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    HEADER    HORMONE                                 05-JUL-07   2QIU              
    TITLE     STRUCTURE OF HUMAN ARG-INSULIN                                        
    COMPND    MOL_ID: 1;                                                            
    COMPND   2 MOLECULE: INSULIN;                                                   
    COMPND   3 CHAIN: A, C;                                                         
    COMPND   4 FRAGMENT: INSULIN A CHAIN;                                           
    COMPND   5 MOL_ID: 2;                                                           
    COMPND   6 MOLECULE: INSULIN;                                                   
    COMPND   7 CHAIN: B, D;                                                         
    COMPND   8 FRAGMENT: INSULIN B CHAIN                                            
    SOURCE    MOL_ID: 1;                                                            
    SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
    SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
    SOURCE   4 ORGANISM_TAXID: 9606;                                                
    SOURCE   5 MOL_ID: 2;                                                           
    SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
    SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
    SOURCE   8 ORGANISM_TAXID: 9606                                                 
    KEYWDS    HORMONE, GLUCOSE UTILISATION, T3R3 CONFORMATION                       
    EXPDTA    X-RAY DIFFRACTION                                                     
    AUTHOR    R.SREEKANTH,V.PATTABHI,S.S.RAJAN                                      
    REVDAT   2   24-FEB-09 2QIU    1       VERSN                                    
    REVDAT   1   26-FEB-08 2QIU    0                                                
    JRNL        AUTH   R.SREEKANTH,V.PATTABHI,S.S.RAJAN                             
    JRNL        TITL   STRUCTURAL INTERPRETATION OF REDUCED INSULIN                 
    JRNL        TITL 2 ACTIVITY AS SEEN IN THE CRYSTAL STRUCTURE OF HUMAN           
    JRNL        TITL 3 ARG-INSULIN                                                  
    JRNL        REF    BIOCHIMIE                     V.  90   467 2008              
    JRNL        REFN                   ISSN 0300-9084                               
    JRNL        PMID   18029081                                                     
    JRNL        DOI    10.1016/J.BIOCHI.2007.09.012                                 
    REMARK   1                                                                      
    REMARK   1 REFERENCE 1                                                          
    REMARK   1  AUTH   G.BENTLEY,E.DODSON,G.DODSON,D.HODGKIN,D.MERCOLA              
    REMARK   1  TITL   STRUCTURE OF INSULIN IN 4-ZINC INSULIN                       
    REMARK   1  REF    NATURE                        V. 261   166 1976              
    REMARK   1  REFN                   ISSN 0028-0836                               
    REMARK   1  PMID   1272390                                                      
    REMARK   1  DOI    10.1038/261166A0                                             
    REMARK   2                                                                      
    REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
    REMARK   3                                                                      
    REMARK   3 REFINEMENT.                                                          
    REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
    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) : 40.26                          
    REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
    REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.0                           
    REMARK   3   NUMBER OF REFLECTIONS             : 5193                           
    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) : 0.203                           
    REMARK   3   R VALUE            (WORKING SET) : 0.197                           
    REMARK   3   FREE R VALUE                     : 0.249                           
    REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.800                          
    REMARK   3   FREE R VALUE TEST SET COUNT      : 628                             
    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) : 301                          
    REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.37                        
    REMARK   3   BIN R VALUE           (WORKING SET) : 0.3380                       
    REMARK   3   BIN FREE R VALUE SET COUNT          : 36                           
    REMARK   3   BIN FREE R VALUE                    : 0.3720                       
    REMARK   3                                                                      
    REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
    REMARK   3   PROTEIN ATOMS            : 832                                     
    REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
    REMARK   3   HETEROGEN ATOMS          : 2                                       
    REMARK   3   SOLVENT ATOMS            : 57                                      
    REMARK   3                                                                      
    REMARK   3  B VALUES.                                                           
    REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
    REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.19                          
    REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
    REMARK   3    B11 (A**2) : -0.01000                                             
    REMARK   3    B22 (A**2) : -0.01000                                             
    REMARK   3    B33 (A**2) : 0.01000                                              
    REMARK   3    B12 (A**2) : 0.00000                                              
    REMARK   3    B13 (A**2) : 0.00000                                              
    REMARK   3    B23 (A**2) : 0.00000                                              
    REMARK   3                                                                      
    REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
    REMARK   3   ESU BASED ON R VALUE                            (A): 0.313         
    REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.220         
    REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.254         
    REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.949         
    REMARK   3                                                                      
    REMARK   3 CORRELATION COEFFICIENTS.                                            
    REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
    REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
    REMARK   3                                                                      
    REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
    REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   854 ; 0.087 ; 0.022       
    REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
    REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1158 ; 2.101 ; 1.954       
    REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
    REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   100 ;15.512 ; 5.000       
    REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    42 ;33.529 ;23.810       
    REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   136 ;23.961 ;15.000       
    REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     4 ;22.555 ;15.000       
    REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   126 ; 0.699 ; 0.200       
    REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   654 ; 0.009 ; 0.020       
    REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
    REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   460 ; 0.419 ; 0.800       
    REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
    REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   561 ; 0.363 ; 0.700       
    REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
    REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    73 ; 0.386 ; 0.800       
    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):    55 ; 0.510 ; 0.800       
    REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
    REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    13 ; 0.653 ; 0.800       
    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):   555 ; 6.777 ; 1.500       
    REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
    REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   826 ; 7.511 ; 2.000       
    REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   378 ; 8.844 ; 3.000       
    REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   332 ; 9.557 ; 4.500       
    REMARK   3                                                                      
    REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
    REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
    REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
    REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
    REMARK   3                                                                      
    REMARK   3  NCS RESTRAINTS STATISTICS                                           
    REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 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   : 0.80                                          
    REMARK   3                                                                      
    REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
    REMARK   4                                                                      
    REMARK   4 2QIU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
    REMARK 100                                                                      
    REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JUL-07.                  
