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Database: PDB
Entry: 1H6G
LinkDB: 1H6G
Original site: 1H6G 
HEADER    CELL ADHESION                           14-JUN-01   1H6G              
TITLE     ALPHA-CATENIN M-DOMAIN                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-1 CATENIN;                                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: M-FRAGMENT, RESIDUES 377-632;                              
COMPND   5 SYNONYM: CADHERIN-ASSOCIATED PROTEIN, ALPHA E-CATENIN;               
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28M                                    
KEYWDS    ALPHA-CATENIN, ADHESION MODULATION, CYTOSKELETON, CELL ADHESION       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.YANG,P.DOKURNO,N.K.TONKS,D.BARFORD                                  
REVDAT   3   10-FEB-16 1H6G    1       HEADER KEYWDS JRNL   REMARK              
REVDAT   3 2                           VERSN  SEQADV MODRES FORMUL              
REVDAT   3 3                           HELIX  MASTER                            
REVDAT   2   24-FEB-09 1H6G    1       VERSN                                    
REVDAT   1   07-AUG-01 1H6G    0                                                
JRNL        AUTH   J.YANG,P.DOKURNO,N.K.TONKS,D.BARFORD                         
JRNL        TITL   CRYSTAL STRUCTURE OF THE M-FRAGMENT OF ALPHA-CATENIN:        
JRNL        TITL 2 IMPLICATIONS FOR MODULATION OF CELL ADHESION.                
JRNL        REF    EMBO J.                       V.  20  3645 2001              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   11447106                                                     
JRNL        DOI    10.1093/EMBOJ/20.14.3645                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.2  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.74                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 11930144.31                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 27080                          
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 SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1370                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.9                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4244                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.210                        
REMARK   3   BIN FREE R VALUE                    : 0.290                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.4                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 242                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3703                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 100                                     
REMARK   3   SOLVENT ATOMS            : 393                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.6                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.6                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.42                                                
REMARK   3    B22 (A**2) : 0.82                                                 
REMARK   3    B33 (A**2) : 5.60                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -1.23                                                
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.23                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.17                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.32                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.22                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.5                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 18.0                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.12                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.59  ; 1.50                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.53  ; 2.00                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.68  ; 2.00                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.92  ; 2.50                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.330463                                             
REMARK   3   BSOL        : 87.3308                                              
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : MPD.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : MPD.TOPOLOGY                                   
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 1H6G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JUN-01.                  
REMARK 100 THE PDBE ID CODE IS EBI-8173.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-SEP-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27803                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.25                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE, SHARP                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 49                                         
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30 % (V/V) MPD,                          
REMARK 280  0.1 M SODIUM ACETETE BUFFER, PH 4.6,                                
