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LongText Report for: 6l4g-pdb

Name Class
6l4g-pdb
HEADER    SIGNALING PROTEIN                       16-OCT-19   6L4G              
TITLE     CRYSTAL STRUCTURE OF HUMAN NDRG3 I171M/S176H MUTANT                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN NDRG3;                                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: N-MYC DOWNSTREAM-REGULATED GENE 3 PROTEIN;                  
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: NDRG3;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ALPHA/BETA-HYDROLASE FOLD, NDRG3, UNFOLDED HELIX, SIGNALING PROTEIN   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.R.KIM,B.W.HAN                                                       
REVDAT   1   26-AUG-20 6L4G    0                                                
JRNL        AUTH   K.R.KIM,K.A.KIM,J.S.PARK,J.Y.JANG,Y.CHOI,H.H.LEE,D.C.LEE,    
JRNL        AUTH 2 K.C.PARK,Y.I.YEOM,H.J.KIM,B.W.HAN                            
JRNL        TITL   STRUCTURAL AND BIOPHYSICAL ANALYSES OF HUMAN N-MYC           
JRNL        TITL 2 DOWNSTREAM-REGULATED GENE 3 (NDRG3) PROTEIN.                 
JRNL        REF    BIOMOLECULES                  V.  10       2020              
JRNL        REFN                   ESSN 2218-273X                               
JRNL        PMID   31935861                                                     
JRNL        DOI    10.3390/BIOM10010090                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0257                                      
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) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 9141                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R-VALUE                    
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.792                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 438                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.39                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 352                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 49.46                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2300                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 17                           
REMARK   3   BIN FREE R VALUE                    : 0.2260                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4344                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 6                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.22                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -8.69400                                             
REMARK   3    B22 (A**2) : -8.69400                                             
REMARK   3    B33 (A**2) : 17.38900                                             
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.118         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.882                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.868                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4437 ; 0.004 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  4040 ; 0.036 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6033 ; 1.279 ; 1.635       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9424 ; 2.319 ; 1.567       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   556 ; 6.054 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   226 ;29.968 ;24.381       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   733 ;11.691 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;15.386 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   585 ; 0.047 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4980 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   832 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1084 ; 0.214 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    73 ; 0.330 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2166 ; 0.151 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    98 ; 0.190 ; 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):  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):  2236 ; 1.828 ; 3.610       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2235 ; 1.827 ; 3.609       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2788 ; 3.282 ; 5.400       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2789 ; 3.281 ; 5.402       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2201 ; 1.226 ; 3.694       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2201 ; 1.226 ; 3.694       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3245 ; 2.305 ; 5.499       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3246 ; 2.305 ; 5.500       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.4992                                          
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : -K, -H, -L                                      
REMARK   3      TWIN FRACTION : 0.5008                                          
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 THEIR        
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 6L4G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-OCT-19.                  
