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Database: PDB
Entry: 2VKW
LinkDB: 2VKW
Original site: 2VKW 
HEADER    CELL ADHESION                           04-JAN-08   2VKW              
TITLE     HUMAN NCAM, FN3 DOMAINS 1 AND 2                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEURAL CELL ADHESION MOLECULE 1,140 KDA ISOFORM;           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: FN3 DOMAINS, RESIDUES 496-598,601-692;                     
COMPND   5 SYNONYM: N-CAM 140, NCAM-140, CD56 ANTIGEN, NEURAL CELL ADHESION     
COMPND   6 MOLECULE;                                                            
COMPND   7 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: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: 293-EBNA;                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PCEP-PU                                    
KEYWDS    ADHESION RECEPTOR, CELL ADHESION                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.CARAFOLI,J.L.SAFFELL,E.HOHENESTER                                   
REVDAT   4   08-NOV-17 2VKW    1       SOURCE                                   
REVDAT   3   24-FEB-09 2VKW    1       VERSN                                    
REVDAT   2   18-MAR-08 2VKW    1       JRNL                                     
REVDAT   1   26-FEB-08 2VKW    0                                                
JRNL        AUTH   F.CARAFOLI,J.L.SAFFELL,E.HOHENESTER                          
JRNL        TITL   STRUCTURE OF THE TANDEM FIBRONECTIN TYPE 3 DOMAINS OF NEURAL 
JRNL        TITL 2 CELL ADHESION MOLECULE                                       
JRNL        REF    J.MOL.BIOL.                   V. 377   524 2008              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   18261743                                                     
JRNL        DOI    10.1016/J.JMB.2008.01.030                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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 : MAXIMUM LIKELIHOOD                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000.000                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 16920                          
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) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1691                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3058                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 25                                      
REMARK   3   SOLVENT ATOMS            : 98                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.76900                                              
REMARK   3    B22 (A**2) : -0.08400                                             
REMARK   3    B33 (A**2) : -1.68400                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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) : 1.330 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.250 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.100 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.320 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : 0.45                                                 
REMARK   3   BSOL        : 38.39                                                
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2VKW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-JAN-08.                  
REMARK 100 THE DEPOSITION ID IS D_1290034906.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-FEB-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.2                                
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) : 1.49                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16957                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.7000                            
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.12000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 11.10                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: AUTOSHARP                                             
