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Database: PDB
Entry: 3ZYL
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Original site: 3ZYL 
HEADER    ENDOCYTOSIS                             23-AUG-11   3ZYL              
TITLE     STRUCTURE OF A TRUNCATED CALM (PICALM) ANTH DOMAIN                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHATIDYLINOSITOL-BINDING CLATHRIN ASSEMBLY PROTEIN;    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: TRUNCATED ANTH DOMAIN, RESIDUES 1-264;                     
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(1-264)                  
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 3ZYL    1       JRNL   REMARK                            
REVDAT   1   07-DEC-11 3ZYL    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.    1.70 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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.51                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 72462                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.191                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3652                            
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 35.5168 -  5.0317    0.96     2627   143  0.1851 0.2060        
REMARK   3     2  5.0317 -  3.9955    0.99     2644   134  0.1446 0.1502        
REMARK   3     3  3.9955 -  3.4910    0.98     2612   154  0.1570 0.1706        
REMARK   3     4  3.4910 -  3.1720    0.99     2654   140  0.1681 0.1771        
REMARK   3     5  3.1720 -  2.9448    0.99     2617   134  0.1644 0.1691        
REMARK   3     6  2.9448 -  2.7712    0.99     2658   147  0.1580 0.1548        
REMARK   3     7  2.7712 -  2.6325    0.99     2643   129  0.1593 0.1925        
REMARK   3     8  2.6325 -  2.5179    0.99     2604   164  0.1683 0.1905        
REMARK   3     9  2.5179 -  2.4210    0.99     2668   136  0.1641 0.2035        
REMARK   3    10  2.4210 -  2.3375    1.00     2641   146  0.1543 0.2183        
REMARK   3    11  2.3375 -  2.2644    0.99     2644   138  0.1570 0.1637        
REMARK   3    12  2.2644 -  2.1997    1.00     2619   160  0.1562 0.2075        
REMARK   3    13  2.1997 -  2.1418    1.00     2653   149  0.1671 0.1950        
REMARK   3    14  2.1418 -  2.0895    1.00     2622   144  0.1645 0.1967        
REMARK   3    15  2.0895 -  2.0420    1.00     2697   141  0.1761 0.2201        
REMARK   3    16  2.0420 -  1.9986    1.00     2616   150  0.1708 0.2178        
REMARK   3    17  1.9986 -  1.9586    1.00     2678   138  0.1701 0.2130        
REMARK   3    18  1.9586 -  1.9217    1.00     2658   134  0.1706 0.1977        
REMARK   3    19  1.9217 -  1.8873    1.00     2644   142  0.1759 0.2279        
REMARK   3    20  1.8873 -  1.8553    1.00     2695   124  0.1930 0.2207        
REMARK   3    21  1.8553 -  1.8254    1.00     2625   130  0.2070 0.2569        
REMARK   3    22  1.8254 -  1.7973    1.00     2668   132  0.2286 0.2857        
REMARK   3    23  1.7973 -  1.7709    1.00     2648   138  0.2467 0.2815        
REMARK   3    24  1.7709 -  1.7460    0.99     2667   140  0.2599 0.2678        
REMARK   3    25  1.7460 -  1.7224    1.00     2638   127  0.2823 0.3354        
REMARK   3    26  1.7224 -  1.7000    1.00     2670   138  0.2881 0.2967        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.95                                          
REMARK   3   K_SOL              : 0.36                                          
REMARK   3   B_SOL              : 46.30                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.960           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.93                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.08090                                              
REMARK   3    B22 (A**2) : 0.35790                                              
REMARK   3    B33 (A**2) : -5.43880                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 9.71390                                              
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      :  0.010           4322                                  
REMARK   3   ANGLE     :  1.110           5863                                  
REMARK   3   CHIRALITY :  0.070            668                                  
REMARK   3   PLANARITY :  0.005            749                                  
REMARK   3   DIHEDRAL  : 11.788           1663                                  
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):   5.4482  -9.0046  66.5129              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0580 T22:   0.0596                                     
REMARK   3      T33:   0.0696 T12:  -0.0159                                     
REMARK   3      T13:  -0.0119 T23:  -0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5208 L22:   0.3522                                     
REMARK   3      L33:   0.7572 L12:  -0.3399                                     
REMARK   3      L13:  -0.3480 L23:  -0.0321                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0175 S12:   0.0255 S13:  -0.0472                       
REMARK   3      S21:   0.0254 S22:  -0.0082 S23:   0.0556                       
REMARK   3      S31:  -0.0423 S32:   0.0049 S33:   0.0123                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  16.7392  16.2932  25.7137              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0888 T22:   0.1174                                     
REMARK   3      T33:   0.1248 T12:   0.0546                                     
REMARK   3      T13:  -0.0073 T23:   0.0344                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2996 L22:   0.8044                                     
REMARK   3      L33:   0.7385 L12:   0.1691                                     
REMARK   3      L13:  -0.2797 L23:   0.4265                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0198 S12:  -0.0205 S13:   0.0736                       
REMARK   3      S21:  -0.0430 S22:   0.0325 S23:   0.0858                       
REMARK   3      S31:   0.0510 S32:   0.0102 S33:  -0.0024                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND NOT (RESID 28 OR RESID 65 OR    
REMARK   3                          RESID 111:115 OR RESID 186:190 OR RESID     
REMARK   3                          237 OR RESID 252)                           
REMARK   3     SELECTION          : CHAIN B                                     
REMARK   3     ATOM PAIRS NUMBER  : 1851                                        
REMARK   3     RMSD               : 0.055                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3ZYL 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_1290049397.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
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   : 72568                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
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   (%): 55.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
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  (15% V/V ETHANOL, 100 MM IMIDAZOLE PH 8.0, 200 MM MGCL2) AND        
REMARK 280  EQUILIBRATED AGAINST 80 UL OF RESERVOIR SOLUTION AT 16C.            