REMARK 100 THE DEPOSITION ID IS D_1300014172.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-OCT-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 11C                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97942                            
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 : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10073                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 10.50                              
REMARK 200  R MERGE                    (I) : 0.16400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.36                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 6L4B                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM AMMONIUM CITRATE TRIBASIC PH      
REMARK 280  7.0 AND 20% PEG3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  295K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
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   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.50400            
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       37.25200            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       37.25200            
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       74.50400            
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: DIMERIC                           
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     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     VAL A     7                                                      
REMARK 465     GLN A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     THR A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     ILE A    12                                                      
REMARK 465     LYS A    13                                                      
REMARK 465     PRO A    14                                                      
REMARK 465     LEU A    15                                                      
REMARK 465     LEU A    16                                                      
REMARK 465     ASN A    17                                                      
REMARK 465     ASP A    18                                                      
REMARK 465     LYS A    19                                                      
REMARK 465     ASN A    20                                                      
REMARK 465     GLY A    21                                                      
REMARK 465     THR A    22                                                      
REMARK 465     ARG A    23                                                      
REMARK 465     ASN A    24                                                      
REMARK 465     PHE A    25                                                      
REMARK 465     GLN A    26                                                      
REMARK 465     ASP A    27                                                      
REMARK 465     PHE A    28                                                      
REMARK 465     GLY A   169                                                      
REMARK 465     TRP A   170                                                      
REMARK 465     MET A   171                                                      
REMARK 465     ASP A   172                                                      
REMARK 465     TRP A   173                                                      
REMARK 465     ALA A   174                                                      
REMARK 465     ALA A   175                                                      
REMARK 465     HIS A   176                                                      
REMARK 465     LYS A   177                                                      
REMARK 465     LEU A   178                                                      
REMARK 465     SER A   179                                                      
REMARK 465     GLY A   180                                                      
REMARK 465     LEU A   181                                                      
REMARK 465     THR A   182                                                      
REMARK 465     MET A   321                                                      
REMARK 465     THR A   322                                                      
REMARK 465     ARG A   323                                                      
REMARK 465     LEU A   324                                                      
REMARK 465     ALA A   325                                                      
REMARK 465     ARG A   326                                                      
REMARK 465     SER A   327                                                      
REMARK 465     ARG A   328                                                      
REMARK 465     THR A   329                                                      
REMARK 465     HIS A   330                                                      
