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Database: PDB
Entry: 4JPZ
LinkDB: 4JPZ
Original site: 4JPZ 
HEADER    TRANSPORT PROTEIN                       19-MAR-13   4JPZ              
TITLE     VOLTAGE-GATED SODIUM CHANNEL 1.2 C-TERMINAL DOMAIN IN COMPLEX WITH    
TITLE    2 FGF13U AND CA2+/CALMODULIN                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBROBLAST GROWTH FACTOR 13;                               
COMPND   3 CHAIN: A, E;                                                         
COMPND   4 SYNONYM: FGF-13, FIBROBLAST GROWTH FACTOR HOMOLOGOUS FACTOR 2, FHF-2;
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: SODIUM CHANNEL PROTEIN TYPE 2 SUBUNIT ALPHA;               
COMPND   8 CHAIN: B, H;                                                         
COMPND   9 SYNONYM: HBSC II, SODIUM CHANNEL PROTEIN BRAIN II SUBUNIT ALPHA,     
COMPND  10 SODIUM CHANNEL PROTEIN TYPE II SUBUNIT ALPHA, VOLTAGE-GATED SODIUM   
COMPND  11 CHANNEL SUBUNIT ALPHA NAV1.2;                                        
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: CALMODULIN;                                                
COMPND  15 CHAIN: C, I;                                                         
COMPND  16 SYNONYM: CAM;                                                        
COMPND  17 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: FGF13, FHF2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: SCN2A, NAC2, SCN2A1, SCN2A2;                                   
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2,      
SOURCE  20 CAM3, CAMC, CAMIII;                                                  
SOURCE  21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  22 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    EF HAND AND IQ MOTIF, ION CHANNEL, MEMBRANE, TRANSPORT PROTEIN        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.WANG,B.C.CHUNG,H.YAN,H.G.WANG,S.Y.LEE,G.S.PITT                      
REVDAT   5   28-FEB-24 4JPZ    1       REMARK SEQADV LINK                       
REVDAT   4   15-NOV-17 4JPZ    1       REMARK                                   
REVDAT   3   03-DEC-14 4JPZ    1       AUTHOR                                   
REVDAT   2   22-OCT-14 4JPZ    1       JRNL                                     
REVDAT   1   16-APR-14 4JPZ    0                                                
JRNL        AUTH   C.WANG,B.C.CHUNG,H.YAN,H.G.WANG,S.Y.LEE,G.S.PITT             
JRNL        TITL   STRUCTURAL ANALYSES OF CA(2+)/CAM INTERACTION WITH NAV       
JRNL        TITL 2 CHANNEL C-TERMINI REVEAL MECHANISMS OF CALCIUM-DEPENDENT     
JRNL        TITL 3 REGULATION.                                                  
JRNL        REF    NAT COMMUN                    V.   5  4896 2014              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   25232683                                                     
JRNL        DOI    10.1038/NCOMMS5896                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.02 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.02                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.23                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.400                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 49449                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.240                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3581                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.2365 -  6.5016    1.00     4992   394  0.1756 0.1827        
REMARK   3     2  6.5016 -  5.1625    1.00     4937   391  0.1886 0.2295        
REMARK   3     3  5.1625 -  4.5104    1.00     4995   390  0.1828 0.2186        
REMARK   3     4  4.5104 -  4.0983    0.99     4978   393  0.2100 0.2725        
REMARK   3     5  4.0983 -  3.8047    0.99     4910   384  0.2274 0.2766        
REMARK   3     6  3.8047 -  3.5804    0.97     4854   372  0.2415 0.2732        
REMARK   3     7  3.5804 -  3.4012    0.96     4766   381  0.2681 0.3356        
REMARK   3     8  3.4012 -  3.2531    0.89     4478   340  0.2910 0.3282        
REMARK   3     9  3.2531 -  3.1279    0.79     3926   288  0.3037 0.3252        
REMARK   3    10  3.1279 -  3.0200    0.60     3032   248  0.3191 0.3668        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.440            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.430           
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) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.011           7122                                  
REMARK   3   ANGLE     :  1.041           9621                                  
REMARK   3   CHIRALITY :  0.071           1036                                  
REMARK   3   PLANARITY :  0.004           1242                                  
REMARK   3   DIHEDRAL  : 14.966           2708                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4JPZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000078357.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-AUG-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL, SI 111             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53782                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.020                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.02                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: SAD                          
REMARK 200 SOFTWARE USED: PHASER, SHELX                                         
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG3350, 300 MM SODIUM ACETATE,50    
REMARK 280  MM TRIS PH 7.5, AND 2 MM CACL2, EVAPORATION, TEMPERATURE 290K       
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       76.56650            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.05300            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       76.56650            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       43.05300            
