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Database: PDB
Entry: 3ZYK
LinkDB: 3ZYK
Original site: 3ZYK 
HEADER    ENDOCYTOSIS                             23-AUG-11   3ZYK              
TITLE     STRUCTURE OF CALM (PICALM) ANTH DOMAIN                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHATIDYLINOSITOL-BINDING CLATHRIN ASSEMBLY PROTEIN;    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: ANTH DOMAIN, RESIDUES 1-289;                               
COMPND   5 SYNONYM: CALM, CLATHRIN ASSEMBLY LYMPHOID MYELOID LEUKEMIA PROTEIN,  
COMPND   6 RCALM;                                                               
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: PLYSS;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX 4T2 CALMANTH(1-289)                  
KEYWDS    ENDOCYTOSIS, ENDOBREVIN, SYNAPTOBREVIN, VAMP2, VAMP3, AP180, PLASMA   
KEYWDS   2 MEMBRANE, ADAPTOR PROTEIN                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.E.MILLER,D.A.SAHLENDER,S.C.GRAHAM,S.HONING,M.S.ROBINSON,A.A.PEDEN,  
AUTHOR   2 D.J.OWEN                                                             
REVDAT   2   13-MAR-19 3ZYK    1       JRNL   REMARK                            
REVDAT   1   07-DEC-11 3ZYK    0                                                
JRNL        AUTH   S.E.MILLER,D.A.SAHLENDER,S.C.GRAHAM,S.HONING,M.S.ROBINSON,   
JRNL        AUTH 2 A.A.PEDEN,D.J.OWEN                                           
JRNL        TITL   THE MOLECULAR BASIS FOR THE ENDOCYTOSIS OF SMALL R-SNARES BY 
JRNL        TITL 2 THE CLATHRIN ADAPTOR CALM.                                   
JRNL        REF    CELL                          V. 147  1118 2011              
JRNL        REFN                   ISSN 1097-4172                               
JRNL        PMID   22118466                                                     
JRNL        DOI    10.1016/J.CELL.2011.10.038                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.01                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 64141                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3237                            
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 40.0184 -  5.1155    0.98     2853   141  0.2018 0.2034        
REMARK   3     2  5.1155 -  4.0616    0.98     2718   133  0.1571 0.2098        
REMARK   3     3  4.0616 -  3.5486    1.00     2711   146  0.1613 0.2075        
REMARK   3     4  3.5486 -  3.2243    0.99     2710   136  0.1779 0.1880        
REMARK   3     5  3.2243 -  2.9932    0.99     2670   143  0.1906 0.2307        
REMARK   3     6  2.9932 -  2.8168    0.99     2677   134  0.1828 0.2275        
REMARK   3     7  2.8168 -  2.6758    0.99     2700   133  0.1781 0.2095        
REMARK   3     8  2.6758 -  2.5593    0.99     2615   158  0.1783 0.2138        
REMARK   3     9  2.5593 -  2.4608    0.99     2649   154  0.1718 0.1671        
REMARK   3    10  2.4608 -  2.3759    0.99     2635   152  0.1728 0.2049        
REMARK   3    11  2.3759 -  2.3016    0.99     2637   134  0.1751 0.2130        
REMARK   3    12  2.3016 -  2.2358    0.99     2621   132  0.1713 0.2109        
REMARK   3    13  2.2358 -  2.1770    0.99     2630   148  0.1764 0.2116        
REMARK   3    14  2.1770 -  2.1239    0.99     2622   156  0.1796 0.2388        
REMARK   3    15  2.1239 -  2.0756    0.99     2631   139  0.1794 0.2244        
REMARK   3    16  2.0756 -  2.0314    0.98     2601   144  0.1887 0.2172        
REMARK   3    17  2.0314 -  1.9908    0.98     2590   135  0.1840 0.2451        
REMARK   3    18  1.9908 -  1.9532    0.98     2624   137  0.1931 0.2390        
REMARK   3    19  1.9532 -  1.9183    0.98     2597   139  0.1989 0.2544        
REMARK   3    20  1.9183 -  1.8858    0.98     2605   127  0.2122 0.2705        
REMARK   3    21  1.8858 -  1.8554    0.98     2600   154  0.2536 0.2667        