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.2                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.38500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.10850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.67300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.10850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.38500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.67300            
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: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 3310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.8 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     ALA A   492                                                      
REMARK 465     PRO A   493                                                      
REMARK 465     LEU A   494                                                      
REMARK 465     ALA A   495                                                      
REMARK 465     ALA A   694                                                      
REMARK 465     HIS A   695                                                      
REMARK 465     HIS A   696                                                      
REMARK 465     HIS A   697                                                      
REMARK 465     HIS A   698                                                      
REMARK 465     HIS A   699                                                      
REMARK 465     HIS A   700                                                      
REMARK 465     ALA B   492                                                      
REMARK 465     PRO B   493                                                      
REMARK 465     LEU B   494                                                      
REMARK 465     ALA B   495                                                      
REMARK 465     GLN B   496                                                      
REMARK 465     ALA B   693                                                      
REMARK 465     ALA B   694                                                      
REMARK 465     HIS B   695                                                      
REMARK 465     HIS B   696                                                      
REMARK 465     HIS B   697                                                      
REMARK 465     HIS B   698                                                      
REMARK 465     HIS B   699                                                      
REMARK 465     HIS B   700                                                      
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     ALA A 693    CA   C    O    CB                                   
REMARK 470     ALA B 692    CA   C    O    CB                                   
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    TYR A 511     -150.99   -121.51                                   
REMARK 500    ARG A 599     -158.65   -152.73                                   
REMARK 500    TYR B 511     -148.41   -119.32                                   
REMARK 500    ASN B 615       49.70    -93.48                                   
REMARK 500    HIS B 633      164.94    177.65                                   
REMARK 500    SER B 643     -165.73   -125.02                                   
REMARK 500    ASN B 677     -168.39   -123.25                                   
REMARK 500    THR B 691     -174.35    -66.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1692                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1693                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1693                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1694                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1695                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VKX   RELATED DB: PDB                                   
REMARK 900 HUMAN NCAM, FN3 DOMAINS 1 AND 2, M610R MUTANT                        
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 N-TERMINAL APLA AND C-TERMINAL AAAHHHHHH ARE VECTOR-                 
REMARK 999 DERIVED. QG (POSITIONS 599-600) OF P13591 REPLACED BY R (            
REMARK 999 NATURAL MUSCLE- AND BRAIN-SPECIFIC SPLICE VARIANT)                   
DBREF  2VKW A  492   495  PDB    2VKW     2VKW           492    495             
DBREF  2VKW A  496   598  UNP    P13591   NCA11_HUMAN    496    598             