REMARK 290   SMTRY3   4  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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, H, I                               
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     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     ARG A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     TYR A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     GLU A    10                                                      
REMARK 465     LEU A   159                                                      
REMARK 465     THR A   160                                                      
REMARK 465     GLU A   161                                                      
REMARK 465     PHE A   162                                                      
REMARK 465     SER A   163                                                      
REMARK 465     ARG A   164                                                      
REMARK 465     SER A   165                                                      
REMARK 465     GLY A   166                                                      
REMARK 465     SER A   167                                                      
REMARK 465     GLY A   168                                                      
REMARK 465     THR A   169                                                      
REMARK 465     PRO A   170                                                      
REMARK 465     THR A   171                                                      
REMARK 465     LYS A   172                                                      
REMARK 465     SER A   173                                                      
REMARK 465     ARG A   174                                                      
REMARK 465     SER A   175                                                      
REMARK 465     VAL A   176                                                      
REMARK 465     SER A   177                                                      
REMARK 465     GLY A   178                                                      
REMARK 465     VAL A   179                                                      
REMARK 465     LEU A   180                                                      
REMARK 465     ASN A   181                                                      
REMARK 465     GLY A   182                                                      
REMARK 465     GLY A   183                                                      
REMARK 465     LYS A   184                                                      
REMARK 465     SER A   185                                                      
REMARK 465     MET A   186                                                      
REMARK 465     SER A   187                                                      
REMARK 465     HIS A   188                                                      
REMARK 465     ASN A   189                                                      
REMARK 465     GLU A   190                                                      
REMARK 465     SER A   191                                                      
REMARK 465     THR A   192                                                      
REMARK 465     MET B  1754                                                      
REMARK 465     GLY B  1755                                                      
REMARK 465     SER B  1756                                                      
REMARK 465     SER B  1757                                                      
REMARK 465     HIS B  1758                                                      
REMARK 465     HIS B  1759                                                      
REMARK 465     HIS B  1760                                                      
REMARK 465     HIS B  1761                                                      
REMARK 465     HIS B  1762                                                      
REMARK 465     HIS B  1763                                                      
REMARK 465     SER B  1764                                                      
REMARK 465     SER B  1765                                                      
REMARK 465     GLY B  1766                                                      
REMARK 465     LEU B  1767                                                      
REMARK 465     VAL B  1768                                                      
REMARK 465     PRO B  1769                                                      
REMARK 465     ARG B  1770                                                      
REMARK 465     GLY B  1771                                                      
REMARK 465     SER B  1772                                                      
REMARK 465     HIS B  1773                                                      
REMARK 465     MET B  1774                                                      
REMARK 465     ALA B  1775                                                      
REMARK 465     SER B  1776                                                      
REMARK 465     GLU B  1777                                                      
REMARK 465     ASN B  1778                                                      
REMARK 465     PHE B  1779                                                      
REMARK 465     SER B  1780                                                      
REMARK 465     VAL B  1781                                                      
REMARK 465     ALA B  1782                                                      
REMARK 465     THR B  1783                                                      
REMARK 465     GLU B  1784                                                      
REMARK 465     GLU B  1785                                                      
