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Database: PDB
Entry: 1CMY
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HEADER    OXYGEN TRANSPORT                        18-SEP-92   1CMY              
TITLE     THE MUTATION BETA99 ASP-TYR STABILIZES Y-A NEW, COMPOSITE QUATERNARY  
TITLE    2 STATE OF HUMAN HEMOGLOBIN                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEMOGLOBIN YPSILANTI (CARBONMONOXY) (ALPHA CHAIN);         
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HEMOGLOBIN YPSILANTI (CARBONMONOXY) (BETA CHAIN);          
COMPND   7 CHAIN: B, D;                                                         
COMPND   8 ENGINEERED: YES                                                      
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    OXYGEN TRANSPORT                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.R.SMITH,E.E.LATTMAN,C.W.CARTER JUNIOR                               
REVDAT   4   07-FEB-24 1CMY    1       REMARK SEQADV LINK                       
REVDAT   3   24-FEB-09 1CMY    1       VERSN                                    
REVDAT   2   01-APR-03 1CMY    1       JRNL                                     
REVDAT   1   31-OCT-93 1CMY    0                                                
JRNL        AUTH   F.R.SMITH,E.E.LATTMAN,C.W.CARTER JR.                         
JRNL        TITL   THE MUTATION BETA 99 ASP-TYR STABILIZES Y--A NEW, COMPOSITE  
JRNL        TITL 2 QUATERNARY STATE OF HUMAN HEMOGLOBIN.                        
JRNL        REF    PROTEINS                      V.  10    81 1991              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   1896430                                                      
JRNL        DOI    10.1002/PROT.340100202                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
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) : 0.269                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
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) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4392                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 172                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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) : 0.008 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.021 ; 0.030               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.027 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.007 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.113 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.210 ; 0.500               
REMARK   3    MULTIPLE TORSION                (A) : 0.279 ; 0.500               
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : 0.250 ; 0.500               
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 1.300 ; 3.000               
REMARK   3    STAGGERED                 (DEGREES) : 23.000; 15.000              
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 1CMY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000172402.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
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: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-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       96.40000            
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       48.20000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       48.20000            
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       96.40000            
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: TETRAMERIC                        
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASN B   139     OH   TYR D   145              1.70            
REMARK 500   OH   TYR B   145     OD1  ASN D   139              1.89            
REMARK 500   O    PHE C    36     OG1  THR C    39              2.08            
REMARK 500   OE2  GLU D     7     NZ   LYS D   132              2.12            
REMARK 500   NH2  ARG C    31     O    PHE D   122              2.17            
REMARK 500   OD2  ASP C    47     OG   SER C    49              2.17            
REMARK 500   O    LEU B    32     NE2  GLN B    39              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CA   LYS A    16     OE2  GLU D    90     4567     0.76            
REMARK 500   CE   LYS C    90     CA   SER D    44     2664     1.03            
REMARK 500   CE   LYS C    90     C    SER D    44     2664     1.19            
REMARK 500   NZ   LYS C    90     CB   SER D    44     2664     1.25            
REMARK 500   O    GLY A    15     OE1  GLU D    90     4567     1.29            
REMARK 500   CD   LYS C    90     O    SER D    44     2664     1.38            
REMARK 500   N    LYS A    16     OE2  GLU D    90     4567     1.38            
REMARK 500   CE   LYS C    90     CB   SER D    44     2664     1.47            
