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Database: PDB
Entry: 4LTR
LinkDB: 4LTR
Original site: 4LTR 
HEADER    TRANSPORT PROTEIN                       23-JUL-13   4LTR              
TITLE     BACTERIAL SODIUM CHANNEL, HIS245GLY MUTANT, I222 SPACE GROUP          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ION TRANSPORT PROTEIN;                                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: PORE AND CYTOPLASMIC DOMAINS (UNP RESIDUES 143-288);       
COMPND   5 SYNONYM: SODIUM CHANNEL;                                             
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ALKALILIMNICOLA EHRLICHII;                      
SOURCE   3 ORGANISM_TAXID: 351052;                                              
SOURCE   4 GENE: MLG_0322;                                                      
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: C41(DE3);                                  
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET24B HM3C-LIC                           
KEYWDS    CATION CHANNEL FOLD, COILED COIL SODIUM CHANNEL, PLASMA MEMBRANE,     
KEYWDS   2 TRANSPORT PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.SHAYA,F.FINDEISEN,F.ABDEREMANE-ALI,C.ARRIGONI,S.WONG,S.REDDY NURVA, 
AUTHOR   2 G.LOUSSOUARN,D.L.MINOR                                               
REVDAT   3   22-JAN-14 4LTR    1       JRNL                                     
REVDAT   2   06-NOV-13 4LTR    1       JRNL                                     
REVDAT   1   23-OCT-13 4LTR    0                                                
JRNL        AUTH   D.SHAYA,F.FINDEISEN,F.ABDEREMANE-ALI,C.ARRIGONI,S.WONG,      
JRNL        AUTH 2 S.R.NURVA,G.LOUSSOUARN,D.L.MINOR                             
JRNL        TITL   STRUCTURE OF A PROKARYOTIC SODIUM CHANNEL PORE REVEALS       
JRNL        TITL 2 ESSENTIAL GATING ELEMENTS AND AN OUTER ION BINDING SITE      
JRNL        TITL 3 COMMON TO EUKARYOTIC CHANNELS.                               
JRNL        REF    J.MOL.BIOL.                   V. 426   467 2014              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   24120938                                                     
JRNL        DOI    10.1016/J.JMB.2013.10.010                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    5.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 5.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 5684                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.265                           
REMARK   3   R VALUE            (WORKING SET) : 0.262                           
REMARK   3   FREE R VALUE                     : 0.318                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 292                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 5.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 5.93                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 345                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.57                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5490                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 17                           
REMARK   3   BIN FREE R VALUE                    : 0.5760                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4034                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 305.00                         
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 308.05                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 13.56000                                             
REMARK   3    B22 (A**2) : -37.37000                                            
REMARK   3    B33 (A**2) : 23.81000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 1.593         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 1.535         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 156.651       
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.890                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4152 ; 0.007 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5689 ; 0.966 ; 1.934       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   540 ; 5.366 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   135 ;39.646 ;22.815       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   566 ;21.392 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;11.360 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   685 ; 0.060 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3070 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2172 ;42.916 ;92.306       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2708 ;67.165 ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1980 ;49.297 ;90.669       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6545 ;84.075 ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    150       A     285      1                      
REMARK   3           1     B    150       B     285      1                      
REMARK   3           1     C    150       C     285      1                      
REMARK   3           1     D    150       D     285      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      1    A (A**2):    996 ;53.500 ; 0.500           