REMARK 465     SER B  1786                                                      
REMARK 465     ALA B  1787                                                      
REMARK 465     SER B  1930                                                      
REMARK 465     ILE B  1931                                                      
REMARK 465     TYR B  1932                                                      
REMARK 465     LYS B  1933                                                      
REMARK 465     LYS B  1934                                                      
REMARK 465     ASP B  1935                                                      
REMARK 465     LYS B  1936                                                      
REMARK 465     GLY B  1937                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     ASP C     3                                                      
REMARK 465     GLN C     4                                                      
REMARK 465     LEU C     5                                                      
REMARK 465     THR C     6                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     LEU E     3                                                      
REMARK 465     LEU E     4                                                      
REMARK 465     ARG E     5                                                      
REMARK 465     LYS E     6                                                      
REMARK 465     SER E     7                                                      
REMARK 465     TYR E     8                                                      
REMARK 465     SER E     9                                                      
REMARK 465     GLU E    10                                                      
REMARK 465     LEU E   159                                                      
REMARK 465     THR E   160                                                      
REMARK 465     GLU E   161                                                      
REMARK 465     PHE E   162                                                      
REMARK 465     SER E   163                                                      
REMARK 465     ARG E   164                                                      
REMARK 465     SER E   165                                                      
REMARK 465     GLY E   166                                                      
REMARK 465     SER E   167                                                      
REMARK 465     GLY E   168                                                      
REMARK 465     THR E   169                                                      
REMARK 465     PRO E   170                                                      
REMARK 465     THR E   171                                                      
REMARK 465     LYS E   172                                                      
REMARK 465     SER E   173                                                      
REMARK 465     ARG E   174                                                      
REMARK 465     SER E   175                                                      
REMARK 465     VAL E   176                                                      
REMARK 465     SER E   177                                                      
REMARK 465     GLY E   178                                                      
REMARK 465     VAL E   179                                                      
REMARK 465     LEU E   180                                                      
REMARK 465     ASN E   181                                                      
REMARK 465     GLY E   182                                                      
REMARK 465     GLY E   183                                                      
REMARK 465     LYS E   184                                                      
REMARK 465     SER E   185                                                      
REMARK 465     MET E   186                                                      
REMARK 465     SER E   187                                                      
REMARK 465     HIS E   188                                                      
REMARK 465     ASN E   189                                                      
REMARK 465     GLU E   190                                                      
REMARK 465     SER E   191                                                      
REMARK 465     THR E   192                                                      
REMARK 465     MET H  1754                                                      
REMARK 465     GLY H  1755                                                      
REMARK 465     SER H  1756                                                      
REMARK 465     SER H  1757                                                      
REMARK 465     HIS H  1758                                                      
REMARK 465     HIS H  1759                                                      
REMARK 465     HIS H  1760                                                      
REMARK 465     HIS H  1761                                                      
REMARK 465     HIS H  1762                                                      
REMARK 465     HIS H  1763                                                      
REMARK 465     SER H  1764                                                      
REMARK 465     SER H  1765                                                      
REMARK 465     GLY H  1766                                                      
REMARK 465     LEU H  1767                                                      
REMARK 465     VAL H  1768                                                      
REMARK 465     PRO H  1769                                                      
REMARK 465     ARG H  1770                                                      
