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Entry: 5Y4F
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HEADER    PROTEIN BINDING                         03-AUG-17   5Y4F              
TITLE     CRYSTAL STRUCTURE OF ANKB ANKYRIN REPEATS R13-24 IN COMPLEX WITH      
TITLE    2 AUTOINHIBITION SEGMENT AI-C                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANKYRIN-2;                                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 430-873;                                      
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                                         
KEYWDS    ANK REPEAT, PROTEIN-PROTEIN INTERACTION, STRUCTURAL PROTEIN, AUTO-    
KEYWDS   2 INHIBITION, PROTEIN BINDING                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.CHEN,J.LI,C.WANG,Z.WEI,M.ZHANG                                      
REVDAT   1   13-SEP-17 5Y4F    0                                                
JRNL        AUTH   K.CHEN,J.LI,C.WANG,Z.WEI,M.ZHANG                             
JRNL        TITL   AUTOINHIBITION OF ANKYRIN-B/G MEMBRANE TARGET BINDINGS BY    
JRNL        TITL 2 INTRINSICALLY DISORDERED SEGMENTS FROM THE TAIL REGIONS.     
JRNL        REF    ELIFE                         V.   6       2017              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   28841137                                                     
JRNL        DOI    10.7554/ELIFE.29150                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_2689                                      
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.16                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 67875                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.950                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3357                            
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 38.1682 -  5.6279    0.91     2909   137  0.1880 0.1944        
REMARK   3     2  5.6279 -  4.4693    0.98     2956   142  0.1554 0.1854        
REMARK   3     3  4.4693 -  3.9050    0.98     2869   148  0.1457 0.1783        
REMARK   3     4  3.9050 -  3.5482    0.96     2787   155  0.1574 0.1765        
REMARK   3     5  3.5482 -  3.2940    0.98     2789   146  0.1730 0.2233        
REMARK   3     6  3.2940 -  3.0999    0.97     2853   142  0.1963 0.2222        
REMARK   3     7  3.0999 -  2.9447    0.97     2739   144  0.1909 0.2384        
REMARK   3     8  2.9447 -  2.8166    0.97     2814   155  0.1895 0.2142        
REMARK   3     9  2.8166 -  2.7082    0.97     2725   143  0.1941 0.2317        
REMARK   3    10  2.7082 -  2.6148    0.96     2758   135  0.1892 0.2373        
REMARK   3    11  2.6148 -  2.5330    0.95     2737   162  0.1912 0.2228        
REMARK   3    12  2.5330 -  2.4606    0.96     2635   137  0.1913 0.2271        
REMARK   3    13  2.4606 -  2.3959    0.95     2725   156  0.1966 0.2772        
REMARK   3    14  2.3959 -  2.3374    0.95     2682   138  0.1956 0.2412        
REMARK   3    15  2.3374 -  2.2843    0.94     2635   134  0.2082 0.2562        
REMARK   3    16  2.2843 -  2.2357    0.93     2596   152  0.2002 0.2440        
REMARK   3    17  2.2357 -  2.1910    0.92     2643   136  0.2087 0.2563        
REMARK   3    18  2.1910 -  2.1496    0.93     2606   128  0.2160 0.3077        
REMARK   3    19  2.1496 -  2.1112    0.94     2598   134  0.2139 0.2937        
REMARK   3    20  2.1112 -  2.0755    0.90     2530   144  0.2194 0.2504        
REMARK   3    21  2.0755 -  2.0420    0.88     2521   126  0.2289 0.2488        
REMARK   3    22  2.0420 -  2.0106    0.91     2530   149  0.2388 0.2770        
REMARK   3    23  2.0106 -  1.9810    0.92     2555   128  0.2373 0.2636        
REMARK   3    24  1.9810 -  1.9531    0.84     2326    86  0.2545 0.3411        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.040           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.19                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.93                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.010           6234                                  
REMARK   3   ANGLE     :  0.993           8505                                  
REMARK   3   CHIRALITY :  0.058           1060                                  
