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Database: PDB
Entry: 1G0A
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HEADER    OXYGEN STORAGE/TRANSPORT                05-OCT-00   1G0A              
TITLE     CARBONMONOXY LIGANDED BOVINE HEMOGLOBIN PH 8.5                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEMOGLOBIN ALPHA CHAIN;                                    
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: HEMOGLOBIN BETA CHAIN;                                     
COMPND   6 CHAIN: B, D                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: CATTLE;                                             
SOURCE   4 ORGANISM_TAXID: 9913;                                                
SOURCE   5 TISSUE: BLOOD;                                                       
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   8 ORGANISM_COMMON: CATTLE;                                             
SOURCE   9 ORGANISM_TAXID: 9913;                                                
SOURCE  10 TISSUE: BLOOD                                                        
KEYWDS    BOVINE, HEMOGLOBIN, LIGANDED, CARBONMONOXY, PROTOPORPHYRIN IX, OXYGEN 
KEYWDS   2 STORAGE-TRANSPORT COMPLEX                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.C.MUESER,P.H.ROGERS,A.ARNONE                                        
REVDAT   3   07-FEB-24 1G0A    1       REMARK LINK                              
REVDAT   2   24-FEB-09 1G0A    1       VERSN                                    
REVDAT   1   27-DEC-00 1G0A    0                                                
JRNL        AUTH   T.C.MUESER,P.H.ROGERS,A.ARNONE                               
JRNL        TITL   INTERFACE SLIDING AS ILLUSTRATED BY THE MULTIPLE QUATERNARY  
JRNL        TITL 2 STRUCTURES OF LIGANDED HEMOGLOBIN.                           
JRNL        REF    BIOCHEMISTRY                  V.  39 15353 2000              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   11112521                                                     
JRNL        DOI    10.1021/BI0012944                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.04 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 36902                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 37869                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4386                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 180                                     
REMARK   3   SOLVENT ATOMS            : 145                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.009 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.023 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1G0A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000012072.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JAN-92                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 8.5                                
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 RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SDMS                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SDMS                               
REMARK 200  DATA SCALING SOFTWARE          : SDMS                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38330                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.530                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 7.950                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: MERLOT                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM TAPS, AMMONIUM SULPHATE,          
REMARK 280  POTASSIUM CHLORIDE, POLYETHYLENE GLYCOL 3350, PH 8.5, VAPOR         
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-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 -1.000000  0.000000  0.000000       36.90000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       31.55000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       65.70000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       31.55000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.90000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       65.70000            
REMARK 290   SMTRY3   4  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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER CONSTRUCTED FROM       
REMARK 300 THE HETERODIMER OF CHAIN A (ALPHA) AND CHAIN B (BETA) AND            
REMARK 300 THE HETERODIMER OF CHAIN C (ALPHA) AND CHAIN D (BETA)                
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11610 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 22850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -118.0 KCAL/MOL                       
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 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     HIS A   50   CG   ND1  CD2  CE1  NE2                             
REMARK 480     ARG A  141   CD   NE   CZ   NH1  NH2                             
REMARK 480     GLU B    6   CG   CD   OE1  OE2                                  
REMARK 480     GLU B   22   CD   OE1  OE2                                       
REMARK 480     HIS C   50   NE2                                                 
REMARK 480     GLU D    6   CD   OE1  OE2                                       
REMARK 480     LYS D   95   NZ                                                  
REMARK 480     ARG D  144   NH1                                                 