REMARK 465     GLY H  1771                                                      
REMARK 465     SER H  1772                                                      
REMARK 465     HIS H  1773                                                      
REMARK 465     MET H  1774                                                      
REMARK 465     ALA H  1775                                                      
REMARK 465     SER H  1776                                                      
REMARK 465     GLU H  1777                                                      
REMARK 465     ASN H  1778                                                      
REMARK 465     PHE H  1779                                                      
REMARK 465     SER H  1780                                                      
REMARK 465     VAL H  1781                                                      
REMARK 465     ALA H  1782                                                      
REMARK 465     THR H  1783                                                      
REMARK 465     GLU H  1784                                                      
REMARK 465     GLU H  1785                                                      
REMARK 465     SER H  1786                                                      
REMARK 465     ALA H  1787                                                      
REMARK 465     SER H  1930                                                      
REMARK 465     ILE H  1931                                                      
REMARK 465     TYR H  1932                                                      
REMARK 465     LYS H  1933                                                      
REMARK 465     LYS H  1934                                                      
REMARK 465     ASP H  1935                                                      
REMARK 465     LYS H  1936                                                      
REMARK 465     GLY H  1937                                                      
REMARK 465     MET I     1                                                      
REMARK 465     ALA I     2                                                      
REMARK 465     ASP I     3                                                      
REMARK 465     GLN I     4                                                      
REMARK 465     LEU I     5                                                      
REMARK 465     THR I     6                                                      
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     LYS C 149    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   NH2  ARG I   107     OD1  ASP I   123              2.16            
REMARK 500   O    GLU I    83     N    GLU I    85              2.16            
REMARK 500   O    SER I    82     N    GLU I    84              2.16            
REMARK 500   O    VAL C    36     OG   SER C    39              2.18            
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    PRO A  53       96.27    -68.06                                   
REMARK 500    TYR A  98      -31.37   -146.13                                   
REMARK 500    GLN A 110      -37.93     64.43                                   
REMARK 500    GLN A 111      -61.00    -90.07                                   
REMARK 500    HIS A 157     -151.07   -134.68                                   
REMARK 500    PRO B1789     -156.94    -61.11                                   
REMARK 500    SER B1869     -163.53   -168.66                                   
REMARK 500    ALA B1885      -71.72    -79.17                                   
REMARK 500    ASP C  81       72.56   -101.51                                   
REMARK 500    GLU C 115       70.43    -69.44                                   
REMARK 500    PRO E  53       96.72    -66.94                                   
REMARK 500    TYR E  98      -32.10   -147.50                                   
REMARK 500    HIS E 157     -153.12   -133.20                                   
REMARK 500    PRO H1789     -174.18    -60.83                                   
REMARK 500    SER H1869     -162.82   -166.93                                   
REMARK 500    ALA H1885      -70.83    -76.61                                   
REMARK 500    THR H1898     -159.21   -146.54                                   
REMARK 500    GLU I  83       45.52     -2.45                                   
REMARK 500    GLU I  84      -55.15     52.08                                   
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 C 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  21   OD1                                                    
REMARK 620 2 ASP C  23   OD1  95.4                                              
REMARK 620 3 ASP C  25   OD1  85.2  89.8                                        
REMARK 620 4 THR C  27   O    81.9 156.1  66.3                                  
REMARK 620 5 GLU C  32   OE2 110.4  75.3 159.1 128.0                            
REMARK 620 6 GLU C  32   OE1  91.9 125.4 144.8  78.5  51.7                      
REMARK 620 7 HOH C 301   O   168.7  86.3 105.9 101.0  59.2  78.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  57   OD1                                                    
REMARK 620 2 ASN C  61   OD1 114.7                                              
REMARK 620 3 THR C  63   O   101.9  75.9                                        
REMARK 620 4 GLU C  68   OE1  94.3 141.2  73.3                                  
REMARK 620 5 GLU C  68   OE2  67.8 169.3 114.3  45.5                            
REMARK 620 6 HOH C 302   O   149.6  92.5  70.7  55.3  88.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  94   OD1                                                    
REMARK 620 2 ASP C  96   OD1  97.5                                              
REMARK 620 3 ASN C  98   OD1  80.5  96.0                                        
