238                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 61.59                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 52770                          
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) : 0.156                           
REMARK   3   R VALUE            (WORKING SET) : 0.154                           
REMARK   3   FREE R VALUE                     : 0.200                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1984                            
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) : 1.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.49                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3864                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.98                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 147                          
REMARK   3   BIN FREE R VALUE                    : 0.3150                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2334                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 183                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.26                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.66000                                              
REMARK   3    B22 (A**2) : -0.04000                                             
REMARK   3    B33 (A**2) : -0.62000                                             
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.070         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.067         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.049         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.926         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.952                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2599 ; 0.012 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  2402 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3507 ; 1.695 ; 1.649       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5596 ; 1.459 ; 1.581       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   317 ; 6.669 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   150 ;30.935 ;21.800       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   466 ;13.645 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;18.946 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   315 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2893 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   584 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  1214 ; 3.403 ; 2.267       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1213 ; 3.404 ; 2.265       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1525 ; 3.957 ; 3.418       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1526 ; 3.956 ; 3.420       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1385 ; 4.539 ; 2.801       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1383 ; 4.536 ; 2.800       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1975 ; 5.683 ; 4.007       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  2826 ; 5.256 ;26.435       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  2796 ; 5.242 ;26.198       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  5001 ; 3.032 ; 3.000       
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 : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 6IBE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-NOV-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200013159.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-MAY-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9762                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DIALS                              
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54827                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 78.690                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.53600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2HE7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 M AMMONIUM NITRATE, 0.1 M MES, 5%   
REMARK 280  (V/V) ETHYLENE GLYCOL, 5% (W/V) PEG 2000, 5% (W/V) PEG 3350, 5%     
REMARK 280  (W/V) PEG 4000, 5% (W/V) PEG 5000 MME, PH 6.0, VAPOR DIFFUSION,     
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       19.45750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.49050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.34350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.49050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.45750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.34350            
REMARK 290   SMTRY3   4  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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 19.0 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 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     SER A   105                                                      
REMARK 465     MET A   106                                                      
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    HOH A   588     O    HOH A   597              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CE   LYS A   128     OG   SER A   251     3654     2.01            
REMARK 500   CD   LYS A   128     O    SER A   251     3654     2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 176     -104.48     53.07                                   
REMARK 500    PHE A 255       19.23   -150.77                                   
REMARK 500    ASP A 325       47.30     91.69                                   
REMARK 500    ILE A 329      -73.63   -128.32                                   
REMARK 500    ARG A 344     -126.43     59.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 407                 
