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Database: PDB
Entry: 4ZMW
LinkDB: 4ZMW
Original site: 4ZMW 
HEADER    CELL ADHESION                           04-MAY-15   4ZMW              
TITLE     CRYSTAL STRUCTURE OF HUMAN P-CADHERIN (ENC-X-DIMER)                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CADHERIN-3;                                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 108-320;                                      
COMPND   5 SYNONYM: PLACENTAL CADHERIN,P-CADHERIN;                              
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDH3, CDHP;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: CHAMPION PET SUMO                         
KEYWDS    DIMERIZATION, CONFORMATIONAL CHANGE, CELL ADHESION                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.M.CAAVEIRO,S.KUDO,K.TSUMOTO                                       
REVDAT   4   08-NOV-23 4ZMW    1       LINK                                     
REVDAT   3   19-FEB-20 4ZMW    1       JRNL   REMARK                            
REVDAT   2   21-SEP-16 4ZMW    1       JRNL                                     
REVDAT   1   07-SEP-16 4ZMW    0                                                
JRNL        AUTH   S.KUDO,J.M.CAAVEIRO,K.TSUMOTO                                
JRNL        TITL   ADHESIVE DIMERIZATION OF HUMAN P-CADHERIN CATALYZED BY A     
JRNL        TITL 2 CHAPERONE-LIKE MECHANISM                                     
JRNL        REF    STRUCTURE                     V.  24  1523 2016              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   27545624                                                     
JRNL        DOI    10.1016/J.STR.2016.07.002                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.02                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 31831                          
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) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1798                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2111                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.11                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2660                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 98                           
REMARK   3   BIN FREE R VALUE                    : 0.2570                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3274                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 41                                      
REMARK   3   SOLVENT ATOMS            : 102                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.71000                                             
REMARK   3    B22 (A**2) : -2.43000                                             
REMARK   3    B33 (A**2) : 3.05000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.29000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.236         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.213         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.162         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.571         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.910                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.862                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3390 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3125 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4622 ; 1.592 ; 1.961       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7252 ; 0.804 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   430 ; 7.007 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   151 ;37.326 ;25.762       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   549 ;15.766 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;10.384 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   536 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3789 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   691 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1708 ; 2.569 ; 3.557       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1707 ; 2.568 ; 3.556       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2133 ; 4.062 ; 5.322       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2134 ; 4.061 ; 5.323       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1682 ; 3.278 ; 3.970       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1652 ; 2.805 ; 3.933       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2444 ; 4.471 ; 5.750       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3554 ; 6.799 ;27.894       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3522 ; 6.700 ;27.912       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4ZMW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAY-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000209556.