REMARK   3   PLANARITY :  0.007           1091                                  
REMARK   3   DIHEDRAL  :  3.557           5072                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 430:492 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -25.090  -29.118  -11.114              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2648 T22:   0.2905                                     
REMARK   3      T33:   0.1939 T12:   0.0388                                     
REMARK   3      T13:   0.0082 T23:   0.0703                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5998 L22:   5.7005                                     
REMARK   3      L33:   1.6045 L12:   1.6949                                     
REMARK   3      L13:   1.1156 L23:   2.1522                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0671 S12:  -0.0056 S13:   0.1836                       
REMARK   3      S21:  -0.0219 S22:  -0.0734 S23:   0.2251                       
REMARK   3      S31:   0.0938 S32:   0.0334 S33:   0.0123                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 493:624 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -14.228   -4.271   -4.033              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1519 T22:   0.2256                                     
REMARK   3      T33:   0.2100 T12:   0.0396                                     
REMARK   3      T13:   0.0165 T23:   0.0546                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3885 L22:   7.3059                                     
REMARK   3      L33:   0.9185 L12:   1.8322                                     
REMARK   3      L13:  -0.0762 L23:  -0.8493                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0476 S12:  -0.0141 S13:  -0.0378                       
REMARK   3      S21:   0.1980 S22:   0.0056 S23:   0.0273                       
REMARK   3      S31:   0.0137 S32:   0.0485 S33:  -0.0645                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 625:780 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   -3.523   30.911  -18.962              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1182 T22:   0.2118                                     
REMARK   3      T33:   0.1511 T12:  -0.0125                                     
REMARK   3      T13:  -0.0165 T23:  -0.0267                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7169 L22:   1.3218                                     
REMARK   3      L33:   2.1541 L12:   0.3022                                     
REMARK   3      L13:  -0.6040 L23:  -1.0953                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0292 S12:  -0.0235 S13:   0.0416                       
REMARK   3      S21:   0.1791 S22:  -0.0013 S23:  -0.0379                       
REMARK   3      S31:  -0.1762 S32:   0.0794 S33:  -0.0207                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 781:819 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):    2.211   41.584  -43.814              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2122 T22:   0.3226                                     
REMARK   3      T33:   0.1988 T12:  -0.0010                                     
REMARK   3      T13:  -0.0313 T23:  -0.0180                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3525 L22:   0.9084                                     
REMARK   3      L33:   1.1031 L12:  -0.4493                                     
REMARK   3      L13:  -0.5592 L23:   0.9464                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0635 S12:   0.1707 S13:  -0.0672                       
REMARK   3      S21:  -0.2474 S22:  -0.0404 S23:  -0.0097                       
REMARK   3      S31:   0.1840 S32:   0.1218 S33:  -0.0404                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 430:591 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -24.582    9.923  -58.797              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2315 T22:   0.2605                                     
REMARK   3      T33:   0.2563 T12:  -0.0428                                     
REMARK   3      T13:  -0.0086 T23:   0.0125                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4520 L22:   7.1246                                     
REMARK   3      L33:  -0.0138 L12:  -2.5317                                     