REMARK 280  20 MM CALCIUM CHLORIDE                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       42.85150            
REMARK 290   SMTRY3   2  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: 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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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     ILE A   632                                                      
REMARK 465     ASP B   377                                                      
REMARK 465     LEU B   378                                                      
REMARK 465     ARG B   379                                                      
REMARK 465     ARG B   380                                                      
REMARK 465     GLN B   381                                                      
REMARK 465     LEU B   382                                                      
REMARK 465     ARG B   383                                                      
REMARK 465     LYS B   384                                                      
REMARK 465     ALA B   385                                                      
REMARK 465     VAL B   386                                                      
REMARK 465     MSE B   387                                                      
REMARK 465     ASP B   388                                                      
REMARK 465     HIS B   389                                                      
REMARK 465     VAL B   390                                                      
REMARK 465     SER B   391                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU A 378    CG   CD1  CD2                                       
REMARK 470     ARG A 379    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 380    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 381    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 384    CG   CD   CE   NZ                                   
REMARK 470     VAL A 386    CG1  CG2                                            
REMARK 470     MSE A 387    CG  SE    CE                                        
REMARK 470     ASP A 388    CG   OD1  OD2                                       
REMARK 470     HIS A 389    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL A 390    CG1  CG2                                            
REMARK 470     SER A 391    OG                                                  
REMARK 470     ASP A 392    CG   OD1  OD2                                       
REMARK 470     SER A 393    OG                                                  
REMARK 470     LYS A 414    CG   CD   CE   NZ                                   
REMARK 470     ASP B 392    CG   OD1  OD2                                       
REMARK 470     LYS B 414    CG   CD   CE   NZ                                   
REMARK 470     GLU B 444    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 445    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 532    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 533    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP A   485     O    HOH A  2060              2.18            
REMARK 500   OD2  ASP A   510     O    HOH A  2083              2.10            
REMARK 500   N    GLU A   570     O    HOH A  2144              2.02            
REMARK 500   OE1  GLU B   406     O    HOH B  2007              1.97            
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    MSE A 387        8.35    -67.06                                   
REMARK 500    ASP A 392      143.88    -39.10                                   
REMARK 500    ASN A 562        0.02   -160.65                                   
REMARK 500    ASP A 601       87.62   -171.61                                   
REMARK 500    PRO A 605      170.03    -48.97                                   
REMARK 500    THR B 582      -64.88   -123.72                                   
REMARK 500    ALA B 603       88.17     52.22                                   
REMARK 500    PRO B 605      154.70    -49.70                                   
REMARK 500    MSE B 631       76.84     63.89                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1632  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2184   O                                                      
REMARK 620 2 GLU B 521   OE1  81.4                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1633                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B1632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A1631                 
DBREF  1H6G A  377   632  UNP    P35221   CTN1_HUMAN     377    632             
DBREF  1H6G B  377   632  UNP    P35221   CTN1_HUMAN     377    632             
SEQRES   1 A  256  ASP LEU ARG ARG GLN LEU ARG LYS ALA VAL MSE ASP HIS          
SEQRES   2 A  256  VAL SER ASP SER PHE LEU GLU THR ASN VAL PRO LEU LEU          
SEQRES   3 A  256  VAL LEU ILE GLU ALA ALA LYS ASN GLY ASN GLU LYS GLU          
SEQRES   4 A  256  VAL LYS GLU TYR ALA GLN VAL PHE ARG GLU HIS ALA ASN          
SEQRES   5 A  256  LYS LEU ILE GLU VAL ALA ASN LEU ALA CYS SER ILE SER          