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-NOV-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-5A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33629                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.020                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.800                              
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: 4ZMN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.15 M LITHIUM SULFATE 7.5 MM NICKEL     
REMARK 280  SULFATE 100 MM TRIS, PH 8.5, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 293K                                                    
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       47.18450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       53.40500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       47.18450            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       53.40500            
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: 2700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -141.0 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 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     0                                                      
REMARK 465     MET B     0                                                      
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    TRP A   2       66.49   -101.01                                   
REMARK 500    ASN A  12       48.70     38.74                                   
REMARK 500    ALA A  43      -76.98   -102.48                                   
REMARK 500    LYS A 156       46.93    -96.38                                   
REMARK 500    ASP A 180      103.68   -173.34                                   
REMARK 500    ALA B  43      -79.70   -106.52                                   
REMARK 500    LYS B 156       31.06    -97.05                                   
REMARK 500    HIS B 159     -169.88   -125.30                                   
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 A 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  11   OE2                                                    
REMARK 620 2 GLU A  69   OE1  83.3                                              
REMARK 620 3 GLU A  69   OE2 106.8  50.2                                        
REMARK 620 4 ASP A 100   OD1  83.6 117.9  77.0                                  
REMARK 620 5 GLN A 101   O    80.4 147.2 162.6  88.4                            
REMARK 620 6 ASP A 103   OD1  90.9  78.3 121.1 161.9  73.7                      
REMARK 620 7 ASP A 136   OD1 165.6  97.7  84.4 108.1  91.5  75.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 302  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 102   OD1                                                    
REMARK 620 2 HIS A 104   O    95.8                                              
REMARK 620 3 ASP A 134   OD1 157.1  86.6                                        
REMARK 620 4 ASP A 134   OD2 148.5  96.6  52.7                                  
REMARK 620 5 ASP A 136   OD2  73.2  80.6 129.5  80.4                            
REMARK 620 6 ASN A 143   O    84.9 176.2  91.4  84.7 103.1                      
REMARK 620 7 ASP A 195   OD2  79.6  79.6  78.4 131.2 144.3  96.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI A 305  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 104   NE2                                                    
REMARK 620 2 SO4 A 303   S   149.0                                              
REMARK 620 3 SO4 A 303   O1  111.5  40.3                                        
REMARK 620 4 SO4 A 303   O4  144.5  39.5  76.1                                  
