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Database: PDB
Entry: 4D8O
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Original site: 4D8O 
HEADER    PROTEIN BINDING                         11-JAN-12   4D8O              
TITLE     CRYSTAL STRUCTURE OF THE ANKYRIN-B ZU5-ZU5-UPA-DD TANDEM              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANKYRIN-2;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 966-1535;                                         
COMPND   5 SYNONYM: ANK-2, ANKYRIN-B, BRAIN ANKYRIN, NON-ERYTHROID ANKYRIN;     
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: ANK2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET32A                                    
KEYWDS    ZU5, UPA, DEATH DOMAIN, SUPRAMODULE, PROTEIN BINDING                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.WEI,C.WANG,C.YU,M.ZHANG                                             
REVDAT   4   15-NOV-17 4D8O    1       REMARK                                   
REVDAT   3   16-AUG-17 4D8O    1       SOURCE REMARK                            
REVDAT   2   26-JUN-13 4D8O    1       JRNL                                     
REVDAT   1   28-MAR-12 4D8O    0                                                
JRNL        AUTH   C.WANG,C.YU,F.YE,Z.WEI,M.ZHANG                               
JRNL        TITL   STRUCTURE OF THE ZU5-ZU5-UPA-DD TANDEM OF ANKYRIN-B REVEALS  
JRNL        TITL 2 INTERACTION SURFACES NECESSARY FOR ANKYRIN FUNCTION          
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 109  4822 2012              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   22411828                                                     
JRNL        DOI    10.1073/PNAS.1200613109                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.6.4_486                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.89                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 28402                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.130                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1457                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 36.8918 -  4.7433    0.95     2855   137  0.2052 0.2309        
REMARK   3     2  4.7433 -  3.7661    0.99     2870   144  0.1753 0.1727        
REMARK   3     3  3.7661 -  3.2904    1.00     2816   153  0.2016 0.2895        
REMARK   3     4  3.2904 -  2.9897    0.99     2815   162  0.2218 0.2488        
REMARK   3     5  2.9897 -  2.7755    0.97     2707   163  0.2331 0.2657        
REMARK   3     6  2.7755 -  2.6119    0.96     2698   149  0.2284 0.2904        
REMARK   3     7  2.6119 -  2.4811    0.94     2636   141  0.2332 0.3035        
REMARK   3     8  2.4811 -  2.3731    0.93     2589   145  0.2352 0.2974        
REMARK   3     9  2.3731 -  2.2818    0.90     2524   122  0.2396 0.2909        
REMARK   3    10  2.2818 -  2.2030    0.89     2435   141  0.2536 0.2988        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.30                                          
REMARK   3   SHRINKAGE RADIUS   : 1.06                                          
REMARK   3   K_SOL              : 0.38                                          
REMARK   3   B_SOL              : 59.33                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.650           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 15.18160                                             
REMARK   3    B22 (A**2) : -6.49460                                             
REMARK   3    B33 (A**2) : -8.68690                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           4076                                  
REMARK   3   ANGLE     :  0.874           5527                                  
REMARK   3   CHIRALITY :  0.059            631                                  
REMARK   3   PLANARITY :  0.004            715                                  
REMARK   3   DIHEDRAL  : 13.521           1509                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESSEQ 964:1124                            
REMARK   3    ORIGIN FOR THE GROUP (A): -28.2016 -22.3099  34.5137              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4399 T22:   0.3420                                     
REMARK   3      T33:   0.3158 T12:   0.0105                                     
REMARK   3      T13:   0.0367 T23:   0.0092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3405 L22:   1.4262                                     
REMARK   3      L33:   3.8855 L12:   1.6989                                     
REMARK   3      L13:  -1.2893 L23:  -1.8471                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1385 S12:  -0.2502 S13:  -0.0619                       
REMARK   3      S21:   0.1088 S22:  -0.1579 S23:  -0.0161                       
REMARK   3      S31:   0.3297 S32:   0.2674 S33:   0.0209                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND RESSEQ 1125:1289                           
REMARK   3    ORIGIN FOR THE GROUP (A): -38.6041 -13.9007   3.6514              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3111 T22:   0.2955                                     
REMARK   3      T33:   0.3435 T12:  -0.0445                                     
REMARK   3      T13:  -0.0165 T23:  -0.0145                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5745 L22:   1.3897                                     
REMARK   3      L33:   2.3705 L12:   0.0550                                     
REMARK   3      L13:   0.5349 L23:  -1.0386                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0373 S12:  -0.1119 S13:  -0.1427                       
REMARK   3      S21:  -0.1251 S22:   0.0224 S23:   0.1597                       