REMARK   3      L13:  -0.2270 L23:   0.5944                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0178 S12:   0.0197 S13:   0.0109                       
REMARK   3      S21:  -0.1765 S22:   0.0008 S23:  -0.0745                       
REMARK   3      S31:   0.0779 S32:  -0.0009 S33:  -0.0203                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 592:819 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -18.042  -37.349  -43.647              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1707 T22:   0.2083                                     
REMARK   3      T33:   0.1730 T12:   0.0401                                     
REMARK   3      T13:  -0.0183 T23:  -0.0278                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7943 L22:   1.2751                                     
REMARK   3      L33:   2.7155 L12:   0.2993                                     
REMARK   3      L13:  -0.2172 L23:  -1.1145                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0248 S12:  -0.0755 S13:  -0.1188                       
REMARK   3      S21:   0.0659 S22:  -0.0221 S23:  -0.1498                       
REMARK   3      S31:   0.0976 S32:   0.0377 S33:   0.0627                       
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 5Y4F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300004647.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-SEP-13                          
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                       : BL17U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 68019                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
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     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.74200                            
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: 4RLV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CACL2, 0.1 M HEPES (PH 7.5), 28%   
REMARK 280  V/V PEG 400, VAPOR DIFFUSION, HANGING DROP, 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       14.65200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      128.77500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       63.90150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      128.77500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       14.65200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       63.90150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     SER A   429                                                      
REMARK 465     SER A   845                                                      
REMARK 465     ASP A   846                                                      
REMARK 465     GLU A   847                                                      
REMARK 465     GLU A   848                                                      
REMARK 465     GLY A   849                                                      
REMARK 465     ASP A   850                                                      
REMARK 465     ASP A   851                                                      
REMARK 465     THR A   852                                                      
REMARK 465     MET A   853                                                      
REMARK 465     THR A   854                                                      
REMARK 465     GLY A   855                                                      
REMARK 465     ASP A   856                                                      
REMARK 465     GLY A   857                                                      
REMARK 465     GLY A   858                                                      
REMARK 465     GLU A   859                                                      
REMARK 465     TYR A   860                                                      
REMARK 465     LEU A   861                                                      
REMARK 465     ARG A   862                                                      
REMARK 465     PRO A   863                                                      
REMARK 465     GLU A   864                                                      
REMARK 465     ASP A   865                                                      
REMARK 465     LEU A   866                                                      