REMARK   3    22  1.8554 -  1.8269    0.98     2579   147  0.2655 0.3331        
REMARK   3    23  1.8269 -  1.8000    0.98     2629   115  0.3013 0.3472        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.36                                          
REMARK   3   B_SOL              : 50.68                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.410           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.84                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.69                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.45950                                              
REMARK   3    B22 (A**2) : 1.86710                                              
REMARK   3    B33 (A**2) : -5.32660                                             
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      :  0.009           4510                                  
REMARK   3   ANGLE     :  1.077           6104                                  
REMARK   3   CHIRALITY :  0.075            695                                  
REMARK   3   PLANARITY :  0.005            782                                  
REMARK   3   DIHEDRAL  : 12.450           1740                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -29.2251  -1.3104   0.4530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0405 T22:   0.0651                                     
REMARK   3      T33:   0.0699 T12:   0.0064                                     
REMARK   3      T13:  -0.0002 T23:  -0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4246 L22:   0.9338                                     
REMARK   3      L33:   1.3394 L12:  -0.3856                                     
REMARK   3      L13:   0.1143 L23:  -0.3480                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0172 S12:   0.0371 S13:   0.0245                       
REMARK   3      S21:  -0.0430 S22:  -0.0021 S23:   0.0208                       
REMARK   3      S31:  -0.0720 S32:  -0.1917 S33:   0.0005                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -18.2652 -11.4547  30.3847              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0940 T22:   0.1616                                     
REMARK   3      T33:   0.1099 T12:   0.0001                                     
REMARK   3      T13:  -0.0413 T23:   0.0272                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7357 L22:   1.4000                                     
REMARK   3      L33:   3.9479 L12:  -0.0772                                     
REMARK   3      L13:   0.5114 L23:   0.0865                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0271 S12:  -0.0381 S13:   0.0373                       
REMARK   3      S21:   0.1985 S22:  -0.0224 S23:  -0.1911                       
REMARK   3      S31:   0.3393 S32:   0.5942 S33:   0.0081                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND NOT (RESI 44 OR RESI 47:48 OR   
REMARK   3                          RESI 51 OR RESI 92 OR RESI 105 OR RESI      
REMARK   3                          115 OR RESI 118:119 OR RESI 147 OR RESI     
REMARK   3                          150 OR RESI 202 OR RESI 268:288)            
REMARK   3     SELECTION          : CHAIN B                                     
REMARK   3     ATOM PAIRS NUMBER  : 1929                                        
REMARK   3     RMSD               : 0.075                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND RESI 271:288                    
REMARK   3     SELECTION          : CHAIN B                                     
REMARK   3     ATOM PAIRS NUMBER  : 111                                         
REMARK   3     RMSD               : 0.024                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3ZYK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-AUG-11.                  
