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    HEADER    HORMONE/GROWTH FACTOR                   09-NOV-00   1G7A              
    TITLE     1.2 A STRUCTURE OF T3R3 HUMAN INSULIN AT 100 K                        
    COMPND    MOL_ID: 1;                                                            
    COMPND   2 MOLECULE: INSULIN A-CHAIN;                                           
    COMPND   3 CHAIN: A, C, E, G;                                                   
    COMPND   4 FRAGMENT: A-CHAIN;                                                   
    COMPND   5 ENGINEERED: YES;                                                     
    COMPND   6 MOL_ID: 2;                                                           
    COMPND   7 MOLECULE: INSULIN B-CHAIN;                                           
    COMPND   8 CHAIN: B, D, F, H;                                                   
    COMPND   9 FRAGMENT: B-CHAIN;                                                   
    COMPND  10 ENGINEERED: YES                                                      
    SOURCE    MOL_ID: 1;                                                            
    SOURCE   2 SYNTHETIC: YES;                                                      
    SOURCE   3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HOMO                
    SOURCE   4 SAPIENS (HUMAN);                                                     
    SOURCE   5 MOL_ID: 2;                                                           
    SOURCE   6 SYNTHETIC: YES;                                                      
    SOURCE   7 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HOMO                
    SOURCE   8 SAPIENS (HUMAN)                                                      
    KEYWDS    T3R3 INSULIN HEXAMER, HORMONE/GROWTH FACTOR COMPLEX                   
    EXPDTA    X-RAY DIFFRACTION                                                     
    AUTHOR    G.D.SMITH,W.A.PANGBORN,R.H.BLESSING                                   
    REVDAT   3   24-FEB-09 1G7A    1       VERSN                                    
    REVDAT   2   12-APR-05 1G7A    3       SCALE1 SCALE2 SCALE3 REMARK              
    REVDAT   1   03-AUG-01 1G7A    0                                                
    JRNL        AUTH   G.D.SMITH,W.A.PANGBORN,R.H.BLESSING                          
    JRNL        TITL   PHASE CHANGES IN T(3)R(3)(F) HUMAN INSULIN:                  
    JRNL        TITL 2 TEMPERATURE OR PRESSURE INDUCED?                             
    JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  57  1091 2001              
    JRNL        REFN                   ISSN 0907-4449                               
    JRNL        PMID   11468392                                                     
    JRNL        DOI    10.1107/S0907444901007685                                    
    REMARK   1                                                                      
    REMARK   1 REFERENCE 1                                                          
    REMARK   1  AUTH   J.L.WHITTINGHAM,S.CHAUDHURI,E.J.DODSON,P.C.E.MOODY,          
    REMARK   1  AUTH 2 G.G.DODSON                                                   
    REMARK   1  TITL   X-RAY CRYSTALLOGRAPHIC STUDIES ON HEXAMERIC                  
    REMARK   1  TITL 2 INSULINS IN THE PRESENCE OF HELIX-STABILIZING                
    REMARK   1  TITL 3 AGENTS, THIOCYANATE, METHYLPARABEN, AND PHENOL               
    REMARK   1  REF    BIOCHEMISTRY                  V.  34 15553 1995              
    REMARK   1  REFN                   ISSN 0006-2960                               
    REMARK   1 REFERENCE 2                                                          
    REMARK   1  AUTH   E.CISZAK,G.D.SMITH                                           
    REMARK   1  TITL   CRYSTALLOGRAPHIC EVIDENCE FOR DUAL COORDINATION              
    REMARK   1  TITL 2 AROUND ZINC IN THE T3R3 HUMAN INSULIN HEXAMER                
    REMARK   1  REF    BIOCHEMISTRY                  V.  33  1512 1994              
    REMARK   1  REFN                   ISSN 0006-2960                               
    REMARK   1 REFERENCE 3                                                          
    REMARK   1  AUTH   G.D.SMITH,D.C.SWENSON,E.J.DODSON,G.G.DODSON,                 
    REMARK   1  AUTH 2 C.D.REYNOLDS                                                 
    REMARK   1  TITL   STRUCTURAL STABILITY IN THE 4-ZINC HUMAN INSULIN             
    REMARK   1  TITL 2 HEXAMER                                                      
    REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  81  7093 1984              
    REMARK   1  REFN                   ISSN 0027-8424                               
    REMARK   1 REFERENCE 4                                                          
    REMARK   1  AUTH   G.BENTLEY,E.DODSON,G.G.DODSON,D.HODGKIN,D.MERCOLA            
    REMARK   1  TITL   STRUCTURE OF 4-ZINC INSULIN                                  
    REMARK   1  REF    NATURE                        V. 261   166 1976              
    REMARK   1  REFN                   ISSN 0028-0836                               
    REMARK   1 REFERENCE 5                                                          
    REMARK   1  AUTH   R.B.VON DREELE,P.W.STEPHENS,G.D.SMITH,R.H.BLESSING           
    REMARK   1  TITL   THE FIRST PROTEIN CRYSTAL STRUCTURE DETERMINED               
    REMARK   1  TITL 2 FROM HIGH RESOLUTION X-RAY POWDER DIFFRACTION                
    REMARK   1  TITL 3 DATA: A VARIANT OF T3R3 HUMAN INSULIN ZINC COMPLEX           
    REMARK   1  TITL 4 PRODUCED BY GRINDING                                         
    REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  56  1549 2000              
    REMARK   1  REFN                   ISSN 0907-4449                               
    REMARK   1  DOI    10.1107/S0907444900013901                                    
    REMARK   2                                                                      
    REMARK   2 RESOLUTION.    1.20 ANGSTROMS.                                       
    REMARK   3                                                                      
    REMARK   3 REFINEMENT.                                                          
    REMARK   3   PROGRAM     : CNS 1.0                                              
    REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
    REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
    REMARK   3               : READ,RICE,SIMONSON,WARREN                            
    REMARK   3                                                                      
    REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
    REMARK   3                                                                      
    REMARK   3  DATA USED IN REFINEMENT.                                            
    REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20                           
    REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.20                          
    REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
    REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
    REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
    REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 100.0                          
    REMARK   3   NUMBER OF REFLECTIONS             : 53646                          
    REMARK   3                                                                      
    REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
    REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
    REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
    REMARK   3   R VALUE            (WORKING SET) : 0.169                           
    REMARK   3   FREE R VALUE                     : 0.193                           
    REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.200                          
    REMARK   3   FREE R VALUE TEST SET COUNT      : 5461                            
    REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
    REMARK   3                                                                      
    REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
    REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
    REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.20                         
    REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.28                         
    REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
    REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 8098                         
    REMARK   3   BIN R VALUE           (WORKING SET) : 0.2400                       
    REMARK   3   BIN FREE R VALUE                    : 0.2590                       
    REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.90                         
    REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 888                          
    REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.009                        
    REMARK   3                                                                      
    REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
    REMARK   3   PROTEIN ATOMS            : 3293                                    
    REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
    REMARK   3   HETEROGEN ATOMS          : 28                                      
    REMARK   3   SOLVENT ATOMS            : 355                                     
    REMARK   3                                                                      
    REMARK   3  B VALUES.                                                           
    REMARK   3   FROM WILSON PLOT           (A**2) : 17.60                          
    REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.00                          
    REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
    REMARK   3    B11 (A**2) : -0.51000                                             
    REMARK   3    B22 (A**2) : -0.51000                                             
    REMARK   3    B33 (A**2) : 1.03000                                              
    REMARK   3    B12 (A**2) : -0.04000                                             
    REMARK   3    B13 (A**2) : 0.00000                                              
    REMARK   3    B23 (A**2) : 0.00000                                              
    REMARK   3                                                                      
    REMARK   3  ESTIMATED COORDINATE ERROR.                                         
    REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.12                            
    REMARK   3   ESD FROM SIGMAA              (A) : 0.11                            
    REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
    REMARK   3                                                                      
    REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
    REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.13                            
    REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.12                            
    REMARK   3                                                                      
    REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
    REMARK   3   BOND LENGTHS                 (A) : 0.009                           
    REMARK   3   BOND ANGLES            (DEGREES) : 1.88                            
    REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.60                           
    REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.92                            
    REMARK   3                                                                      
    REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
    REMARK   3                                                                      
    REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
    REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.990 ; 2.000                
    REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.750 ; 2.500                
    REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.290 ; 2.500                
    REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.800 ; 3.000                
    REMARK   3                                                                      
    REMARK   3  BULK SOLVENT MODELING.                                              
    REMARK   3   METHOD USED : FLAT MODEL                                           
    REMARK   3   KSOL        : 0.44                                                 
    REMARK   3   BSOL        : 73.90                                                
    REMARK   3                                                                      
    REMARK   3  NCS MODEL : NULL                                                    
    REMARK   3                                                                      
    REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
    REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
    REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
    REMARK   3                                                                      
    REMARK   3  PARAMETER FILE  1  : NULL                                           
    REMARK   3  TOPOLOGY FILE  1   : NULL                                           
    REMARK   3                                                                      
    REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
    REMARK   4                                                                      
    REMARK   4 1G7A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
    REMARK 100                                                                      
    REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-00.                  
    REMARK 100 THE RCSB ID CODE IS RCSB012322.                                      