REMARK 465     SER A   331                                                      
REMARK 465     THR A   332                                                      
REMARK 465     SER A   333                                                      
REMARK 465     SER A   334                                                      
REMARK 465     SER A   335                                                      
REMARK 465     LEU A   336                                                      
REMARK 465     GLY A   337                                                      
REMARK 465     SER A   338                                                      
REMARK 465     GLY A   339                                                      
REMARK 465     GLU A   340                                                      
REMARK 465     SER A   341                                                      
REMARK 465     PRO A   342                                                      
REMARK 465     PHE A   343                                                      
REMARK 465     SER A   344                                                      
REMARK 465     ARG A   345                                                      
REMARK 465     SER A   346                                                      
REMARK 465     VAL A   347                                                      
REMARK 465     THR A   348                                                      
REMARK 465     SER A   349                                                      
REMARK 465     ASN A   350                                                      
REMARK 465     GLN A   351                                                      
REMARK 465     SER A   352                                                      
REMARK 465     ASP A   353                                                      
REMARK 465     GLY A   354                                                      
REMARK 465     THR A   355                                                      
REMARK 465     GLN A   356                                                      
REMARK 465     GLU A   357                                                      
REMARK 465     SER A   358                                                      
REMARK 465     CYS A   359                                                      
REMARK 465     GLU A   360                                                      
REMARK 465     SER A   361                                                      
REMARK 465     PRO A   362                                                      
REMARK 465     ASP A   363                                                      
REMARK 465     VAL A   364                                                      
REMARK 465     LEU A   365                                                      
REMARK 465     ASP A   366                                                      
REMARK 465     ARG A   367                                                      
REMARK 465     HIS A   368                                                      
REMARK 465     GLN A   369                                                      
REMARK 465     THR A   370                                                      
REMARK 465     MET A   371                                                      
REMARK 465     GLU A   372                                                      
REMARK 465     VAL A   373                                                      
REMARK 465     SER A   374                                                      
REMARK 465     CYS A   375                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     GLN B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     VAL B     7                                                      
REMARK 465     GLN B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     THR B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     ILE B    12                                                      
REMARK 465     LYS B    13                                                      
REMARK 465     PRO B    14                                                      
REMARK 465     LEU B    15                                                      
REMARK 465     LEU B    16                                                      
REMARK 465     ASN B    17                                                      
REMARK 465     ASP B    18                                                      
REMARK 465     LYS B    19                                                      
REMARK 465     ASN B    20                                                      
REMARK 465     GLY B    21                                                      
REMARK 465     THR B    22                                                      
REMARK 465     ARG B    23                                                      
REMARK 465     ASN B    24                                                      
REMARK 465     PHE B    25                                                      