DBREF  2VKW A  599   599  PDB    2VKW     2VKW           599    599             
DBREF  2VKW A  600   691  UNP    P13591   NCA11_HUMAN    601    692             
DBREF  2VKW A  692   700  PDB    2VKW     2VKW           692    700             
DBREF  2VKW B  492   495  PDB    2VKW     2VKW           492    495             
DBREF  2VKW B  496   598  UNP    P13591   NCA11_HUMAN    496    598             
DBREF  2VKW B  599   599  PDB    2VKW     2VKW           599    599             
DBREF  2VKW B  600   691  UNP    P13591   NCA11_HUMAN    601    692             
DBREF  2VKW B  692   700  PDB    2VKW     2VKW           692    700             
SEQRES   1 A  209  ALA PRO LEU ALA GLN ALA ASP THR PRO SER SER PRO SER          
SEQRES   2 A  209  ILE ASP GLN VAL GLU PRO TYR SER SER THR ALA GLN VAL          
SEQRES   3 A  209  GLN PHE ASP GLU PRO GLU ALA THR GLY GLY VAL PRO ILE          
SEQRES   4 A  209  LEU LYS TYR LYS ALA GLU TRP ARG ALA VAL GLY GLU GLU          
SEQRES   5 A  209  VAL TRP HIS SER LYS TRP TYR ASP ALA LYS GLU ALA SER          
SEQRES   6 A  209  MET GLU GLY ILE VAL THR ILE VAL GLY LEU LYS PRO GLU          
SEQRES   7 A  209  THR THR TYR ALA VAL ARG LEU ALA ALA LEU ASN GLY LYS          
SEQRES   8 A  209  GLY LEU GLY GLU ILE SER ALA ALA SER GLU PHE LYS THR          
SEQRES   9 A  209  GLN PRO VAL ARG GLU PRO SER ALA PRO LYS LEU GLU GLY          
SEQRES  10 A  209  GLN MET GLY GLU ASP GLY ASN SER ILE LYS VAL ASN LEU          
SEQRES  11 A  209  ILE LYS GLN ASP ASP GLY GLY SER PRO ILE ARG HIS TYR          
SEQRES  12 A  209  LEU VAL ARG TYR ARG ALA LEU SER SER GLU TRP LYS PRO          
SEQRES  13 A  209  GLU ILE ARG LEU PRO SER GLY SER ASP HIS VAL MET LEU          
SEQRES  14 A  209  LYS SER LEU ASP TRP ASN ALA GLU TYR GLU VAL TYR VAL          
SEQRES  15 A  209  VAL ALA GLU ASN GLN GLN GLY LYS SER LYS ALA ALA HIS          
SEQRES  16 A  209  PHE VAL PHE ARG THR ALA ALA ALA HIS HIS HIS HIS HIS          
SEQRES  17 A  209  HIS                                                          
SEQRES   1 B  209  ALA PRO LEU ALA GLN ALA ASP THR PRO SER SER PRO SER          
SEQRES   2 B  209  ILE ASP GLN VAL GLU PRO TYR SER SER THR ALA GLN VAL          
SEQRES   3 B  209  GLN PHE ASP GLU PRO GLU ALA THR GLY GLY VAL PRO ILE          
SEQRES   4 B  209  LEU LYS TYR LYS ALA GLU TRP ARG ALA VAL GLY GLU GLU          
SEQRES   5 B  209  VAL TRP HIS SER LYS TRP TYR ASP ALA LYS GLU ALA SER          
SEQRES   6 B  209  MET GLU GLY ILE VAL THR ILE VAL GLY LEU LYS PRO GLU          
SEQRES   7 B  209  THR THR TYR ALA VAL ARG LEU ALA ALA LEU ASN GLY LYS          
SEQRES   8 B  209  GLY LEU GLY GLU ILE SER ALA ALA SER GLU PHE LYS THR          
SEQRES   9 B  209  GLN PRO VAL ARG GLU PRO SER ALA PRO LYS LEU GLU GLY          
SEQRES  10 B  209  GLN MET GLY GLU ASP GLY ASN SER ILE LYS VAL ASN LEU          
SEQRES  11 B  209  ILE LYS GLN ASP ASP GLY GLY SER PRO ILE ARG HIS TYR          
SEQRES  12 B  209  LEU VAL ARG TYR ARG ALA LEU SER SER GLU TRP LYS PRO          
SEQRES  13 B  209  GLU ILE ARG LEU PRO SER GLY SER ASP HIS VAL MET LEU          
SEQRES  14 B  209  LYS SER LEU ASP TRP ASN ALA GLU TYR GLU VAL TYR VAL          
SEQRES  15 B  209  VAL ALA GLU ASN GLN GLN GLY LYS SER LYS ALA ALA HIS          
SEQRES  16 B  209  PHE VAL PHE ARG THR ALA ALA ALA HIS HIS HIS HIS HIS          
SEQRES  17 B  209  HIS                                                          
HET    SO4  A1693       5                                                       
HET    SO4  B1692       5                                                       
HET    SO4  B1693       5                                                       
HET    SO4  B1694       5                                                       
HET    SO4  B1695       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    5(O4 S 2-)                                                   
FORMUL   8  HOH   *98(H2 O)                                                     
HELIX    1   1 ALA A  552  GLY A  559  1                                   8    
HELIX    2   2 ALA B  552  GLY B  559  1                                   8    
SHEET    1  AA 3 SER A 504  PRO A 510  0                                        
SHEET    2  AA 3 ALA A 515  ASP A 520 -1  O  GLN A 516   N  GLU A 509           