    REMARK 200                                                                      
    REMARK 200 EXPERIMENTAL DETAILS                                                 
    REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
    REMARK 200  DATE OF DATA COLLECTION        : 20-MAR-99                          
    REMARK 200  TEMPERATURE           (KELVIN) : 100                                
    REMARK 200  PH                             : 6.3                                
    REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
    REMARK 200                                                                      
    REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
    REMARK 200  RADIATION SOURCE               : NSLS                               
    REMARK 200  BEAMLINE                       : X8C                                
    REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
    REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
    REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8000                             
    REMARK 200  MONOCHROMATOR                  : SILICON                            
    REMARK 200  OPTICS                         : NULL                               
    REMARK 200                                                                      
    REMARK 200  DETECTOR TYPE                  : CCD                                
    REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
    REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
    REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
    REMARK 200                                                                      
    REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53646                              
    REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.200                              
    REMARK 200  RESOLUTION RANGE LOW       (A) : 31.200                             
    REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
    REMARK 200                                                                      
    REMARK 200 OVERALL.                                                             
    REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
    REMARK 200  DATA REDUNDANCY                : 8.600                              
    REMARK 200  R MERGE                    (I) : 0.04900                            
    REMARK 200  R SYM                      (I) : NULL                               
    REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 42.8000                            
    REMARK 200                                                                      
    REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
    REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20                     
    REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.23                     
    REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
    REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
    REMARK 200  R MERGE FOR SHELL          (I) : 0.29900                            
    REMARK 200  R SYM FOR SHELL            (I) : NULL                               
    REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.100                              
    REMARK 200                                                                      
    REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
    REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
    REMARK 200 SOFTWARE USED: CNS                                                   
    REMARK 200 STARTING MODEL: PDB ENTRY 1TRZ                                       
    REMARK 200                                                                      
    REMARK 200 REMARK: NULL                                                         
    REMARK 280                                                                      
    REMARK 280 CRYSTAL                                                              
    REMARK 280 SOLVENT CONTENT, VS   (%): 35.26                                     
    REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90                     
    REMARK 280                                                                      
    REMARK 280 CRYSTALLIZATION CONDITIONS: 5 MG/ML HUMAN INSULIN, 0.01 M HCL,       
    REMARK 280  0.007 M ZINC ACETATE, 0.05 M SODIUM CITRATE, 17% ACETONE, 1.0       
    REMARK 280  M NACL. PH 6.3, SLOW COOLING AT 298K                                
    REMARK 290                                                                      
    REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
    REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
    REMARK 290                                                                      
    REMARK 290      SYMOP   SYMMETRY                                                
    REMARK 290     NNNMMM   OPERATOR                                                
    REMARK 290       1555   X,Y,Z                                                   
    REMARK 290       2555   -Y,X-Y,Z                                                
    REMARK 290       3555   -X+Y,-X,Z                                               
    REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
    REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
    REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
    REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
    REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
    REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
    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        0.00000            
    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        0.00000            
    REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.06350            
    REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.13067            
    REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       23.86067            
    REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       40.06350            
    REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       23.13067            
    REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       23.86067            
    REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       40.06350            
    REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       23.13067            
    REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       23.86067            
    REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
    REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       46.26135            
    REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       47.72133            
    REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
    REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       46.26135            
    REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       47.72133            
    REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
    REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       46.26135            
    REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       47.72133            
    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 300 REMARK: THE SECOND DIMER OF THE T3R3 INSULIN HEXAMER IS              
    REMARK 300 GENERATED BY THE CRYSTALLOGRAPHIC THREE-FOLD AXIS: -Y, X-Y, Z        
    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: DODECAMERIC                       
    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 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
    REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
    REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
    REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
    REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
    REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
    REMARK 350                                                                      
    REMARK 350 BIOMOLECULE: 2                                                       
    REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC                       
    REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
    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 -0.500000 -0.866025  0.000000        0.00000            
    REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
    REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
    REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
    REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
    REMARK 350   BIOMT3   3  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 ZN    ZN B 901  LIES ON A SPECIAL POSITION.                          
    REMARK 375 ZN    ZN D 911  LIES ON A SPECIAL POSITION.                          
    REMARK 375 ZN    ZN F 931  LIES ON A SPECIAL POSITION.                          
    REMARK 375 ZN    ZN H 941  LIES ON A SPECIAL POSITION.                          
    REMARK 375 CL    CL B 902  LIES ON A SPECIAL POSITION.                          
    REMARK 375 CL    CL D 912  LIES ON A SPECIAL POSITION.                          
    REMARK 375 CL    CL F 932  LIES ON A SPECIAL POSITION.                          
    REMARK 375 CL    CL H 942  LIES ON A SPECIAL POSITION.                          
    REMARK 375      HOH B1214  LIES ON A SPECIAL POSITION.                          
    REMARK 375      HOH D1150  LIES ON A SPECIAL POSITION.                          
    REMARK 375      HOH D1814  LIES ON A SPECIAL POSITION.                          
    REMARK 375      HOH D1950  LIES ON A SPECIAL POSITION.                          
    REMARK 375      HOH F1181  LIES ON A SPECIAL POSITION.                          
    REMARK 375      HOH F1870  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     THR D    30                                                      
    REMARK 465     PHE H     1                                                      
    REMARK 465     THR H    30                                                      
    REMARK 470                                                                      
    REMARK 470 MISSING ATOM                                                         
    REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
    REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
    REMARK 470 I=INSERTION CODE):                                                   
    REMARK 470   M RES CSSEQI  ATOMS                                                
    REMARK 470     LYS B  29    CG   CD   CE   NZ                                   
    REMARK 470     THR B  30    OG1  CG2                                            
    REMARK 470     LYS D  29    CG   CD   CE   NZ                                   
    REMARK 470     VAL H   2    CG1  CG2                                            
    REMARK 470     GLN H   4    CG   CD   OE1  NE2                                  
    REMARK 470     LYS H  29    CG   CD   CE   NZ                                   
    REMARK 525                                                                      
    REMARK 525 SOLVENT                                                              
    REMARK 525                                                                      
    REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
    REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
    REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
    REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
    REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
    REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
    REMARK 525 NUMBER; I=INSERTION CODE):                                           
    REMARK 525                                                                      
    REMARK 525  M RES CSSEQI                                                        
    REMARK 525    HOH B1301        DISTANCE =  6.38 ANGSTROMS                       
    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                              ZN B 961  ZN                            
    REMARK 620 N RES CSSEQI ATOM                                                    
    REMARK 620 1 HIS B   5   ND1                                                    
    REMARK 620 2 HOH B 964   O   128.9                                              
    REMARK 620 3 HOH B1811   O   108.4  37.9                                        
    REMARK 620 4 HOH B 963   O    94.4  96.6 133.6                                  
    REMARK 620 5 HOH B 962   O   111.9 109.6  96.5 111.9                            
    REMARK 620 6 HOH B1810   O    72.0 131.3 166.6  34.8  95.6                      
    REMARK 620 N                    1     2     3     4     5                       
    REMARK 620                                                                      
    REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
    REMARK 620                              ZN B 951  ZN                            
    REMARK 620 N RES CSSEQI ATOM                                                    
    REMARK 620 1 HIS B   5   CE1                                                    
    REMARK 620 2 HIS B   5   NE2  36.3                                              
    REMARK 620 3 HIS B   5   NE2  32.3   8.6                                        
    REMARK 620 4 HOH B 952   O    71.0 102.2 101.8                                  
    REMARK 620 5 HOH B 953   O   139.2 106.3 113.2 120.9                            
    REMARK 620 6 HIS H   5   NE2 111.2 117.3 109.9 110.0 101.0                      
    REMARK 620 N                    1     2     3     4     5                       
    REMARK 620                                                                      
    REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
    REMARK 620                              ZN B 901  ZN                            
