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Database: PDB
Entry: 6BUT
LinkDB: 6BUT
Original site: 6BUT 
HEADER    MEMBRANE PROTEIN                        11-DEC-17   6BUT              
TITLE     SOLUTION STRUCTURE OF FULL-LENGTH APO MAMMALIAN CALMODULIN BOUND TO   
TITLE    2 THE IQ MOTIF OF THE HUMAN VOLTAGE-GATED SODIUM CHANNEL NAV1.2        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN-1;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: SODIUM CHANNEL PROTEIN TYPE 2 SUBUNIT ALPHA;               
COMPND   7 CHAIN: B;                                                            
COMPND   8 SYNONYM: HBSC II,SODIUM CHANNEL PROTEIN BRAIN II SUBUNIT ALPHA,SODIUM
COMPND   9 CHANNEL PROTEIN TYPE II SUBUNIT ALPHA,VOLTAGE-GATED SODIUM CHANNEL   
COMPND  10 SUBUNIT ALPHA NAV1.2;                                                
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 OTHER_DETAILS: FIRST FOUR RESIDUES (GPGS) ARE PART OF A 3C PROTEASE  
COMPND  13 CLEAVAGE SITE, AND IN THE DEPOSIT HAVE BEEN NUMBERED -4 TO -1. NAV1.2
COMPND  14 RESIDUE 1901 IS RESIDUE 5 OF THE PEPTIDE.                            
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CALM1, CALM, CAM, CAM1;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT7-7;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: SCN2A, NAC2, SCN2A1, SCN2A2;                                   
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PBG101                                    
KEYWDS    CALCIUM-BINDING PROTEIN, METAL TRANSPORT ION CHANNEL NEURONAL         
KEYWDS   2 MOLECULAR RECOGNITION, MEMBRANE PROTEIN                              
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    R.MAHLING,A.M.KILPATRICK,M.A.SHEA                                     
REVDAT   2   18-DEC-19 6BUT    1       REMARK                                   
REVDAT   1   19-JUN-19 6BUT    0                                                
JRNL        AUTH   R.MAILING,A.M.KILPATRICK,L.HOVEY,D.C.MARX,L.D.WEAVER,        
JRNL        AUTH 2 J.B.YODER,M.S.MILLER,E.H.KIM,K.M.TEFFT,C.N.ANDRESEN,M.A.SHEA 
JRNL        TITL   VOLTAGE-GATED SODIUM CHANNEL NAV1.2 IQ MOTIF ANCHORS         
JRNL        TITL 2 CALMODULIN C-DOMAIN TO MAKE ALL FOUR SITES EQUIVALENT IN     
JRNL        TITL 3 AFFINITY FOR CALCIUM                                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.MAHLING,A.M.KILPATRICK,M.A.SHEA                            
REMARK   1  TITL   BACKBONE RESONANCE ASSIGNMENTS OF COMPLEXES OF HUMAN         
REMARK   1  TITL 2 VOLTAGE-DEPENDENT SODIUM CHANNEL NAV1.2 IQ MOTIF PEPTIDE     
REMARK   1  TITL 3 BOUND TO APO CALMODULIN AND TO THE C-DOMAIN FRAGMENT OF APO  
REMARK   1  TITL 4 CALMODULIN.                                                  
REMARK   1  REF    BIOMOL NMR ASSIGN             V.  11   297 2017              
REMARK   1  REFN                   ESSN 1874-270X                               
REMARK   1  PMID   28823028                                                     
REMARK   1  DOI    10.1007/S12104-017-9767-2                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : AMBER AMBERTOOLS 17                                  
REMARK   3   AUTHORS     : CASE, DARDEN, CHEATHAM III, SIMMERLING, WANG,        
REMARK   3                 DUKE, LUO, ... AND KOLLMAN                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6BUT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000231214.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298; 298                           
REMARK 210  PH                             : 6.5; 6.5                           
REMARK 210  IONIC STRENGTH                 : 100; 100                           
REMARK 210  PRESSURE                       : 1 ATM; 1 ATM                       
REMARK 210  SAMPLE CONTENTS                : 0.950 MM U-99% C13, U-99% N15      
REMARK 210                                   CALMODULIN, 0.950 MM U-99% C13,    
REMARK 210                                   U-99% N15 VOLTAGE-GATED SODIUM     
REMARK 210                                   CHANNEL NAV1.2 IQ MOTIF, 0.1 MM    
REMARK 210                                   U-98% 2H EDTA, 100 MM KCL, 10 MM   
REMARK 210                                   [U-99% 2H] IMIDAZOLE, 0.01 % W/V   
REMARK 210                                   SODIUM AZIDE, 90% H2O/10% D2O;     
REMARK 210                                   0.95 MM U-99% C13, U-99% N15       
REMARK 210                                   CALMODULIN, 0.95 MM U-99% C13, U-  
REMARK 210                                   99% N15 VOLTAGE-GATED SODIUM       
REMARK 210                                   CHANNEL NAV1.2 IQ MOTIF, 0.1 MM    
REMARK 210                                   U-98% 2H EDTA, 100 MM POTASSIUM    
REMARK 210                                   CHLORIDE, 10 MM [U-99% 2H]         
REMARK 210                                   IMIDAZOLE, 0.01 % W/V SODIUM       
REMARK 210                                   AZIDE, 100% D2O                    
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D 1H-15N HSQC; 3D HNCACB; 3D      
REMARK 210                                   CBCA(CO)NH; 3D HNCO; 3D HACACO;    
REMARK 210                                   3D C(CO)NH; 3D H(CCO)NH; 2D 1H-    
REMARK 210                                   13C HMQC; 3D HCCH-TOCSY; 3D 1H-    
REMARK 210                                   13C NOESY                          
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ; 500 MHZ; 800 MHZ          
REMARK 210  SPECTROMETER MODEL             : INOVA; AVANCE II                   
REMARK 210  SPECTROMETER MANUFACTURER      : VARIAN; BRUKER                     
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : VNMR, TOPSPIN, NMRPIPE, ANALYSIS   
REMARK 210                                   2.4, CYANA 2.1                     
REMARK 210   METHOD USED                   : MOLECULAR DYNAMICS                 
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 40                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST         