REMARK 480     HIS D  146   OXT                                                 
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HIS A    45     O    HOH C   164     2564     1.62            
REMARK 500   C    HIS A    45     O    HOH C   164     2564     1.63            
REMARK 500   OD2  ASP B    52     O    HOH C   169     4556     2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG C  92   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG C 141   CD  -  NE  -  CZ  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    ARG C 141   NE  -  CZ  -  NH1 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    ARG C 141   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG D  30   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG D 116   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
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    ASP A  75       63.64   -156.31                                   
REMARK 500    GLU B   6      -70.74    -68.88                                   
REMARK 500    ASP B  21      -73.23    -45.55                                   
REMARK 500    ASP C  75       69.94   -155.04                                   
REMARK 500    LYS C 139       77.43   -103.51                                   
REMARK 500    ARG D 144       -9.43    -59.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  92         0.10    SIDE CHAIN                              
REMARK 500    ARG C 141         0.08    SIDE CHAIN                              
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                             HEM A 142  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  87   NE2                                                    
REMARK 620 2 HEM A 142   NA   90.8                                              
REMARK 620 3 HEM A 142   NB   91.6  90.9                                        
REMARK 620 4 HEM A 142   NC   89.9 179.1  89.6                                  
REMARK 620 5 HEM A 142   ND   91.2  90.0 177.1  89.6                            
REMARK 620 6 CMO A 143   C   175.3  93.5  90.2  85.8  86.9                      
REMARK 620 7 CMO A 143   O   172.7  96.2  86.2  83.1  90.9   4.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 147  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  92   NE2                                                    
REMARK 620 2 HEM B 147   NA   87.8                                              
REMARK 620 3 HEM B 147   NB   93.5  89.4                                        
REMARK 620 4 HEM B 147   NC   90.8 178.4  89.9                                  
REMARK 620 5 HEM B 147   ND   85.8  91.6 178.8  89.1                            
REMARK 620 6 CMO B 148   C   173.7  95.4  92.0  86.1  88.7                      
REMARK 620 7 CMO B 148   O   174.1  97.3  89.5  84.2  91.1   3.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 142  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  87   NE2                                                    
REMARK 620 2 HEM C 142   NA   86.9                                              
REMARK 620 3 HEM C 142   NB   89.4  89.7                                        
REMARK 620 4 HEM C 142   NC   91.3 178.1  90.0                                  
REMARK 620 5 HEM C 142   ND   93.5  91.7 176.9  88.6                            
REMARK 620 6 CMO C 143   C   174.3  89.5  95.0  92.4  82.3                      
REMARK 620 7 CMO C 143   O   177.6  95.5  90.2  86.4  86.9   7.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 147  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  92   NE2                                                    
REMARK 620 2 HEM D 147   NA   77.6                                              
REMARK 620 3 HEM D 147   NB   89.9  88.8                                        
REMARK 620 4 HEM D 147   NC   91.0 168.4  89.1                                  
REMARK 620 5 HEM D 147   ND   80.3  91.2 170.0  88.9                            
REMARK 620 6 CMO D 148   C   161.6 101.2 108.4  90.3  81.4                      
REMARK 620 7 CMO D 148   O   177.7 100.6  91.6  90.8  98.2  16.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO A 143                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 147                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO B 148                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO C 143                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 147                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO D 148                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1G08   RELATED DB: PDB                                   
REMARK 900 CARBONMONOXY LIGANDED BOVINE HEMOGLOBIN PH 5.0                       
REMARK 900 RELATED ID: 1G09   RELATED DB: PDB                                   
REMARK 900 CARBONMONOXY LIGANDED BOVINE HEMOGLOBIN PH 7.2                       
REMARK 900 RELATED ID: 1G0B   RELATED DB: PDB                                   
REMARK 900 CARBONMONOXY LIGANDED EQUINE HEMOGLOBIN PH 8.5                       
DBREF  1G0A A    1   141  UNP    P01966   HBA_BOVIN        1    141             
DBREF  1G0A C    1   141  UNP    P01966   HBA_BOVIN        1    141             
DBREF  1G0A B    2   146  UNP    P02070   HBB_BOVIN        1    145             
DBREF  1G0A D    2   146  UNP    P02070   HBB_BOVIN        1    145             