REMARK 280  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: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       47.94400            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.54100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       47.94400            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       60.54100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2202  LIES ON A SPECIAL POSITION.                          
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     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 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     -122.66   -123.14                                   
REMARK 500    LEU B 103     -123.66   -124.16                                   
REMARK 500    ASP B 111       78.64   -102.99                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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: 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: 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: 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: 3ZYK   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF 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  3ZYL A    1   264  UNP    O55012   PICA_RAT         1    264             
DBREF  3ZYL B    1   264  UNP    O55012   PICA_RAT         1    264             
SEQADV 3ZYL GLY A   -6  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYL SER A   -5  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYL PRO A   -4  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYL ILE A   -3  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYL GLY A   -2  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYL ILE A   -1  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYL HIS A    0  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYL GLY B   -6  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYL SER B   -5  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYL PRO B   -4  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYL ILE B   -3  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYL GLY B   -2  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYL ILE B   -1  UNP  O55012              EXPRESSION TAG                 
SEQADV 3ZYL HIS B    0  UNP  O55012              EXPRESSION TAG                 
SEQRES   1 A  271  GLY SER PRO ILE GLY ILE HIS MET SER GLY GLN SER LEU          
SEQRES   2 A  271  THR ASP ARG ILE THR ALA ALA GLN HIS SER VAL THR GLY          
SEQRES   3 A  271  SER ALA VAL SER LYS THR VAL CYS LYS ALA THR THR HIS          
SEQRES   4 A  271  GLU ILE MET GLY PRO LYS LYS LYS HIS LEU ASP TYR LEU          
SEQRES   5 A  271  ILE GLN CYS THR ASN GLU MET ASN VAL ASN ILE PRO GLN          
SEQRES   6 A  271  LEU ALA ASP SER LEU PHE GLU ARG THR THR ASN SER SER          
SEQRES   7 A  271  TRP VAL VAL VAL PHE LYS SER LEU ILE THR THR HIS HIS          
SEQRES   8 A  271  LEU MET VAL TYR GLY ASN GLU ARG PHE ILE GLN TYR LEU          
SEQRES   9 A  271  ALA SER ARG ASN THR LEU PHE ASN LEU SER ASN PHE LEU          
SEQRES  10 A  271  ASP LYS SER GLY LEU GLN GLY TYR ASP MET SER THR PHE          
SEQRES  11 A  271  ILE ARG ARG TYR SER ARG TYR LEU ASN GLU LYS ALA VAL          
SEQRES  12 A  271  SER TYR ARG GLN VAL ALA PHE ASP PHE THR LYS VAL LYS          
SEQRES  13 A  271  ARG GLY ALA ASP GLY VAL MET ARG THR MET ASN THR GLU          
SEQRES  14 A  271  LYS LEU LEU LYS THR VAL PRO ILE ILE GLN ASN GLN MET          
SEQRES  15 A  271  ASP ALA LEU LEU ASP PHE ASN VAL ASN SER ASN GLU LEU          
SEQRES  16 A  271  THR ASN GLY VAL ILE ASN ALA ALA PHE MET LEU LEU PHE          
SEQRES  17 A  271  LYS ASP ALA ILE ARG LEU PHE ALA ALA TYR ASN GLU GLY          
SEQRES  18 A  271  ILE ILE ASN LEU LEU GLU LYS TYR PHE ASP MET LYS LYS          
SEQRES  19 A  271  ASN GLN CYS LYS GLU GLY LEU ASP ILE TYR LYS LYS PHE          