REMARK 465     GLN B    26                                                      
REMARK 465     ASP B    27                                                      
REMARK 465     PHE B    28                                                      
REMARK 465     TRP B   173                                                      
REMARK 465     ALA B   174                                                      
REMARK 465     ALA B   175                                                      
REMARK 465     HIS B   176                                                      
REMARK 465     LYS B   177                                                      
REMARK 465     LEU B   178                                                      
REMARK 465     SER B   179                                                      
REMARK 465     GLY B   180                                                      
REMARK 465     LEU B   181                                                      
REMARK 465     THR B   182                                                      
REMARK 465     MET B   321                                                      
REMARK 465     THR B   322                                                      
REMARK 465     ARG B   323                                                      
REMARK 465     LEU B   324                                                      
REMARK 465     ALA B   325                                                      
REMARK 465     ARG B   326                                                      
REMARK 465     SER B   327                                                      
REMARK 465     ARG B   328                                                      
REMARK 465     THR B   329                                                      
REMARK 465     HIS B   330                                                      
REMARK 465     SER B   331                                                      
REMARK 465     THR B   332                                                      
REMARK 465     SER B   333                                                      
REMARK 465     SER B   334                                                      
REMARK 465     SER B   335                                                      
REMARK 465     LEU B   336                                                      
REMARK 465     GLY B   337                                                      
REMARK 465     SER B   338                                                      
REMARK 465     GLY B   339                                                      
REMARK 465     GLU B   340                                                      
REMARK 465     SER B   341                                                      
REMARK 465     PRO B   342                                                      
REMARK 465     PHE B   343                                                      
REMARK 465     SER B   344                                                      
REMARK 465     ARG B   345                                                      
REMARK 465     SER B   346                                                      
REMARK 465     VAL B   347                                                      
REMARK 465     THR B   348                                                      
REMARK 465     SER B   349                                                      
REMARK 465     ASN B   350                                                      
REMARK 465     GLN B   351                                                      
REMARK 465     SER B   352                                                      
REMARK 465     ASP B   353                                                      
REMARK 465     GLY B   354                                                      
REMARK 465     THR B   355                                                      
REMARK 465     GLN B   356                                                      
REMARK 465     GLU B   357                                                      
REMARK 465     SER B   358                                                      
REMARK 465     CYS B   359                                                      
REMARK 465     GLU B   360                                                      
REMARK 465     SER B   361                                                      
REMARK 465     PRO B   362                                                      
REMARK 465     ASP B   363                                                      
REMARK 465     VAL B   364                                                      
REMARK 465     LEU B   365                                                      
REMARK 465     ASP B   366                                                      
REMARK 465     ARG B   367                                                      
REMARK 465     HIS B   368                                                      
REMARK 465     GLN B   369                                                      