REMARK 620 4 TYR C 100   O    78.1 175.2  85.3                                  
REMARK 620 5 HOH C 303   O   172.8  85.8 105.6  98.3                            
REMARK 620 6 HOH C 304   O    78.0  78.3 156.8  98.7  96.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 130   OD1                                                    
REMARK 620 2 ASP C 132   OD1  89.2                                              
REMARK 620 3 ASP C 134   OD1  77.6  72.6                                        
REMARK 620 4 GLN C 136   O    74.1 149.9  79.3                                  
REMARK 620 5 HOH C 305   O   161.8  85.8  84.2 102.2                            
REMARK 620 6 HOH C 306   O   111.7 107.8 170.6 101.7  86.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA I 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP I  21   OD1                                                    
REMARK 620 2 ASP I  23   OD1 113.9                                              
REMARK 620 3 ASP I  25   OD1  73.8  83.5                                        
REMARK 620 4 THR I  27   O    72.7 145.6  65.5                                  
REMARK 620 5 GLU I  32   OE2 131.1  82.2 154.8 120.0                            
REMARK 620 6 GLU I  32   OE1 103.7 128.0 142.9  78.3  45.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA I 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP I  57   OD1                                                    
REMARK 620 2 ASN I  61   OD1  97.0                                              
REMARK 620 3 THR I  63   O    86.3  77.1                                        
REMARK 620 4 GLU I  68   OE1 109.8 140.9  76.8                                  
REMARK 620 5 GLU I  68   OE2  96.6 151.6 128.5  53.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA I 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP I  94   OD1                                                    
REMARK 620 2 ASP I  96   OD1  91.3                                              
REMARK 620 3 ASN I  98   OD1  68.2  91.4                                        
REMARK 620 4 TYR I 100   O    82.8 173.9  88.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA I 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP I 130   OD1                                                    
REMARK 620 2 ASP I 132   OD1  64.4                                              
REMARK 620 3 ASP I 132   OD2 116.0  53.4                                        
REMARK 620 4 ASP I 134   OD1  75.7  78.9  79.4                                  
REMARK 620 5 GLN I 136   O    66.8 130.9 162.0  84.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA I 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA I 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA I 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA I 204                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4JQ0   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE RESIDUES RRRP AT POSITIONS 59-62 ARE ISOFORM 2 NATURAL VARIANTS, 
REMARK 999 UNP CODE Q92913-2                                                    
DBREF  4JPZ A    5   192  UNP    Q92913   FGF13_HUMAN     58    245             
DBREF  4JPZ B 1777  1937  UNP    Q99250   SCN2A_HUMAN   1777   1937             
DBREF  4JPZ C    1   149  UNP    P62158   CALM_HUMAN       1    149             
DBREF  4JPZ E    5   192  UNP    Q92913   FGF13_HUMAN     58    245             
DBREF  4JPZ H 1777  1937  UNP    Q99250   SCN2A_HUMAN   1777   1937             
DBREF  4JPZ I    1   149  UNP    P62158   CALM_HUMAN       1    149             
SEQADV 4JPZ MET A    1  UNP  Q92913              EXPRESSION TAG                 
SEQADV 4JPZ ALA A    2  UNP  Q92913              EXPRESSION TAG                 
SEQADV 4JPZ LEU A    3  UNP  Q92913              EXPRESSION TAG                 
SEQADV 4JPZ LEU A    4  UNP  Q92913              EXPRESSION TAG                 
SEQADV 4JPZ LYS A    6  UNP  Q92913    ARG    59 SEE REMARK 999                 
SEQADV 4JPZ SER A    7  UNP  Q92913    ARG    60 SEE REMARK 999                 
SEQADV 4JPZ TYR A    8  UNP  Q92913    ARG    61 SEE REMARK 999                 
SEQADV 4JPZ SER A    9  UNP  Q92913    PRO    62 SEE REMARK 999                 
SEQADV 4JPZ MET B 1754  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ GLY B 1755  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ SER B 1756  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ SER B 1757  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ HIS B 1758  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ HIS B 1759  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ HIS B 1760  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ HIS B 1761  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ HIS B 1762  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ HIS B 1763  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ SER B 1764  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ SER B 1765  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ GLY B 1766  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ LEU B 1767  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ VAL B 1768  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ PRO B 1769  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ ARG B 1770  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ GLY B 1771  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ SER B 1772  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ HIS B 1773  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ MET B 1774  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ ALA B 1775  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ SER B 1776  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ MET E    1  UNP  Q92913              EXPRESSION TAG                 
SEQADV 4JPZ ALA E    2  UNP  Q92913              EXPRESSION TAG                 
