spacer
spacer

PDBsum entry 1mbn

Go to PDB code: 
Top Page protein ligands links
Oxygen storage PDB id
1mbn
Jmol
Contents
Protein chain
153 a.a.
Ligands
_OH-HEM
HEADER    OXYGEN STORAGE                          05-APR-73   1MBN
TITLE     THE STEREOCHEMISTRY OF THE PROTEIN MYOGLOBIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MYOGLOBIN;
COMPND   3 CHAIN: A;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PHYSETER CATODON;
SOURCE   3 ORGANISM_COMMON: SPERM WHALE;
SOURCE   4 ORGANISM_TAXID: 9755
KEYWDS    OXYGEN STORAGE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.C.WATSON,J.C.KENDREW
REVDAT  21   24-FEB-09 1MBN    1       VERSN
REVDAT  20   27-OCT-83 1MBN    1       REMARK
REVDAT  19   30-SEP-83 1MBN    1       REVDAT
REVDAT  18   12-MAY-83 1MBN    3       REMARK SEQRES ATOM
REVDAT  17   07-MAR-83 1MBN    3       ATOM
REVDAT  16   15-JAN-82 1MBN    1       REMARK
REVDAT  15   15-JUL-81 1MBN    1       REMARK SITE
REVDAT  14   31-DEC-80 1MBN    1       SOURCE REMARK
REVDAT  13   07-APR-80 1MBN    3       ATOM
REVDAT  12   06-FEB-79 1MBN    1       TURN
REVDAT  11   15-JAN-79 1MBN    3       HETATM
REVDAT  10   20-JUL-78 1MBN    2       CONECT
REVDAT   9   24-JAN-78 1MBN    1       HEADER
REVDAT   8   01-NOV-77 1MBN    1       AUTHOR JRNL   REMARK FORMUL
REVDAT   7   09-SEP-77 1MBN    1       REMARK
REVDAT   6   23-AUG-77 1MBN    3       HETATM CONECT
REVDAT   5   13-JUN-77 1MBN    1       FTNOTE HET
REVDAT   4   28-MAR-77 1MBN    1       REMARK
REVDAT   3   20-SEP-76 1MBN    2       CONECT
REVDAT   2   28-JUN-76 1MBN    1       HEADER
REVDAT   1   19-MAY-76 1MBN    0
JRNL        AUTH   H.C.WATSON
JRNL        TITL   THE STEREOCHEMISTRY OF THE PROTEIN MYOGLOBIN
JRNL        REF    PROG.STEREOCHEM.              V.   4   299 1969
JRNL        REFN                   ISSN 0079-6808
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   J.C.KENDREW
REMARK   1  TITL   MYOGLOBIN AND THE STRUCTURE OF PROTEINS (NOBEL
REMARK   1  TITL 2 LECTURE, DECEMBER 11, 1962)
REMARK   1  REF    PRIX NOBEL                             103 1963
REMARK   1  REFN                   ISSN 0546-8175
REMARK   1 REFERENCE 2
REMARK   1  EDIT   R.J.FELDMANN
REMARK   1  REF    ATLAS OF MACROMOLECULAR                125 1976
REMARK   1  REF  2 STRUCTURE ON MICROFICHE
REMARK   1  PUBL   TRACOR JITCO INC.,ROCKVILLE,MD.
REMARK   1  REFN
REMARK   1 REFERENCE 3
REMARK   1  EDIT   M.O.DAYHOFF
REMARK   1  REF    ATLAS OF PROTEIN SEQUENCE     V.   5    84 1972
REMARK   1  REF  2 AND STRUCTURE (DATA SECTION)
REMARK   1  PUBL   NATIONAL BIOMEDICAL RESEARCH FOUNDATION, SILVER
REMARK   1  PUBL 2 SPRING,MD.