SHEET    3  AA 3 ILE A 560  ILE A 563 -1  O  VAL A 561   N  VAL A 517           
SHEET    1  AB 4 HIS A 546  ASP A 551  0                                        
SHEET    2  AB 4 LYS A 532  ALA A 539 -1  O  TYR A 533   N  TYR A 550           
SHEET    3  AB 4 THR A 571  ASN A 580 -1  O  ALA A 573   N  ARG A 538           
SHEET    4  AB 4 SER A 591  LYS A 594 -1  O  SER A 591   N  VAL A 574           
SHEET    1  AC 4 HIS A 546  ASP A 551  0                                        
SHEET    2  AC 4 LYS A 532  ALA A 539 -1  O  TYR A 533   N  TYR A 550           
SHEET    3  AC 4 THR A 571  ASN A 580 -1  O  ALA A 573   N  ARG A 538           
SHEET    4  AC 4 GLY A 583  LEU A 584 -1  O  GLY A 583   N  ASN A 580           
SHEET    1  AD 3 LYS A 605  MET A 610  0                                        
SHEET    2  AD 3 ILE A 617  ILE A 622 -1  O  LYS A 618   N  GLN A 609           
SHEET    3  AD 3 HIS A 657  LEU A 660 -1  O  VAL A 658   N  VAL A 619           
SHEET    1  AE 7 ILE A 649  LEU A 651  0                                        
SHEET    2  AE 7 HIS A 633  ALA A 640 -1  O  TYR A 634   N  LEU A 651           
SHEET    3  AE 7 GLU A 668  ASN A 677 -1  O  GLU A 670   N  ARG A 639           
SHEET    4  AE 7 ALA A 685  ARG A 690 -1  O  ALA A 685   N  VAL A 673           
SHEET    5  AE 7 LYS B 605  MET B 610  1  O  LEU B 606   N  VAL A 688           
SHEET    6  AE 7 ILE B 617  ILE B 622 -1  O  LYS B 618   N  GLN B 609           
SHEET    7  AE 7 HIS B 657  LEU B 660 -1  O  VAL B 658   N  VAL B 619           
SHEET    1  AF 4 ILE A 649  LEU A 651  0                                        
SHEET    2  AF 4 HIS A 633  ALA A 640 -1  O  TYR A 634   N  LEU A 651           
SHEET    3  AF 4 GLU A 668  ASN A 677 -1  O  GLU A 670   N  ARG A 639           
SHEET    4  AF 4 GLY A 680  LYS A 681 -1  O  GLY A 680   N  ASN A 677           
SHEET    1  BA 3 SER B 504  PRO B 510  0                                        
SHEET    2  BA 3 ALA B 515  ASP B 520 -1  O  GLN B 516   N  GLU B 509           
SHEET    3  BA 3 VAL B 561  ILE B 563 -1  O  VAL B 561   N  VAL B 517           
SHEET    1  BB 4 HIS B 546  ASP B 551  0                                        
SHEET    2  BB 4 ILE B 530  ALA B 539 -1  O  TYR B 533   N  TYR B 550           
SHEET    3  BB 4 THR B 571  ASN B 580 -1  O  ALA B 573   N  ARG B 538           
SHEET    4  BB 4 SER B 591  LYS B 594 -1  O  SER B 591   N  VAL B 574           
SHEET    1  BC 4 HIS B 546  ASP B 551  0                                        
SHEET    2  BC 4 ILE B 530  ALA B 539 -1  O  TYR B 533   N  TYR B 550           
SHEET    3  BC 4 THR B 571  ASN B 580 -1  O  ALA B 573   N  ARG B 538           
SHEET    4  BC 4 GLY B 583  LEU B 584 -1  O  GLY B 583   N  ASN B 580           
SHEET    1  BD 4 ILE B 649  PRO B 652  0                                        
SHEET    2  BD 4 ILE B 631  ALA B 640 -1  O  TYR B 634   N  LEU B 651           
SHEET    3  BD 4 GLU B 668  ASN B 677 -1  O  GLU B 670   N  ARG B 639           
SHEET    4  BD 4 ALA B 685  ARG B 690 -1  O  ALA B 685   N  VAL B 673           
SITE     1 AC1  7 LYS A 534  TRP A 549  ARG A 639  LYS B 532                    
SITE     2 AC1  7 ASP B 551  HOH B2044  HOH B2045                               
SITE     1 AC2  6 LYS A 548  TRP A 549  LYS B 548  TRP B 549                    
SITE     2 AC2  6 HOH B2046  HOH B2047                                          
SITE     1 AC3  5 LYS A 532  ASP A 551  HOH A2051  TRP B 549                    
SITE     2 AC3  5 ARG B 639                                                     
SITE     1 AC4  1 ARG B 637                                                     
SITE     1 AC5  2 HIS B 546  SER B 547                                          
CRYST1   52.770   71.346   98.217  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018950  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014016  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010182        0.00000                         
MTRIX1   1 -0.711740  0.701500  0.036370       42.05063    1                    
MTRIX2   1  0.702440  0.710990  0.032850      -17.72883    1                    
MTRIX3   1 -0.002820  0.048930 -0.998800       21.91621    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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