    REMARK 620 N RES CSSEQI ATOM                                                    
    REMARK 620 1 HIS B  10   NE2                                                    
    REMARK 620 2  CL B 902  CL   112.2                                              
    REMARK 620 3 HIS B  10   NE2 106.6 112.2                                        
    REMARK 620 4 HIS B  10   NE2 106.6 112.2 106.6                                  
    REMARK 620 5  CL B 902  CL   112.2   0.0 112.2 112.2                            
    REMARK 620 6  CL B 902  CL   112.2   0.0 112.2 112.2   0.0                      
    REMARK 620 N                    1     2     3     4     5                       
    REMARK 620                                                                      
    REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
    REMARK 620                              ZN D 921  ZN                            
    REMARK 620 N RES CSSEQI ATOM                                                    
    REMARK 620 1 HIS D  10   NE2                                                    
    REMARK 620 2  CL D 923  CL   108.5                                              
    REMARK 620 3  CL D 922  CL   105.4 117.1                                        
    REMARK 620 4 HIS D   5   NE2 104.1 107.2 113.7                                  
    REMARK 620 N                    1     2     3                                   
    REMARK 620                                                                      
    REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
    REMARK 620                              ZN D 911  ZN                            
    REMARK 620 N RES CSSEQI ATOM                                                    
    REMARK 620 1 HIS D  10   NE2                                                    
    REMARK 620 2 HOH D1812   O    53.0                                              
    REMARK 620 3  CL D 912  CL   114.7 100.5                                        
    REMARK 620 4 HOH D1812   O    64.0 116.8 100.5                                  
    REMARK 620 5 HOH D1812   O   144.3 116.8 100.5 116.8                            
    REMARK 620 6  CL D 912  CL   114.7 100.5   0.0 100.5 100.5                      
    REMARK 620 7  CL D 912  CL   114.7 100.5   0.0 100.5 100.5   0.0                
    REMARK 620 N                    1     2     3     4     5     6                 
    REMARK 620                                                                      
    REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
    REMARK 620                              ZN F 931  ZN                            
    REMARK 620 N RES CSSEQI ATOM                                                    
    REMARK 620 1 HIS F  10   NE2                                                    
    REMARK 620 2 HOH F 933   O    94.8                                              
    REMARK 620 3  CL F 932  CL   114.8  36.3                                        
    REMARK 620 4 HIS F  10   NE2 103.6  93.2 114.8                                  
    REMARK 620 5 HIS F  10   NE2 103.6 151.1 114.8 103.6                            
    REMARK 620 6  CL F 932  CL   114.8  36.3   0.0 114.8 114.8                      
    REMARK 620 7  CL F 932  CL   114.8  36.3   0.0 114.8 114.8   0.0                
    REMARK 620 8 HOH F 933   O   151.1  61.7  36.3  94.8  93.2  36.3  36.3          
    REMARK 620 9 HOH F 933   O    93.2  61.7  36.3 151.1  94.8  36.3  36.3  61.7    
    REMARK 620 N                    1     2     3     4     5     6     7     8     
    REMARK 620                                                                      
    REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
    REMARK 620                              ZN H 941  ZN                            
    REMARK 620 N RES CSSEQI ATOM                                                    
    REMARK 620 1 HIS H  10   NE2                                                    
    REMARK 620 2  CL H 942  CL   108.7                                              
    REMARK 620 3 HIS H  10   NE2 110.2 108.7                                        
    REMARK 620 4 HIS H  10   NE2 110.2 108.7 110.2                                  
    REMARK 620 5  CL H 942  CL   108.7   0.0 108.7 108.7                            
    REMARK 620 6  CL H 942  CL   108.7   0.0 108.7 108.7   0.0                      
    REMARK 620 N                    1     2     3     4     5                       
    REMARK 800                                                                      
    REMARK 800 SITE                                                                 
    REMARK 800 SITE_IDENTIFIER: AC1                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 901                  
    REMARK 800 SITE_IDENTIFIER: AC2                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 911                  
    REMARK 800 SITE_IDENTIFIER: AC3                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 921                  
    REMARK 800 SITE_IDENTIFIER: AC4                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 931                  
    REMARK 800 SITE_IDENTIFIER: AC5                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 941                  
    REMARK 800 SITE_IDENTIFIER: AC6                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 951                  
    REMARK 800 SITE_IDENTIFIER: AC7                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 961                  
    REMARK 800 SITE_IDENTIFIER: AC8                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 902                  
    REMARK 800 SITE_IDENTIFIER: AC9                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 912                  
    REMARK 800 SITE_IDENTIFIER: BC1                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 922                  
    REMARK 800 SITE_IDENTIFIER: BC2                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 923                  
    REMARK 800 SITE_IDENTIFIER: BC3                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 932                  
    REMARK 800 SITE_IDENTIFIER: BC4                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 942                  
    REMARK 800 SITE_IDENTIFIER: BC5                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 1101                 
    REMARK 800 SITE_IDENTIFIER: BC6                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 995                 
    REMARK 800 SITE_IDENTIFIER: BC7                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACN G 991                 
    REMARK 800 SITE_IDENTIFIER: BC8                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACN F 992                 
    REMARK 900                                                                      
    REMARK 900 RELATED ENTRIES                                                      