REMARK 210                                   ENERGY                             
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500  1 ARG A  74   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500  1 ARG A  86   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500  1 ARG B1902   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500  1 ARG B1917   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500  2 ARG A  86   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500  2 ARG B1914   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500  3 ARG A  86   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500  3 ARG A 106   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500  3 ARG A 126   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500  3 ARG B1902   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500  3 ARG B1914   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500  3 ARG B1917   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500  4 ARG A 106   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500  4 ARG A 126   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500  4 ARG B1902   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500  4 ARG B1914   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500  4 ARG B1918   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500  5 ARG A 106   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500  5 ARG A 126   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500  5 ARG B1902   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500  5 ARG B1918   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500  6 ARG A 106   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500  6 ARG B1902   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500  6 ARG B1914   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500  7 ARG A  86   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500  8 ARG A  86   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500  8 ARG A 106   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500  8 ARG B1902   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500  8 ARG B1918   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500  9 ARG A  86   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500  9 ARG A  90   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500  9 ARG A  90   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500  9 ARG A 106   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500  9 ARG B1914   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500  9 ARG B1917   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500 10 ARG A 106   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500 10 ARG B1902   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500 10 ARG B1914   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500 10 ARG B1918   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500 11 ARG A 106   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500 11 ARG A 126   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500 11 ARG B1902   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500 11 ARG B1914   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500 12 ARG A  86   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500 12 ARG A 106   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500 12 ARG A 126   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500 12 ARG B1902   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500 13 ARG A  37   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500 13 ARG A  86   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500 13 ARG A 106   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      81 ANGLE DEVIATIONS.                             
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  1 ASP A  56       45.31   -104.38                                   
REMARK 500  1 ASP A  80       19.56   -155.78                                   
REMARK 500  1 LYS A 115      129.57     64.20                                   
REMARK 500  1 ASP A 131       -2.48   -147.42                                   
REMARK 500  1 LYS B1901       11.50   -155.49                                   
REMARK 500  2 LYS A 115       99.95     56.88                                   
REMARK 500  3 ASP A  56       46.27   -141.52                                   
REMARK 500  3 LYS A 115      103.18     60.08                                   
REMARK 500  4 LYS A  77       39.87    -77.75                                   
REMARK 500  4 ASP A  95        9.17   -150.64                                   
REMARK 500  4 LYS A 115       97.83     53.91                                   
REMARK 500  5 ASN A  42       77.05   -159.76                                   
REMARK 500  5 LYS A  77       42.61    -80.00                                   
REMARK 500  5 ASP A  80       31.15    -82.59                                   
REMARK 500  5 SER A  81       78.21     58.36                                   
REMARK 500  5 ASP A  93       71.21    -68.79                                   
REMARK 500  5 LYS A 115      111.47    -13.53                                   
REMARK 500  6 ASP A  22        9.94   -158.25                                   
REMARK 500  6 LYS A  77       45.10    -85.35                                   
REMARK 500  6 GLU A 114       23.20    -75.97                                   
REMARK 500  6 LYS A 115      100.55     24.91                                   
REMARK 500  6 ASP A 131        4.06   -155.89                                   
REMARK 500  6 SER B  -1     -177.34     57.58                                   
REMARK 500  7 ASP A  56       49.07   -102.47                                   
REMARK 500  7 SER A  81      105.32     56.90                                   
REMARK 500  7 LYS A 115      107.59     36.04                                   
REMARK 500  7 VAL B1925       37.89    -76.71                                   
REMARK 500  8 ASN A  42       79.70   -159.71                                   
