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    HEADER    TRANSPORT PROTEIN                       13-FEB-06   2G0Z              
    TITLE     PHOTOLYZED CO L29F MYOGLOBIN: 1NS                                     
    COMPND    MOL_ID: 1;                                                            
    COMPND   2 MOLECULE: MYOGLOBIN;                                                 
    COMPND   3 CHAIN: A;                                                            
    COMPND   4 ENGINEERED: YES;                                                     
    COMPND   5 MUTATION: YES                                                        
    SOURCE    MOL_ID: 1;                                                            
    SOURCE   2 ORGANISM_SCIENTIFIC: PHYSETER CATODON;                               
    SOURCE   3 ORGANISM_COMMON: SPERM WHALE;                                        
    SOURCE   4 GENE: MB;                                                            
    SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI                                  
    KEYWDS    TIME-RESOLVED CRYSTALLOGRAPHY; MYOGLOBIN; DIFFERENCE                  
    KEYWDS   2 REFINEMENT; STRUCTURE-FUNCTION RELATIONSHIP; INTERMEDIATE            
    KEYWDS   3 STATES, TRANSPORT PROTEIN                                            
    EXPDTA    X-RAY DIFFRACTION                                                     
    AUTHOR    R.ARANDA,E.J.LEVIN,F.SCHOTTE,P.A.ANFINRUD,G.N.PHILLIPS                
    REVDAT   2   24-FEB-09 2G0Z    1       VERSN                                    
    REVDAT   1   04-JUL-06 2G0Z    0                                                
    JRNL        AUTH   R.ARANDA,E.J.LEVIN,F.SCHOTTE,P.A.ANFINRUD,                   
    JRNL        AUTH 2 G.N.PHILLIPS                                                 
    JRNL        TITL   TIME-DEPENDENT ATOMIC COORDINATES FOR THE                    
    JRNL        TITL 2 DISSOCIATION OF CARBON MONOXIDE FROM MYOGLOBIN.              
    JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  62   776 2006              
    JRNL        REFN                   ISSN 0907-4449                               
    JRNL        PMID   16790933                                                     
    JRNL        DOI    10.1107/S0907444906017318                                    
    REMARK   1                                                                      
    REMARK   2                                                                      
    REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
    REMARK   3                                                                      
    REMARK   3 REFINEMENT.                                                          
    REMARK   3   PROGRAM     : CNS 1.1                                              
    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) : 1.95                           
    REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.70                          
    REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
    REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1535611.030                    
    REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
    REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.0                           
    REMARK   3   NUMBER OF REFLECTIONS             : 14754                          
    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) : 0.058                           
    REMARK   3   FREE R VALUE                     : 0.070                           
    REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
    REMARK   3   FREE R VALUE TEST SET COUNT      : 736                             
    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) : 1.95                         
    REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07                         
    REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.80                        
    REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2185                         
    REMARK   3   BIN R VALUE           (WORKING SET) : 0.1300                       
    REMARK   3   BIN FREE R VALUE                    : 0.1560                       
    REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.70                         
    REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 107                          
    REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015                        
    REMARK   3                                                                      
    REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
    REMARK   3   PROTEIN ATOMS            : 1228                                    
    REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
    REMARK   3   HETEROGEN ATOMS          : 50                                      
    REMARK   3   SOLVENT ATOMS            : 147                                     
    REMARK   3                                                                      
    REMARK   3  B VALUES.                                                           
    REMARK   3   FROM WILSON PLOT           (A**2) : 15.80                          
    REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.50                          
    REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
    REMARK   3    B11 (A**2) : 0.00000                                              
    REMARK   3    B22 (A**2) : 0.00000                                              
    REMARK   3    B33 (A**2) : 0.00000                                              
    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 COORDINATE ERROR.                                         
    REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.07                            
    REMARK   3   ESD FROM SIGMAA              (A) : 0.14                            