REMARK 500   NZ   LYS C    90     OG   SER D    44     2664     1.50            
REMARK 500   O    GLY A    15     CD   GLU D    90     4567     1.50            
REMARK 500   CE   LYS C    90     O    SER D    44     2664     1.58            
REMARK 500   NE2  HIS A    20     O    GLY D    83     4567     1.61            
REMARK 500   C    LYS A    16     OE2  GLU D    90     4567     1.70            
REMARK 500   C    GLY A    15     CD   GLU D    90     4567     1.84            
REMARK 500   NZ   LYS B    95     O2D  HEM A   142     2664     1.91            
REMARK 500   CD   LYS C    90     C    SER D    44     2664     1.98            
REMARK 500   CA   LYS A    16     CD   GLU D    90     4567     1.98            
REMARK 500   N    LYS A    16     CD   GLU D    90     4567     2.02            
REMARK 500   C    GLY A    15     OE2  GLU D    90     4567     2.03            
REMARK 500   CG   LYS C    90     O    SER D    44     2664     2.04            
REMARK 500   CB   ASN D    19     ND2  ASN D    19     4557     2.05            
REMARK 500   NZ   LYS A    61     NZ   LYS B    95     3565     2.06            
REMARK 500   OD2  ASP B    47     NE2  HIS C    20     6666     2.08            
REMARK 500   NZ   LYS C    90     CA   SER D    44     2664     2.19            
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 141   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    THR D  50   N   -  CA  -  CB  ANGL. DEV. =  12.8 DEGREES          
REMARK 500    HIS D  77   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    ASP D  79   CB  -  CG  -  OD1 ANGL. DEV. =  -7.3 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    LEU A   2      102.67     85.58                                   
REMARK 500    PHE A  43       61.18   -119.51                                   
REMARK 500    HIS A  50      -72.93    -24.16                                   
REMARK 500    HIS A  72       18.16    132.96                                   
REMARK 500    ASP A  75       44.79   -162.20                                   
REMARK 500    HIS A  89      -72.39    -77.38                                   
REMARK 500    HIS B   2      -63.75   -136.69                                   
REMARK 500    LEU B   3      108.45     42.46                                   
REMARK 500    ALA B  76       53.40   -117.88                                   
REMARK 500    HIS B  77       28.75   -175.52                                   
REMARK 500    CYS B  93      -84.89    -71.87                                   
REMARK 500    ASP B  94       53.58   -103.45                                   
REMARK 500    LYS B  95      -39.31   -155.72                                   
REMARK 500    PHE B 122       70.98   -106.23                                   
REMARK 500    LEU C   2      104.32     86.05                                   
REMARK 500    PHE C  43       60.17   -115.78                                   
REMARK 500    HIS C  50      -78.98    -23.24                                   
REMARK 500    HIS C  72       18.84    132.47                                   
REMARK 500    ASP C  75       48.72   -161.82                                   
REMARK 500    HIS D   2      -66.55   -131.98                                   
REMARK 500    LEU D   3      104.97     46.61                                   
REMARK 500    ALA D  76       50.07   -116.30                                   
REMARK 500    HIS D  77       36.74   -178.89                                   
REMARK 500    CYS D  93      -78.86    -76.30                                   
REMARK 500    ASP D  94       50.89   -103.17                                   
REMARK 500    LYS D  95      -34.96   -154.70                                   
REMARK 500    PRO D 100      -28.44    -39.77                                   
REMARK 500    PHE D 122       71.53   -105.73                                   
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   92.2                                              
REMARK 620 3 HEM A 142   NB   91.5  90.6                                        
REMARK 620 4 HEM A 142   NC   88.2 179.5  89.8                                  
REMARK 620 5 HEM A 142   ND   87.4  89.6 178.9  90.0                            
REMARK 620 N                    1     2     3     4                             
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   84.5                                              
REMARK 620 3 HEM B 147   NB   92.1  90.7                                        
REMARK 620 4 HEM B 147   NC   91.6 176.1  90.0                                  
REMARK 620 5 HEM B 147   ND   84.6  89.8 176.6  89.3                            
REMARK 620 N                    1     2     3     4                             
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   84.0                                              