REMARK   3   TIGHT THERMAL      1    B (A**2):    996 ;57.360 ; 0.500           
REMARK   3   TIGHT THERMAL      1    C (A**2):    996 ;59.080 ; 0.500           
REMARK   3   TIGHT THERMAL      1    D (A**2):    996 ;58.650 ; 0.500           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4LTR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB081075.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JAN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.70192                            
REMARK 200  MONOCHROMATOR                  : DOUBLE FLAT CRYSTAL, SI(111)       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 5978                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 5.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 13.100                             
REMARK 200  R MERGE                    (I) : 0.13000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 0.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 5.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 6.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.60                              
REMARK 200  R MERGE FOR SHELL          (I) : 4.18100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4LTO                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 83.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 7.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG400, 100 MM SODIUM ACETATE, PH    
REMARK 280  4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       78.60250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       80.69200            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       82.72450            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       78.60250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       80.69200            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       82.72450            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       78.60250            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       80.69200            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       82.72450            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       78.60250            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       80.69200            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       82.72450            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10990 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -121.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     GLY A   137                                                      
REMARK 465     PRO A   138                                                      
REMARK 465     SER A   139                                                      
REMARK 465     SER A   140                                                      
REMARK 465     PRO A   141                                                      
REMARK 465     SER A   142                                                      
REMARK 465     LEU A   143                                                      
REMARK 465     LEU A   144                                                      
REMARK 465     ARG A   145                                                      
REMARK 465     ALA A   146                                                      
REMARK 465     ILE A   147                                                      
REMARK 465     PRO A   148                                                      
REMARK 465     GLY A   149                                                      
REMARK 465     GLY A   286                                                      
REMARK 465     LYS A   287                                                      
REMARK 465     ARG A   288                                                      
REMARK 465     GLY B   137                                                      
REMARK 465     PRO B   138                                                      
REMARK 465     SER B   139                                                      
REMARK 465     SER B   140                                                      
REMARK 465     PRO B   141                                                      
REMARK 465     SER B   142                                                      
REMARK 465     LEU B   143                                                      
REMARK 465     LEU B   144                                                      
REMARK 465     ARG B   145                                                      
REMARK 465     ALA B   146                                                      
REMARK 465     ILE B   147                                                      
REMARK 465     PRO B   148                                                      
REMARK 465     GLY B   149                                                      
REMARK 465     GLY B   286                                                      
REMARK 465     LYS B   287                                                      
REMARK 465     ARG B   288                                                      
REMARK 465     GLY C   137                                                      