REMARK   3      S31:   0.0887 S32:  -0.1679 S33:  -0.0332                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND RESSEQ 1290:1423                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.1032  -0.5432  24.0622              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3377 T22:   0.3152                                     
REMARK   3      T33:   0.2964 T12:  -0.0449                                     
REMARK   3      T13:   0.0512 T23:   0.0110                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1789 L22:   2.7071                                     
REMARK   3      L33:   1.9270 L12:   1.6010                                     
REMARK   3      L13:   0.1522 L23:   0.9869                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0884 S12:   0.0954 S13:  -0.0274                       
REMARK   3      S21:  -0.2854 S22:   0.1900 S23:  -0.1811                       
REMARK   3      S31:  -0.3410 S32:   0.2359 S33:  -0.1027                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND RESSEQ 1452:1529                           
REMARK   3    ORIGIN FOR THE GROUP (A):  11.1842 -15.9627  21.3993              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5062 T22:   0.4596                                     
REMARK   3      T33:   0.4440 T12:  -0.0068                                     
REMARK   3      T13:   0.0384 T23:  -0.1092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9104 L22:   4.5910                                     
REMARK   3      L33:   1.8036 L12:   1.3817                                     
REMARK   3      L13:   0.5274 L23:   2.2729                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1953 S12:   0.2347 S13:   0.2141                       
REMARK   3      S21:   0.3847 S22:   0.2913 S23:   0.2817                       
REMARK   3      S31:   0.4602 S32:   0.3209 S33:  -0.0474                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4D8O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JAN-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000070021.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29634                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
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     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> 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: PHASER                                                
REMARK 200 STARTING MODEL: 3F59, 3G5B, 2YVI                                     
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG3350, 0.2M AMMONIUM ACETATE, 5%   
REMARK 280  N-OCTYL-BETA-D-GLUCOSIDE, PH 7.5, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  TEMPERATURE 289K                                                    
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       37.83700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.49400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.02800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       47.49400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.83700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.02800            
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 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     MET A   946                                                      
REMARK 465     HIS A   947                                                      
REMARK 465     HIS A   948                                                      
REMARK 465     HIS A   949                                                      
REMARK 465     HIS A   950                                                      
REMARK 465     HIS A   951                                                      
REMARK 465     HIS A   952                                                      
REMARK 465     SER A   953                                                      
REMARK 465     SER A   954                                                      
REMARK 465     GLY A   955                                                      
REMARK 465     LEU A   956                                                      
REMARK 465     GLU A   957                                                      
REMARK 465     VAL A   958                                                      
REMARK 465     LEU A   959                                                      
REMARK 465     PHE A   960                                                      
REMARK 465     GLN A   961                                                      
REMARK 465     GLY A   962                                                      
REMARK 465     PRO A   963                                                      
REMARK 465     THR A  1080                                                      
REMARK 465     GLU A  1081                                                      
REMARK 465     ASP A  1082                                                      
REMARK 465     GLU A  1083                                                      
REMARK 465     LEU A  1084                                                      
REMARK 465     ASN A  1085                                                      
REMARK 465     GLU A  1086                                                      
REMARK 465     ILE A  1087                                                      
REMARK 465     LEU A  1088                                                      
REMARK 465     ASN A  1089                                                      
REMARK 465     LYS A  1361                                                      
REMARK 465     SER A  1362                                                      
REMARK 465     GLY A  1363                                                      
REMARK 465     LYS A  1402                                                      
REMARK 465     SER A  1403                                                      
REMARK 465     THR A  1404                                                      
REMARK 465     ARG A  1405                                                      