    REMARK 100 THE RCSB ID CODE IS RCSB043652.                                      
    REMARK 200                                                                      
    REMARK 200 EXPERIMENTAL DETAILS                                                 
    REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
    REMARK 200  DATE OF DATA COLLECTION        : 31-AUG-06                          
    REMARK 200  TEMPERATURE           (KELVIN) : 298                                
    REMARK 200  PH                             : 6.7                                
    REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
    REMARK 200                                                                      
    REMARK 200  SYNCHROTRON              (Y/N) : N                                  
    REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
    REMARK 200  BEAMLINE                       : NULL                               
    REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
    REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
    REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
    REMARK 200  MONOCHROMATOR                  : NIL                                
    REMARK 200  OPTICS                         : NULL                               
    REMARK 200                                                                      
    REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
    REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
    REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
    REMARK 200  DATA SCALING SOFTWARE          : AUTOMAR                            
    REMARK 200                                                                      
    REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6141                               
    REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
    REMARK 200  RESOLUTION RANGE LOW       (A) : 40.260                             
    REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
    REMARK 200                                                                      
    REMARK 200 OVERALL.                                                             
    REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
    REMARK 200  DATA REDUNDANCY                : 5.000                              
    REMARK 200  R MERGE                    (I) : 0.12000                            
    REMARK 200  R SYM                      (I) : NULL                               
    REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 3.4000                             
    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       : 4.86                               
    REMARK 200  R MERGE FOR SHELL          (I) : 0.44000                            
    REMARK 200  R SYM FOR SHELL            (I) : NULL                               
    REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.200                              
    REMARK 200                                                                      
    REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
    REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
    REMARK 200 SOFTWARE USED: AMORE                                                 
    REMARK 200 STARTING MODEL: 1ZNI                                                 
    REMARK 200                                                                      
    REMARK 200 REMARK: NULL                                                         
    REMARK 280                                                                      
    REMARK 280 CRYSTAL                                                              
    REMARK 280 SOLVENT CONTENT, VS   (%): 37.35                                     
    REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96                     
    REMARK 280                                                                      
    REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, ACETONE, ZINC            
    REMARK 280  SULPHATE, PH 6.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE        
    REMARK 280  293K                                                                
    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       40.24550            
    REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.23575            
    REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       12.54667            
    REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       40.24550            
    REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       23.23575            
    REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       12.54667            
    REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       40.24550            
    REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       23.23575            
    REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       12.54667            
    REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
    REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       46.47150            
    REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       25.09333            
    REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
    REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       46.47150            
    REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       25.09333            
    REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
    REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       46.47150            
    REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       25.09333            
    REMARK 290                                                                      
    REMARK 290 REMARK: NULL                                                         
    REMARK 300                                                                      
    REMARK 300 BIOMOLECULE: 1                                                       
    REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
    REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
    REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
    REMARK 300 BURIED SURFACE AREA.                                                 
    REMARK 350                                                                      
    REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
    REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
    REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
    REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
    REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
    REMARK 350                                                                      
    REMARK 350 BIOMOLECULE: 1                                                       
    REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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 101  LIES ON A SPECIAL POSITION.                          
    REMARK 375      HOH B 108  LIES ON A SPECIAL POSITION.                          