SEQRES  20 A  271  LEU THR ARG MET THR ARG ILE SER GLU PHE LEU LYS VAL          
SEQRES  21 A  271  ALA GLU GLN VAL GLY ILE ASP ARG GLY ASP ILE                  
SEQRES   1 B  271  GLY SER PRO ILE GLY ILE HIS MET SER GLY GLN SER LEU          
SEQRES   2 B  271  THR ASP ARG ILE THR ALA ALA GLN HIS SER VAL THR GLY          
SEQRES   3 B  271  SER ALA VAL SER LYS THR VAL CYS LYS ALA THR THR HIS          
SEQRES   4 B  271  GLU ILE MET GLY PRO LYS LYS LYS HIS LEU ASP TYR LEU          
SEQRES   5 B  271  ILE GLN CYS THR ASN GLU MET ASN VAL ASN ILE PRO GLN          
SEQRES   6 B  271  LEU ALA ASP SER LEU PHE GLU ARG THR THR ASN SER SER          
SEQRES   7 B  271  TRP VAL VAL VAL PHE LYS SER LEU ILE THR THR HIS HIS          
SEQRES   8 B  271  LEU MET VAL TYR GLY ASN GLU ARG PHE ILE GLN TYR LEU          
SEQRES   9 B  271  ALA SER ARG ASN THR LEU PHE ASN LEU SER ASN PHE LEU          
SEQRES  10 B  271  ASP LYS SER GLY LEU GLN GLY TYR ASP MET SER THR PHE          
SEQRES  11 B  271  ILE ARG ARG TYR SER ARG TYR LEU ASN GLU LYS ALA VAL          
SEQRES  12 B  271  SER TYR ARG GLN VAL ALA PHE ASP PHE THR LYS VAL LYS          
SEQRES  13 B  271  ARG GLY ALA ASP GLY VAL MET ARG THR MET ASN THR GLU          
SEQRES  14 B  271  LYS LEU LEU LYS THR VAL PRO ILE ILE GLN ASN GLN MET          
SEQRES  15 B  271  ASP ALA LEU LEU ASP PHE ASN VAL ASN SER ASN GLU LEU          
SEQRES  16 B  271  THR ASN GLY VAL ILE ASN ALA ALA PHE MET LEU LEU PHE          
SEQRES  17 B  271  LYS ASP ALA ILE ARG LEU PHE ALA ALA TYR ASN GLU GLY          
SEQRES  18 B  271  ILE ILE ASN LEU LEU GLU LYS TYR PHE ASP MET LYS LYS          
SEQRES  19 B  271  ASN GLN CYS LYS GLU GLY LEU ASP ILE TYR LYS LYS PHE          
SEQRES  20 B  271  LEU THR ARG MET THR ARG ILE SER GLU PHE LEU LYS VAL          
SEQRES  21 B  271  ALA GLU GLN VAL GLY ILE ASP ARG GLY ASP ILE                  
FORMUL   3  HOH   *444(H2 O)                                                    
HELIX    1   1 SER A    5  THR A   30  1                                  26    
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  LYS A  221  1                                  32    
HELIX   11  11 TYR A  222  MET A  225  5                                   4    
HELIX   12  12 LYS A  226  VAL A  257  1                                  32    
HELIX   13  13 ASP A  260  ILE A  264  5                                   5    
HELIX   14  14 THR B   18  THR B   30  1                                  13    
HELIX   15  15 LYS B   38  GLU B   51  1                                  14    
HELIX   16  16 ASN B   55  THR B   67  1                                  13    
HELIX   17  17 SER B   71  GLY B   89  1                                  19    
HELIX   18  18 ASN B   90  ARG B  100  1                                  11    
HELIX   19  19 GLY B  114  ALA B  142  1                                  29    
HELIX   20  20 GLY B  154  MET B  159  1                                   6    
HELIX   21  21 ASN B  160  ASP B  180  1                                  21    
HELIX   22  22 ASN B  184  LEU B  188  5                                   5    
HELIX   23  23 ASN B  190  LYS B  221  1                                  32    
HELIX   24  24 TYR B  222  MET B  225  5                                   4    
HELIX   25  25 LYS B  226  VAL B  257  1                                  32    
HELIX   26  26 ASP B  260  ILE B  264  5                                   5    
CRYST1   95.888  121.082   62.418  90.00 110.75  90.00 C 1 2 1       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      0.010429  0.000000  0.003951        0.00000                         
SCALE2      0.000000  0.008259  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017132        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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