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Database: PDB
Entry: 1HG2
LinkDB: 1HG2
Original site: 1HG2 
HEADER    ENDOCYTOSIS                             12-DEC-00   1HG2              
TITLE     CALM-N N-TERMINAL DOMAIN OF CLATHRIN ASSEMBLY LYMPHOID MYELOID        
TITLE    2 LEUKAEMIA PROTEIN, INOSITOL(4,5)P2 COMPLEX                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CLATHRIN ASSEMBLY PROTEIN SHORT FORM;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN RESIDUES 1-289;                          
COMPND   5 SYNONYM: CALM-N, AP180-2;                                            
COMPND   6 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_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX4T2;                                  
SOURCE  10 EXPRESSION_SYSTEM_GENE: CALM-N                                       
KEYWDS    ENDOCYTOSIS, ADAPTOR                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.G.J.FORD,P.R.EVANS,H.T.MCMAHON                                      
REVDAT   3   09-OCT-19 1HG2    1       REMARK                                   
REVDAT   2   24-FEB-09 1HG2    1       VERSN                                    
REVDAT   1   12-FEB-01 1HG2    0                                                
JRNL        AUTH   M.G.J.FORD,B.M.F.PEARSE,M.K.HIGGINS,Y.VALLIS,D.J.OWEN,       
JRNL        AUTH 2 A.GIBSON,C.R.HOPKINS,P.R.EVANS,H.T.MCMAHON                   
JRNL        TITL   SIMULTANEOUS BINDING OF PTDINS(4,5)P2 AND CLATHRIN BY AP180  
JRNL        TITL 2 IN THE NUCLEATION OF CLATHRIN LATTICES ON MEMBRANES          
JRNL        REF    SCIENCE                       V. 291  1051 2001              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   11161218                                                     
JRNL        DOI    10.1126/SCIENCE.291.5506.1051                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 65.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 24532                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1315                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2114                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 128                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.59000                                              
REMARK   3    B22 (A**2) : 1.59000                                              
REMARK   3    B33 (A**2) : -3.18000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.154         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.135         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.188         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.970         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.033 ; 0.022               
REMARK   3    ANGLE DISTANCE                  (A) : 2.460 ; 1.950               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.011 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.160 ; 0.200               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.600 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.900 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.200 ; 3.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.600 ; 4.500                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS SCALING DETAILS BABINET"S PRINCIPLE FOR SCALING HAS       
REMARK   3  BEEN USED BULK SOLVENT CORRECTION BASED ON CONSTANT VALUE HAS       
REMARK   3  BEEN U PARAMETERS FOR MASK CALCULATION VDW PROB RADII = 1.40 ION    
REMARK   3  PROB RADII = 0.80 SHRINKAGE RADII = 0.80                            
REMARK   4                                                                      
REMARK   4 1HG2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-DEC-00.                  
REMARK 100 THE DEPOSITION ID IS D_1290005668.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-APR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 293.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87                               
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25871                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 6.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.12600                            
REMARK 200  R SYM                      (I) : 0.12600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.95800                            
REMARK 200  R SYM FOR SHELL            (I) : 1.95800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 1HF8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, PH 7.5, 12% PEG 8K, 8%       
REMARK 280  ETHYLENE GLYCOL CRYSTALS SOAKED IN 1MM LIGAND FOR 1 HOUR, PH        
REMARK 280  7.50, VAPOR DIFFUSION, HANGING DROP                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       61.16650            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       38.92950            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       38.92950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       30.58325            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       38.92950            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       38.92950            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       91.74975            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       38.92950            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       38.92950            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       30.58325            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       38.92950            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       38.92950            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       91.74975            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       61.16650            
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: PQS                                                   
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   BIOMT1   2  0.000000 -1.000000  0.000000       77.85900            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000       77.85900            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       61.16650            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     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     LEU A   282                                                      