REMARK 465     PRO C   138                                                      
REMARK 465     SER C   139                                                      
REMARK 465     SER C   140                                                      
REMARK 465     PRO C   141                                                      
REMARK 465     SER C   142                                                      
REMARK 465     LEU C   143                                                      
REMARK 465     LEU C   144                                                      
REMARK 465     ARG C   145                                                      
REMARK 465     ALA C   146                                                      
REMARK 465     ILE C   147                                                      
REMARK 465     PRO C   148                                                      
REMARK 465     GLY C   149                                                      
REMARK 465     GLY C   286                                                      
REMARK 465     LYS C   287                                                      
REMARK 465     ARG C   288                                                      
REMARK 465     GLY D   137                                                      
REMARK 465     PRO D   138                                                      
REMARK 465     SER D   139                                                      
REMARK 465     SER D   140                                                      
REMARK 465     PRO D   141                                                      
REMARK 465     SER D   142                                                      
REMARK 465     LEU D   143                                                      
REMARK 465     LEU D   144                                                      
REMARK 465     ARG D   145                                                      
REMARK 465     ALA D   146                                                      
REMARK 465     ILE D   147                                                      
REMARK 465     PRO D   148                                                      
REMARK 465     GLY D   149                                                      
REMARK 465     GLY D   286                                                      
REMARK 465     LYS D   287                                                      
REMARK 465     ARG D   288                                                      
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     ILE A 150    CG1  CG2  CD1                                       
REMARK 470     LYS A 170    CG   CD   CE   NZ                                   
REMARK 470     GLU A 239    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 242    CG   CD   OE1  NE2                                  
REMARK 470     TRP A 246    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 246    CZ3  CH2                                            
REMARK 470     GLU A 247    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 249    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 250    CG   OD1  OD2                                       
REMARK 470     LYS A 252    CG   CD   CE   NZ                                   
REMARK 470     ARG A 253    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 254    CG1  CG2  CD1                                       
REMARK 470     GLN A 256    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 257    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 259    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 264    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 265    CG   CD1  CD2                                       
REMARK 470     ASP A 273    CG   OD1  OD2                                       
REMARK 470     SER A 276    OG                                                  
REMARK 470     LYS A 277    CG   CD   CE   NZ                                   
REMARK 470     ARG A 280    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 283    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 284    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 285    OG                                                  
REMARK 470     ILE B 150    CG1  CG2  CD1                                       
REMARK 470     LYS B 170    CG   CD   CE   NZ                                   
REMARK 470     GLU B 239    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 242    CG   CD   OE1  NE2                                  
REMARK 470     TRP B 246    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 246    CZ3  CH2                                            
REMARK 470     GLU B 247    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 249    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 252    CG   CD   CE   NZ                                   
REMARK 470     ARG B 253    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 256    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 257    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 258    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 259    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 262    CG   OD1  OD2                                       
