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Database: PDB
Entry: 4GJG
LinkDB: 4GJG
Original site: 4GJG 
HEADER    CONTRACTILE PROTEIN                     09-AUG-12   4GJG              
TITLE     CRYSTAL STRUCTURE OF THE AMINO-TERMINAL DOMAIN OF HUMAN CARDIAC       
TITLE    2 TROPONIN C MUTANT D2N/V28I/L29Q/G30D (NIQD) IN COMPLEX WITH CADMIUM. 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TROPONIN C, SLOW SKELETAL AND CARDIAC MUSCLES;             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN (UNP RESIDUES 1-89);                     
COMPND   5 SYNONYM: TN-C;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TNNC, TNNC1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21A                                    
KEYWDS    HELIX-LOOP-HELIX EF-HAND MOTIF, CONTRACTILE PROTEIN, CALCIUM SENSOR,  
KEYWDS   2 CADMIUM BINDING                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.ZHANG,M.PAETZEL                                                     
REVDAT   3   15-NOV-17 4GJG    1       REMARK                                   
REVDAT   2   22-MAY-13 4GJG    1       JRNL                                     
REVDAT   1   06-FEB-13 4GJG    0                                                
JRNL        AUTH   X.L.ZHANG,G.F.TIBBITS,M.PAETZEL                              
JRNL        TITL   THE STRUCTURE OF CARDIAC TROPONIN C REGULATORY DOMAIN WITH   
JRNL        TITL 2 BOUND CD(2+) REVEALS A CLOSED CONFORMATION AND UNIQUE ION    
JRNL        TITL 3 COORDINATION.                                                
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  69   722 2013              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   23633581                                                     
JRNL        DOI    10.1107/S0907444913001182                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 6101                           
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) : 0.146                           
REMARK   3   R VALUE            (WORKING SET) : 0.144                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 281                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 418                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.21                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 21                           
REMARK   3   BIN FREE R VALUE                    : 0.1950                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 673                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 34                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.69                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.27000                                              
REMARK   3    B22 (A**2) : 0.27000                                              
REMARK   3    B33 (A**2) : -0.40000                                             
REMARK   3    B12 (A**2) : 0.13000                                              
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): 0.143         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.081         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.516         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   691 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):   924 ; 1.585 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):    84 ; 6.449 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    37 ;45.842 ;27.297       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   131 ;16.845 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     2 ;28.364 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   102 ; 0.114 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   521 ; 0.009 ; 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):   431 ; 2.074 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   689 ; 3.503 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   260 ; 5.687 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   235 ; 8.736 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  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):   691 ; 2.999 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 1.00                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 4GJG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000074259.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUL-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6190                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
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                : 9.200                              
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40900                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CADMIUM SULPHATE OCTAHYDRATE 0.02M,      
REMARK 280  SODIUM ACETATE 0.6M, 0.1M TRIS-HCL, PH 8.0, VAPOR DIFFUSION,        
REMARK 280  SITTING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.38033            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       76.76067            
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       57.57050            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       95.95083            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       19.19017            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       38.38033            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       76.76067            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       95.95083            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       57.57050            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       19.19017            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9540 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -163.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 228  LIES ON A SPECIAL POSITION.                          
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     ASP A    67                                                      
REMARK 465     GLY A    68                                                      
REMARK 465     SER A    69                                                      
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     ASP A   3    CG   OD1  OD2                                       
REMARK 470     ILE A   4    CG1  CG2  CD1                                       
REMARK 470     LYS A  39    CD   CE   NZ                                        
REMARK 470     GLU A  55    CG   CD   OE1  OE2                                  
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   OD2  ASP A    30     O    HOH A   225              1.38            
REMARK 500   OD1  ASP A    30     O    HOH A   218              1.98            