REMARK 465     LYS A   867                                                      
REMARK 465     GLU A   868                                                      
REMARK 465     LEU A   869                                                      
REMARK 465     GLY A   870                                                      
REMARK 465     ASP A   871                                                      
REMARK 465     ASP A   872                                                      
REMARK 465     SER B   429                                                      
REMARK 465     THR B   820                                                      
REMARK 465     THR B   821                                                      
REMARK 465     SER B   845                                                      
REMARK 465     ASP B   846                                                      
REMARK 465     GLU B   847                                                      
REMARK 465     GLU B   848                                                      
REMARK 465     GLY B   849                                                      
REMARK 465     ASP B   850                                                      
REMARK 465     ASP B   851                                                      
REMARK 465     THR B   852                                                      
REMARK 465     MET B   853                                                      
REMARK 465     THR B   854                                                      
REMARK 465     GLY B   855                                                      
REMARK 465     ASP B   856                                                      
REMARK 465     GLY B   857                                                      
REMARK 465     GLY B   858                                                      
REMARK 465     GLU B   859                                                      
REMARK 465     TYR B   860                                                      
REMARK 465     LEU B   861                                                      
REMARK 465     ARG B   862                                                      
REMARK 465     PRO B   863                                                      
REMARK 465     GLU B   864                                                      
REMARK 465     ASP B   865                                                      
REMARK 465     LEU B   866                                                      
REMARK 465     LYS B   867                                                      
REMARK 465     GLU B   868                                                      
REMARK 465     LEU B   869                                                      
REMARK 465     GLY B   870                                                      
REMARK 465     ASP B   871                                                      
REMARK 465     ASP B   872                                                      
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 A 462    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 494    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 560    CG   CD   CE   NZ                                   
REMARK 470     LYS A 561    CG   CD   CE   NZ                                   
REMARK 470     ARG A 585    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 593    CG   CD   CE   NZ                                   
REMARK 470     LYS A 626    CG   CD   CE   NZ                                   
REMARK 470     GLU A 818    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 494    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 550    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 560    CG   CD   CE   NZ                                   
REMARK 470     LYS B 561    CG   CD   CE   NZ                                   
REMARK 470     ARG B 585    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 616    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 725    CG   CD   CE   NZ                                   
REMARK 470     LYS B 741    CG   CD   CE   NZ                                   
REMARK 470     LYS B 748    CG   CD   CE   NZ                                   
REMARK 470     GLU B 818    CG   CD   OE1  OE2                                  