REMARK 470     ARG B 264    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 265    CG   CD1  CD2                                       
REMARK 470     ASP B 273    CG   OD1  OD2                                       
REMARK 470     SER B 276    OG                                                  
REMARK 470     LYS B 277    CG   CD   CE   NZ                                   
REMARK 470     ASP B 279    CG   OD1  OD2                                       
REMARK 470     ARG B 280    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 283    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 284    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 285    OG                                                  
REMARK 470     ILE C 150    CG1  CG2  CD1                                       
REMARK 470     LYS C 170    CG   CD   CE   NZ                                   
REMARK 470     GLU C 178    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 239    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 242    CG   CD   OE1  NE2                                  
REMARK 470     TRP C 246    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP C 246    CZ3  CH2                                            
REMARK 470     GLU C 247    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 249    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 252    CG   CD   CE   NZ                                   
REMARK 470     ARG C 253    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE C 254    CG1  CG2  CD1                                       
REMARK 470     GLN C 256    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 257    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 258    CG   CD   OE1  NE2                                  
REMARK 470     ARG C 259    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 262    CG   OD1  OD2                                       
REMARK 470     ARG C 264    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU C 265    CG   CD1  CD2                                       
REMARK 470     ASP C 273    CG   OD1  OD2                                       
REMARK 470     SER C 276    OG                                                  
REMARK 470     LYS C 277    CG   CD   CE   NZ                                   
REMARK 470     ASP C 279    CG   OD1  OD2                                       
REMARK 470     ARG C 280    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 283    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 284    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER C 285    OG                                                  
REMARK 470     ILE D 150    CG1  CG2  CD1                                       
REMARK 470     LYS D 170    CG   CD   CE   NZ                                   
REMARK 470     GLU D 178    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 209    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 239    CG   CD   OE1  OE2                                  
REMARK 470     GLN D 242    CG   CD   OE1  NE2                                  
REMARK 470     TRP D 246    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP D 246    CZ3  CH2                                            
REMARK 470     GLU D 247    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 249    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 250    CG   OD1  OD2                                       
REMARK 470     LYS D 252    CG   CD   CE   NZ                                   
REMARK 470     ARG D 253    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE D 254    CG1  CG2  CD1                                       
REMARK 470     GLN D 256    CG   CD   OE1  NE2                                  
REMARK 470     GLU D 257    CG   CD   OE1  OE2                                  
REMARK 470     GLN D 258    CG   CD   OE1  NE2                                  
REMARK 470     ARG D 259    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D 262    CG   OD1  OD2                                       
REMARK 470     ARG D 264    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU D 265    CG   CD1  CD2                                       
REMARK 470     SER D 276    OG                                                  
REMARK 470     LYS D 277    CG   CD   CE   NZ                                   
REMARK 470     ASP D 279    CG   OD1  OD2                                       
REMARK 470     ARG D 280    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 282    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 283    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 284    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER D 285    OG                                                  
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    SER A 200      -65.93    -96.45                                   
REMARK 500    ILE A 203      -62.73   -106.81                                   
REMARK 500    SER B 198       45.81     39.85                                   
REMARK 500    SER B 200      -65.55    -95.19                                   