SEQRES   1 A  141  VAL LEU SER ALA ALA ASP LYS GLY ASN VAL LYS ALA ALA          
SEQRES   2 A  141  TRP GLY LYS VAL GLY GLY HIS ALA ALA GLU TYR GLY ALA          
SEQRES   3 A  141  GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR          
SEQRES   4 A  141  LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER          
SEQRES   5 A  141  ALA GLN VAL LYS GLY HIS GLY ALA LYS VAL ALA ALA ALA          
SEQRES   6 A  141  LEU THR LYS ALA VAL GLU HIS LEU ASP ASP LEU PRO GLY          
SEQRES   7 A  141  ALA LEU SER GLU LEU SER ASP LEU HIS ALA HIS LYS LEU          
SEQRES   8 A  141  ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS SER          
SEQRES   9 A  141  LEU LEU VAL THR LEU ALA SER HIS LEU PRO SER ASP PHE          
SEQRES  10 A  141  THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA          
SEQRES  11 A  141  ASN VAL SER THR VAL LEU THR SER LYS TYR ARG                  
SEQRES   1 B  145  MET LEU THR ALA GLU GLU LYS ALA ALA VAL THR ALA PHE          
SEQRES   2 B  145  TRP GLY LYS VAL LYS VAL ASP GLU VAL GLY GLY GLU ALA          
SEQRES   3 B  145  LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN ARG          
SEQRES   4 B  145  PHE PHE GLU SER PHE GLY ASP LEU SER THR ALA ASP ALA          
SEQRES   5 B  145  VAL MET ASN ASN PRO LYS VAL LYS ALA HIS GLY LYS LYS          
SEQRES   6 B  145  VAL LEU ASP SER PHE SER ASN GLY MET LYS HIS LEU ASP          
SEQRES   7 B  145  ASP LEU LYS GLY THR PHE ALA ALA LEU SER GLU LEU HIS          
SEQRES   8 B  145  CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE LYS LEU          
SEQRES   9 B  145  LEU GLY ASN VAL LEU VAL VAL VAL LEU ALA ARG ASN PHE          
SEQRES  10 B  145  GLY LYS GLU PHE THR PRO VAL LEU GLN ALA ASP PHE GLN          
SEQRES  11 B  145  LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS ARG          
SEQRES  12 B  145  TYR HIS                                                      
SEQRES   1 C  141  VAL LEU SER ALA ALA ASP LYS GLY ASN VAL LYS ALA ALA          
SEQRES   2 C  141  TRP GLY LYS VAL GLY GLY HIS ALA ALA GLU TYR GLY ALA          
SEQRES   3 C  141  GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR          
SEQRES   4 C  141  LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER          
SEQRES   5 C  141  ALA GLN VAL LYS GLY HIS GLY ALA LYS VAL ALA ALA ALA          
SEQRES   6 C  141  LEU THR LYS ALA VAL GLU HIS LEU ASP ASP LEU PRO GLY          
SEQRES   7 C  141  ALA LEU SER GLU LEU SER ASP LEU HIS ALA HIS LYS LEU          
SEQRES   8 C  141  ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS SER          
SEQRES   9 C  141  LEU LEU VAL THR LEU ALA SER HIS LEU PRO SER ASP PHE          
SEQRES  10 C  141  THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA          
SEQRES  11 C  141  ASN VAL SER THR VAL LEU THR SER LYS TYR ARG                  
SEQRES   1 D  145  MET LEU THR ALA GLU GLU LYS ALA ALA VAL THR ALA PHE          
SEQRES   2 D  145  TRP GLY LYS VAL LYS VAL ASP GLU VAL GLY GLY GLU ALA          
SEQRES   3 D  145  LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN ARG          
SEQRES   4 D  145  PHE PHE GLU SER PHE GLY ASP LEU SER THR ALA ASP ALA          
SEQRES   5 D  145  VAL MET ASN ASN PRO LYS VAL LYS ALA HIS GLY LYS LYS          
SEQRES   6 D  145  VAL LEU ASP SER PHE SER ASN GLY MET LYS HIS LEU ASP          
SEQRES   7 D  145  ASP LEU LYS GLY THR PHE ALA ALA LEU SER GLU LEU HIS          
SEQRES   8 D  145  CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE LYS LEU          
SEQRES   9 D  145  LEU GLY ASN VAL LEU VAL VAL VAL LEU ALA ARG ASN PHE          
SEQRES  10 D  145  GLY LYS GLU PHE THR PRO VAL LEU GLN ALA ASP PHE GLN          
SEQRES  11 D  145  LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS ARG          
SEQRES  12 D  145  TYR HIS                                                      
HET    HEM  A 142      43                                                       
HET    CMO  A 143       2                                                       
HET    HEM  B 147      43                                                       
HET    CMO  B 148       2                                                       
HET    HEM  C 142      43                                                       
HET    CMO  C 143       2                                                       
HET    HEM  D 147      43                                                       
HET    CMO  D 148       2                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     CMO CARBON MONOXIDE                                                  
HETSYN     HEM HEME                                                             
FORMUL   5  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   6  CMO    4(C O)                                                       
FORMUL  13  HOH   *145(H2 O)                                                    
HELIX    1   1 SER A    3  GLY A   18  1                                  16    
HELIX    2   2 HIS A   20  PHE A   36  1                                  17    
HELIX    3   3 PRO A   37  PHE A   43  5                                   7    
HELIX    4   4 SER A   52  HIS A   72  1                                  21    
HELIX    5   5 ASP A   75  SER A   81  1                                   7    
HELIX    6   6 LEU A   80  ALA A   88  1                                   9    
HELIX    7   7 PRO A   95  LEU A  113  1                                  19    
HELIX    8   8 THR A  118  THR A  137  1                                  20    