SEQADV 4JPZ LEU E    3  UNP  Q92913              EXPRESSION TAG                 
SEQADV 4JPZ LEU E    4  UNP  Q92913              EXPRESSION TAG                 
SEQADV 4JPZ LYS E    6  UNP  Q92913    ARG    59 SEE REMARK 999                 
SEQADV 4JPZ SER E    7  UNP  Q92913    ARG    60 SEE REMARK 999                 
SEQADV 4JPZ TYR E    8  UNP  Q92913    ARG    61 SEE REMARK 999                 
SEQADV 4JPZ SER E    9  UNP  Q92913    PRO    62 SEE REMARK 999                 
SEQADV 4JPZ MET H 1754  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ GLY H 1755  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ SER H 1756  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ SER H 1757  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ HIS H 1758  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ HIS H 1759  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ HIS H 1760  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ HIS H 1761  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ HIS H 1762  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ HIS H 1763  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ SER H 1764  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ SER H 1765  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ GLY H 1766  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ LEU H 1767  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ VAL H 1768  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ PRO H 1769  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ ARG H 1770  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ GLY H 1771  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ SER H 1772  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ HIS H 1773  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ MET H 1774  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ ALA H 1775  UNP  Q99250              EXPRESSION TAG                 
SEQADV 4JPZ SER H 1776  UNP  Q99250              EXPRESSION TAG                 
SEQRES   1 A  192  MET ALA LEU LEU ARG LYS SER TYR SER GLU PRO GLN LEU          
SEQRES   2 A  192  LYS GLY ILE VAL THR LYS LEU TYR SER ARG GLN GLY TYR          
SEQRES   3 A  192  HIS LEU GLN LEU GLN ALA ASP GLY THR ILE ASP GLY THR          
SEQRES   4 A  192  LYS ASP GLU ASP SER THR TYR THR LEU PHE ASN LEU ILE          
SEQRES   5 A  192  PRO VAL GLY LEU ARG VAL VAL ALA ILE GLN GLY VAL GLN          
SEQRES   6 A  192  THR LYS LEU TYR LEU ALA MET ASN SER GLU GLY TYR LEU          
SEQRES   7 A  192  TYR THR SER GLU LEU PHE THR PRO GLU CYS LYS PHE LYS          
SEQRES   8 A  192  GLU SER VAL PHE GLU ASN TYR TYR VAL THR TYR SER SER          
SEQRES   9 A  192  MET ILE TYR ARG GLN GLN GLN SER GLY ARG GLY TRP TYR          
SEQRES  10 A  192  LEU GLY LEU ASN LYS GLU GLY GLU ILE MET LYS GLY ASN          
SEQRES  11 A  192  HIS VAL LYS LYS ASN LYS PRO ALA ALA HIS PHE LEU PRO          
SEQRES  12 A  192  LYS PRO LEU LYS VAL ALA MET TYR LYS GLU PRO SER LEU          
SEQRES  13 A  192  HIS ASP LEU THR GLU PHE SER ARG SER GLY SER GLY THR          
SEQRES  14 A  192  PRO THR LYS SER ARG SER VAL SER GLY VAL LEU ASN GLY          
SEQRES  15 A  192  GLY LYS SER MET SER HIS ASN GLU SER THR                      
SEQRES   1 B  184  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  184  LEU VAL PRO ARG GLY SER HIS MET ALA SER GLU ASN PHE          
SEQRES   3 B  184  SER VAL ALA THR GLU GLU SER ALA GLU PRO LEU SER GLU          
SEQRES   4 B  184  ASP ASP PHE GLU MET PHE TYR GLU VAL TRP GLU LYS PHE          
SEQRES   5 B  184  ASP PRO ASP ALA THR GLN PHE ILE GLU PHE ALA LYS LEU          
SEQRES   6 B  184  SER ASP PHE ALA ASP ALA LEU ASP PRO PRO LEU LEU ILE          
SEQRES   7 B  184  ALA LYS PRO ASN LYS VAL GLN LEU ILE ALA MET ASP LEU          
SEQRES   8 B  184  PRO MET VAL SER GLY ASP ARG ILE HIS CYS LEU ASP ILE          
SEQRES   9 B  184  LEU PHE ALA PHE THR LYS ARG VAL LEU GLY GLU SER GLY          
SEQRES  10 B  184  GLU MET ASP ALA LEU ARG ILE GLN MET GLU GLU ARG PHE          
SEQRES  11 B  184  MET ALA SER ASN PRO SER LYS VAL SER TYR GLU PRO ILE          
SEQRES  12 B  184  THR THR THR LEU LYS ARG LYS GLN GLU GLU VAL SER ALA          
SEQRES  13 B  184  ILE ILE ILE GLN ARG ALA TYR ARG ARG TYR LEU LEU LYS          
SEQRES  14 B  184  GLN LYS VAL LYS LYS VAL SER SER ILE TYR LYS LYS ASP          
SEQRES  15 B  184  LYS GLY                                                      
SEQRES   1 C  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 C  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 C  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 C  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 C  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 C  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 C  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 C  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 C  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 C  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 C  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 C  149  GLN MET MET THR ALA LYS                                      
SEQRES   1 E  192  MET ALA LEU LEU ARG LYS SER TYR SER GLU PRO GLN LEU          
SEQRES   2 E  192  LYS GLY ILE VAL THR LYS LEU TYR SER ARG GLN GLY TYR          
SEQRES   3 E  192  HIS LEU GLN LEU GLN ALA ASP GLY THR ILE ASP GLY THR          
SEQRES   4 E  192  LYS ASP GLU ASP SER THR TYR THR LEU PHE ASN LEU ILE          
SEQRES   5 E  192  PRO VAL GLY LEU ARG VAL VAL ALA ILE GLN GLY VAL GLN          
SEQRES   6 E  192  THR LYS LEU TYR LEU ALA MET ASN SER GLU GLY TYR LEU          
SEQRES   7 E  192  TYR THR SER GLU LEU PHE THR PRO GLU CYS LYS PHE LYS          
SEQRES   8 E  192  GLU SER VAL PHE GLU ASN TYR TYR VAL THR TYR SER SER          
SEQRES   9 E  192  MET ILE TYR ARG GLN GLN GLN SER GLY ARG GLY TRP TYR          