    REMARK 900 RELATED ID: 1TRZ   RELATED DB: PDB                                   
    REMARK 900 ROOM TEMPERATURE STRUCTURE OF T3R3 HUMAN INSULIN                     
    REMARK 900 RELATED ID: 1TCI   RELATED DB: PDB                                   
    REMARK 900 ROOM TEMPERATURE STRUCTURE OF T3R3 PORCINE INSULIN                   
    REMARK 900 RELATED ID: 1ZNI   RELATED DB: PDB                                   
    REMARK 900 ROOM TEMPERATURE STRUCTURE OF T3R3 PORCINE INSULIN                   
    REMARK 900 RELATED ID: 1G7B   RELATED DB: PDB                                   
    REMARK 900 1.3 A STRUCTURE OF T3R3 HUMAN INSULIN AT 100 K                       
    DBREF  1G7A A    1    21  UNP    P01308   INS_HUMAN       87    107             
    DBREF  1G7A C    1    21  UNP    P01308   INS_HUMAN       87    107             
    DBREF  1G7A E    1    21  UNP    P01308   INS_HUMAN       87    107             
    DBREF  1G7A G    1    21  UNP    P01308   INS_HUMAN       87    107             
    DBREF  1G7A B    1    30  UNP    P01308   INS_HUMAN       25     54             
    DBREF  1G7A D    1    30  UNP    P01308   INS_HUMAN       25     54             
    DBREF  1G7A F    1    30  UNP    P01308   INS_HUMAN       25     54             
    DBREF  1G7A H    1    30  UNP    P01308   INS_HUMAN       25     54             
    SEQRES   1 A   21  GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU          
    SEQRES   2 A   21  TYR GLN LEU GLU ASN TYR CYS ASN                              
    SEQRES   1 B   30  PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU          
    SEQRES   2 B   30  ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR          
    SEQRES   3 B   30  THR PRO LYS THR                                              
    SEQRES   1 C   21  GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU          
    SEQRES   2 C   21  TYR GLN LEU GLU ASN TYR CYS ASN                              
    SEQRES   1 D   30  PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU          
    SEQRES   2 D   30  ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR          
    SEQRES   3 D   30  THR PRO LYS THR                                              
    SEQRES   1 E   21  GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU          
    SEQRES   2 E   21  TYR GLN LEU GLU ASN TYR CYS ASN                              
    SEQRES   1 F   30  PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU          
    SEQRES   2 F   30  ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR          
    SEQRES   3 F   30  THR PRO LYS THR                                              
    SEQRES   1 G   21  GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU          
    SEQRES   2 G   21  TYR GLN LEU GLU ASN TYR CYS ASN                              
    SEQRES   1 H   30  PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU          
    SEQRES   2 H   30  ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR          
    SEQRES   3 H   30  THR PRO LYS THR                                              
    HET     ZN  B 901       1                                                       
    HET     ZN  D 911       1                                                       
    HET     ZN  D 921       1                                                       
    HET     ZN  F 931       1                                                       
    HET     ZN  H 941       1                                                       
    HET     ZN  B 951       1                                                       
    HET     ZN  B 961       1                                                       
    HET     CL  B 902       1                                                       
    HET     CL  D 912       1                                                       
    HET     CL  D 922       1                                                       
    HET     CL  D 923       1                                                       
    HET     CL  F 932       1                                                       
    HET     CL  H 942       1                                                       
    HET     CL  E1101       1                                                       
    HET    GOL  G 995      14                                                       
    HET    ACN  G 991      10                                                       
    HET    ACN  F 992      10                                                       
    HETNAM      ZN ZINC ION                                                         
    HETNAM      CL CHLORIDE ION                                                     
    HETNAM     GOL GLYCEROL                                                         
    HETNAM     ACN ACETONE                                                          
    FORMUL   9   ZN    7(ZN 2+)                                                     
    FORMUL  16   CL    7(CL 1-)                                                     
    FORMUL  23  GOL    C3 H8 O3                                                     
    FORMUL  24  ACN    2(C3 H6 O)                                                   
    FORMUL  26  HOH   *275(H2 O)                                                    
    HELIX    1   1 GLY A    1  CYS A    7  1                                   7    
    HELIX    2   2 SER A   12  ASN A   18  1                                   7    
    HELIX    3   3 CYS B    7  GLY B   20  1                                  14    
    HELIX    4   4 GLU B   21  GLY B   23  5                                   3    
    HELIX    5   5 GLY C    1  CYS C    7  1                                   7    
    HELIX    6   6 SER C   12  GLU C   17  1                                   6    
    HELIX    7   7 ASN D    3  GLY D   20  1                                  18    
    HELIX    8   8 GLU D   21  GLY D   23  5                                   3    
    HELIX    9   9 GLY E    1  CYS E    7  1                                   7    
    HELIX   10  10 SER E   12  GLU E   17  1                                   6    
    HELIX   11  11 CYS F    7  GLY F   20  1                                  14    
    HELIX   12  12 GLU F   21  GLY F   23  5                                   3    
    HELIX   13  13 GLY G    1  THR G    8  1                                   8    
    HELIX   14  14 SER G   12  GLU G   17  1                                   6    
    HELIX   15  15 ASN H    3  GLY H   20  1                                  18    
    HELIX   16  16 GLU H   21  GLY H   23  5                                   3    
    SHEET    1   A 2 PHE B  24  TYR B  26  0                                        
    SHEET    2   A 2 PHE D  24  TYR D  26 -1  O  PHE D  24   N  TYR B  26           
    SHEET    1   B 2 PHE F  24  TYR F  26  0                                        