REMARK 465     THR B   370                                                      
REMARK 465     MET B   371                                                      
REMARK 465     GLU B   372                                                      
REMARK 465     VAL B   373                                                      
REMARK 465     SER B   374                                                      
REMARK 465     CYS B   375                                                      
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    PRO B   294     O    VAL B   297              2.10            
REMARK 500   O    GLU A   272     OG   SER A   275              2.18            
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    TRP B 170       64.91   -119.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6L4G A    1   375  UNP    Q9UGV2   NDRG3_HUMAN      1    375             
DBREF  6L4G B    1   375  UNP    Q9UGV2   NDRG3_HUMAN      1    375             
SEQADV 6L4G MET A  171  UNP  Q9UGV2    ILE   171 ENGINEERED MUTATION            
SEQADV 6L4G HIS A  176  UNP  Q9UGV2    SER   176 ENGINEERED MUTATION            
SEQADV 6L4G MET B  171  UNP  Q9UGV2    ILE   171 ENGINEERED MUTATION            
SEQADV 6L4G HIS B  176  UNP  Q9UGV2    SER   176 ENGINEERED MUTATION            
SEQRES   1 A  375  MET ASP GLU LEU GLN ASP VAL GLN LEU THR GLU ILE LYS          
SEQRES   2 A  375  PRO LEU LEU ASN ASP LYS ASN GLY THR ARG ASN PHE GLN          
SEQRES   3 A  375  ASP PHE ASP CYS GLN GLU HIS ASP ILE GLU THR THR HIS          
SEQRES   4 A  375  GLY VAL VAL HIS VAL THR ILE ARG GLY LEU PRO LYS GLY          
SEQRES   5 A  375  ASN ARG PRO VAL ILE LEU THR TYR HIS ASP ILE GLY LEU          
SEQRES   6 A  375  ASN HIS LYS SER CYS PHE ASN ALA PHE PHE ASN PHE GLU          
SEQRES   7 A  375  ASP MET GLN GLU ILE THR GLN HIS PHE ALA VAL CYS HIS          
SEQRES   8 A  375  VAL ASP ALA PRO GLY GLN GLN GLU GLY ALA PRO SER PHE          
SEQRES   9 A  375  PRO THR GLY TYR GLN TYR PRO THR MET ASP GLU LEU ALA          
SEQRES  10 A  375  GLU MET LEU PRO PRO VAL LEU THR HIS LEU SER LEU LYS          
SEQRES  11 A  375  SER ILE ILE GLY ILE GLY VAL GLY ALA GLY ALA TYR ILE          
SEQRES  12 A  375  LEU SER ARG PHE ALA LEU ASN HIS PRO GLU LEU VAL GLU          
SEQRES  13 A  375  GLY LEU VAL LEU ILE ASN VAL ASP PRO CYS ALA LYS GLY          
SEQRES  14 A  375  TRP MET ASP TRP ALA ALA HIS LYS LEU SER GLY LEU THR          
SEQRES  15 A  375  THR ASN VAL VAL ASP ILE ILE LEU ALA HIS HIS PHE GLY          
SEQRES  16 A  375  GLN GLU GLU LEU GLN ALA ASN LEU ASP LEU ILE GLN THR          
SEQRES  17 A  375  TYR ARG MET HIS ILE ALA GLN ASP ILE ASN GLN ASP ASN          
SEQRES  18 A  375  LEU GLN LEU PHE LEU ASN SER TYR ASN GLY ARG ARG ASP          
SEQRES  19 A  375  LEU GLU ILE GLU ARG PRO ILE LEU GLY GLN ASN ASP ASN          
SEQRES  20 A  375  LYS SER LYS THR LEU LYS CYS SER THR LEU LEU VAL VAL          
SEQRES  21 A  375  GLY ASP ASN SER PRO ALA VAL GLU ALA VAL VAL GLU CYS          
SEQRES  22 A  375  ASN SER ARG LEU ASN PRO ILE ASN THR THR LEU LEU LYS          
SEQRES  23 A  375  MET ALA ASP CYS GLY GLY LEU PRO GLN VAL VAL GLN PRO          
SEQRES  24 A  375  GLY LYS LEU THR GLU ALA PHE LYS TYR PHE LEU GLN GLY          
SEQRES  25 A  375  MET GLY TYR ILE PRO SER ALA SER MET THR ARG LEU ALA          
SEQRES  26 A  375  ARG SER ARG THR HIS SER THR SER SER SER LEU GLY SER          
SEQRES  27 A  375  GLY GLU SER PRO PHE SER ARG SER VAL THR SER ASN GLN          
SEQRES  28 A  375  SER ASP GLY THR GLN GLU SER CYS GLU SER PRO ASP VAL          
SEQRES  29 A  375  LEU ASP ARG HIS GLN THR MET GLU VAL SER CYS                  
SEQRES   1 B  375  MET ASP GLU LEU GLN ASP VAL GLN LEU THR GLU ILE LYS          
SEQRES   2 B  375  PRO LEU LEU ASN ASP LYS ASN GLY THR ARG ASN PHE GLN          
SEQRES   3 B  375  ASP PHE ASP CYS GLN GLU HIS ASP ILE GLU THR THR HIS          
SEQRES   4 B  375  GLY VAL VAL HIS VAL THR ILE ARG GLY LEU PRO LYS GLY          
SEQRES   5 B  375  ASN ARG PRO VAL ILE LEU THR TYR HIS ASP ILE GLY LEU          
SEQRES   6 B  375  ASN HIS LYS SER CYS PHE ASN ALA PHE PHE ASN PHE GLU          
SEQRES   7 B  375  ASP MET GLN GLU ILE THR GLN HIS PHE ALA VAL CYS HIS          
SEQRES   8 B  375  VAL ASP ALA PRO GLY GLN GLN GLU GLY ALA PRO SER PHE          
SEQRES   9 B  375  PRO THR GLY TYR GLN TYR PRO THR MET ASP GLU LEU ALA          
SEQRES  10 B  375  GLU MET LEU PRO PRO VAL LEU THR HIS LEU SER LEU LYS          
SEQRES  11 B  375  SER ILE ILE GLY ILE GLY VAL GLY ALA GLY ALA TYR ILE          
SEQRES  12 B  375  LEU SER ARG PHE ALA LEU ASN HIS PRO GLU LEU VAL GLU          
SEQRES  13 B  375  GLY LEU VAL LEU ILE ASN VAL ASP PRO CYS ALA LYS GLY          
SEQRES  14 B  375  TRP MET ASP TRP ALA ALA HIS LYS LEU SER GLY LEU THR          
SEQRES  15 B  375  THR ASN VAL VAL ASP ILE ILE LEU ALA HIS HIS PHE GLY          
SEQRES  16 B  375  GLN GLU GLU LEU GLN ALA ASN LEU ASP LEU ILE GLN THR          