REMARK 620 5 SO4 A 304   S    82.6 122.0 125.1 122.6                            
REMARK 620 6 SO4 A 304   O3   93.0  98.5  90.3 122.1  34.9                      
REMARK 620 7 SO4 A 304   O4   73.6 137.3 159.2 112.0  34.2  69.1                
REMARK 620 8 HOH A 403   O    83.2 100.6 120.2  64.4 114.0 148.6  80.0          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  11   OE2                                                    
REMARK 620 2 GLU B  69   OE1  86.1                                              
REMARK 620 3 GLU B  69   OE2 113.4  48.8                                        
REMARK 620 4 ASP B 100   OD1  85.0 118.9  81.1                                  
REMARK 620 5 GLN B 101   O    85.3 151.1 157.0  87.7                            
REMARK 620 6 ASP B 103   OD1  90.5  78.3 116.8 161.7  74.2                      
REMARK 620 7 ASP B 136   OD1 160.9  96.3  81.6 110.0  83.5  71.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 302  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 102   OD1                                                    
REMARK 620 2 HIS B 104   O    97.8                                              
REMARK 620 3 ASP B 134   OD1 151.0  95.4                                        
REMARK 620 4 ASP B 134   OD2 151.0  96.8  50.6                                  
REMARK 620 5 ASP B 136   OD2  77.6  76.5 130.8  81.8                            
REMARK 620 6 ASN B 143   O    82.0 177.5  85.9  82.3 101.0                      
REMARK 620 7 ASP B 195   OD2  76.9  81.2  79.8 130.2 143.2 101.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B 308  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 104   NE2                                                    
REMARK 620 2 SO4 B 306   S    88.2                                              
REMARK 620 3 SO4 B 306   O1   98.2  33.8                                        
REMARK 620 4 SO4 B 306   O2   85.5  33.1  66.4                                  
REMARK 620 5 SO4 B 307   S   129.8 132.7 104.4 144.7                            
REMARK 620 6 SO4 B 307   O1   93.9 169.5 135.8 157.4  40.5                      
REMARK 620 7 SO4 B 307   O3  165.6 106.2  94.2 106.2  38.7  72.0                
REMARK 620 8 SO4 B 307   O4  117.0 109.5  76.2 139.0  33.8  60.4  59.2          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NI A 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NI B 308                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ZML   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZMN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZMO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZMP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZMQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZMT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZMV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZMX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZMY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZMZ   RELATED DB: PDB                                   
DBREF  4ZMW A    1   213  UNP    P22223   CADH3_HUMAN    108    320             
DBREF  4ZMW B    1   213  UNP    P22223   CADH3_HUMAN    108    320             
SEQADV 4ZMW MET A    0  UNP  P22223              INITIATING METHIONINE          
SEQADV 4ZMW VAL A   22  UNP  P22223    ASN   129 ENGINEERED MUTATION            
SEQADV 4ZMW MET B    0  UNP  P22223              INITIATING METHIONINE          
SEQADV 4ZMW VAL B   22  UNP  P22223    ASN   129 ENGINEERED MUTATION            
SEQRES   1 A  214  MET ASP TRP VAL VAL ALA PRO ILE SER VAL PRO GLU ASN          
SEQRES   2 A  214  GLY LYS GLY PRO PHE PRO GLN ARG LEU VAL GLN LEU LYS          
SEQRES   3 A  214  SER ASN LYS ASP ARG ASP THR LYS ILE PHE TYR SER ILE          
SEQRES   4 A  214  THR GLY PRO GLY ALA ASP SER PRO PRO GLU GLY VAL PHE          
SEQRES   5 A  214  ALA VAL GLU LYS GLU THR GLY TRP LEU LEU LEU ASN LYS          
SEQRES   6 A  214  PRO LEU ASP ARG GLU GLU ILE ALA LYS TYR GLU LEU PHE          
SEQRES   7 A  214  GLY HIS ALA VAL SER GLU ASN GLY ALA SER VAL GLU ASP          
SEQRES   8 A  214  PRO MET ASN ILE SER ILE ILE VAL THR ASP GLN ASN ASP          
SEQRES   9 A  214  HIS LYS PRO LYS PHE THR GLN ASP THR PHE ARG GLY SER          