    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) : 0.08                            
    REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.20                            
    REMARK   3                                                                      
    REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
    REMARK   3   BOND LENGTHS                 (A) : 0.006                           
    REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
    REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 17.60                           
    REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.82                            
    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) : 1.300 ; 1.500                
    REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.840 ; 2.000                
    REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.220 ; 2.000                
    REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.290 ; 2.500                
    REMARK   3                                                                      
    REMARK   3  BULK SOLVENT MODELING.                                              
    REMARK   3   METHOD USED : NULL                                                 
    REMARK   3   KSOL        : NULL                                                 
    REMARK   3   BSOL        : NULL                                                 
    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  : PROTEIN_REP.PARAM                              
    REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
    REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
    REMARK   3  PARAMETER FILE  4  : CVHEME.PAR                                     
    REMARK   3  PARAMETER FILE  5  : NULL                                           
    REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
    REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
    REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
    REMARK   3  TOPOLOGY FILE  4   : CVHEME.TOP                                     
    REMARK   3  TOPOLOGY FILE  5   : NULL                                           
    REMARK   3                                                                      
    REMARK   3  OTHER REFINEMENT REMARKS: DIFFERENCE REFINEMENT (TERWILLIGER        
    REMARK   3  1995                                                                
    REMARK   4                                                                      
    REMARK   4 2G0Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
    REMARK 100                                                                      
    REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-06.                  
    REMARK 100 THE RCSB ID CODE IS RCSB036551.                                      
    REMARK 200                                                                      
    REMARK 200 EXPERIMENTAL DETAILS                                                 
    REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
    REMARK 200  DATE OF DATA COLLECTION        : 01-APR-02                          
    REMARK 200  TEMPERATURE           (KELVIN) : 283.0                              
    REMARK 200  PH                             : 9.00                               
    REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
    REMARK 200                                                                      
    REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
    REMARK 200  RADIATION SOURCE               : ESRF                               
    REMARK 200  BEAMLINE                       : ID09                               
    REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
    REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : L                                  
    REMARK 200  WAVELENGTH OR RANGE        (A) : 0.79                               
    REMARK 200  MONOCHROMATOR                  : NULL                               
    REMARK 200  OPTICS                         : NULL                               
    REMARK 200                                                                      
    REMARK 200  DETECTOR TYPE                  : CCD                                
    REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
    REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
    REMARK 200  DATA SCALING SOFTWARE          : LAUGEN, PROW, LSCALE               
    REMARK 200                                                                      
    REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18341                              
    REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.801                              
    REMARK 200  RESOLUTION RANGE LOW       (A) : 29.881                             
    REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
    REMARK 200                                                                      
    REMARK 200 OVERALL.                                                             
    REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
    REMARK 200  DATA REDUNDANCY                : NULL                               
    REMARK 200  R MERGE                    (I) : NULL                               
    REMARK 200  R SYM                      (I) : NULL                               
    REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
    REMARK 200                                                                      
    REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
    REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
    REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
    REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
    REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
    REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