REMARK 100 THE DEPOSITION ID IS D_1290049396.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-FEB-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64198                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 73.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 14.10                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.50                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.86000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
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: PDB ENTRY 1HF8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN IN SITTING DROPS     
REMARK 280  CONTAINING EQUAL AMOUNTS (200-400 NL) OF PROTEIN (15 MG/ML IN 20    
REMARK 280  MM HEPES PH 7.4, 120 MM NACL, 4 MM DTT) AND RESERVOIR SOLUTION      
REMARK 280  (100 MM BIS TRIS PROPANE, 200 MM SODIUM MALONATE, 20% (W/V) PEG     
REMARK 280  3350) AND EQUILIBRATED AGAINST 80 UL OF RESERVOIR SOLUTION AT       
REMARK 280  16C. CRYSTALS WERE CRYOPROTECTED BY BRIEF IMMERSION (5-60 S) IN     
REMARK 280  RESERVOIR SOLUTION SUPPLEMENTED WITH 25% GLYCEROL AND WERE          
REMARK 280  RAPIDLY CRYOCOOLED IN LIQUID N2 OR A 100 K STREAM OF N2 GAS.,       
REMARK 280  VAPOR DIFFUSION, SITTING 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       36.77050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.10850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.15650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.10850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.77050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.15650            
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 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     GLY A    -6                                                      
REMARK 465     SER A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ILE A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     ILE A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     ARG A     9                                                      
REMARK 465     ILE A    10                                                      
REMARK 465     THR A    11                                                      
REMARK 465     ALA A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     GLN A    14                                                      
REMARK 465     HIS A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     VAL A    17                                                      
REMARK 465     THR A    18                                                      
REMARK 465     GLY A    19                                                      
REMARK 465     LYS A   289                                                      
REMARK 465     GLY B    -6                                                      
REMARK 465     SER B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ILE B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     ILE B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     ASP B     8                                                      
REMARK 465     ARG B     9                                                      
REMARK 465     ILE B    10                                                      
REMARK 465     THR B    11                                                      
REMARK 465     ALA B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     GLN B    14                                                      
REMARK 465     HIS B    15                                                      
REMARK 465     SER B    16                                                      
REMARK 465     VAL B    17                                                      
REMARK 465     GLU B   286                                                      
REMARK 465     GLY B   287                                                      
REMARK 465     LYS B   288                                                      
REMARK 465     LYS B   289                                                      
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    LEU A 103     -112.28   -115.44                                   
REMARK 500    LEU B 103     -113.89   -115.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2031        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH A2044        DISTANCE =  6.49 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1HG2   RELATED DB: PDB                                   