SEQRES  10 A  214  VAL LEU GLU GLY VAL LEU PRO GLY THR SER VAL MET GLN          
SEQRES  11 A  214  VAL THR ALA THR ASP GLU ASP ASP ALA ILE TYR THR TYR          
SEQRES  12 A  214  ASN GLY VAL VAL ALA TYR SER ILE HIS SER GLN GLU PRO          
SEQRES  13 A  214  LYS ASP PRO HIS ASP LEU MET PHE THR ILE HIS ARG SER          
SEQRES  14 A  214  THR GLY THR ILE SER VAL ILE SER SER GLY LEU ASP ARG          
SEQRES  15 A  214  GLU LYS VAL PRO GLU TYR THR LEU THR ILE GLN ALA THR          
SEQRES  16 A  214  ASP MET ASP GLY ASP GLY SER THR THR THR ALA VAL ALA          
SEQRES  17 A  214  VAL VAL GLU ILE LEU ASP                                      
SEQRES   1 B  214  MET ASP TRP VAL VAL ALA PRO ILE SER VAL PRO GLU ASN          
SEQRES   2 B  214  GLY LYS GLY PRO PHE PRO GLN ARG LEU VAL GLN LEU LYS          
SEQRES   3 B  214  SER ASN LYS ASP ARG ASP THR LYS ILE PHE TYR SER ILE          
SEQRES   4 B  214  THR GLY PRO GLY ALA ASP SER PRO PRO GLU GLY VAL PHE          
SEQRES   5 B  214  ALA VAL GLU LYS GLU THR GLY TRP LEU LEU LEU ASN LYS          
SEQRES   6 B  214  PRO LEU ASP ARG GLU GLU ILE ALA LYS TYR GLU LEU PHE          
SEQRES   7 B  214  GLY HIS ALA VAL SER GLU ASN GLY ALA SER VAL GLU ASP          
SEQRES   8 B  214  PRO MET ASN ILE SER ILE ILE VAL THR ASP GLN ASN ASP          
SEQRES   9 B  214  HIS LYS PRO LYS PHE THR GLN ASP THR PHE ARG GLY SER          
SEQRES  10 B  214  VAL LEU GLU GLY VAL LEU PRO GLY THR SER VAL MET GLN          
SEQRES  11 B  214  VAL THR ALA THR ASP GLU ASP ASP ALA ILE TYR THR TYR          
SEQRES  12 B  214  ASN GLY VAL VAL ALA TYR SER ILE HIS SER GLN GLU PRO          
SEQRES  13 B  214  LYS ASP PRO HIS ASP LEU MET PHE THR ILE HIS ARG SER          
SEQRES  14 B  214  THR GLY THR ILE SER VAL ILE SER SER GLY LEU ASP ARG          
SEQRES  15 B  214  GLU LYS VAL PRO GLU TYR THR LEU THR ILE GLN ALA THR          
SEQRES  16 B  214  ASP MET ASP GLY ASP GLY SER THR THR THR ALA VAL ALA          
SEQRES  17 B  214  VAL VAL GLU ILE LEU ASP                                      
HET     CA  A 301       1                                                       
HET     CA  A 302       1                                                       
HET    SO4  A 303       5                                                       
HET    SO4  A 304       5                                                       
HET     NI  A 305       1                                                       
HET     CA  B 301       1                                                       
HET     CA  B 302       1                                                       
HET    SO4  B 303       5                                                       
HET    SO4  B 304       5                                                       
HET    SO4  B 305       5                                                       
HET    SO4  B 306       5                                                       
HET    SO4  B 307       5                                                       
HET     NI  B 308       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM      NI NICKEL (II) ION                                                  
FORMUL   3   CA    4(CA 2+)                                                     
FORMUL   5  SO4    7(O4 S 2-)                                                   
FORMUL   7   NI    2(NI 2+)                                                     
FORMUL  16  HOH   *102(H2 O)                                                    
HELIX    1 AA1 SER A   26  ASP A   31  5                                   6    
HELIX    2 AA2 MET A  196  ASP A  199  5                                   4    
HELIX    3 AA3 SER B   26  ASP B   31  5                                   6    
HELIX    4 AA4 MET B  196  ASP B  199  5                                   4    
SHEET    1 AA1 4 ILE A   7  PRO A  10  0                                        
SHEET    2 AA1 4 MET A  92  THR A  99  1  O  ILE A  97   N  ILE A   7           
SHEET    3 AA1 4 LYS A  73  SER A  82 -1  N  GLY A  78   O  MET A  92           
SHEET    4 AA1 4 ILE A  34  THR A  39 -1  N  PHE A  35   O  VAL A  81           
SHEET    1 AA2 3 GLN A  19  GLN A  23  0                                        
SHEET    2 AA2 3 TRP A  59  LEU A  62 -1  O  LEU A  60   N  VAL A  22           