SEQRES  10 E  192  LEU GLY LEU ASN LYS GLU GLY GLU ILE MET LYS GLY ASN          
SEQRES  11 E  192  HIS VAL LYS LYS ASN LYS PRO ALA ALA HIS PHE LEU PRO          
SEQRES  12 E  192  LYS PRO LEU LYS VAL ALA MET TYR LYS GLU PRO SER LEU          
SEQRES  13 E  192  HIS ASP LEU THR GLU PHE SER ARG SER GLY SER GLY THR          
SEQRES  14 E  192  PRO THR LYS SER ARG SER VAL SER GLY VAL LEU ASN GLY          
SEQRES  15 E  192  GLY LYS SER MET SER HIS ASN GLU SER THR                      
SEQRES   1 H  184  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 H  184  LEU VAL PRO ARG GLY SER HIS MET ALA SER GLU ASN PHE          
SEQRES   3 H  184  SER VAL ALA THR GLU GLU SER ALA GLU PRO LEU SER GLU          
SEQRES   4 H  184  ASP ASP PHE GLU MET PHE TYR GLU VAL TRP GLU LYS PHE          
SEQRES   5 H  184  ASP PRO ASP ALA THR GLN PHE ILE GLU PHE ALA LYS LEU          
SEQRES   6 H  184  SER ASP PHE ALA ASP ALA LEU ASP PRO PRO LEU LEU ILE          
SEQRES   7 H  184  ALA LYS PRO ASN LYS VAL GLN LEU ILE ALA MET ASP LEU          
SEQRES   8 H  184  PRO MET VAL SER GLY ASP ARG ILE HIS CYS LEU ASP ILE          
SEQRES   9 H  184  LEU PHE ALA PHE THR LYS ARG VAL LEU GLY GLU SER GLY          
SEQRES  10 H  184  GLU MET ASP ALA LEU ARG ILE GLN MET GLU GLU ARG PHE          
SEQRES  11 H  184  MET ALA SER ASN PRO SER LYS VAL SER TYR GLU PRO ILE          
SEQRES  12 H  184  THR THR THR LEU LYS ARG LYS GLN GLU GLU VAL SER ALA          
SEQRES  13 H  184  ILE ILE ILE GLN ARG ALA TYR ARG ARG TYR LEU LEU LYS          
SEQRES  14 H  184  GLN LYS VAL LYS LYS VAL SER SER ILE TYR LYS LYS ASP          
SEQRES  15 H  184  LYS GLY                                                      
SEQRES   1 I  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 I  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 I  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 I  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 I  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 I  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 I  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 I  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 I  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 I  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 I  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 I  149  GLN MET MET THR ALA LYS                                      
HET     CA  C 201       1                                                       
HET     CA  C 202       1                                                       
HET     CA  C 203       1                                                       
HET     CA  C 204       1                                                       
HET     CA  I 201       1                                                       
HET     CA  I 202       1                                                       
HET     CA  I 203       1                                                       
HET     CA  I 204       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   7   CA    8(CA 2+)                                                     
FORMUL  15  HOH   *31(H2 O)                                                     
HELIX    1   1 SER A   44  THR A   47  5                                   4    
HELIX    2   2 THR A   85  CYS A   88  5                                   4    
HELIX    3   3 LYS A  128  VAL A  132  5                                   5    
HELIX    4   4 LYS A  136  ALA A  139  5                                   4    
HELIX    5   5 SER B 1791  ASP B 1806  1                                  16    
HELIX    6   6 LYS B 1817  ALA B 1824  1                                   8    
HELIX    7   7 ASN B 1835  ILE B 1840  1                                   6    
HELIX    8   8 CYS B 1854  GLY B 1867  1                                  14    
HELIX    9   9 SER B 1869  ASN B 1887  1                                  19    
HELIX   10  10 LEU B 1900  LYS B 1927  1                                  28    
HELIX   11  11 GLN C    9  ASP C   21  1                                  13    
HELIX   12  12 THR C   29  GLY C   41  1                                  13    
HELIX   13  13 THR C   45  GLU C   55  1                                  11    
HELIX   14  14 ASP C   65  LYS C   78  1                                  14    
HELIX   15  15 ILE C   86  VAL C   92  1                                   7    
HELIX   16  16 ALA C  103  LEU C  113  1                                  11    
HELIX   17  17 THR C  118  ASP C  130  1                                  13    
HELIX   18  18 TYR C  139  THR C  147  1                                   9    
HELIX   19  19 SER E   44  THR E   47  5                                   4    
HELIX   20  20 THR E   85  GLU E   87  5                                   3    
HELIX   21  21 LYS E  128  VAL E  132  5                                   5    
HELIX   22  22 LYS E  136  ALA E  139  5                                   4    
HELIX   23  23 SER H 1791  ASP H 1806  1                                  16    
HELIX   24  24 LYS H 1817  ALA H 1824  1                                   8    
HELIX   25  25 ASN H 1835  ILE H 1840  1                                   6    
HELIX   26  26 CYS H 1854  GLY H 1867  1                                  14    
HELIX   27  27 SER H 1869  ASN H 1887  1                                  19    
HELIX   28  28 LEU H 1900  VAL H 1928  1                                  29    
HELIX   29  29 GLU I    8  ASP I   21  1                                  14    
HELIX   30  30 THR I   29  GLY I   41  1                                  13    
HELIX   31  31 THR I   45  GLU I   55  1                                  11    
HELIX   32  32 ASP I   65  LYS I   78  1                                  14    
HELIX   33  33 ILE I   86  VAL I   92  1                                   7    
HELIX   34  34 ALA I  103  LEU I  113  1                                  11    