REMARK 500   O    HOH A   212     O    HOH A   213              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    ACT A   111     O    HOH A   208     5554     1.87            
REMARK 500   OE2  GLU A    59     O    HOH A   202     6555     2.09            
REMARK 500   OD1  ASP A    88    CD     CD A   103     8555     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    GLU A  32       -0.65   -145.46                                   
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                              CD A 107  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 210   O                                                      
REMARK 620 2 HOH A 209   O    79.2                                              
REMARK 620 3 ASP A  65   OD2  74.6  77.5                                        
REMARK 620 4 GLU A  76   OE1 168.9 111.9 108.4                                  
REMARK 620 5 GLU A  76   OE2 139.7  60.5  96.4  51.3                            
REMARK 620 6 THR A  71   O    79.9 148.0  73.7  90.5 136.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 108  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  19   OE2                                                    
REMARK 620 2 GLU A  19   OE1  55.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 104  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ACT A 111   OXT                                                    
REMARK 620 2 ASP A  33   OD1 136.0                                              
REMARK 620 3 CYS A  35   O    79.6  87.2                                        
REMARK 620 4 CYS A  35   SG  119.4 101.5  87.4                                  
REMARK 620 5 ASP A  33   OD2  83.5  52.8  80.3 151.7                            
REMARK 620 6 HOH A 203   O    93.0 100.2 172.0  93.8 101.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 101  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 202   O                                                      
REMARK 620 2 GLU A  40   OE2  90.0                                              
REMARK 620 3 GLU A  40   OE1  87.0  57.4                                        
REMARK 620 4 PHE A  27   O   169.3  99.9  95.0                                  
REMARK 620 5 HOH A 201   O    81.9 142.9  85.9  87.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 102  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  87   OD2                                                    
REMARK 620 2 GLU A  56   OE1 122.4                                              
REMARK 620 3 GLU A  56   OE2  85.1  57.3                                        
REMARK 620 4 CYS A  84   SG  111.3 123.4 115.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 105  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  66   OE2                                                    
REMARK 620 2 ASP A  73   OD2 128.0                                              
REMARK 620 3 ASP A  75   OD2  81.8 137.3                                        
REMARK 620 4 ASP A  75   OD1 136.7  89.0  55.0                                  
REMARK 620 5 ASP A  73   OD1 108.6  52.9  91.8  73.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 103  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  84   O                                                      
REMARK 620 2 ASP A  87   OD1  73.5                                              
REMARK 620 3 GLN A  50   OE1  78.8 149.0                                        
REMARK 620 4 CYS A  84   SG   91.4 106.1  87.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 106  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  59   OE1                                                    
REMARK 620 2 HOH A 206   O    65.1                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 103                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 104                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 105                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 106                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 107                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 108                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 110                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 111                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 112                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3SD6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CARDIAC TROPONIN C REGULATORY DOMAIN WITH       
REMARK 900 BOUND CD2+                                                           
REMARK 900 RELATED ID: 3SWB   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE AMINO-TERMINAL DOMAIN OF HUMAN CARDIAC      
REMARK 900 TROPONIN C IN COMPLEX WITH CADMIUM                                   
REMARK 900 RELATED ID: 1AP4   RELATED DB: PDB                                   
REMARK 900 CALCIUM BOUND HUMAN N-CTNC                                           
REMARK 900 RELATED ID: 1J1D   RELATED DB: PDB                                   
REMARK 900 FULL LENGTH & CALCUIM SATURATED HUMAN CTNC IN COMPLEX WITH CTNI AND  
REMARK 900 CTNT                                                                 
REMARK 900 RELATED ID: 1MXL   RELATED DB: PDB                                   
REMARK 900 CALCIUM BOUND HUMAN N-CTNC IN COMPLEX WITH CTNI (147-163)            
REMARK 900 RELATED ID: 1SPY   RELATED DB: PDB                                   
REMARK 900 CALCIUM FREE HUMAN N-CTNC                                            
REMARK 900 RELATED ID: 4GJF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4GJE   RELATED DB: PDB                                   
DBREF  4GJG A    1    89  UNP    P63316   TNNC1_HUMAN      1     89             
SEQADV 4GJG ASN A    2  UNP  P63316    ASP     2 ENGINEERED MUTATION            
SEQADV 4GJG ILE A   28  UNP  P63316    VAL    28 ENGINEERED MUTATION            
SEQADV 4GJG GLN A   29  UNP  P63316    LEU    29 ENGINEERED MUTATION            
SEQADV 4GJG ASP A   30  UNP  P63316    GLY    30 ENGINEERED MUTATION            
SEQRES   1 A   89  MET ASN ASP ILE TYR LYS ALA ALA VAL GLU GLN LEU THR          
SEQRES   2 A   89  GLU GLU GLN LYS ASN GLU PHE LYS ALA ALA PHE ASP ILE          
SEQRES   3 A   89  PHE ILE GLN ASP ALA GLU ASP GLY CYS ILE SER THR LYS          
SEQRES   4 A   89  GLU LEU GLY LYS VAL MET ARG MET LEU GLY GLN ASN PRO          
SEQRES   5 A   89  THR PRO GLU GLU LEU GLN GLU MET ILE ASP GLU VAL ASP          
SEQRES   6 A   89  GLU ASP GLY SER GLY THR VAL ASP PHE ASP GLU PHE LEU          
SEQRES   7 A   89  VAL MET MET VAL ARG CYS MET LYS ASP ASP SER                  