SHEET    3 AA2 3 PHE A  51  VAL A  53 -1  N  ALA A  52   O  LEU A  61           
SHEET    1 AA3 2 LYS A 107  PHE A 108  0                                        
SHEET    2 AA3 2 ALA A 132  THR A 133 -1  O  THR A 133   N  LYS A 107           
SHEET    1 AA4 4 THR A 112  LEU A 118  0                                        
SHEET    2 AA4 4 THR A 202  LEU A 212  1  O  LEU A 212   N  VAL A 117           
SHEET    3 AA4 4 GLU A 186  THR A 194 -1  N  LEU A 189   O  ALA A 207           
SHEET    4 AA4 4 ALA A 147  GLU A 154 -1  N  SER A 152   O  THR A 190           
SHEET    1 AA5 3 SER A 126  GLN A 129  0                                        
SHEET    2 AA5 3 THR A 171  VAL A 174 -1  O  ILE A 172   N  MET A 128           
SHEET    3 AA5 3 PHE A 163  ILE A 165 -1  N  THR A 164   O  SER A 173           
SHEET    1 AA6 4 ILE B   7  PRO B  10  0                                        
SHEET    2 AA6 4 MET B  92  THR B  99  1  O  ILE B  97   N  ILE B   7           
SHEET    3 AA6 4 LYS B  73  SER B  82 -1  N  LEU B  76   O  ILE B  94           
SHEET    4 AA6 4 ILE B  34  THR B  39 -1  N  SER B  37   O  HIS B  79           
SHEET    1 AA7 3 GLN B  19  GLN B  23  0                                        
SHEET    2 AA7 3 TRP B  59  LEU B  62 -1  O  LEU B  60   N  VAL B  22           
SHEET    3 AA7 3 PHE B  51  VAL B  53 -1  N  ALA B  52   O  LEU B  61           
SHEET    1 AA8 2 LYS B 107  PHE B 108  0                                        
SHEET    2 AA8 2 ALA B 132  THR B 133 -1  O  THR B 133   N  LYS B 107           
SHEET    1 AA9 4 THR B 112  LEU B 118  0                                        
SHEET    2 AA9 4 THR B 202  LEU B 212  1  O  GLU B 210   N  GLY B 115           
SHEET    3 AA9 4 GLU B 186  THR B 194 -1  N  LEU B 189   O  ALA B 207           
SHEET    4 AA9 4 ALA B 147  GLU B 154 -1  N  SER B 152   O  THR B 190           
SHEET    1 AB1 3 SER B 126  GLN B 129  0                                        
SHEET    2 AB1 3 THR B 171  VAL B 174 -1  O  ILE B 172   N  VAL B 127           
SHEET    3 AB1 3 PHE B 163  ILE B 165 -1  N  THR B 164   O  SER B 173           
LINK         OE2 GLU A  11                CA    CA A 301     1555   1555  2.31  
LINK         OE1 GLU A  69                CA    CA A 301     1555   1555  2.73  
LINK         OE2 GLU A  69                CA    CA A 301     1555   1555  2.33  
LINK         OD1 ASP A 100                CA    CA A 301     1555   1555  2.30  
LINK         O   GLN A 101                CA    CA A 301     1555   1555  2.39  
LINK         OD1 ASN A 102                CA    CA A 302     1555   1555  2.23  
LINK         OD1 ASP A 103                CA    CA A 301     1555   1555  2.32  
LINK         O   HIS A 104                CA    CA A 302     1555   1555  2.24  
LINK         NE2 HIS A 104                NI    NI A 305     1555   1555  2.19  
LINK         OD1 ASP A 134                CA    CA A 302     1555   1555  2.49  
LINK         OD2 ASP A 134                CA    CA A 302     1555   1555  2.36  
LINK         OD1 ASP A 136                CA    CA A 301     1555   1555  2.42  
LINK         OD2 ASP A 136                CA    CA A 302     1555   1555  2.30  
LINK         O   ASN A 143                CA    CA A 302     1555   1555  2.36  
LINK         OD2 ASP A 195                CA    CA A 302     1555   1555  2.22  
LINK         S   SO4 A 303                NI    NI A 305     1555   1555  2.30  
LINK         O1  SO4 A 303                NI    NI A 305     1555   1555  1.87  
LINK         O4  SO4 A 303                NI    NI A 305     1555   1555  2.02  
LINK         S   SO4 A 304                NI    NI A 305     1555   1555  2.63  
LINK         O3  SO4 A 304                NI    NI A 305     1555   1555  2.43  
LINK         O4  SO4 A 304                NI    NI A 305     1555   1555  1.85  
LINK        NI    NI A 305                 O   HOH A 403     1555   1555  2.61  
LINK         OE2 GLU B  11                CA    CA B 301     1555   1555  2.25  
LINK         OE1 GLU B  69                CA    CA B 301     1555   1555  2.77  
LINK         OE2 GLU B  69                CA    CA B 301     1555   1555  2.35  
LINK         OD1 ASP B 100                CA    CA B 301     1555   1555  2.27  
LINK         O   GLN B 101                CA    CA B 301     1555   1555  2.43  
LINK         OD1 ASN B 102                CA    CA B 302     1555   1555  2.22  