    REMARK 375      HOH B 116  LIES ON A SPECIAL POSITION.                          
    REMARK 375      HOH D 103  LIES ON A SPECIAL POSITION.                          
    REMARK 375      HOH D 111  LIES ON A SPECIAL POSITION.                          
    REMARK 375      HOH D 116  LIES ON A SPECIAL POSITION.                          
    REMARK 500                                                                      
    REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
    REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
    REMARK 500                                                                      
    REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
    REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
    REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
    REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
    REMARK 500                                                                      
    REMARK 500 STANDARD TABLE:                                                      
    REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
    REMARK 500                                                                      
    REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
    REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
    REMARK 500                                                                      
    REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
    REMARK 500    THR B  30   C     THR B  30   OXT     0.215                       
    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    LYS B  29     -135.52     49.37                                   
    REMARK 500    TYR C  14       39.50    -93.77                                   
    REMARK 500                                                                      
    REMARK 500 REMARK: NULL                                                         
    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 D 103        DISTANCE =  8.65 ANGSTROMS                       
    REMARK 525    HOH C  24        DISTANCE =  5.06 ANGSTROMS                       
    REMARK 525    HOH C  30        DISTANCE =  9.90 ANGSTROMS                       
    REMARK 525    HOH B 113        DISTANCE =  5.26 ANGSTROMS                       
    REMARK 525    HOH D 116        DISTANCE = 10.52 ANGSTROMS                       
    REMARK 525    HOH D 117        DISTANCE = 11.46 ANGSTROMS                       
    REMARK 650                                                                      
    REMARK 650 HELIX                                                                
    REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED                              
    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 101                  
    REMARK 800 SITE_IDENTIFIER: AC2                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 102                  
    REMARK 900                                                                      
    REMARK 900 RELATED ENTRIES                                                      
    REMARK 900 RELATED ID: 1ZNI   RELATED DB: PDB                                   
    REMARK 900 T3R3 PORCINE INSULIN AT 1.5 ANG RESOLUTION                           
    DBREF  2QIU A    0    21  UNP    P01308   INS_HUMAN       89    110             
    DBREF  2QIU B    1    30  UNP    P01308   INS_HUMAN       25     54             
    DBREF  2QIU C    0    21  UNP    P01308   INS_HUMAN       89    110             
    DBREF  2QIU D    1    30  UNP    P01308   INS_HUMAN       25     54             
    SEQRES   1 A   22  ARG GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER          
    SEQRES   2 A   22  LEU 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   22  ARG GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER          
    SEQRES   2 C   22  LEU 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                                              
    HET     ZN  B 101       1                                                       
    HET     ZN  D 102       1                                                       
    HETNAM      ZN ZINC ION                                                         
    FORMUL   5   ZN    2(ZN 2+)                                                     
    FORMUL   7  HOH   *57(H2 O)                                                     
    HELIX    1   1 VAL A    3  THR A    8  1                                   6    
    HELIX    2   2 GLN A   15  CYS A   20  5                                   6    
    HELIX    3   3 GLN B    4  GLY B   20  1                                  17    
    HELIX    4   4 GLU B   21  GLY B   23  5                                   3    
    HELIX    5   5 ILE C    2  CYS C    7  1                                   6    
    HELIX    6   6 SER C   12  GLU C   17  1                                   6    
    HELIX    7   7 ASN C   18  CYS C   20  5                                   3    
    HELIX    8   8 CYS D    7  GLY D   20  1                                  14    
    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           
    SSBOND   1 CYS A    6    CYS A   11                          1555   1555  2.04  
    SSBOND   2 CYS A    7    CYS B    7                          1555   1555  2.03  
    SSBOND   3 CYS A   20    CYS B   19                          1555   1555  2.03  
    SSBOND   4 CYS C    6    CYS C   11                          1555   1555  2.03  
    SSBOND   5 CYS C    7    CYS D    7                          1555   1555  2.03  
    SSBOND   6 CYS C   20    CYS D   19                          1555   1555  2.03  
    LINK        ZN    ZN B 101                 NE2 HIS B  10     1555   1555  2.07  
    LINK        ZN    ZN D 102                 NE2 HIS D  10     1555   1555  2.06  
    SITE     1 AC1  2 HIS B  10  HOH B 108                                          
    SITE     1 AC2  2 HIS D  10  HOH D 111                                          
    CRYST1   80.491   80.491   37.640  90.00  90.00 120.00 H 3          18          
    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      0.012424  0.007173  0.000000        0.00000                         
    SCALE2      0.000000  0.014346  0.000000        0.00000                         
    SCALE3      0.000000  0.000000  0.026567        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 : pdb2qiu.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