    REMARK 200  R SYM FOR SHELL            (I) : NULL                               
    REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
    REMARK 200                                                                      
    REMARK 200 DIFFRACTION PROTOCOL: LAUE                                           
    REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
    REMARK 200 SOFTWARE USED: CNS                                                   
    REMARK 200 STARTING MODEL: PDB ENTRY: 2SPL                                      
    REMARK 200                                                                      
    REMARK 200 REMARK: NULL                                                         
    REMARK 280                                                                      
    REMARK 280 CRYSTAL                                                              
    REMARK 280 SOLVENT CONTENT, VS   (%): 61.13                                     
    REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
    REMARK 280                                                                      
    REMARK 280 CRYSTALLIZATION CONDITIONS: 2.6M AMMONIUM SULFATE, 20MM              
    REMARK 280  TRISHCL, 1MM EDTA, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
    REMARK 280  298K, PH 9.00                                                       
    REMARK 290                                                                      
    REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
    REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6                              
    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,-Y,Z                                                 
    REMARK 290       5555   Y,-X+Y,Z                                                
    REMARK 290       6555   X-Y,X,Z                                                 
    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        0.00000            
    REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
    REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
    REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
    REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
    REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
    REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
    REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
    REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
    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: MONOMERIC                         
    REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
    REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
    REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
    REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
    REMARK 500                                                                      
    REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
    REMARK 500 SUBTOPIC: TORSION ANGLES                                             
    REMARK 500                                                                      
    REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
    REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
    REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
    REMARK 500                                                                      
    REMARK 500 STANDARD TABLE:                                                      
    REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
    REMARK 500                                                                      
    REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
    REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
    REMARK 500                                                                      
    REMARK 500  M RES CSSEQI        PSI       PHI                                   
    REMARK 500  1 ASP A  20       74.04   -154.02                                   
    REMARK 500  1 LYS A  47       -9.68    -59.67                                   
    REMARK 500  2 ASP A  20       74.83   -153.33                                   
    REMARK 500  2 LYS A  47       -8.74    -57.24                                   
    REMARK 500                                                                      
    REMARK 500 REMARK: NULL                                                         
    REMARK 620                                                                      
    REMARK 620 METAL COORDINATION                                                   
    REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
    REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
    REMARK 620                                                                      
    REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
    REMARK 620                           1 HEM A 154  FE                            
    REMARK 620 N RES CSSEQI ATOM                                                    
    REMARK 620 1 CMO A 155   C                                                      
    REMARK 620 2 HIS A  93   NE2 177.7                                              
    REMARK 620 3 HIS A  93   NE2 173.2   5.2                                        
    REMARK 620 4 CMO A 155   O     7.2 175.1 174.9                                  
    REMARK 620 N                    1     2     3                                   
    REMARK 800                                                                      
    REMARK 800 SITE                                                                 
    REMARK 800 SITE_IDENTIFIER: AC1                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 156                 
    REMARK 800 SITE_IDENTIFIER: AC2                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 154                 
    REMARK 800 SITE_IDENTIFIER: AC3                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO A 155                 