REMARK 465     GLY A  1406                                                      
REMARK 465     LEU A  1407                                                      
REMARK 465     VAL A  1408                                                      
REMARK 465     LYS A  1424                                                      
REMARK 465     GLU A  1425                                                      
REMARK 465     SER A  1426                                                      
REMARK 465     GLU A  1427                                                      
REMARK 465     SER A  1428                                                      
REMARK 465     ASP A  1429                                                      
REMARK 465     GLN A  1430                                                      
REMARK 465     GLU A  1431                                                      
REMARK 465     GLN A  1432                                                      
REMARK 465     GLU A  1433                                                      
REMARK 465     GLU A  1434                                                      
REMARK 465     GLU A  1435                                                      
REMARK 465     ILE A  1436                                                      
REMARK 465     ASP A  1437                                                      
REMARK 465     MET A  1438                                                      
REMARK 465     THR A  1439                                                      
REMARK 465     SER A  1440                                                      
REMARK 465     GLU A  1441                                                      
REMARK 465     LYS A  1442                                                      
REMARK 465     ASN A  1443                                                      
REMARK 465     PRO A  1444                                                      
REMARK 465     GLN A  1445                                                      
REMARK 465     ASP A  1446                                                      
REMARK 465     GLU A  1447                                                      
REMARK 465     GLN A  1448                                                      
REMARK 465     GLU A  1449                                                      
REMARK 465     ARG A  1450                                                      
REMARK 465     ILE A  1451                                                      
REMARK 465     LEU A  1530                                                      
REMARK 465     MET A  1531                                                      
REMARK 465     GLU A  1532                                                      
REMARK 465     THR A  1533                                                      
REMARK 465     ASN A  1534                                                      
REMARK 465     THR A  1535                                                      
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     ARG A1011    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1057    CG   CD   CE   NZ                                   
REMARK 470     ASP A1078    CG   OD1  OD2                                       
REMARK 470     GLU A1171    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1175    CG   CD   CE   NZ                                   
REMARK 470     ILE A1307    CG1  CG2  CD1                                       
REMARK 470     LYS A1323    CG   CD   CE   NZ                                   
REMARK 470     GLU A1326    CG   CD   OE1  OE2                                  
REMARK 470     GLN A1327    CG   CD   OE1  NE2                                  
REMARK 470     GLN A1364    CG   CD   OE1  NE2                                  
REMARK 470     GLU A1390    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1452    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1453    CG   CD   OE1  OE2                                  
REMARK 470     LEU A1455    CG   CD1  CD2                                       
REMARK 470     GLU A1468    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1508    CG   CD   CE   NZ                                   
REMARK 470     GLU A1517    CG   CD   OE1  OE2                                  
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    SER A 971      111.42   -161.84                                   
REMARK 500    ASP A 975     -150.29   -140.59                                   
REMARK 500    ARG A 985      -81.39   -115.75                                   
REMARK 500    PHE A1051       21.08   -141.69                                   
REMARK 500    ASP A1070      -70.85    -81.93                                   
REMARK 500    ARG A1193       51.34     71.03                                   
REMARK 500    SER A1210     -165.67   -103.32                                   
REMARK 500    GLU A1254       25.73     46.22                                   
REMARK 500    ALA A1264     -168.50   -162.59                                   
REMARK 500    ASP A1305     -170.76   -171.95                                   
REMARK 500    LYS A1320       -1.40     74.29                                   
REMARK 500    GLN A1328       45.96    -96.92                                   
REMARK 500    ASN A1330      -12.25     89.77                                   
REMARK 500    ALA A1335      149.27   -172.04                                   
REMARK 500    ALA A1510       70.39   -103.11                                   
REMARK 500    ARG A1524       51.49   -116.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 A PART OF RESIDUES 1211-1219 IN Q01484 HAS BEEN DELETED.             
REMARK 999 THE SEQUENCE OF RESIDUES 1220-1535 IS FROM                           
REMARK 999 ISOFORM 2 OF ANKYRIN-2 (Q01484-2).                                   