HET     CD  A 101       1                                                       
HET     CD  A 102       1                                                       
HET     CD  A 103       1                                                       
HET     CD  A 104       1                                                       
HET     CD  A 105       1                                                       
HET     CD  A 106       1                                                       
HET     CD  A 107       1                                                       
HET     CA  A 108       1                                                       
HET     CA  A 109       1                                                       
HET     CA  A 110       1                                                       
HET    ACT  A 111       4                                                       
HET    GOL  A 112       6                                                       
HETNAM      CD CADMIUM ION                                                      
HETNAM      CA CALCIUM ION                                                      
HETNAM     ACT ACETATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2   CD    7(CD 2+)                                                     
FORMUL   9   CA    3(CA 2+)                                                     
FORMUL  12  ACT    C2 H3 O2 1-                                                  
FORMUL  13  GOL    C3 H8 O3                                                     
FORMUL  14  HOH   *34(H2 O)                                                     
HELIX    1   1 ASN A    2  GLU A   10  1                                   9    
HELIX    2   2 THR A   13  ILE A   26  1                                  14    
HELIX    3   3 THR A   38  LEU A   48  1                                  11    
HELIX    4   4 THR A   53  ASP A   65  1                                  13    
HELIX    5   5 ASP A   73  LYS A   86  1                                  14    
SHEET    1   A 2 ILE A  36  SER A  37  0                                        
SHEET    2   A 2 THR A  71  VAL A  72 -1  O  VAL A  72   N  ILE A  36           
LINK        CD    CD A 107                 O   HOH A 210     1555   1555  1.77  
LINK         OE2 GLU A  19                CA    CA A 108     1555   1555  1.89  
LINK        CD    CD A 104                 OXT ACT A 111     1555   1555  1.94  
LINK        CD    CD A 101                 O   HOH A 202     1555   1555  1.97  
LINK        CD    CD A 107                 O   HOH A 209     1555   1555  2.02  
LINK         OD2 ASP A  87                CD    CD A 102     1555   1555  2.11  
LINK         OE2 GLU A  66                CD    CD A 105     1555   1555  2.15  
LINK         OD2 ASP A  73                CD    CD A 105     1555   1555  2.21  
LINK         O   CYS A  84                CD    CD A 103     1555   1555  2.24  
LINK         OE1 GLU A  59                CD    CD A 106     1555   1555  2.24  
LINK         OE2 GLU A  40                CD    CD A 101     1555   1555  2.25  
LINK         OE1 GLU A  56                CD    CD A 102     1555   1555  2.28  
LINK         OE2 GLU A  56                CD    CD A 102     1555   1555  2.28  
LINK         OD1 ASP A  33                CD    CD A 104     1555   1555  2.28  
LINK         OD2 ASP A  65                CD    CD A 107     1555   1555  2.28  
LINK         OE1 GLU A  40                CD    CD A 101     1555   1555  2.30  
LINK         OD2 ASP A  75                CD    CD A 105     1555   1555  2.30  
LINK         OD1 ASP A  87                CD    CD A 103     1555   1555  2.34  
LINK         O   PHE A  27                CD    CD A 101     1555   1555  2.37  
LINK        CD    CD A 101                 O   HOH A 201     1555   1555  2.37  
LINK         OE1 GLN A  50                CD    CD A 103     1555   1555  2.39  
LINK         OE1 GLU A  76                CD    CD A 107     1555   1555  2.40  
LINK         OD1 ASP A  75                CD    CD A 105     1555   1555  2.42  
LINK         O   CYS A  35                CD    CD A 104     1555   1555  2.47  
LINK        CD    CD A 106                 O   HOH A 206     1555   1555  2.47  
LINK         SG  CYS A  35                CD    CD A 104     1555   1555  2.48  
LINK         SG  CYS A  84                CD    CD A 102     1555   1555  2.51  
LINK         SG  CYS A  84                CD    CD A 103     1555   1555  2.54  
LINK         OD2 ASP A  33                CD    CD A 104     1555   1555  2.55  
LINK         OD1 ASP A  73                CD    CD A 105     1555   1555  2.60  
LINK         OE2 GLU A  76                CD    CD A 107     1555   1555  2.61  
LINK         OE1 GLU A  19                CA    CA A 108     1555   1555  2.61  
LINK         O   THR A  71                CD    CD A 107     1555   1555  2.61  
LINK        CD    CD A 104                 O   HOH A 203     1555   1555  2.61  
LINK         OE2 GLU A  19                CA    CA A 110     1555   1555  2.72  
SITE     1 AC1  5 PHE A  27  GLU A  40  GLU A  63  HOH A 201                    
SITE     2 AC1  5 HOH A 202                                                     
SITE     1 AC2  5 GLU A  56  CYS A  84  ASP A  87  SER A  89                    
SITE     2 AC2  5  CD A 103                                                     
SITE     1 AC3  6 GLN A  50  CYS A  84  ASP A  87  ASP A  88                    
SITE     2 AC3  6 SER A  89   CD A 102                                          
SITE     1 AC4  4 ASP A  33  CYS A  35  ACT A 111  HOH A 203                    
SITE     1 AC5  4 CYS A  35  GLU A  66  ASP A  73  ASP A  75                    
SITE     1 AC6  3 MET A   1  GLU A  59  HOH A 206                               
SITE     1 AC7  6 ASP A  65  THR A  71  GLU A  76  HOH A 209                    
SITE     2 AC7  6 HOH A 210  HOH A 211                                          
SITE     1 AC8  3 GLU A  10  GLU A  15  GLU A  19                               
SITE     1 AC9  2 GLU A  15  GLU A  19                                          
SITE     1 BC1  9 MET A   1  ASP A  33  CYS A  35  ILE A  36                    
SITE     2 BC1  9 SER A  37  THR A  71   CD A 104  HOH A 201                    
SITE     3 BC1  9 HOH A 208                                                     
SITE     1 BC2  2 LYS A  17  GLU A  32                                          
CRYST1   49.583   49.583  115.141  90.00  90.00 120.00 P 61 2 2     12          
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      0.020168  0.011644  0.000000        0.00000                         
SCALE2      0.000000  0.023288  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008685        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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