REMARK 620 3 HEM C 142   NB   92.3  89.7                                        
REMARK 620 4 HEM C 142   NC   89.3 173.2  89.3                                  
REMARK 620 5 HEM C 142   ND   80.0  89.3 172.3  90.8                            
REMARK 620 N                    1     2     3     4                             
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   93.4                                              
REMARK 620 3 HEM D 147   NB  101.4  90.0                                        
REMARK 620 4 HEM D 147   NC   84.2 177.5  90.0                                  
REMARK 620 5 HEM D 147   ND   76.5  90.5 177.8  89.4                            
REMARK 620 N                    1     2     3     4                             
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 HEM B 147                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 147                 
DBREF  1CMY A    1   141  UNP    P69905   HBA_HUMAN        1    141             
DBREF  1CMY B    1   146  UNP    P68871   HBB_HUMAN        1    146             
DBREF  1CMY C    1   141  UNP    P69905   HBA_HUMAN        1    141             
DBREF  1CMY D    1   146  UNP    P68871   HBB_HUMAN        1    146             
SEQADV 1CMY TYR B   99  UNP  P68871    ASP    99 CONFLICT                       
SEQADV 1CMY TYR D   99  UNP  P68871    ASP    99 CONFLICT                       
SEQRES   1 A  141  VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA          
SEQRES   2 A  141  TRP GLY LYS VAL GLY ALA HIS ALA GLY 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 LYS LYS VAL ALA ASP ALA          
SEQRES   6 A  141  LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN          
SEQRES   7 A  141  ALA LEU SER ALA 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 CYS          
SEQRES   9 A  141  LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE          
SEQRES  10 A  141  THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA          
SEQRES  11 A  141  SER VAL SER THR VAL LEU THR SER LYS TYR ARG                  
SEQRES   1 B  146  VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA          
SEQRES   2 B  146  LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU          
SEQRES   3 B  146  ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN          
SEQRES   4 B  146  ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP          
SEQRES   5 B  146  ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS          
SEQRES   6 B  146  LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU          
SEQRES   7 B  146  ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU          
SEQRES   8 B  146  HIS CYS ASP LYS LEU HIS VAL TYR PRO GLU ASN PHE ARG          
SEQRES   9 B  146  LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS          
SEQRES  10 B  146  PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR          
SEQRES  11 B  146  GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS          
SEQRES  12 B  146  LYS TYR HIS                                                  
SEQRES   1 C  141  VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA          
SEQRES   2 C  141  TRP GLY LYS VAL GLY ALA HIS ALA GLY 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 LYS LYS VAL ALA ASP ALA          
SEQRES   6 C  141  LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN          
SEQRES   7 C  141  ALA LEU SER ALA 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 CYS          
SEQRES   9 C  141  LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE          
SEQRES  10 C  141  THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA          
SEQRES  11 C  141  SER VAL SER THR VAL LEU THR SER LYS TYR ARG                  
SEQRES   1 D  146  VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA          
SEQRES   2 D  146  LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU          
SEQRES   3 D  146  ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN          
SEQRES   4 D  146  ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP          
SEQRES   5 D  146  ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS          
SEQRES   6 D  146  LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU          
SEQRES   7 D  146  ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU          
SEQRES   8 D  146  HIS CYS ASP LYS LEU HIS VAL TYR PRO GLU ASN PHE ARG          
SEQRES   9 D  146  LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS          
SEQRES  10 D  146  PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR          
SEQRES  11 D  146  GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS          
SEQRES  12 D  146  LYS TYR HIS                                                  
HET    HEM  A 142      43                                                       
HET    HEM  B 147      43                                                       