REMARK 465     ALA A   283                                                      
REMARK 465     SER A   284                                                      
REMARK 465     LEU A   285                                                      
REMARK 465     GLU A   286                                                      
REMARK 465     GLY A   287                                                      
REMARK 465     LYS A   288                                                      
REMARK 465     LYS A   289                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  2044     O    HOH A  2044     7556     2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    MET A  86   SD    MET A  86   CE     -0.617                       
REMARK 500    MET A 156   SD    MET A 156   CE     -0.410                       
REMARK 500    MET A 175   SD    MET A 175   CE     -0.440                       
REMARK 500    MET A 198   SD    MET A 198   CE     -0.365                       
REMARK 500    TYR A 211   CD1   TYR A 211   CE1     0.099                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 144   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    MET A 175   CG  -  SD  -  CE  ANGL. DEV. = -12.5 DEGREES          
REMARK 500    TYR A 211   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    TYR A 211   CB  -  CG  -  CD1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ASP A 224   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A 235   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG A 261   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ALA A 270   N   -  CA  -  C   ANGL. DEV. =  16.7 DEGREES          
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    LEU A 103     -120.06   -124.78                                   
REMARK 500    THR A 158       68.74   -110.62                                   
REMARK 500    ASN A 160      158.96    -46.42                                   
REMARK 500    LEU A 218      -77.21    -49.37                                   
REMARK 500    LYS A 226      152.80    -45.62                                   
REMARK 500    CYS A 230      -36.14    -38.46                                   
REMARK 500    ALA A 270       23.49     80.41                                   
REMARK 500    SER A 273       20.73    -58.96                                   
REMARK 500    LEU A 274       -7.41    -56.43                                   
REMARK 500    LEU A 275       59.40    -95.02                                   
REMARK 500    GLU A 279        4.27    -68.03                                   
REMARK 500    GLN A 280       61.57   -101.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IP2 A1282                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
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: 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                   
DBREF  1HG2 A    1   289  UNP    O55011   O55011           1    289             
SEQRES   1 A  289  MET SER GLY GLN SER LEU THR ASP ARG ILE THR ALA ALA          
SEQRES   2 A  289  GLN HIS SER VAL THR GLY SER ALA VAL SER LYS THR VAL          
SEQRES   3 A  289  CYS LYS ALA THR THR HIS GLU ILE MET GLY PRO LYS LYS          
SEQRES   4 A  289  LYS HIS LEU ASP TYR LEU ILE GLN CYS THR ASN GLU MET          
SEQRES   5 A  289  ASN VAL ASN ILE PRO GLN LEU ALA ASP SER LEU PHE GLU          
SEQRES   6 A  289  ARG THR THR ASN SER SER TRP VAL VAL VAL PHE LYS SER          
SEQRES   7 A  289  LEU ILE THR THR HIS HIS LEU MET VAL TYR GLY ASN GLU          
SEQRES   8 A  289  ARG PHE ILE GLN TYR LEU ALA SER ARG ASN THR LEU PHE          
SEQRES   9 A  289  ASN LEU SER ASN PHE LEU ASP LYS SER GLY LEU GLN GLY          
SEQRES  10 A  289  TYR ASP MET SER THR PHE ILE ARG ARG TYR SER ARG TYR          
SEQRES  11 A  289  LEU ASN GLU LYS ALA VAL SER TYR ARG GLN VAL ALA PHE          
SEQRES  12 A  289  ASP PHE THR LYS VAL LYS ARG GLY ALA ASP GLY VAL MET          
SEQRES  13 A  289  ARG THR MET ASN THR GLU LYS LEU LEU LYS THR VAL PRO          
SEQRES  14 A  289  ILE ILE GLN ASN GLN MET ASP ALA LEU LEU ASP PHE ASN          
SEQRES  15 A  289  VAL ASN SER ASN GLU LEU THR ASN GLY VAL ILE ASN ALA          
SEQRES  16 A  289  ALA PHE MET LEU LEU PHE LYS ASP ALA ILE ARG LEU PHE          
SEQRES  17 A  289  ALA ALA TYR ASN GLU GLY ILE ILE ASN LEU LEU GLU LYS          
SEQRES  18 A  289  TYR PHE ASP MET LYS LYS ASN GLN CYS LYS GLU GLY LEU          
SEQRES  19 A  289  ASP ILE TYR LYS LYS PHE LEU THR ARG MET THR ARG ILE          
SEQRES  20 A  289  SER GLU PHE LEU LYS VAL ALA GLU GLN VAL GLY ILE ASP          
SEQRES  21 A  289  ARG GLY ASP ILE PRO ASP LEU SER GLN ALA PRO SER SER          
SEQRES  22 A  289  LEU LEU ASP ALA LEU GLU GLN HIS LEU ALA SER LEU GLU          
SEQRES  23 A  289  GLY LYS LYS                                                  
HET    IP2  A1282      40                                                       
HETNAM     IP2 D-MYO-INOSITOL-4,5-BISPHOSPHATE                                  
FORMUL   2  IP2    C6 H14 O12 P2                                                
FORMUL   3  HOH   *128(H2 O)                                                    
HELIX    1   1 GLY A   19  THR A   30  1                                  12    
HELIX    2   2 LYS A   38  ASN A   50  1                                  13    
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 GLU A   91  ARG A  100  1                                  10    
HELIX    6   6 GLY A  114  ALA A  142  1                                  29    
HELIX    7   7 ASN A  160  ASP A  180  1                                  21    
HELIX    8   8 ASN A  184  LEU A  188  5                                   5    
HELIX    9   9 ASN A  190  PHE A  223  1                                  34    
HELIX   10  10 LYS A  226  GLY A  258  1                                  33    
HELIX   11  11 ASP A  260  ILE A  264  5                                   5    
SITE     1 AC1  3 LYS A  38  LYS A  40  HIS A  41                               
CRYST1   77.859   77.859  122.333  90.00  90.00  90.00 P 41 21 2     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      0.012844  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012844  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008174        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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