REMARK 500  8 ASP A  56       31.25    -90.87                                   
REMARK 500  8 LYS A 115      134.26     61.50                                   
REMARK 500  9 ASP A  95        6.69   -154.90                                   
REMARK 500  9 LYS A 115      119.60     60.55                                   
REMARK 500 10 LYS A 115      107.55     64.82                                   
REMARK 500 10 LYS B1901      -36.08   -143.01                                   
REMARK 500 11 ASP A  22      -10.47   -142.33                                   
REMARK 500 11 ASP A  56       52.48   -140.04                                   
REMARK 500 11 ASP A  80       31.61    -72.08                                   
REMARK 500 11 LYS A 115      103.70     39.88                                   
REMARK 500 11 ASP A 131       -5.64   -143.52                                   
REMARK 500 11 SER B  -1     -165.73    -77.99                                   
REMARK 500 12 ASP A  56       51.16   -118.23                                   
REMARK 500 12 ASP A  95        4.95   -153.85                                   
REMARK 500 12 GLU A 114       49.20    -78.10                                   
REMARK 500 12 LYS A 115      108.10     -4.47                                   
REMARK 500 12 SER B  -1       31.20    -72.73                                   
REMARK 500 12 LYS B1901       -7.34   -155.49                                   
REMARK 500 13 ASN A  42       77.37   -114.44                                   
REMARK 500 13 ASP A  56       48.43    -95.66                                   
REMARK 500 13 LYS A  75       36.37    -74.50                                   
REMARK 500 13 LYS A  77      -23.36     53.60                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      81 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500  1 TYR A  99         0.06    SIDE CHAIN                              
REMARK 500  3 TYR A  99         0.07    SIDE CHAIN                              
REMARK 500  4 TYR A  99         0.08    SIDE CHAIN                              
REMARK 500  9 TYR A  99         0.07    SIDE CHAIN                              
REMARK 500 10 TYR A  99         0.07    SIDE CHAIN                              
REMARK 500 13 TYR A  99         0.06    SIDE CHAIN                              
REMARK 500 13 ARG B1917         0.10    SIDE CHAIN                              
REMARK 500 14 TYR A  99         0.07    SIDE CHAIN                              
REMARK 500 15 TYR A  99         0.07    SIDE CHAIN                              
REMARK 500 16 TYR A  99         0.06    SIDE CHAIN                              
REMARK 500 16 TYR A 138         0.07    SIDE CHAIN                              
REMARK 500 19 TYR A  99         0.08    SIDE CHAIN                              
REMARK 500 20 TYR A  99         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 27094   RELATED DB: BMRB                                 
REMARK 900 RELATED ID: 27095   RELATED DB: BMRB                                 
DBREF  6BUT A    1   148  UNP    P0DP23   CALM1_HUMAN      2    149             
DBREF  6BUT B 1901  1927  UNP    Q99250   SCN2A_HUMAN   1901   1927             
SEQADV 6BUT GLY B   -4  UNP  Q99250              EXPRESSION TAG                 
SEQADV 6BUT PRO B   -3  UNP  Q99250              EXPRESSION TAG                 
SEQADV 6BUT GLY B   -2  UNP  Q99250              EXPRESSION TAG                 
SEQADV 6BUT SER B   -1  UNP  Q99250              EXPRESSION TAG                 
SEQRES   1 A  148  ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS          
SEQRES   2 A  148  GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR          
SEQRES   3 A  148  ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU          
SEQRES   4 A  148  GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE          
SEQRES   5 A  148  ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE          
SEQRES   6 A  148  PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP          
SEQRES   7 A  148  THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL          
SEQRES   8 A  148  PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU          
SEQRES   9 A  148  LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR          
SEQRES  10 A  148  ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE          
SEQRES  11 A  148  ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN          
SEQRES  12 A  148  MET MET THR ALA LYS                                          
SEQRES   1 B   31  GLY PRO GLY SER LYS ARG LYS GLN GLU GLU VAL SER ALA          
SEQRES   2 B   31  ILE ILE ILE GLN ARG ALA TYR ARG ARG TYR LEU LEU LYS          
SEQRES   3 B   31  GLN LYS VAL LYS LYS                                          
HELIX    1 AA1 THR A    5  LEU A   18  1                                  14    
HELIX    2 AA2 GLU A   31  LEU A   39  1                                   9    
HELIX    3 AA3 THR A   44  ASP A   56  1                                  13    
HELIX    4 AA4 PHE A   65  ASP A   78  1                                  14    
HELIX    5 AA5 SER A   81  ASP A   93  1                                  13    
HELIX    6 AA6 ALA A  102  LEU A  112  1                                  11    
HELIX    7 AA7 THR A  117  ASP A  129  1                                  13    
HELIX    8 AA8 ASN A  137  ALA A  147  1                                  11    
HELIX    9 AA9 LYS B 1901  LEU B 1921  1                                  21    
HELIX   10 AB1 LYS B 1922  VAL B 1925  5                                   4    
SHEET    1 AA1 2 THR A  26  THR A  28  0                                        
SHEET    2 AA1 2 THR A  62  ASP A  64 -1  O  ILE A  63   N  ILE A  27           
SHEET    1 AA2 2 ILE A 100  SER A 101  0                                        
SHEET    2 AA2 2 GLN A 135  VAL A 136 -1  O  VAL A 136   N  ILE A 100           
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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