DBREF  4D8O A  966  1210  UNP    Q01484   ANK2_HUMAN     966   1210             
DBREF  4D8O A 1220  1535  UNP    Q01484   ANK2_HUMAN    1253   1568             
SEQADV 4D8O MET A  946  UNP  Q01484              EXPRESSION TAG                 
SEQADV 4D8O HIS A  947  UNP  Q01484              EXPRESSION TAG                 
SEQADV 4D8O HIS A  948  UNP  Q01484              EXPRESSION TAG                 
SEQADV 4D8O HIS A  949  UNP  Q01484              EXPRESSION TAG                 
SEQADV 4D8O HIS A  950  UNP  Q01484              EXPRESSION TAG                 
SEQADV 4D8O HIS A  951  UNP  Q01484              EXPRESSION TAG                 
SEQADV 4D8O HIS A  952  UNP  Q01484              EXPRESSION TAG                 
SEQADV 4D8O SER A  953  UNP  Q01484              EXPRESSION TAG                 
SEQADV 4D8O SER A  954  UNP  Q01484              EXPRESSION TAG                 
SEQADV 4D8O GLY A  955  UNP  Q01484              EXPRESSION TAG                 
SEQADV 4D8O LEU A  956  UNP  Q01484              EXPRESSION TAG                 
SEQADV 4D8O GLU A  957  UNP  Q01484              EXPRESSION TAG                 
SEQADV 4D8O VAL A  958  UNP  Q01484              EXPRESSION TAG                 
SEQADV 4D8O LEU A  959  UNP  Q01484              EXPRESSION TAG                 
SEQADV 4D8O PHE A  960  UNP  Q01484              EXPRESSION TAG                 
SEQADV 4D8O GLN A  961  UNP  Q01484              EXPRESSION TAG                 
SEQADV 4D8O GLY A  962  UNP  Q01484              EXPRESSION TAG                 
SEQADV 4D8O PRO A  963  UNP  Q01484              EXPRESSION TAG                 
SEQADV 4D8O GLU A  964  UNP  Q01484              EXPRESSION TAG                 
SEQADV 4D8O PHE A  965  UNP  Q01484              EXPRESSION TAG                 
SEQRES   1 A  581  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU VAL          
SEQRES   2 A  581  LEU PHE GLN GLY PRO GLU PHE SER GLY PHE LEU VAL SER          
SEQRES   3 A  581  PHE MET VAL ASP ALA ARG GLY GLY ALA MET ARG GLY CYS          
SEQRES   4 A  581  ARG HIS ASN GLY LEU ARG ILE ILE ILE PRO PRO ARG LYS          
SEQRES   5 A  581  CYS THR ALA PRO THR ARG VAL THR CYS ARG LEU VAL LYS          
SEQRES   6 A  581  ARG HIS ARG LEU ALA THR MET PRO PRO MET VAL GLU GLY          
SEQRES   7 A  581  GLU GLY LEU ALA SER ARG LEU ILE GLU VAL GLY PRO SER          
SEQRES   8 A  581  GLY ALA GLN PHE LEU GLY PRO VAL ILE VAL GLU ILE PRO          
SEQRES   9 A  581  HIS PHE ALA ALA LEU ARG GLY LYS GLU ARG GLU LEU VAL          
SEQRES  10 A  581  VAL LEU ARG SER GLU ASN GLY ASP SER TRP LYS GLU HIS          
SEQRES  11 A  581  PHE CYS ASP TYR THR GLU ASP GLU LEU ASN GLU ILE LEU          
SEQRES  12 A  581  ASN GLY MET ASP GLU VAL LEU ASP SER PRO GLU ASP LEU          
SEQRES  13 A  581  GLU LYS LYS ARG ILE CYS ARG ILE ILE THR ARG ASP PHE          
SEQRES  14 A  581  PRO GLN TYR PHE ALA VAL VAL SER ARG ILE LYS GLN ASP          
SEQRES  15 A  581  SER ASN LEU ILE GLY PRO GLU GLY GLY VAL LEU SER SER          
SEQRES  16 A  581  THR VAL VAL PRO GLN VAL GLN ALA VAL PHE PRO GLU GLY          
SEQRES  17 A  581  ALA LEU THR LYS ARG ILE ARG VAL GLY LEU GLN ALA GLN          
SEQRES  18 A  581  PRO MET HIS SER GLU LEU VAL LYS LYS ILE LEU GLY ASN          
SEQRES  19 A  581  LYS ALA THR PHE SER PRO ILE VAL THR LEU GLU PRO ARG          
SEQRES  20 A  581  ARG ARG LYS PHE HIS LYS PRO ILE THR MET THR ILE PRO          