LINK         OD1 ASP B 103                CA    CA B 301     1555   1555  2.31  
LINK         O   HIS B 104                CA    CA B 302     1555   1555  2.28  
LINK         NE2 HIS B 104                NI    NI B 308     1555   1555  2.12  
LINK         OD1 ASP B 134                CA    CA B 302     1555   1555  2.60  
LINK         OD2 ASP B 134                CA    CA B 302     1555   1555  2.63  
LINK         OD1 ASP B 136                CA    CA B 301     1555   1555  2.25  
LINK         OD2 ASP B 136                CA    CA B 302     1555   1555  2.49  
LINK         O   ASN B 143                CA    CA B 302     1555   1555  2.29  
LINK         OD2 ASP B 195                CA    CA B 302     1555   1555  2.33  
LINK         S   SO4 B 306                NI    NI B 308     1555   1555  2.66  
LINK         O1  SO4 B 306                NI    NI B 308     1555   1555  2.49  
LINK         O2  SO4 B 306                NI    NI B 308     1555   1555  1.87  
LINK         S   SO4 B 307                NI    NI B 308     1555   1555  2.27  
LINK         O1  SO4 B 307                NI    NI B 308     1555   1555  1.98  
LINK         O3  SO4 B 307                NI    NI B 308     1555   1555  2.22  
LINK         O4  SO4 B 307                NI    NI B 308     1555   1555  2.65  
CISPEP   1 GLY A   15    PRO A   16          0        11.58                     
CISPEP   2 PHE A   17    PRO A   18          0         5.20                     
CISPEP   3 PRO A   46    PRO A   47          0        -4.34                     
CISPEP   4 GLU A  154    PRO A  155          0        -5.36                     
CISPEP   5 ASP A  157    PRO A  158          0         6.72                     
CISPEP   6 GLY B   15    PRO B   16          0        10.91                     
CISPEP   7 PHE B   17    PRO B   18          0         3.88                     
CISPEP   8 PRO B   46    PRO B   47          0        -5.15                     
CISPEP   9 GLU B  154    PRO B  155          0       -15.02                     
CISPEP  10 ASP B  157    PRO B  158          0         6.29                     
SITE     1 AC1  6 GLU A  11  GLU A  69  ASP A 100  GLN A 101                    
SITE     2 AC1  6 ASP A 103  ASP A 136                                          
SITE     1 AC2  6 ASN A 102  HIS A 104  ASP A 134  ASP A 136                    
SITE     2 AC2  6 ASN A 143  ASP A 195                                          
SITE     1 AC3  6 ASP A  67  GLU A  69  HIS A 104  SO4 A 304                    
SITE     2 AC3  6  NI A 305  HOH A 403                                          
SITE     1 AC4  6 ASP A  67  ASP A 103  HIS A 104  SO4 A 303                    
SITE     2 AC4  6  NI A 305  HOH A 403                                          
SITE     1 AC5  4 HIS A 104  SO4 A 303  SO4 A 304  HOH A 403                    
SITE     1 AC6  6 GLU B  11  GLU B  69  ASP B 100  GLN B 101                    
SITE     2 AC6  6 ASP B 103  ASP B 136                                          
SITE     1 AC7  6 ASN B 102  HIS B 104  ASP B 134  ASP B 136                    
SITE     2 AC7  6 ASN B 143  ASP B 195                                          
SITE     1 AC8  7 ARG A  68  GLU A 135  HOH A 401  GLN B 110                    
SITE     2 AC8  7 PHE B 113  ARG B 114  HOH B 427                               
SITE     1 AC9  2 ARG A 181  ARG B  20                                          
SITE     1 AD1  4 THR B  32  SER B  82  ASN B  84  ALA B  86                    
SITE     1 AD2  5 ASP B  67  ASP B 103  HIS B 104  SO4 B 307                    
SITE     2 AD2  5  NI B 308                                                     
SITE     1 AD3  5 ASP B  67  HIS B 104  GLU B 135  SO4 B 306                    
SITE     2 AD3  5  NI B 308                                                     
SITE     1 AD4  3 HIS B 104  SO4 B 306  SO4 B 307                               
CRYST1   94.369  106.810   77.579  90.00  94.86  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      0.010597  0.000000  0.000901        0.00000                         
SCALE2      0.000000  0.009362  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012937        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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