REMARK 900 CALM-N N-TERMINAL DOMAIN OF CLATHRIN ASSEMBLY LYMPHOID MYELOID       
REMARK 900 LEUKAEMIA PROTEIN, I(4,5)P2 COMPLEX                                  
REMARK 900 RELATED ID: 1HG5   RELATED DB: PDB                                   
REMARK 900 CALM-N N-TERMINAL DOMAIN OF CLATHRIN ASSEMBLY LYMPHOID MYELOID       
REMARK 900 LEUKAEMIA PROTEIN, INOSITOL(1,2,3,4,5,6) P6 COMPLEX                  
REMARK 900 RELATED ID: 1HFA   RELATED DB: PDB                                   
REMARK 900 CALM-N N-TERMINAL DOMAIN OF CLATHRIN ASSEMBLY LYMPHOID MYELOID       
REMARK 900 LEUKAEMIA PROTEIN, PI(4,5)P2 COMPLEX                                 
REMARK 900 RELATED ID: 1HF8   RELATED DB: PDB                                   
REMARK 900 CALM-N N-TERMINAL DOMAIN OF CLATHRIN ASSEMBLY LYMPHOID MYELOID       
REMARK 900 LEUKAEMIA PROTEIN                                                    
REMARK 900 RELATED ID: 3ZYM   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CALM (PICALM) IN COMPLEX WITH VAMP8                     
REMARK 900 RELATED ID: 3ZYL   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF A TRUNCATED CALM (PICALM) ANTH DOMAIN                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 N-TERMINAL GSPIGIH SEQUENCE IS RESIDUAL FROM AFFINITY TAG            
REMARK 999 AND CLONING.                                                         
DBREF  3ZYK A    1   289  UNP    O55012   PICA_RAT         1    289             
DBREF  3ZYK B    1   289  UNP    O55012   PICA_RAT         1    289             
SEQADV 3ZYK GLY A   -6  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYK SER A   -5  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYK PRO A   -4  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYK ILE A   -3  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYK GLY A   -2  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYK ILE A   -1  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYK HIS A    0  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYK GLY B   -6  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYK SER B   -5  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYK PRO B   -4  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYK ILE B   -3  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYK GLY B   -2  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYK ILE B   -1  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYK HIS B    0  UNP  O55012              EXPRESSION TAG                 
SEQRES   1 A  296  GLY SER PRO ILE GLY ILE HIS MET SER GLY GLN SER LEU          
SEQRES   2 A  296  THR ASP ARG ILE THR ALA ALA GLN HIS SER VAL THR GLY          
SEQRES   3 A  296  SER ALA VAL SER LYS THR VAL CYS LYS ALA THR THR HIS          
SEQRES   4 A  296  GLU ILE MET GLY PRO LYS LYS LYS HIS LEU ASP TYR LEU          
SEQRES   5 A  296  ILE GLN CYS THR ASN GLU MET ASN VAL ASN ILE PRO GLN          
SEQRES   6 A  296  LEU ALA ASP SER LEU PHE GLU ARG THR THR ASN SER SER          
SEQRES   7 A  296  TRP VAL VAL VAL PHE LYS SER LEU ILE THR THR HIS HIS          
SEQRES   8 A  296  LEU MET VAL TYR GLY ASN GLU ARG PHE ILE GLN TYR LEU          
SEQRES   9 A  296  ALA SER ARG ASN THR LEU PHE ASN LEU SER ASN PHE LEU          
SEQRES  10 A  296  ASP LYS SER GLY LEU GLN GLY TYR ASP MET SER THR PHE          
SEQRES  11 A  296  ILE ARG ARG TYR SER ARG TYR LEU ASN GLU LYS ALA VAL          
SEQRES  12 A  296  SER TYR ARG GLN VAL ALA PHE ASP PHE THR LYS VAL LYS          
SEQRES  13 A  296  ARG GLY ALA ASP GLY VAL MET ARG THR MET ASN THR GLU          
SEQRES  14 A  296  LYS LEU LEU LYS THR VAL PRO ILE ILE GLN ASN GLN MET          
SEQRES  15 A  296  ASP ALA LEU LEU ASP PHE ASN VAL ASN SER ASN GLU LEU          
SEQRES  16 A  296  THR ASN GLY VAL ILE ASN ALA ALA PHE MET LEU LEU PHE          
SEQRES  17 A  296  LYS ASP ALA ILE ARG LEU PHE ALA ALA TYR ASN GLU GLY          
SEQRES  18 A  296  ILE ILE ASN LEU LEU GLU LYS TYR PHE ASP MET LYS LYS          
SEQRES  19 A  296  ASN GLN CYS LYS GLU GLY LEU ASP ILE TYR LYS LYS PHE          
SEQRES  20 A  296  LEU THR ARG MET THR ARG ILE SER GLU PHE LEU LYS VAL          
SEQRES  21 A  296  ALA GLU GLN VAL GLY ILE ASP ARG GLY ASP ILE PRO ASP          
SEQRES  22 A  296  LEU SER GLN ALA PRO SER SER LEU LEU ASP ALA LEU GLU          
SEQRES  23 A  296  GLN HIS LEU ALA SER LEU GLU GLY LYS LYS                      
SEQRES   1 B  296  GLY SER PRO ILE GLY ILE HIS MET SER GLY GLN SER LEU          
SEQRES   2 B  296  THR ASP ARG ILE THR ALA ALA GLN HIS SER VAL THR GLY          