SEQRES   6 A  256  ASN ASN GLU GLU GLY VAL LYS LEU VAL ARG MSE SER ALA          
SEQRES   7 A  256  SER GLN LEU GLU ALA LEU CYS PRO GLN VAL ILE ASN ALA          
SEQRES   8 A  256  ALA LEU ALA LEU ALA ALA LYS PRO GLN SER LYS LEU ALA          
SEQRES   9 A  256  GLN GLU ASN MSE ASP LEU PHE LYS GLU GLN TRP GLU LYS          
SEQRES  10 A  256  GLN VAL ARG VAL LEU THR ASP ALA VAL ASP ASP ILE THR          
SEQRES  11 A  256  SER ILE ASP ASP PHE LEU ALA VAL SER GLU ASN HIS ILE          
SEQRES  12 A  256  LEU GLU ASP VAL ASN LYS CYS VAL ILE ALA LEU GLN GLU          
SEQRES  13 A  256  LYS ASP VAL ASP GLY LEU ASP ARG THR ALA GLY ALA ILE          
SEQRES  14 A  256  ARG GLY ARG ALA ALA ARG VAL ILE HIS VAL VAL THR SER          
SEQRES  15 A  256  GLU MSE ASP ASN TYR GLU PRO GLY VAL TYR THR GLU LYS          
SEQRES  16 A  256  VAL LEU GLU ALA THR LYS LEU LEU SER ASN THR VAL MSE          
SEQRES  17 A  256  PRO ARG PHE THR GLU GLN VAL GLU ALA ALA VAL GLU ALA          
SEQRES  18 A  256  LEU SER SER ASP PRO ALA GLN PRO MSE ASP GLU ASN GLU          
SEQRES  19 A  256  PHE ILE ASP ALA SER ARG LEU VAL TYR ASP GLY ILE ARG          
SEQRES  20 A  256  ASP ILE ARG LYS ALA VAL LEU MSE ILE                          
SEQRES   1 B  256  ASP LEU ARG ARG GLN LEU ARG LYS ALA VAL MSE ASP HIS          
SEQRES   2 B  256  VAL SER ASP SER PHE LEU GLU THR ASN VAL PRO LEU LEU          
SEQRES   3 B  256  VAL LEU ILE GLU ALA ALA LYS ASN GLY ASN GLU LYS GLU          
SEQRES   4 B  256  VAL LYS GLU TYR ALA GLN VAL PHE ARG GLU HIS ALA ASN          
SEQRES   5 B  256  LYS LEU ILE GLU VAL ALA ASN LEU ALA CYS SER ILE SER          
SEQRES   6 B  256  ASN ASN GLU GLU GLY VAL LYS LEU VAL ARG MSE SER ALA          
SEQRES   7 B  256  SER GLN LEU GLU ALA LEU CYS PRO GLN VAL ILE ASN ALA          
SEQRES   8 B  256  ALA LEU ALA LEU ALA ALA LYS PRO GLN SER LYS LEU ALA          
SEQRES   9 B  256  GLN GLU ASN MSE ASP LEU PHE LYS GLU GLN TRP GLU LYS          
SEQRES  10 B  256  GLN VAL ARG VAL LEU THR ASP ALA VAL ASP ASP ILE THR          
SEQRES  11 B  256  SER ILE ASP ASP PHE LEU ALA VAL SER GLU ASN HIS ILE          
SEQRES  12 B  256  LEU GLU ASP VAL ASN LYS CYS VAL ILE ALA LEU GLN GLU          
SEQRES  13 B  256  LYS ASP VAL ASP GLY LEU ASP ARG THR ALA GLY ALA ILE          
SEQRES  14 B  256  ARG GLY ARG ALA ALA ARG VAL ILE HIS VAL VAL THR SER          
SEQRES  15 B  256  GLU MSE ASP ASN TYR GLU PRO GLY VAL TYR THR GLU LYS          
SEQRES  16 B  256  VAL LEU GLU ALA THR LYS LEU LEU SER ASN THR VAL MSE          
SEQRES  17 B  256  PRO ARG PHE THR GLU GLN VAL GLU ALA ALA VAL GLU ALA          
SEQRES  18 B  256  LEU SER SER ASP PRO ALA GLN PRO MSE ASP GLU ASN GLU          
SEQRES  19 B  256  PHE ILE ASP ALA SER ARG LEU VAL TYR ASP GLY ILE ARG          
SEQRES  20 B  256  ASP ILE ARG LYS ALA VAL LEU MSE ILE                          
MODRES 1H6G MSE A  387  MET  SELENOMETHIONINE                                   
MODRES 1H6G MSE A  452  MET  SELENOMETHIONINE                                   
MODRES 1H6G MSE A  484  MET  SELENOMETHIONINE                                   
MODRES 1H6G MSE A  560  MET  SELENOMETHIONINE                                   
MODRES 1H6G MSE A  584  MET  SELENOMETHIONINE                                   
MODRES 1H6G MSE A  606  MET  SELENOMETHIONINE                                   
MODRES 1H6G MSE A  631  MET  SELENOMETHIONINE                                   
MODRES 1H6G MSE B  452  MET  SELENOMETHIONINE                                   
MODRES 1H6G MSE B  484  MET  SELENOMETHIONINE                                   
MODRES 1H6G MSE B  560  MET  SELENOMETHIONINE                                   
MODRES 1H6G MSE B  584  MET  SELENOMETHIONINE                                   
MODRES 1H6G MSE B  606  MET  SELENOMETHIONINE                                   
MODRES 1H6G MSE B  631  MET  SELENOMETHIONINE                                   
HET    MSE  A 387       5                                                       
HET    MSE  A 452       8                                                       
HET    MSE  A 484       8                                                       
HET    MSE  A 560       8                                                       
HET    MSE  A 584       8                                                       
HET    MSE  A 606       8                                                       
HET    MSE  A 631       9                                                       
HET    MSE  B 452       8                                                       
HET    MSE  B 484       8                                                       
HET    MSE  B 560       8                                                       
HET    MSE  B 584       8                                                       
HET    MSE  B 606       8                                                       
HET    MSE  B 631       8                                                       
HET     CA  A1632       1                                                       
HET     CL  A1633       1                                                       
HET     CA  B1632       1                                                       