SEQRES  21 A  581  VAL PRO LYS ALA SER GLY ASP ALA PRO THR LEU ARG LEU          
SEQRES  22 A  581  LEU CYS SER ILE THR GLY GLY THR THR PRO ALA GLN TRP          
SEQRES  23 A  581  GLU ASP ILE THR GLY THR THR PRO LEU THR PHE VAL ASN          
SEQRES  24 A  581  GLU CYS VAL SER PHE THR THR ASN VAL SER ALA ARG PHE          
SEQRES  25 A  581  TRP LEU ILE ASP CYS ARG GLN ILE GLN GLU SER VAL THR          
SEQRES  26 A  581  PHE ALA SER GLN VAL TYR ARG GLU ILE ILE CYS VAL PRO          
SEQRES  27 A  581  TYR MET ALA LYS PHE VAL VAL PHE ALA LYS SER HIS ASP          
SEQRES  28 A  581  PRO ILE GLU ALA ARG LEU ARG CYS PHE CYS MET THR ASP          
SEQRES  29 A  581  ASP LYS VAL ASP LYS THR LEU GLU GLN GLN GLU ASN PHE          
SEQRES  30 A  581  ALA GLU VAL ALA ARG SER ARG ASP VAL GLU VAL LEU GLU          
SEQRES  31 A  581  GLY LYS PRO ILE TYR VAL ASP CYS PHE GLY ASN LEU VAL          
SEQRES  32 A  581  PRO LEU THR LYS SER GLY GLN HIS HIS ILE PHE SER PHE          
SEQRES  33 A  581  PHE ALA PHE LYS GLU ASN ARG LEU PRO LEU PHE VAL LYS          
SEQRES  34 A  581  VAL ARG ASP THR THR GLN GLU PRO CYS GLY ARG LEU SER          
SEQRES  35 A  581  PHE MET LYS GLU PRO LYS SER THR ARG GLY LEU VAL HIS          
SEQRES  36 A  581  GLN ALA ILE CYS ASN LEU ASN ILE THR LEU PRO ILE TYR          
SEQRES  37 A  581  THR LYS GLU SER GLU SER ASP GLN GLU GLN GLU GLU GLU          
SEQRES  38 A  581  ILE ASP MET THR SER GLU LYS ASN PRO GLN ASP GLU GLN          
SEQRES  39 A  581  GLU ARG ILE GLU GLU ARG LEU ALA TYR ILE ALA ASP HIS          
SEQRES  40 A  581  LEU GLY PHE SER TRP THR GLU LEU ALA ARG GLU LEU ASP          
SEQRES  41 A  581  PHE THR GLU GLU GLN ILE HIS GLN ILE ARG ILE GLU ASN          
SEQRES  42 A  581  PRO ASN SER LEU GLN ASP GLN SER HIS ALA LEU LEU LYS          
SEQRES  43 A  581  TYR TRP LEU GLU ARG ASP GLY LYS HIS ALA THR ASP THR          
SEQRES  44 A  581  ASN LEU VAL GLU CYS LEU THR LYS ILE ASN ARG MET ASP          
SEQRES  45 A  581  ILE VAL HIS LEU MET GLU THR ASN THR                          
FORMUL   2  HOH   *101(H2 O)                                                    
HELIX    1   1 SER A 1097  ARG A 1105  1                                   9    
HELIX    2   2 HIS A 1169  GLY A 1178  1                                  10    
HELIX    3   3 THR A 1244  THR A 1247  5                                   4    
HELIX    4   4 GLN A 1273  GLN A 1275  5                                   3    
HELIX    5   5 GLU A 1276  ILE A 1289  1                                  14    
HELIX    6   6 LYS A 1323  GLN A 1327  5                                   5    
HELIX    7   7 GLU A 1453  GLY A 1463  1                                  11    
HELIX    8   8 PHE A 1464  LEU A 1473  1                                  10    
HELIX    9   9 THR A 1476  ASN A 1487  1                                  12    
HELIX   10  10 SER A 1490  GLY A 1507  1                                  18    
HELIX   11  11 LYS A 1508  ALA A 1510  5                                   3    
HELIX   12  12 THR A 1511  ILE A 1522  1                                  12    
HELIX   13  13 ARG A 1524  HIS A 1529  1                                   6    
SHEET    1   A 3 VAL A 970  VAL A 974  0                                        
SHEET    2   A 3 THR A1002  LEU A1008 -1  O  THR A1002   N  VAL A 974           
SHEET    3   A 3 ILE A1031  GLY A1034 -1  O  GLU A1032   N  ARG A1007           