DBREF  6IBE A  107   390  UNP    Q9Y2J2   E41L3_HUMAN    107    390             
SEQADV 6IBE SER A  105  UNP  Q9Y2J2              EXPRESSION TAG                 
SEQADV 6IBE MET A  106  UNP  Q9Y2J2              EXPRESSION TAG                 
SEQRES   1 A  286  SER MET PRO LYS SER MET GLN CYS LYS VAL ILE LEU LEU          
SEQRES   2 A  286  ASP GLY SER GLU TYR THR CYS ASP VAL GLU LYS ARG SER          
SEQRES   3 A  286  ARG GLY GLN VAL LEU PHE ASP LYS VAL CYS GLU HIS LEU          
SEQRES   4 A  286  ASN LEU LEU GLU LYS ASP TYR PHE GLY LEU THR TYR ARG          
SEQRES   5 A  286  ASP ALA GLU ASN GLN LYS ASN TRP LEU ASP PRO ALA LYS          
SEQRES   6 A  286  GLU ILE LYS LYS GLN VAL ARG SER GLY ALA TRP HIS PHE          
SEQRES   7 A  286  SER PHE ASN VAL LYS PHE TYR PRO PRO ASP PRO ALA GLN          
SEQRES   8 A  286  LEU SER GLU ASP ILE THR ARG TYR TYR LEU CYS LEU GLN          
SEQRES   9 A  286  LEU ARG ASP ASP ILE VAL SER GLY ARG LEU PRO CYS SER          
SEQRES  10 A  286  PHE VAL THR LEU ALA LEU LEU GLY SER TYR THR VAL GLN          
SEQRES  11 A  286  SER GLU LEU GLY ASP TYR ASP PRO ASP GLU CYS GLY SER          
SEQRES  12 A  286  ASP TYR ILE SER GLU PHE ARG PHE ALA PRO ASN HIS THR          
SEQRES  13 A  286  LYS GLU LEU GLU ASP LYS VAL ILE GLU LEU HIS LYS SER          
SEQRES  14 A  286  HIS ARG GLY MET THR PRO ALA GLU ALA GLU MET HIS PHE          
SEQRES  15 A  286  LEU GLU ASN ALA LYS LYS LEU SER MET TYR GLY VAL ASP          
SEQRES  16 A  286  LEU HIS HIS ALA LYS ASP SER GLU GLY VAL GLU ILE MET          
SEQRES  17 A  286  LEU GLY VAL CYS ALA SER GLY LEU LEU ILE TYR ARG ASP          
SEQRES  18 A  286  ARG LEU ARG ILE ASN ARG PHE ALA TRP PRO LYS VAL LEU          
SEQRES  19 A  286  LYS ILE SER TYR LYS ARG ASN ASN PHE TYR ILE LYS ILE          
SEQRES  20 A  286  ARG PRO GLY GLU PHE GLU GLN PHE GLU SER THR ILE GLY          
SEQRES  21 A  286  PHE LYS LEU PRO ASN HIS ARG ALA ALA LYS ARG LEU TRP          
SEQRES  22 A  286  LYS VAL CYS VAL GLU HIS HIS THR PHE PHE ARG LEU LEU          
HET    EDO  A 401       4                                                       
HET    EDO  A 402       4                                                       
HET    EDO  A 403       4                                                       
HET    EDO  A 404       4                                                       
HET    EDO  A 405       4                                                       
HET    EDO  A 406       4                                                       
HET    MES  A 407      12                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  EDO    6(C2 H6 O2)                                                  
FORMUL   8  MES    C6 H13 N O4 S                                                
FORMUL   9  HOH   *183(H2 O)                                                    
HELIX    1 AA1 ARG A  131  LEU A  143  1                                  13    
HELIX    2 AA2 GLU A  147  ASP A  149  5                                   3    
HELIX    3 AA3 ILE A  171  ARG A  176  1                                   6    
HELIX    4 AA4 ASP A  192  LEU A  196  5                                   5    
HELIX    5 AA5 GLU A  198  SER A  215  1                                  18    
HELIX    6 AA6 SER A  221  GLY A  238  1                                  18    
HELIX    7 AA7 THR A  260  SER A  273  1                                  14    
HELIX    8 AA8 THR A  278  LYS A  291  1                                  14    
HELIX    9 AA9 ASN A  369  LEU A  390  1                                  22    
SHEET    1 AA1 5 GLU A 121  GLU A 127  0                                        
SHEET    2 AA1 5 SER A 109  ILE A 115 -1  N  CYS A 112   O  CYS A 124           
SHEET    3 AA1 5 HIS A 181  VAL A 186  1  O  PHE A 182   N  LYS A 113           
SHEET    4 AA1 5 PHE A 151  ARG A 156 -1  N  THR A 154   O  SER A 183           
SHEET    5 AA1 5 LYS A 162  TRP A 164 -1  O  ASN A 163   N  TYR A 155           
SHEET    1 AA2 7 ARG A 328  ALA A 333  0                                        
SHEET    2 AA2 7 GLY A 319  TYR A 323 -1  N  LEU A 320   O  PHE A 332           
SHEET    3 AA2 7 GLU A 310  VAL A 315 -1  N  MET A 312   O  TYR A 323           
SHEET    4 AA2 7 ASP A 299  ASP A 305 -1  N  ALA A 303   O  ILE A 311           
SHEET    5 AA2 7 SER A 361  LYS A 366 -1  O  LYS A 366   N  LYS A 304           
SHEET    6 AA2 7 ASN A 346  ILE A 351 -1  N  ILE A 351   O  SER A 361           
SHEET    7 AA2 7 VAL A 337  LYS A 343 -1  N  LYS A 339   O  LYS A 350           
SITE     1 AC1  6 TYR A 203  LEU A 207  ARG A 210  SER A 235                    
SITE     2 AC1  6 GLU A 236  HOH A 550                                          
SITE     1 AC2  3 SER A 318  ARG A 331  HOH A 521                               
SITE     1 AC3  6 LEU A 116  ASP A 118  SER A 120  HIS A 142                    
SITE     2 AC3  6 LEU A 143  HOH A 642                                          
SITE     1 AC4  7 TYR A 189  ASP A 212  ARG A 217  VAL A 298                    
SITE     2 AC4  7 HOH A 505  HOH A 546  HOH A 655                               
SITE     1 AC5  5 THR A 154  TYR A 155  ARG A 156  PHE A 182                    
SITE     2 AC5  5 SER A 183                                                     
SITE     1 AC6  4 VAL A 134  ASP A 137  LYS A 292  HOH A 534                    
SITE     1 AC7  6 PHE A 222  GLU A 262  PHE A 386  HOH A 524                    
SITE     2 AC7  6 HOH A 574  HOH A 632                                          
CRYST1   38.915   78.687   98.981  90.00  90.00  90.00 P 21 21 21    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      0.025697  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012709  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010103        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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