SEQRES   3 B  296  SER ALA VAL SER LYS THR VAL CYS LYS ALA THR THR HIS          
SEQRES   4 B  296  GLU ILE MET GLY PRO LYS LYS LYS HIS LEU ASP TYR LEU          
SEQRES   5 B  296  ILE GLN CYS THR ASN GLU MET ASN VAL ASN ILE PRO GLN          
SEQRES   6 B  296  LEU ALA ASP SER LEU PHE GLU ARG THR THR ASN SER SER          
SEQRES   7 B  296  TRP VAL VAL VAL PHE LYS SER LEU ILE THR THR HIS HIS          
SEQRES   8 B  296  LEU MET VAL TYR GLY ASN GLU ARG PHE ILE GLN TYR LEU          
SEQRES   9 B  296  ALA SER ARG ASN THR LEU PHE ASN LEU SER ASN PHE LEU          
SEQRES  10 B  296  ASP LYS SER GLY LEU GLN GLY TYR ASP MET SER THR PHE          
SEQRES  11 B  296  ILE ARG ARG TYR SER ARG TYR LEU ASN GLU LYS ALA VAL          
SEQRES  12 B  296  SER TYR ARG GLN VAL ALA PHE ASP PHE THR LYS VAL LYS          
SEQRES  13 B  296  ARG GLY ALA ASP GLY VAL MET ARG THR MET ASN THR GLU          
SEQRES  14 B  296  LYS LEU LEU LYS THR VAL PRO ILE ILE GLN ASN GLN MET          
SEQRES  15 B  296  ASP ALA LEU LEU ASP PHE ASN VAL ASN SER ASN GLU LEU          
SEQRES  16 B  296  THR ASN GLY VAL ILE ASN ALA ALA PHE MET LEU LEU PHE          
SEQRES  17 B  296  LYS ASP ALA ILE ARG LEU PHE ALA ALA TYR ASN GLU GLY          
SEQRES  18 B  296  ILE ILE ASN LEU LEU GLU LYS TYR PHE ASP MET LYS LYS          
SEQRES  19 B  296  ASN GLN CYS LYS GLU GLY LEU ASP ILE TYR LYS LYS PHE          
SEQRES  20 B  296  LEU THR ARG MET THR ARG ILE SER GLU PHE LEU LYS VAL          
SEQRES  21 B  296  ALA GLU GLN VAL GLY ILE ASP ARG GLY ASP ILE PRO ASP          
SEQRES  22 B  296  LEU SER GLN ALA PRO SER SER LEU LEU ASP ALA LEU GLU          
SEQRES  23 B  296  GLN HIS LEU ALA SER LEU GLU GLY LYS LYS                      
FORMUL   3  HOH   *415(H2 O)                                                    
HELIX    1   1 SER A   20  THR A   30  1                                  11    
HELIX    2   2 LYS A   38  GLU A   51  1                                  14    
HELIX    3   3 ASN A   55  THR A   67  1                                  13    
HELIX    4   4 SER A   71  GLY A   89  1                                  19    
HELIX    5   5 ASN A   90  ARG A  100  1                                  11    
HELIX    6   6 GLY A  114  ALA A  142  1                                  29    
HELIX    7   7 GLY A  154  MET A  159  1                                   6    
HELIX    8   8 ASN A  160  ASP A  180  1                                  21    
HELIX    9   9 ASN A  184  LEU A  188  5                                   5    
HELIX   10  10 ASN A  190  TYR A  222  1                                  33    
HELIX   11  11 PHE A  223  MET A  225  5                                   3    
HELIX   12  12 LYS A  226  GLY A  258  1                                  33    
HELIX   13  13 ASP A  260  ILE A  264  5                                   5    
HELIX   14  14 ASP A  266  ALA A  270  5                                   5    
HELIX   15  15 LEU A  274  GLU A  286  1                                  13    
HELIX   16  16 THR B   18  THR B   30  1                                  13    
HELIX   17  17 LYS B   38  GLU B   51  1                                  14    
HELIX   18  18 ASN B   55  THR B   67  1                                  13    
HELIX   19  19 SER B   71  GLY B   89  1                                  19    
HELIX   20  20 ASN B   90  ARG B  100  1                                  11    
HELIX   21  21 GLY B  114  ALA B  142  1                                  29    
HELIX   22  22 GLY B  154  MET B  159  1                                   6    
HELIX   23  23 ASN B  160  ASP B  180  1                                  21    
HELIX   24  24 ASN B  184  LEU B  188  5                                   5    
HELIX   25  25 ASN B  190  TYR B  222  1                                  33    
HELIX   26  26 PHE B  223  MET B  225  5                                   3    
HELIX   27  27 LYS B  226  GLY B  258  1                                  33    
HELIX   28  28 ASP B  260  ILE B  264  5                                   5    
HELIX   29  29 ASP B  266  ALA B  270  5                                   5    
HELIX   30  30 LEU B  274  LEU B  285  1                                  12    
CRYST1   73.541   78.313  120.217  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      0.013598  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012769  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008318        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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