REMARK 500    ILE B 203      -63.23   -105.58                                   
REMARK 500    SER C 200      -65.71    -96.24                                   
REMARK 500    ILE C 203      -64.63   -105.52                                   
REMARK 500    SER D 200      -64.87    -96.16                                   
REMARK 500    ILE D 203      -62.60   -106.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4LTO   RELATED DB: PDB                                   
REMARK 900 BACTERIAL SODIUM CHANNEL IN HIGH CALCIUM, I222 SPACE GROUP           
REMARK 900 RELATED ID: 4LTP   RELATED DB: PDB                                   
REMARK 900 BACTERIAL SODIUM CHANNEL IN HIGH CALCIUM, I222 SPACE GROUP           
REMARK 900 RELATED ID: 4LTQ   RELATED DB: PDB                                   
REMARK 900 BACTERIAL SODIUM CHANNEL IN LOW CALCIUM, P42 SPACE GROUP             
DBREF  4LTR A  143   288  UNP    Q0ABW0   Q0ABW0_ALHEH   143    288             
DBREF  4LTR B  143   288  UNP    Q0ABW0   Q0ABW0_ALHEH   143    288             
DBREF  4LTR C  143   288  UNP    Q0ABW0   Q0ABW0_ALHEH   143    288             
DBREF  4LTR D  143   288  UNP    Q0ABW0   Q0ABW0_ALHEH   143    288             
SEQADV 4LTR GLY A  137  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR PRO A  138  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR SER A  139  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR SER A  140  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR PRO A  141  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR SER A  142  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR GLY A  245  UNP  Q0ABW0    HIS   245 ENGINEERED MUTATION            
SEQADV 4LTR GLY B  137  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR PRO B  138  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR SER B  139  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR SER B  140  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR PRO B  141  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR SER B  142  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR GLY B  245  UNP  Q0ABW0    HIS   245 ENGINEERED MUTATION            
SEQADV 4LTR GLY C  137  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR PRO C  138  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR SER C  139  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR SER C  140  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR PRO C  141  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR SER C  142  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR GLY C  245  UNP  Q0ABW0    HIS   245 ENGINEERED MUTATION            
SEQADV 4LTR GLY D  137  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR PRO D  138  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR SER D  139  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR SER D  140  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR PRO D  141  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR SER D  142  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 4LTR GLY D  245  UNP  Q0ABW0    HIS   245 ENGINEERED MUTATION            
SEQRES   1 A  152  GLY PRO SER SER PRO SER LEU LEU ARG ALA ILE PRO GLY          
SEQRES   2 A  152  ILE ALA TRP ILE ALA LEU LEU LEU LEU VAL ILE PHE TYR          
SEQRES   3 A  152  VAL PHE ALA VAL MET GLY THR LYS LEU PHE ALA GLN SER          
SEQRES   4 A  152  PHE PRO GLU TRP PHE GLY THR LEU GLY ALA SER MET TYR          
SEQRES   5 A  152  THR LEU PHE GLN VAL MET THR LEU GLU SER TRP SER MET          
SEQRES   6 A  152  GLY ILE ALA ARG PRO VAL ILE GLU ALA TYR PRO TRP ALA          
SEQRES   7 A  152  TRP ILE TYR PHE VAL SER PHE ILE LEU VAL SER SER PHE          
SEQRES   8 A  152  THR VAL LEU ASN LEU PHE ILE GLY ILE ILE ILE GLU SER          
SEQRES   9 A  152  MET GLN SER ALA GLY TRP GLU ALA GLU ASP ALA LYS ARG          
SEQRES  10 A  152  ILE GLU GLN GLU GLN ARG ALA HIS ASP GLU ARG LEU GLU          
SEQRES  11 A  152  MET LEU GLN LEU ILE ARG ASP LEU SER SER LYS VAL ASP          
SEQRES  12 A  152  ARG LEU GLU ARG ARG SER GLY LYS ARG                          
SEQRES   1 B  152  GLY PRO SER SER PRO SER LEU LEU ARG ALA ILE PRO GLY          
SEQRES   2 B  152  ILE ALA TRP ILE ALA LEU LEU LEU LEU VAL ILE PHE TYR          
SEQRES   3 B  152  VAL PHE ALA VAL MET GLY THR LYS LEU PHE ALA GLN SER          
SEQRES   4 B  152  PHE PRO GLU TRP PHE GLY THR LEU GLY ALA SER MET TYR          
SEQRES   5 B  152  THR LEU PHE GLN VAL MET THR LEU GLU SER TRP SER MET          
SEQRES   6 B  152  GLY ILE ALA ARG PRO VAL ILE GLU ALA TYR PRO TRP ALA          
SEQRES   7 B  152  TRP ILE TYR PHE VAL SER PHE ILE LEU VAL SER SER PHE          
SEQRES   8 B  152  THR VAL LEU ASN LEU PHE ILE GLY ILE ILE ILE GLU SER          
SEQRES   9 B  152  MET GLN SER ALA GLY TRP GLU ALA GLU ASP ALA LYS ARG          
SEQRES  10 B  152  ILE GLU GLN GLU GLN ARG ALA HIS ASP GLU ARG LEU GLU          
SEQRES  11 B  152  MET LEU GLN LEU ILE ARG ASP LEU SER SER LYS VAL ASP          
SEQRES  12 B  152  ARG LEU GLU ARG ARG SER GLY LYS ARG                          
SEQRES   1 C  152  GLY PRO SER SER PRO SER LEU LEU ARG ALA ILE PRO GLY          