HELIX   35  35 THR I  118  ASP I  130  1                                  13    
HELIX   36  36 TYR I  139  ALA I  148  1                                  10    
LINK         OD1 ASP C  21                CA    CA C 201     1555   1555  2.19  
LINK         OD1 ASP C  23                CA    CA C 201     1555   1555  2.34  
LINK         OD1 ASP C  25                CA    CA C 201     1555   1555  2.29  
LINK         O   THR C  27                CA    CA C 201     1555   1555  2.57  
LINK         OE2 GLU C  32                CA    CA C 201     1555   1555  2.40  
LINK         OE1 GLU C  32                CA    CA C 201     1555   1555  2.59  
LINK         OD1 ASP C  57                CA    CA C 202     1555   1555  2.40  
LINK         OD1 ASN C  61                CA    CA C 202     1555   1555  2.31  
LINK         O   THR C  63                CA    CA C 202     1555   1555  2.54  
LINK         OE1 GLU C  68                CA    CA C 202     1555   1555  2.58  
LINK         OE2 GLU C  68                CA    CA C 202     1555   1555  3.00  
LINK         OD1 ASP C  94                CA    CA C 203     1555   1555  2.39  
LINK         OD1 ASP C  96                CA    CA C 203     1555   1555  2.39  
LINK         OD1 ASN C  98                CA    CA C 203     1555   1555  2.28  
LINK         O   TYR C 100                CA    CA C 203     1555   1555  2.43  
LINK         OD1 ASP C 130                CA    CA C 204     1555   1555  2.46  
LINK         OD1 ASP C 132                CA    CA C 204     1555   1555  2.26  
LINK         OD1 ASP C 134                CA    CA C 204     1555   1555  2.46  
LINK         O   GLN C 136                CA    CA C 204     1555   1555  2.28  
LINK        CA    CA C 201                 O   HOH C 301     1555   1555  2.90  
LINK        CA    CA C 202                 O   HOH C 302     1555   1555  2.52  
LINK        CA    CA C 203                 O   HOH C 303     1555   1555  2.34  
LINK        CA    CA C 203                 O   HOH C 304     1555   1555  2.50  
LINK        CA    CA C 204                 O   HOH C 305     1555   1555  2.26  
LINK        CA    CA C 204                 O   HOH C 306     1555   1555  2.28  
LINK         OD1 ASP I  21                CA    CA I 201     1555   1555  2.25  
LINK         OD1 ASP I  23                CA    CA I 201     1555   1555  2.28  
LINK         OD1 ASP I  25                CA    CA I 201     1555   1555  2.36  
LINK         O   THR I  27                CA    CA I 201     1555   1555  2.56  
LINK         OE2 GLU I  32                CA    CA I 201     1555   1555  2.36  
LINK         OE1 GLU I  32                CA    CA I 201     1555   1555  3.04  
LINK         OD1 ASP I  57                CA    CA I 202     1555   1555  2.35  
LINK         OD1 ASN I  61                CA    CA I 202     1555   1555  2.32  
LINK         O   THR I  63                CA    CA I 202     1555   1555  2.50  
LINK         OE1 GLU I  68                CA    CA I 202     1555   1555  2.42  
LINK         OE2 GLU I  68                CA    CA I 202     1555   1555  2.43  
LINK         OD1 ASP I  94                CA    CA I 203     1555   1555  2.63  
LINK         OD1 ASP I  96                CA    CA I 203     1555   1555  2.34  
LINK         OD1 ASN I  98                CA    CA I 203     1555   1555  2.37  
LINK         O   TYR I 100                CA    CA I 203     1555   1555  2.23  
LINK         OD1 ASP I 130                CA    CA I 204     1555   1555  2.52  
LINK         OD1 ASP I 132                CA    CA I 204     1555   1555  2.30  
LINK         OD2 ASP I 132                CA    CA I 204     1555   1555  2.54  
LINK         OD1 ASP I 134                CA    CA I 204     1555   1555  2.45  
LINK         O   GLN I 136                CA    CA I 204     1555   1555  2.41  
CISPEP   1 PRO B 1827    PRO B 1828          0         3.28                     
CISPEP   2 LYS B 1833    PRO B 1834          0        -1.60                     
CISPEP   3 SER B 1848    GLY B 1849          0        -0.92                     
CISPEP   4 LEU B 1866    GLY B 1867          0       -13.38                     
CISPEP   5 PRO H 1827    PRO H 1828          0         3.86                     
CISPEP   6 LYS H 1833    PRO H 1834          0        -1.52                     
CISPEP   7 SER H 1848    GLY H 1849          0        -0.56                     
SITE     1 AC1  6 ASP C  21  ASP C  23  ASP C  25  THR C  27                    
SITE     2 AC1  6 GLU C  32  HOH C 301                                          
SITE     1 AC2  6 ASP C  57  ASP C  59  ASN C  61  THR C  63                    
SITE     2 AC2  6 GLU C  68  HOH C 302                                          
SITE     1 AC3  6 ASP C  94  ASP C  96  ASN C  98  TYR C 100                    
SITE     2 AC3  6 HOH C 303  HOH C 304                                          
SITE     1 AC4  6 ASP C 130  ASP C 132  ASP C 134  GLN C 136                    
SITE     2 AC4  6 HOH C 305  HOH C 306                                          
SITE     1 AC5  5 ASP I  21  ASP I  23  ASP I  25  THR I  27                    
SITE     2 AC5  5 GLU I  32                                                     
SITE     1 AC6  5 ASP I  57  ASP I  59  ASN I  61  THR I  63                    
SITE     2 AC6  5 GLU I  68                                                     
SITE     1 AC7  4 ASP I  94  ASP I  96  ASN I  98  TYR I 100                    
SITE     1 AC8  4 ASP I 130  ASP I 132  ASP I 134  GLN I 136                    
CRYST1  153.133   86.106  109.399  90.00 100.90  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      0.006530  0.000000  0.001258        0.00000                         
SCALE2      0.000000  0.011614  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009309        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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