    SHEET    2   B 2 PHE H  24  TYR H  26 -1  O  PHE H  24   N  TYR F  26           
    SSBOND   1 CYS A    6    CYS A   11                          1555   1555  2.02  
    SSBOND   2 CYS A    7    CYS B    7                          1555   1555  2.05  
    SSBOND   3 CYS A   20    CYS B   19                          1555   1555  2.04  
    SSBOND   4 CYS C    6    CYS C   11                          1555   1555  2.03  
    SSBOND   5 CYS C    7    CYS D    7                          1555   1555  2.02  
    SSBOND   6 CYS C   20    CYS D   19                          1555   1555  2.01  
    SSBOND   7 CYS E    6    CYS E   11                          1555   1555  1.97  
    SSBOND   8 CYS E    7    CYS F    7                          1555   1555  2.03  
    SSBOND   9 CYS E   20    CYS F   19                          1555   1555  2.02  
    SSBOND  10 CYS G    6    CYS G   11                          1555   1555  2.01  
    SSBOND  11 CYS G    7    CYS H    7                          1555   1555  2.04  
    SSBOND  12 CYS G   20    CYS H   19                          1555   1555  2.03  
    LINK         ND1BHIS B   5                ZN    ZN B 961     1555   1555  1.80  
    LINK         CE1BHIS B   5                ZN    ZN B 951     1555   1555  2.45  
    LINK         NE2AHIS B   5                ZN    ZN B 951     1555   1555  1.94  
    LINK         NE2BHIS B   5                ZN    ZN B 951     1555   1555  2.23  
    LINK         NE2 HIS B  10                ZN    ZN B 901     1555   1555  2.01  
    LINK         NE2AHIS D  10                ZN    ZN D 921     1555   1555  2.00  
    LINK         NE2BHIS D  10                ZN    ZN D 911     1555   1555  2.03  
    LINK         NE2 HIS F  10                ZN    ZN F 931     1555   1555  2.00  
    LINK         NE2 HIS H  10                ZN    ZN H 941     1555   1555  1.97  
    LINK        ZN    ZN D 911                 O   HOH D1812     1555   1555  2.47  
    LINK        ZN    ZN F 931                 O  BHOH F 933     1555   1555  2.42  
    LINK        ZN    ZN B 951                 O   HOH B 952     1555   1555  2.24  
    LINK        ZN    ZN B 951                 O   HOH B 953     1555   1555  2.40  
    LINK        ZN    ZN B 961                 O   HOH B 964     1555   1555  2.19  
    LINK        ZN    ZN B 961                 O   HOH B1811     1555   1555  2.17  
    LINK        ZN    ZN B 961                 O   HOH B 963     1555   1555  2.17  
    LINK        ZN    ZN B 901                CL    CL B 902     1555   1555  2.20  
    LINK        ZN    ZN B 961                 O   HOH B 962     1555   1555  1.74  
    LINK        ZN    ZN B 961                 O   HOH B1810     1555   1555  2.69  
    LINK        ZN    ZN D 911                CL    CL D 912     1555   1555  2.15  
    LINK        ZN    ZN D 921                CL    CL D 923     1555   1555  2.22  
    LINK        ZN    ZN D 921                CL    CL D 922     1555   1555  2.25  
    LINK        ZN    ZN F 931                CL  A CL F 932     1555   1555  2.12  
    LINK        ZN    ZN H 941                CL    CL H 942     1555   1555  2.25  
    LINK        ZN    ZN B 901                 NE2 HIS B  10     1555   2555  2.01  
    LINK        ZN    ZN B 901                 NE2 HIS B  10     1555   3555  2.01  
    LINK        ZN    ZN B 901                CL    CL B 902     1555   2555  2.20  
    LINK        ZN    ZN B 901                CL    CL B 902     1555   3555  2.20  
    LINK        ZN    ZN B 951                 NE2 HIS H   5     1555   1554  1.90  
    LINK        ZN    ZN D 911                 O   HOH D1812     1555   2555  2.47  
    LINK        ZN    ZN D 911                 O   HOH D1812     1555   3555  2.47  
    LINK        ZN    ZN D 911                CL    CL D 912     1555   2555  2.15  
    LINK        ZN    ZN D 911                CL    CL D 912     1555   3555  2.15  
    LINK        ZN    ZN D 921                 NE2 HIS D   5     1555   2555  2.02  
    LINK        ZN    ZN F 931                 NE2 HIS F  10     1555   2555  2.00  
    LINK        ZN    ZN F 931                 NE2 HIS F  10     1555   3555  2.00  
    LINK        ZN    ZN F 931                CL  A CL F 932     1555   2555  2.12  
    LINK        ZN    ZN F 931                CL  A CL F 932     1555   3555  2.12  
    LINK        ZN    ZN F 931                 O  BHOH F 933     1555   2555  2.42  
    LINK        ZN    ZN F 931                 O  BHOH F 933     1555   3555  2.42  
    LINK        ZN    ZN H 941                 NE2 HIS H  10     1555   2555  1.97  
    LINK        ZN    ZN H 941                 NE2 HIS H  10     1555   3555  1.97  
    LINK        ZN    ZN H 941                CL    CL H 942     1555   2555  2.25  
    LINK        ZN    ZN H 941                CL    CL H 942     1555   3555  2.25  
    SITE     1 AC1  2 HIS B  10   CL B 902                                          
    SITE     1 AC2  3 HIS D  10   CL D 912  HOH D1812                               
    SITE     1 AC3  4 HIS D   5  HIS D  10   CL D 922   CL D 923                    
    SITE     1 AC4  3 HIS F  10   CL F 932  HOH F 933                               
    SITE     1 AC5  2 HIS H  10   CL H 942                                          
    SITE     1 AC6  4 HIS B   5  HOH B 952  HOH B 953  HIS H   5                    
    SITE     1 AC7  7 HIS B   5  HOH B 962  HOH B 963  HOH B 964                    
    SITE     2 AC7  7 HOH B1810  HOH B1811  HOH G1900                               
    SITE     1 AC8  2 HIS B  10   ZN B 901                                          
    SITE     1 AC9  4 LEU D   6  HIS D  10   ZN D 911  HOH D1814                    
    SITE     1 BC1  3 HIS D   5  HIS D  10   ZN D 921                               
    SITE     1 BC2  4 LEU B  17  HIS D   5  HIS D  10   ZN D 921                    
    SITE     1 BC3  4 HIS F  10   ZN F 931  HOH F 933  HOH F1803                    
    SITE     1 BC4  3 LEU H   6  HIS H  10   ZN H 941                               
    SITE     1 BC5  6 GLY E   1  ILE E   2  VAL E   3  GLU E   4                    
    SITE     2 BC5  6 LYS F  29  THR F  30                                          
    SITE     1 BC6  6 HOH F1940  CYS G  11  LEU G  16  HOH G1166                    
    SITE     2 BC6  6 HOH G1866  CYS H   7                                          
    SITE     1 BC7  4 PHE F   1  HOH F1127  LEU G  13  TYR G  14                    
    SITE     1 BC8  5 PHE D   1  HIS F   5  LEU F   6  CYS F   7                    
    SITE     2 BC8  5 HIS F  10                                                     
    CRYST1   80.127   80.127   71.582  90.00  90.00 120.00 H 3          36          
    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      0.012480  0.007205  0.000000        0.00000                         
    SCALE2      0.000000  0.014411  0.000000        0.00000                         
    SCALE3      0.000000  0.000000  0.013970        0.00000                         