SHEET    1   B 4 GLY A 979  ARG A 982  0                                        
SHEET    2   B 4 ARG A 990  ILE A 993 -1  O  ILE A 993   N  GLY A 979           
SHEET    3   B 4 GLN A1039  PRO A1049 -1  O  GLU A1047   N  ARG A 990           
SHEET    4   B 4 ILE A1106  ASP A1113 -1  O  CYS A1107   N  ILE A1048           
SHEET    1   C 4 GLY A1025  LEU A1026  0                                        
SHEET    2   C 4 TYR A1117  ILE A1124 -1  O  SER A1122   N  GLY A1025           
SHEET    3   C 4 ARG A1059  SER A1066 -1  N  LEU A1064   O  ALA A1119           
SHEET    4   C 4 LYS A1073  GLU A1074 -1  O  LYS A1073   N  ARG A1065           
SHEET    1   D 5 GLN A1126  ILE A1131  0                                        
SHEET    2   D 5 ILE A1159  GLN A1166 -1  O  LEU A1163   N  ASP A1127           
SHEET    3   D 5 ILE A1186  GLU A1190 -1  O  GLU A1190   N  GLY A1162           
SHEET    4   D 5 ARG A1265  CYS A1271 -1  O  PHE A1266   N  VAL A1187           
SHEET    5   D 5 ALA A1181  PHE A1183 -1  N  THR A1182   O  ASP A1270           
SHEET    1   E 6 GLN A1126  ILE A1131  0                                        
SHEET    2   E 6 ILE A1159  GLN A1166 -1  O  LEU A1163   N  ASP A1127           
SHEET    3   E 6 ILE A1186  GLU A1190 -1  O  GLU A1190   N  GLY A1162           
SHEET    4   E 6 ARG A1265  CYS A1271 -1  O  PHE A1266   N  VAL A1187           
SHEET    5   E 6 LEU A1225  SER A1230 -1  N  ARG A1226   O  ILE A1269           
SHEET    6   E 6 GLU A1241  ASP A1242 -1  O  GLU A1241   N  CYS A1229           
SHEET    1   F 5 GLY A1136  SER A1139  0                                        
SHEET    2   F 5 GLN A1147  PHE A1150 -1  O  ALA A1148   N  LEU A1138           
SHEET    3   F 5 LYS A1195  PRO A1205 -1  O  THR A1203   N  GLN A1147           
SHEET    4   F 5 CYS A1255  VAL A1262 -1  O  VAL A1256   N  ILE A1204           
SHEET    5   F 5 THR A1250  VAL A1252 -1  N  THR A1250   O  SER A1257           
SHEET    1   G 3 ALA A1332  ARG A1336  0                                        
SHEET    2   G 3 PRO A1292  LYS A1302 -1  N  VAL A1299   O  VAL A1334           
SHEET    3   G 3 VAL A1340  LEU A1343 -1  O  VAL A1340   N  ALA A1295           
SHEET    1   H 5 ALA A1332  ARG A1336  0                                        
SHEET    2   H 5 PRO A1292  LYS A1302 -1  N  VAL A1299   O  VAL A1334           
SHEET    3   H 5 GLU A1308  MET A1316 -1  O  ARG A1310   N  LYS A1302           
SHEET    4   H 5 ARG A1377  VAL A1384 -1  O  LEU A1380   N  LEU A1311           
SHEET    5   H 5 LEU A1356  PRO A1358 -1  N  VAL A1357   O  LYS A1383           
SHEET    1   I 4 HIS A1366  SER A1369  0                                        
SHEET    2   I 4 PRO A1347  GLY A1354 -1  N  ILE A1348   O  PHE A1368           
SHEET    3   I 4 CYS A1392  MET A1398 -1  O  MET A1398   N  TYR A1349           
SHEET    4   I 4 CYS A1413  THR A1418 -1  O  LEU A1415   N  LEU A1395           
CISPEP   1 GLY A 1034    PRO A 1035          0         1.95                     
CISPEP   2 GLU A 1190    PRO A 1191          0         0.03                     
CRYST1   75.674   80.056   94.988  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      0.013215  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012491  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010528        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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