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   NZ   LYS B   758     O    HOH B  1001              1.72            
REMARK 500   O    HOH B  1089     O    HOH B  1093              2.18            
REMARK 500   OE1  GLN B   608     O    HOH B  1002              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    ALA A 493     -149.80   -104.13                                   
REMARK 500    THR A 559     -178.51    -63.62                                   
REMARK 500    ALA B 493     -148.77    -99.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 901  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY B 441   O                                                      
REMARK 620 2 HOH B1089   O    75.2                                              
REMARK 620 3 HOH B1093   O    77.1  56.7                                        
REMARK 620 4 ASP B 682   OD1  90.7 133.0  76.6                                  
REMARK 620 5 ASP B 682   OD2  90.9 134.2  77.8   1.2                            
REMARK 620 6 HOH B1105   O   127.6  56.2  90.3 135.9 136.3                      
REMARK 620 7 HOH B1125   O   136.9 124.6  84.3  46.9  46.9  90.5                
REMARK 620 8 HOH B1116   O    84.4 146.6  93.4  19.8  18.8 147.7  58.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 902                 
DBREF  5Y4F A  429   872  UNP    Q01484   ANK2_HUMAN     430    873             
DBREF  5Y4F B  429   872  UNP    Q01484   ANK2_HUMAN     430    873             
SEQRES   1 A  444  SER GLY LEU THR PRO ILE HIS VAL ALA ALA PHE MET GLY          
SEQRES   2 A  444  HIS LEU ASN ILE VAL LEU LEU LEU LEU GLN ASN GLY ALA          
SEQRES   3 A  444  SER PRO ASP VAL THR ASN ILE ARG GLY GLU THR ALA LEU          
SEQRES   4 A  444  HIS MET ALA ALA ARG ALA GLY GLN VAL GLU VAL VAL ARG          
SEQRES   5 A  444  CYS LEU LEU ARG ASN GLY ALA LEU VAL ASP ALA ARG ALA          
SEQRES   6 A  444  ARG GLU GLU GLN THR PRO LEU HIS ILE ALA SER ARG LEU          
SEQRES   7 A  444  GLY LYS THR GLU ILE VAL GLN LEU LEU LEU GLN HIS MET          
SEQRES   8 A  444  ALA HIS PRO ASP ALA ALA THR THR ASN GLY TYR THR PRO          
SEQRES   9 A  444  LEU HIS ILE SER ALA ARG GLU GLY GLN VAL ASP VAL ALA          
SEQRES  10 A  444  SER VAL LEU LEU GLU ALA GLY ALA ALA HIS SER LEU ALA          
SEQRES  11 A  444  THR LYS LYS GLY PHE THR PRO LEU HIS VAL ALA ALA LYS          
SEQRES  12 A  444  TYR GLY SER LEU ASP VAL ALA LYS LEU LEU LEU GLN ARG          
SEQRES  13 A  444  ARG ALA ALA ALA ASP SER ALA GLY LYS ASN GLY LEU THR          
SEQRES  14 A  444  PRO LEU HIS VAL ALA ALA HIS TYR ASP ASN GLN LYS VAL          
SEQRES  15 A  444  ALA LEU LEU LEU LEU GLU LYS GLY ALA SER PRO HIS ALA          
SEQRES  16 A  444  THR ALA LYS ASN GLY TYR THR PRO LEU HIS ILE ALA ALA          
SEQRES  17 A  444  LYS LYS ASN GLN MET GLN ILE ALA SER THR LEU LEU ASN          
SEQRES  18 A  444  TYR GLY ALA GLU THR ASN ILE VAL THR LYS GLN GLY VAL          
SEQRES  19 A  444  THR PRO LEU HIS LEU ALA SER GLN GLU GLY HIS THR ASP          
SEQRES  20 A  444  MET VAL THR LEU LEU LEU ASP LYS GLY ALA ASN ILE HIS          
SEQRES  21 A  444  MET SER THR LYS SER GLY LEU THR SER LEU HIS LEU ALA          
SEQRES  22 A  444  ALA GLN GLU ASP LYS VAL ASN VAL ALA ASP ILE LEU THR          
SEQRES  23 A  444  LYS HIS GLY ALA ASP GLN ASP ALA HIS THR LYS LEU GLY          
SEQRES  24 A  444  TYR THR PRO LEU ILE VAL ALA CYS HIS TYR GLY ASN VAL          
SEQRES  25 A  444  LYS MET VAL ASN PHE LEU LEU LYS GLN GLY ALA ASN VAL          
SEQRES  26 A  444  ASN ALA LYS THR LYS ASN GLY TYR THR PRO LEU HIS GLN          
SEQRES  27 A  444  ALA ALA GLN GLN GLY HIS THR HIS ILE ILE ASN VAL LEU          
SEQRES  28 A  444  LEU GLN HIS GLY ALA LYS PRO ASN ALA THR THR ALA ASN          
SEQRES  29 A  444  GLY ASN THR ALA LEU ALA ILE ALA LYS ARG LEU GLY TYR          
SEQRES  30 A  444  ILE SER VAL VAL ASP THR LEU LYS VAL VAL THR GLU GLU          
SEQRES  31 A  444  VAL THR THR THR THR THR THR ILE THR GLU LYS HIS LYS          
SEQRES  32 A  444  LEU ASN VAL PRO GLU THR MET THR GLU VAL LEU ASP VAL          
SEQRES  33 A  444  SER ASP GLU GLU GLY ASP ASP THR MET THR GLY ASP GLY          
SEQRES  34 A  444  GLY GLU TYR LEU ARG PRO GLU ASP LEU LYS GLU LEU GLY          
SEQRES  35 A  444  ASP ASP                                                      