    3D molecular view of vibration

    Displacement vectors
    Display
    Animation
    Display

    Still image of displacement vectors and GIF animation


    Mode 1

    Time-average properties and properties of the 10 lowest-frequency modes

    Fluctuation of atoms:
    Time average and for the 3 lowest-frequency modes.
    Fluctuation of dihedral angles:
    Time average and for the 3 lowest-frequency modes.
    Fluctuation of atomsFluctuation of dihedral angles

    Correlations between fluctuations of atoms

    Mode 1
    Correlations between fluctuations of atoms - Mode 1
    Time Average
    Time Average
    Distance map
    Distance map

    Calculation note

    PDB file name : pdb1g7a.ent

    Chains and HETATMs selected: 
      ATOM        A
      ATOM        B
      ATOM        C
      ATOM        D
      ATOM        a
      ATOM        b
      ATOM        c
      ATOM        d
      ATOM        e
      ATOM        f
      ATOM        g
      ATOM        h

    = Normal mode analysis calculation =

    No. of modes used in the calculation : All modes.

    Parameters of potential energies:
      1-4 and 1-5 non-bonded interactions: E(d) = A*exp(-d(PDB)**2/B**2)(d-d(PDB))**2.
      Loop-closing potential:              E(d) = A*(d-d(PDB))**2.
        for a disulfide bond and one of the bonds in the DNA and RNA sugar ring.
      where d and d(PDB) are distances between atoms in calculation and in PDB data, 
      respectively.

      Interaction type   A       B      Cutoff distance (A)
        1-4             1.00    5.00      100.00
        1-5             1.00    5.00      100.00
        Loop-closing  100.00

    Temperature adjustment by magnitude of fluctuation:
      Set to mean displacements of atoms       0.500 A

    Animation
      No. of frames: 11
      Mean displacements (A):    0.50

    Displacement vector
      Mean length of vectors (A):    3.00