SEQRES  17 B  375  TYR ARG MET HIS ILE ALA GLN ASP ILE ASN GLN ASP ASN          
SEQRES  18 B  375  LEU GLN LEU PHE LEU ASN SER TYR ASN GLY ARG ARG ASP          
SEQRES  19 B  375  LEU GLU ILE GLU ARG PRO ILE LEU GLY GLN ASN ASP ASN          
SEQRES  20 B  375  LYS SER LYS THR LEU LYS CYS SER THR LEU LEU VAL VAL          
SEQRES  21 B  375  GLY ASP ASN SER PRO ALA VAL GLU ALA VAL VAL GLU CYS          
SEQRES  22 B  375  ASN SER ARG LEU ASN PRO ILE ASN THR THR LEU LEU LYS          
SEQRES  23 B  375  MET ALA ASP CYS GLY GLY LEU PRO GLN VAL VAL GLN PRO          
SEQRES  24 B  375  GLY LYS LEU THR GLU ALA PHE LYS TYR PHE LEU GLN GLY          
SEQRES  25 B  375  MET GLY TYR ILE PRO SER ALA SER MET THR ARG LEU ALA          
SEQRES  26 B  375  ARG SER ARG THR HIS SER THR SER SER SER LEU GLY SER          
SEQRES  27 B  375  GLY GLU SER PRO PHE SER ARG SER VAL THR SER ASN GLN          
SEQRES  28 B  375  SER ASP GLY THR GLN GLU SER CYS GLU SER PRO ASP VAL          
SEQRES  29 B  375  LEU ASP ARG HIS GLN THR MET GLU VAL SER CYS                  
FORMUL   3  HOH   *6(H2 O)                                                      
HELIX    1 AA1 ASN A   66  PHE A   77  1                                  12    
HELIX    2 AA2 PHE A   77  PHE A   87  1                                  11    
HELIX    3 AA3 THR A  112  MET A  119  1                                   8    
HELIX    4 AA4 MET A  119  LEU A  127  1                                   9    
HELIX    5 AA5 GLY A  138  HIS A  151  1                                  14    
HELIX    6 AA6 ASN A  184  PHE A  194  1                                  11    
HELIX    7 AA7 GLY A  195  ALA A  201  1                                   7    
HELIX    8 AA8 LEU A  203  ILE A  217  1                                  15    
HELIX    9 AA9 ASP A  220  GLY A  231  1                                  12    
HELIX   10 AB1 ALA A  266  ARG A  276  1                                  11    
HELIX   11 AB2 LEU A  293  GLN A  298  1                                   6    
HELIX   12 AB3 GLN A  298  GLY A  314  1                                  17    
HELIX   13 AB4 ASN B   66  ASN B   76  1                                  11    
HELIX   14 AB5 PHE B   77  GLN B   85  1                                   9    
HELIX   15 AB6 THR B  112  MET B  119  1                                   8    
HELIX   16 AB7 MET B  119  LEU B  127  1                                   9    
HELIX   17 AB8 GLY B  138  HIS B  151  1                                  14    
HELIX   18 AB9 ASN B  184  PHE B  194  1                                  11    
HELIX   19 AC1 GLY B  195  ASN B  202  1                                   8    
HELIX   20 AC2 LEU B  203  ILE B  217  1                                  15    
HELIX   21 AC3 ASN B  218  GLY B  231  1                                  14    
HELIX   22 AC4 ALA B  266  ARG B  276  1                                  11    
HELIX   23 AC5 GLN B  298  GLY B  314  1                                  17    
SHEET    1 AA1 8 GLN A  31  GLU A  36  0                                        
SHEET    2 AA1 8 VAL A  41  ARG A  47 -1  O  ILE A  46   N  GLN A  31           
SHEET    3 AA1 8 VAL A  89  ASP A  93 -1  O  HIS A  91   N  THR A  45           
SHEET    4 AA1 8 ILE A  57  TYR A  60  1  N  THR A  59   O  VAL A  92           
SHEET    5 AA1 8 ILE A 132  VAL A 137  1  O  ILE A 135   N  TYR A  60           
SHEET    6 AA1 8 VAL A 155  ILE A 161  1  O  ILE A 161   N  GLY A 136           
SHEET    7 AA1 8 SER A 255  GLY A 261  1  O  LEU A 257   N  LEU A 158           
SHEET    8 AA1 8 THR A 282  MET A 287  1  O  THR A 283   N  LEU A 258           
SHEET    1 AA2 8 CYS B  30  THR B  37  0                                        
SHEET    2 AA2 8 GLY B  40  ARG B  47 -1  O  GLY B  40   N  THR B  37           
SHEET    3 AA2 8 VAL B  89  ASP B  93 -1  O  ASP B  93   N  HIS B  43           
SHEET    4 AA2 8 VAL B  56  TYR B  60  1  N  THR B  59   O  CYS B  90           
SHEET    5 AA2 8 ILE B 132  VAL B 137  1  O  ILE B 135   N  LEU B  58           
SHEET    6 AA2 8 VAL B 155  ILE B 161  1  O  ILE B 161   N  GLY B 136           
SHEET    7 AA2 8 SER B 255  GLY B 261  1  O  VAL B 259   N  LEU B 160           
SHEET    8 AA2 8 LEU B 284  MET B 287  1  O  LEU B 285   N  LEU B 258           
SSBOND   1 CYS A   30    CYS B   30                          1555   1555  2.03  
CRYST1  100.387  100.387  111.756  90.00  90.00 120.00 P 32 2 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009961  0.005751  0.000000        0.00000                         
SCALE2      0.000000  0.011502  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008948        0.00000                         
TER    2156      SER A 320                                                      
TER    4346      SER B 320                                                      
MASTER      478    0    0   23   16    0    0    6 4350    2    2   58          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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