SEQRES   1 B  444  SER GLY LEU THR PRO ILE HIS VAL ALA ALA PHE MET GLY          
SEQRES   2 B  444  HIS LEU ASN ILE VAL LEU LEU LEU LEU GLN ASN GLY ALA          
SEQRES   3 B  444  SER PRO ASP VAL THR ASN ILE ARG GLY GLU THR ALA LEU          
SEQRES   4 B  444  HIS MET ALA ALA ARG ALA GLY GLN VAL GLU VAL VAL ARG          
SEQRES   5 B  444  CYS LEU LEU ARG ASN GLY ALA LEU VAL ASP ALA ARG ALA          
SEQRES   6 B  444  ARG GLU GLU GLN THR PRO LEU HIS ILE ALA SER ARG LEU          
SEQRES   7 B  444  GLY LYS THR GLU ILE VAL GLN LEU LEU LEU GLN HIS MET          
SEQRES   8 B  444  ALA HIS PRO ASP ALA ALA THR THR ASN GLY TYR THR PRO          
SEQRES   9 B  444  LEU HIS ILE SER ALA ARG GLU GLY GLN VAL ASP VAL ALA          
SEQRES  10 B  444  SER VAL LEU LEU GLU ALA GLY ALA ALA HIS SER LEU ALA          
SEQRES  11 B  444  THR LYS LYS GLY PHE THR PRO LEU HIS VAL ALA ALA LYS          
SEQRES  12 B  444  TYR GLY SER LEU ASP VAL ALA LYS LEU LEU LEU GLN ARG          
SEQRES  13 B  444  ARG ALA ALA ALA ASP SER ALA GLY LYS ASN GLY LEU THR          
SEQRES  14 B  444  PRO LEU HIS VAL ALA ALA HIS TYR ASP ASN GLN LYS VAL          
SEQRES  15 B  444  ALA LEU LEU LEU LEU GLU LYS GLY ALA SER PRO HIS ALA          
SEQRES  16 B  444  THR ALA LYS ASN GLY TYR THR PRO LEU HIS ILE ALA ALA          
SEQRES  17 B  444  LYS LYS ASN GLN MET GLN ILE ALA SER THR LEU LEU ASN          
SEQRES  18 B  444  TYR GLY ALA GLU THR ASN ILE VAL THR LYS GLN GLY VAL          
SEQRES  19 B  444  THR PRO LEU HIS LEU ALA SER GLN GLU GLY HIS THR ASP          
SEQRES  20 B  444  MET VAL THR LEU LEU LEU ASP LYS GLY ALA ASN ILE HIS          
SEQRES  21 B  444  MET SER THR LYS SER GLY LEU THR SER LEU HIS LEU ALA          
SEQRES  22 B  444  ALA GLN GLU ASP LYS VAL ASN VAL ALA ASP ILE LEU THR          
SEQRES  23 B  444  LYS HIS GLY ALA ASP GLN ASP ALA HIS THR LYS LEU GLY          
SEQRES  24 B  444  TYR THR PRO LEU ILE VAL ALA CYS HIS TYR GLY ASN VAL          
SEQRES  25 B  444  LYS MET VAL ASN PHE LEU LEU LYS GLN GLY ALA ASN VAL          
SEQRES  26 B  444  ASN ALA LYS THR LYS ASN GLY TYR THR PRO LEU HIS GLN          
SEQRES  27 B  444  ALA ALA GLN GLN GLY HIS THR HIS ILE ILE ASN VAL LEU          
SEQRES  28 B  444  LEU GLN HIS GLY ALA LYS PRO ASN ALA THR THR ALA ASN          
SEQRES  29 B  444  GLY ASN THR ALA LEU ALA ILE ALA LYS ARG LEU GLY TYR          
SEQRES  30 B  444  ILE SER VAL VAL ASP THR LEU LYS VAL VAL THR GLU GLU          
SEQRES  31 B  444  VAL THR THR THR THR THR THR ILE THR GLU LYS HIS LYS          
SEQRES  32 B  444  LEU ASN VAL PRO GLU THR MET THR GLU VAL LEU ASP VAL          
SEQRES  33 B  444  SER ASP GLU GLU GLY ASP ASP THR MET THR GLY ASP GLY          
SEQRES  34 B  444  GLY GLU TYR LEU ARG PRO GLU ASP LEU LYS GLU LEU GLY          
SEQRES  35 B  444  ASP ASP                                                      
HET     CA  B 901       1                                                       
HET    ACT  B 902       4                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     ACT ACETATE ION                                                      
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  ACT    C2 H3 O2 1-                                                  
FORMUL   5  HOH   *274(H2 O)                                                    
HELIX    1 AA1 THR A  432  GLY A  441  1                                  10    
HELIX    2 AA2 HIS A  442  ASN A  452  1                                  11    
HELIX    3 AA3 THR A  465  ALA A  473  1                                   9    
HELIX    4 AA4 GLN A  475  ASN A  485  1                                  11    
HELIX    5 AA5 ALA A  493  GLN A  497  5                                   5    
HELIX    6 AA6 THR A  498  LEU A  506  1                                   9    
HELIX    7 AA7 LYS A  508  HIS A  518  1                                  11    
HELIX    8 AA8 THR A  531  GLY A  540  1                                  10    
HELIX    9 AA9 GLN A  541  ALA A  551  1                                  11    
HELIX   10 AB1 THR A  564  GLY A  573  1                                  10    
HELIX   11 AB2 SER A  574  ARG A  584  1                                  11    
HELIX   12 AB3 THR A  597  TYR A  605  1                                   9    
HELIX   13 AB4 ASN A  607  LYS A  617  1                                  11    