SEQRES   2 C  152  ILE ALA TRP ILE ALA LEU LEU LEU LEU VAL ILE PHE TYR          
SEQRES   3 C  152  VAL PHE ALA VAL MET GLY THR LYS LEU PHE ALA GLN SER          
SEQRES   4 C  152  PHE PRO GLU TRP PHE GLY THR LEU GLY ALA SER MET TYR          
SEQRES   5 C  152  THR LEU PHE GLN VAL MET THR LEU GLU SER TRP SER MET          
SEQRES   6 C  152  GLY ILE ALA ARG PRO VAL ILE GLU ALA TYR PRO TRP ALA          
SEQRES   7 C  152  TRP ILE TYR PHE VAL SER PHE ILE LEU VAL SER SER PHE          
SEQRES   8 C  152  THR VAL LEU ASN LEU PHE ILE GLY ILE ILE ILE GLU SER          
SEQRES   9 C  152  MET GLN SER ALA GLY TRP GLU ALA GLU ASP ALA LYS ARG          
SEQRES  10 C  152  ILE GLU GLN GLU GLN ARG ALA HIS ASP GLU ARG LEU GLU          
SEQRES  11 C  152  MET LEU GLN LEU ILE ARG ASP LEU SER SER LYS VAL ASP          
SEQRES  12 C  152  ARG LEU GLU ARG ARG SER GLY LYS ARG                          
SEQRES   1 D  152  GLY PRO SER SER PRO SER LEU LEU ARG ALA ILE PRO GLY          
SEQRES   2 D  152  ILE ALA TRP ILE ALA LEU LEU LEU LEU VAL ILE PHE TYR          
SEQRES   3 D  152  VAL PHE ALA VAL MET GLY THR LYS LEU PHE ALA GLN SER          
SEQRES   4 D  152  PHE PRO GLU TRP PHE GLY THR LEU GLY ALA SER MET TYR          
SEQRES   5 D  152  THR LEU PHE GLN VAL MET THR LEU GLU SER TRP SER MET          
SEQRES   6 D  152  GLY ILE ALA ARG PRO VAL ILE GLU ALA TYR PRO TRP ALA          
SEQRES   7 D  152  TRP ILE TYR PHE VAL SER PHE ILE LEU VAL SER SER PHE          
SEQRES   8 D  152  THR VAL LEU ASN LEU PHE ILE GLY ILE ILE ILE GLU SER          
SEQRES   9 D  152  MET GLN SER ALA GLY TRP GLU ALA GLU ASP ALA LYS ARG          
SEQRES  10 D  152  ILE GLU GLN GLU GLN ARG ALA HIS ASP GLU ARG LEU GLU          
SEQRES  11 D  152  MET LEU GLN LEU ILE ARG ASP LEU SER SER LYS VAL ASP          
SEQRES  12 D  152  ARG LEU GLU ARG ARG SER GLY LYS ARG                          
HELIX    1   1 ILE A  153  ALA A  173  1                                  21    
HELIX    2   2 PHE A  176  GLY A  181  1                                   6    
HELIX    3   3 THR A  182  THR A  195  1                                  14    
HELIX    4   4 ILE A  203  TYR A  211  1                                   9    
HELIX    5   5 ALA A  214  GLN A  242  1                                  29    
HELIX    6   6 ALA A  248  ARG A  259  1                                  12    
HELIX    7   7 ALA A  260  ASP A  279  1                                  20    
HELIX    8   8 ILE B  153  ALA B  173  1                                  21    
HELIX    9   9 PHE B  176  GLY B  181  1                                   6    
HELIX   10  10 THR B  182  THR B  195  1                                  14    
HELIX   11  11 ILE B  203  TYR B  211  1                                   9    
HELIX   12  12 ALA B  214  GLN B  242  1                                  29    
HELIX   13  13 ALA B  248  ARG B  259  1                                  12    
HELIX   14  14 ALA B  260  ASP B  279  1                                  20    
HELIX   15  15 ILE C  153  ALA C  173  1                                  21    
HELIX   16  16 PHE C  176  GLY C  181  1                                   6    
HELIX   17  17 THR C  182  THR C  195  1                                  14    
HELIX   18  18 ILE C  203  TYR C  211  1                                   9    
HELIX   19  19 ALA C  214  GLN C  242  1                                  29    
HELIX   20  20 ALA C  248  ARG C  259  1                                  12    
HELIX   21  21 ALA C  260  ASP C  279  1                                  20    
HELIX   22  22 ILE D  153  ALA D  173  1                                  21    
HELIX   23  23 PHE D  176  GLY D  181  1                                   6    
HELIX   24  24 THR D  182  THR D  195  1                                  14    
HELIX   25  25 ILE D  203  TYR D  211  1                                   9    
HELIX   26  26 ALA D  214  GLN D  242  1                                  29    
HELIX   27  27 ALA D  248  ARG D  259  1                                  12    
HELIX   28  28 ALA D  260  ASP D  279  1                                  20    
CRYST1  157.205  161.384  165.449  90.00  90.00  90.00 I 2 2 2      32          
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      0.006361  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006196  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006044        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2  0.290504  0.283711  0.913847     -171.03464    1                    
MTRIX2   2 -0.907794  0.383652  0.169473       27.22528    1                    
MTRIX3   2 -0.302518 -0.878817  0.369003      178.39412    1                    
MTRIX1   3 -0.450781 -0.616359  0.645676      -48.75360    1                    
MTRIX2   3 -0.660624 -0.256096 -0.705685      223.74321    1                    
MTRIX3   3  0.600310 -0.744658 -0.291739      272.72321    1                    
MTRIX1   4  0.267838 -0.919702 -0.287072      126.88696    1                    
MTRIX2   4  0.267872  0.357295 -0.894754      199.82185    1                    
MTRIX3   4  0.925477  0.162750  0.342060       91.60007    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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