HET    MPD  A1631       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
FORMUL   1  MSE    13(C5 H11 N O2 SE)                                           
FORMUL   3   CA    2(CA 2+)                                                     
FORMUL   4   CL    CL 1-                                                        
FORMUL   6  MPD    C6 H14 O2                                                    
FORMUL   7  HOH   *393(H2 O)                                                    
HELIX    1   1 ASP A  377  MSE A  387  1                                  11    
HELIX    2   2 ASP A  388  VAL A  390  5                                   3    
HELIX    3   3 THR A  397  ASN A  410  1                                  14    
HELIX    4   4 ASN A  412  SER A  439  1                                  28    
HELIX    5   5 ASN A  443  LYS A  474  1                                  32    
HELIX    6   6 SER A  477  SER A  507  1                                  31    
HELIX    7   7 ILE A  508  GLU A  532  1                                  25    
HELIX    8   8 ASP A  534  MSE A  560  1                                  27    
HELIX    9   9 GLY A  566  THR A  582  1                                  17    
HELIX   10  10 THR A  582  SER A  599  1                                  18    
HELIX   11  11 ASP A  607  MSE A  631  1                                  25    
HELIX   12  12 THR B  397  ASN B  410  1                                  14    
HELIX   13  13 ASN B  412  ILE B  440  1                                  29    
HELIX   14  14 ASN B  443  LYS B  474  1                                  32    
HELIX   15  15 SER B  477  SER B  507  1                                  31    
HELIX   16  16 SER B  507  GLU B  532  1                                  26    
HELIX   17  17 ASP B  534  MSE B  560  1                                  27    
HELIX   18  18 ASP B  561  TYR B  563  5                                   3    
HELIX   19  19 GLY B  566  THR B  582  1                                  17    
HELIX   20  20 THR B  582  LEU B  598  1                                  17    
HELIX   21  21 ASP B  607  LEU B  630  1                                  24    
LINK         C   VAL A 386                 N   MSE A 387     1555   1555  1.33  
LINK         C   MSE A 387                 N   ASP A 388     1555   1555  1.34  
LINK         C   ARG A 451                 N   MSE A 452     1555   1555  1.32  
LINK         C   MSE A 452                 N   SER A 453     1555   1555  1.33  
LINK         C   ASN A 483                 N   MSE A 484     1555   1555  1.34  
LINK         C   MSE A 484                 N   ASP A 485     1555   1555  1.33  
LINK         C   GLU A 559                 N   MSE A 560     1555   1555  1.33  
LINK         C   MSE A 560                 N   ASP A 561     1555   1555  1.34  
LINK         C   VAL A 583                 N   MSE A 584     1555   1555  1.33  
LINK         C   MSE A 584                 N   PRO A 585     1555   1555  1.35  
LINK         C   PRO A 605                 N   MSE A 606     1555   1555  1.33  
LINK         C   MSE A 606                 N   ASP A 607     1555   1555  1.33  
LINK         C   LEU A 630                 N   MSE A 631     1555   1555  1.35  
LINK        CA    CA A1632                 O   HOH A2073     1555   1555  2.42  
LINK         C   ARG B 451                 N   MSE B 452     1555   1555  1.32  
LINK         C   MSE B 452                 N   SER B 453     1555   1555  1.33  
LINK         C   ASN B 483                 N   MSE B 484     1555   1555  1.33  
LINK         C   MSE B 484                 N   ASP B 485     1555   1555  1.34  
LINK         C   GLU B 559                 N   MSE B 560     1555   1555  1.32  
LINK         C   MSE B 560                 N   ASP B 561     1555   1555  1.34  
LINK         C   VAL B 583                 N   MSE B 584     1555   1555  1.32  
LINK         C   MSE B 584                 N   PRO B 585     1555   1555  1.35  
LINK         C   PRO B 605                 N   MSE B 606     1555   1555  1.33  
LINK         C   MSE B 606                 N   ASP B 607     1555   1555  1.32  
LINK         C   LEU B 630                 N   MSE B 631     1555   1555  1.34  
LINK         C   MSE B 631                 N   ILE B 632     1555   1555  1.33  
LINK        CA    CA B1632                 OE1 GLU B 521     1555   1555  3.28  
LINK        CA    CA B1632                 O   HOH A2184     1555   1555  2.43  
CISPEP   1 ASP A  601    PRO A  602          0         0.09                     
SITE     1 AC1  2 ASP A 500  HOH A2073                                          
SITE     1 AC2  1 HOH A2034                                                     
SITE     1 AC3  2 HOH A2184  GLU B 521                                          
SITE     1 AC4  3 VAL A 523  ASN A 524  ASN B 517                               
CRYST1   42.863   85.703   75.481  90.00 100.47  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.023330  0.000000  0.004311        0.00000                         
SCALE2      0.000000  0.011668  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013473        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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