HELIX   14 AB5 THR A  630  ASN A  639  1                                  10    
HELIX   15 AB6 GLN A  640  TYR A  650  1                                  11    
HELIX   16 AB7 THR A  663  GLY A  672  1                                  10    
HELIX   17 AB8 HIS A  673  LYS A  683  1                                  11    
HELIX   18 AB9 THR A  696  ASP A  705  1                                  10    
HELIX   19 AC1 LYS A  706  HIS A  716  1                                  11    
HELIX   20 AC2 THR A  729  GLY A  738  1                                  10    
HELIX   21 AC3 ASN A  739  GLN A  749  1                                  11    
HELIX   22 AC4 THR A  762  GLN A  770  1                                   9    
HELIX   23 AC5 HIS A  772  HIS A  782  1                                  11    
HELIX   24 AC6 THR A  795  LEU A  803  1                                   9    
HELIX   25 AC7 TYR A  805  VAL A  814  1                                  10    
HELIX   26 AC8 THR B  432  GLY B  441  1                                  10    
HELIX   27 AC9 HIS B  442  ASN B  452  1                                  11    
HELIX   28 AD1 THR B  465  GLY B  474  1                                  10    
HELIX   29 AD2 GLN B  475  ASN B  485  1                                  11    
HELIX   30 AD3 ALA B  493  GLN B  497  5                                   5    
HELIX   31 AD4 THR B  498  LEU B  506  1                                   9    
HELIX   32 AD5 LYS B  508  HIS B  518  1                                  11    
HELIX   33 AD6 THR B  531  GLY B  540  1                                  10    
HELIX   34 AD7 GLN B  541  ALA B  551  1                                  11    
HELIX   35 AD8 THR B  564  GLY B  573  1                                  10    
HELIX   36 AD9 SER B  574  ARG B  584  1                                  11    
HELIX   37 AE1 THR B  597  TYR B  605  1                                   9    
HELIX   38 AE2 ASN B  607  LYS B  617  1                                  11    
HELIX   39 AE3 THR B  630  LYS B  638  1                                   9    
HELIX   40 AE4 GLN B  640  TYR B  650  1                                  11    
HELIX   41 AE5 THR B  663  GLY B  672  1                                  10    
HELIX   42 AE6 HIS B  673  LYS B  683  1                                  11    
HELIX   43 AE7 THR B  696  GLU B  704  1                                   9    
HELIX   44 AE8 LYS B  706  HIS B  716  1                                  11    
HELIX   45 AE9 THR B  729  GLY B  738  1                                  10    
HELIX   46 AF1 ASN B  739  GLN B  749  1                                  11    
HELIX   47 AF2 THR B  762  GLN B  770  1                                   9    
HELIX   48 AF3 HIS B  772  HIS B  782  1                                  11    
HELIX   49 AF4 THR B  795  GLY B  804  1                                  10    
HELIX   50 AF5 TYR B  805  LYS B  813  1                                   9    
LINK         O   GLY B 441                CA    CA B 901     1555   1555  2.48  
LINK        CA    CA B 901                 O   HOH B1089     1555   1555  2.31  
LINK        CA    CA B 901                 O   HOH B1093     1555   1555  2.28  
LINK         OD1 ASP B 682                CA    CA B 901     1555   3344  2.52  
LINK         OD2 ASP B 682                CA    CA B 901     1555   3344  2.99  
LINK        CA    CA B 901                 O   HOH B1105     1555   3354  2.59  
LINK        CA    CA B 901                 O   HOH B1125     1555   3354  2.63  
LINK        CA    CA B 901                 O   HOH B1116     1555   3354  2.31  
SITE     1 AC1  7 GLY B 441  ASP B 682  HOH B1089  HOH B1093                    
SITE     2 AC1  7 HOH B1105  HOH B1116  HOH B1125                               
SITE     1 AC2  6 LYS B 756  THR B 757  LYS B 758  GLY B 760                    
SITE     2 AC2  6 HIS B 774  ASN B 777                                          
CRYST1   29.304  127.803  257.550  90.00  90.00  90.00 P 21 21 21    8          
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      0.034125  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007825  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003883        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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