HELIX    9   9 THR B    4  GLY B   16  1                                  13    
HELIX   10  10 LYS B   19  TYR B   35  1                                  17    
HELIX   11  11 PRO B   36  GLU B   43  5                                   8    
HELIX   12  12 PHE B   42  GLY B   46  5                                   5    
HELIX   13  13 THR B   50  ASN B   57  1                                   8    
HELIX   14  14 ASN B   57  HIS B   77  1                                  21    
HELIX   15  15 ASP B   80  PHE B   85  1                                   6    
HELIX   16  16 PHE B   85  LYS B   95  1                                  11    
HELIX   17  17 PRO B  100  GLY B  119  1                                  20    
HELIX   18  18 LYS B  120  PHE B  122  5                                   3    
HELIX   19  19 THR B  123  ALA B  142  1                                  20    
HELIX   20  20 HIS B  143  TYR B  145  5                                   3    
HELIX   21  21 SER C    3  GLY C   18  1                                  16    
HELIX   22  22 HIS C   20  PHE C   36  1                                  17    
HELIX   23  23 PRO C   37  PHE C   43  5                                   7    
HELIX   24  24 SER C   52  HIS C   72  1                                  21    
HELIX   25  25 ASP C   75  LEU C   80  1                                   6    
HELIX   26  26 LEU C   80  HIS C   89  1                                  10    
HELIX   27  27 PRO C   95  LEU C  113  1                                  19    
HELIX   28  28 THR C  118  THR C  137  1                                  20    
HELIX   29  29 THR D    4  GLY D   16  1                                  13    
HELIX   30  30 LYS D   19  TYR D   35  1                                  17    
HELIX   31  31 PRO D   36  GLU D   43  5                                   8    
HELIX   32  32 PHE D   42  GLY D   46  5                                   5    
HELIX   33  33 THR D   50  ASN D   57  1                                   8    
HELIX   34  34 ASN D   57  MET D   75  1                                  19    
HELIX   35  35 ASP D   80  PHE D   85  1                                   6    
HELIX   36  36 PHE D   85  LYS D   95  1                                  11    
HELIX   37  37 PRO D  100  GLY D  119  1                                  20    
HELIX   38  38 LYS D  120  PHE D  122  5                                   3    
HELIX   39  39 THR D  123  ALA D  142  1                                  20    
HELIX   40  40 HIS D  143  TYR D  145  5                                   3    
LINK         NE2 HIS A  87                FE   HEM A 142     1555   1555  2.05  
LINK        FE   HEM A 142                 C   CMO A 143     1555   1555  1.77  
LINK        FE   HEM A 142                 O   CMO A 143     1555   1555  2.93  
LINK         NE2 HIS B  92                FE   HEM B 147     1555   1555  2.10  
LINK        FE   HEM B 147                 C   CMO B 148     1555   1555  1.76  
LINK        FE   HEM B 147                 O   CMO B 148     1555   1555  2.92  
LINK         NE2 HIS C  87                FE   HEM C 142     1555   1555  2.15  
LINK        FE   HEM C 142                 C   CMO C 143     1555   1555  1.77  
LINK        FE   HEM C 142                 O   CMO C 143     1555   1555  2.89  
LINK         NE2 HIS D  92                FE   HEM D 147     1555   1555  2.21  
LINK        FE   HEM D 147                 C   CMO D 148     1555   1555  1.75  
LINK        FE   HEM D 147                 O   CMO D 148     1555   1555  2.72  
SITE     1 AC1 16 TYR A  42  PHE A  43  HIS A  45  HIS A  58                    
SITE     2 AC1 16 LYS A  61  LEU A  86  HIS A  87  LEU A  91                    
SITE     3 AC1 16 VAL A  93  ASN A  97  PHE A  98  LEU A 101                    
SITE     4 AC1 16 VAL A 132  LEU A 136  CMO A 143  HOH A 154                    
SITE     1 AC2  3 HIS A  58  VAL A  62  HEM A 142                               
SITE     1 AC3 10 THR B  38  PHE B  41  PHE B  42  HIS B  63                    
SITE     2 AC3 10 SER B  70  HIS B  92  LEU B  96  ASN B 102                    
SITE     3 AC3 10 LEU B 106  CMO B 148                                          
SITE     1 AC4  3 HIS B  63  VAL B  67  HEM B 147                               
SITE     1 AC5 14 ALA A  12  TYR C  42  PHE C  43  HIS C  45                    
SITE     2 AC5 14 HIS C  58  LYS C  61  HIS C  87  LEU C  91                    
SITE     3 AC5 14 VAL C  93  ASN C  97  PHE C  98  LEU C 101                    
SITE     4 AC5 14 LEU C 136  CMO C 143                                          
SITE     1 AC6  3 HIS C  58  VAL C  62  HEM C 142                               
SITE     1 AC7 12 THR D  38  PHE D  41  HIS D  63  SER D  70                    
SITE     2 AC7 12 LEU D  88  HIS D  92  LEU D  96  VAL D  98                    
SITE     3 AC7 12 ASN D 102  LEU D 106  LEU D 141  CMO D 148                    
SITE     1 AC8  3 HIS D  63  VAL D  67  HEM D 147                               
CRYST1   73.800  131.400   63.100  90.00  90.00  90.00 P 21 21 21    8          
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      0.013550  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007610  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015848        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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