    REMARK 900                                                                      
    REMARK 900 RELATED ENTRIES                                                      
    REMARK 900 RELATED ID: 2G0V   RELATED DB: PDB                                   
    REMARK 900 PHOTOLYZED CO L29F MYOGLOBIN: 100PS                                  
    REMARK 900 RELATED ID: 2G0X   RELATED DB: PDB                                   
    REMARK 900 PHOTOLYZED CO L29F MYOGLOBIN: 316PS                                  
    REMARK 900 RELATED ID: 2G10   RELATED DB: PDB                                   
    REMARK 900 PHOTOLYZED CO L29F MYOGLOBIN: 3.16NS                                 
    REMARK 900 RELATED ID: 2G11   RELATED DB: PDB                                   
    REMARK 900 PHOTOLYZED CO L29F MYOGLOBIN: 31.6NS                                 
    REMARK 900 RELATED ID: 2G12   RELATED DB: PDB                                   
    REMARK 900 PHOTOLYZED CO L29F MYOGLOBIN: 316NS                                  
    REMARK 900 RELATED ID: 2G14   RELATED DB: PDB                                   
    REMARK 900 PHOTOLYZED CO L29F MYOGLOBIN: 3.16US                                 
    DBREF  2G0Z A    1   153  UNP    P02185   MYG_PHYCA        1    153             
    SEQADV 2G0Z MET A    0  UNP  P02185              INITIATING METHIONINE          
    SEQADV 2G0Z PHE A   29  UNP  P02185    LEU    29 ENGINEERED                     
    SEQADV 2G0Z ASN A  122  UNP  P02185    ASP   122 VARIANT                        
    SEQRES   1 A  154  MET VAL LEU SER GLU GLY GLU TRP GLN LEU VAL LEU HIS          
    SEQRES   2 A  154  VAL TRP ALA LYS VAL GLU ALA ASP VAL ALA GLY HIS GLY          
    SEQRES   3 A  154  GLN ASP ILE PHE ILE ARG LEU PHE LYS SER HIS PRO GLU          
    SEQRES   4 A  154  THR LEU GLU LYS PHE ASP ARG PHE LYS HIS LEU LYS THR          
    SEQRES   5 A  154  GLU ALA GLU MET LYS ALA SER GLU ASP LEU LYS LYS HIS          
    SEQRES   6 A  154  GLY VAL THR VAL LEU THR ALA LEU GLY ALA ILE LEU LYS          
    SEQRES   7 A  154  LYS LYS GLY HIS HIS GLU ALA GLU LEU LYS PRO LEU ALA          
    SEQRES   8 A  154  GLN SER HIS ALA THR LYS HIS LYS ILE PRO ILE LYS TYR          
    SEQRES   9 A  154  LEU GLU PHE ILE SER GLU ALA ILE ILE HIS VAL LEU HIS          
    SEQRES  10 A  154  SER ARG HIS PRO GLY ASN PHE GLY ALA ASP ALA GLN GLY          
    SEQRES  11 A  154  ALA MET ASN LYS ALA LEU GLU LEU PHE ARG LYS ASP ILE          
    SEQRES  12 A  154  ALA ALA LYS TYR LYS GLU LEU GLY TYR GLN GLY                  
    HET    SO4  A 156       5                                                       
    HET    HEM  A 154      43                                                       
    HET    CMO  A 155       2                                                       
    HETNAM     SO4 SULFATE ION                                                      
    HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
    HETNAM     CMO CARBON MONOXIDE                                                  
    HETSYN     HEM HEME                                                             
    FORMUL   2  SO4    O4 S 2-                                                      
    FORMUL   3  HEM    C34 H32 FE N4 O4                                             
    FORMUL   4  CMO    C O                                                          
    FORMUL   5  HOH   *147(H2 O)                                                    
    HELIX    1   1 SER A    3  GLU A   18  1                                  16    
    HELIX    2   2 ASP A   20  HIS A   36  1                                  17    
    HELIX    3   3 PRO A   37  PHE A   43  5                                   7    
    HELIX    4   4 THR A   51  SER A   58  1                                   8    
    HELIX    5   5 SER A   58  LYS A   77  1                                  20    
    HELIX    6   6 HIS A   82  LYS A   96  1                                  15    
    HELIX    7   7 PRO A  100  HIS A  119  1                                  20    
    HELIX    8   8 PRO A  120  PHE A  123  5                                   4    
    HELIX    9   9 GLY A  124  GLY A  150  1                                  27    
    LINK         C  ACMO A 155                FE  AHEM A 154     1555   1555  1.80  
    LINK         NE2AHIS A  93                FE  AHEM A 154     1555   1555  2.26  
    LINK         NE2BHIS A  93                FE  BHEM A 154     1555   1555  2.20  
    LINK        FE  AHEM A 154                 O  ACMO A 155     1555   1555  2.88  
    SITE     1 AC1  6 SER A   3  GLU A   4  LYS A  34  THR A  51                    
    SITE     2 AC1  6 GLU A  52  HOH A 372                                          
    SITE     1 AC2 14 LYS A  42  PHE A  43  ARG A  45  LEU A  89                    
    SITE     2 AC2 14 SER A  92  HIS A  93  HIS A  97  ILE A  99                    
    SITE     3 AC2 14 TYR A 103  CMO A 155  HOH A 233  HOH A 271                    
    SITE     4 AC2 14 HOH A 272  HOH A 323                                          
    SITE     1 AC3  5 PHE A  29  PHE A  43  HIS A  64  VAL A  68                    
    SITE     2 AC3  5 HEM A 154                                                     
    CRYST1   91.200   91.200   45.870  90.00  90.00 120.00 P 6           6          
    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      0.010965  0.006331  0.000000        0.00000                         
    SCALE2      0.000000  0.012661  0.000000        0.00000                         
    SCALE3      0.000000  0.000000  0.021801        0.00000                         
    MODEL        1                                                                  

    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 : pdb2g0z.ent

    Chains and HETATMs selected: 
      ATOM        A

    = 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