HET    HEM  C 142      43                                                       
HET    HEM  D 147      43                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     HEM HEME                                                             
FORMUL   5  HEM    4(C34 H32 FE N4 O4)                                          
HELIX    1  AA SER A    3  GLY A   18  1                                  16    
HELIX    2  AB HIS A   20  SER A   35  1                                  16    
HELIX    3  AC PHE A   36  TYR A   42  1                                   7    
HELIX    4  AD SER A   52  ALA A   71  1                                  20    
HELIX    5  AE LEU A   80  ALA A   88  1                                   9    
HELIX    6  AG ASP A   94  HIS A  112  1                                  19    
HELIX    7  AH THR A  118  SER A  138  1                                  21    
HELIX    8  BA THR B    4  VAL B   18  1                                  15    
HELIX    9  BB ASN B   19  VAL B   34  1                                  16    
HELIX   10  BC TYR B   35  PHE B   41  1                                   7    
HELIX   11  BD THR B   50  GLY B   56  1                                   7    
HELIX   12  BE ASN B   57  ALA B   76  1                                  20    
HELIX   13  BF PHE B   85  CYS B   93  1                                   9    
HELIX   14  BG TYR B   99  HIS B  117  1                                  19    
HELIX   15  BH THR B  123  HIS B  143  1                                  21    
HELIX   16  CA SER C    3  GLY C   18  1                                  16    
HELIX   17  CB HIS C   20  SER C   35  1                                  16    
HELIX   18  CC PHE C   36  TYR C   42  1                                   7    
HELIX   19  CD SER C   52  ALA C   71  1                                  20    
HELIX   20  CE LEU C   80  ALA C   88  1                                   9    
HELIX   21  CG ASP C   94  HIS C  112  1                                  19    
HELIX   22  CH THR C  118  SER C  138  1                                  21    
HELIX   23  DA THR D    4  VAL D   18  1                                  15    
HELIX   24  DB ASN D   19  VAL D   34  1                                  16    
HELIX   25  DC TYR D   35  PHE D   41  1                                   7    
HELIX   26  DD THR D   50  GLY D   56  1                                   7    
HELIX   27  DE ASN D   57  ALA D   76  1                                  20    
HELIX   28  DF PHE D   85  CYS D   93  1                                   9    
HELIX   29  DG TYR D   99  HIS D  117  1                                  19    
HELIX   30  DH THR D  123  HIS D  143  1                                  21    
LINK         NE2 HIS A  87                FE   HEM A 142     1555   1555  2.02  
LINK         NE2 HIS B  92                FE   HEM B 147     1555   1555  2.03  
LINK         NE2 HIS C  87                FE   HEM C 142     1555   1555  2.09  
LINK         NE2 HIS D  92                FE   HEM D 147     1555   1555  1.99  
SITE     1 AC1 16 TYR A  42  PHE A  43  HIS A  45  PHE A  46                    
SITE     2 AC1 16 HIS A  58  LYS A  61  VAL A  62  ALA A  65                    
SITE     3 AC1 16 HIS A  87  LEU A  91  VAL A  93  ASN A  97                    
SITE     4 AC1 16 PHE A  98  LEU A 101  VAL A 132  LYS B  95                    
SITE     1 AC2 12 THR B  38  PHE B  41  PHE B  42  HIS B  63                    
SITE     2 AC2 12 LYS B  66  PHE B  71  HIS B  92  VAL B  98                    
SITE     3 AC2 12 ASN B 102  LEU B 106  VAL B 137  LEU B 141                    
SITE     1 AC3 14 TYR C  42  PHE C  43  HIS C  45  PHE C  46                    
SITE     2 AC3 14 HIS C  58  LYS C  61  LEU C  83  HIS C  87                    
SITE     3 AC3 14 LEU C  91  VAL C  93  ASN C  97  PHE C  98                    
SITE     4 AC3 14 LEU C 101  VAL C 132                                          
SITE     1 AC4 15 THR D  38  PHE D  41  PHE D  42  HIS D  63                    
SITE     2 AC4 15 LYS D  66  VAL D  67  PHE D  71  LEU D  88                    
SITE     3 AC4 15 LEU D  91  HIS D  92  LEU D  96  VAL D  98                    
SITE     4 AC4 15 ASN D 102  LEU D 106  LEU D 141                               
CRYST1   93.100   93.100  144.600  90.00  90.00 120.00 P 32 2 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010741  0.006201  0.000000        0.00000                         
SCALE2      0.000000  0.012403  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006916        0.00000                         
MTRIX1   1  0.033590  0.987120  0.156400      -75.69865    1                    
MTRIX2   1  0.986080 -0.058230  0.155740       36.84016    1                    
MTRIX3   1  0.162840  0.148990 -0.975340      260.36945    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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