REMARK   1  REFN
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : NULL
REMARK   3   AUTHORS     : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 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 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   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1216
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 44
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  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : 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  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1MBN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
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   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   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   (%): 36.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       15.45000
REMARK 290   SMTRY3   2  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: 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   NZ   LYS A    78     OE1  GLU A    85              1.81
REMARK 500   NZ   LYS A   145     OE1  GLU A   148              2.08
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   O    ALA A    19     NZ   LYS A    63     2646     1.01
REMARK 500   CB   HIS A    48     NZ   LYS A    56     2655     1.64
REMARK 500   C    ALA A    19     NZ   LYS A    63     2646     2.03
REMARK 500   CG   HIS A    48     NZ   LYS A    56     2655     2.14
REMARK 500   O    ALA A    19     CE   LYS A    63     2646     2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLU A   4   CG    GLU A   4   CD      0.125
REMARK 500    GLU A   4   CD    GLU A   4   OE2    -0.152
REMARK 500    GLU A   6   CD    GLU A   6   OE1    -0.094
REMARK 500    TRP A  14   NE1   TRP A  14   CE2    -0.159
REMARK 500    TRP A  14   CE2   TRP A  14   CZ2     0.104
REMARK 500    TRP A  14   CE2   TRP A  14   CD2    -0.075
REMARK 500    GLU A  18   CG    GLU A  18   CD      0.094
REMARK 500    GLU A  18   CD    GLU A  18   OE2    -0.094
REMARK 500    ARG A  31   NE    ARG A  31   CZ      0.081
REMARK 500    SER A  35   CB    SER A  35   OG      0.085
REMARK 500    PRO A  37   CD    PRO A  37   N      -0.118
REMARK 500    GLU A  38   CG    GLU A  38   CD      0.091
REMARK 500    GLU A  41   CG    GLU A  41   CD      0.101
REMARK 500    PHE A  46   C     PHE A  46   O       0.120
REMARK 500    HIS A  48   CG    HIS A  48   CD2     0.060
REMARK 500    GLU A  52   CD    GLU A  52   OE2    -0.116
REMARK 500    GLU A  85   CD    GLU A  85   OE2    -0.077
REMARK 500    ILE A  99   C     ILE A  99   O       0.120
REMARK 500    TYR A 103   CE1   TYR A 103   CZ     -0.093
REMARK 500    TYR A 103   CZ    TYR A 103   CE2     0.116
REMARK 500    GLU A 105   CG    GLU A 105   CD      0.110
REMARK 500    GLU A 105   CD    GLU A 105   OE2    -0.130
REMARK 500    GLU A 105   C     GLU A 105   O       0.146
REMARK 500    PHE A 106   CG    PHE A 106   CD1    -0.098
REMARK 500    HIS A 113   CG    HIS A 113   CD2     0.074
REMARK 500    ASP A 122   CG    ASP A 122   OD1     0.179
REMARK 500    MET A 131   C     MET A 131   O       0.120
REMARK 500    ASN A 132   CG    ASN A 132   OD1     0.241
REMARK 500    GLU A 136   CD    GLU A 136   OE2    -0.094
REMARK 500    ARG A 139   NE    ARG A 139   CZ      0.120
REMARK 500    ARG A 139   CZ    ARG A 139   NH1    -0.089
REMARK 500    GLY A 150   C     GLY A 150   O       0.124
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    SER A   3   CB  -  CA  -  C   ANGL. DEV. = -21.1 DEGREES
REMARK 500    SER A   3   N   -  CA  -  CB  ANGL. DEV. =  15.1 DEGREES
REMARK 500    SER A   3   N   -  CA  -  C   ANGL. DEV. =  19.3 DEGREES
REMARK 500    GLU A   4   N   -  CA  -  CB  ANGL. DEV. =  25.1 DEGREES
REMARK 500    GLU A   4   OE1 -  CD  -  OE2 ANGL. DEV. =   8.2 DEGREES
REMARK 500    GLN A   8   N   -  CA  -  CB  ANGL. DEV. =  21.2 DEGREES
REMARK 500    LEU A   9   CB  -  CA  -  C   ANGL. DEV. = -15.3 DEGREES
REMARK 500    VAL A  10   N   -  CA  -  CB  ANGL. DEV. =  20.9 DEGREES
REMARK 500    VAL A  13   N   -  CA  -  CB  ANGL. DEV. =  25.6 DEGREES
REMARK 500    TRP A  14   CB  -  CA  -  C   ANGL. DEV. =  15.7 DEGREES
REMARK 500    TRP A  14   NE1 -  CE2 -  CZ2 ANGL. DEV. =  -8.5 DEGREES
REMARK 500    TRP A  14   CG  -  CD2 -  CE3 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    TRP A  14   CD2 -  CE3 -  CZ3 ANGL. DEV. =  -9.4 DEGREES
REMARK 500    TRP A  14   CE3 -  CZ3 -  CH2 ANGL. DEV. =   7.3 DEGREES
REMARK 500    TRP A  14   CH2 -  CZ2 -  CE2 ANGL. DEV. =  -6.7 DEGREES
REMARK 500    ALA A  15   CB  -  CA  -  C   ANGL. DEV. = -15.5 DEGREES
REMARK 500    ALA A  15   N   -  CA  -  CB  ANGL. DEV. =   9.5 DEGREES
REMARK 500    LYS A  16   N   -  CA  -  CB  ANGL. DEV. = -11.8 DEGREES
REMARK 500    VAL A  17   CB  -  CA  -  C   ANGL. DEV. = -18.8 DEGREES
REMARK 500    GLU A  18   OE1 -  CD  -  OE2 ANGL. DEV. =  10.1 DEGREES
REMARK 500    ALA A  22   CB  -  CA  -  C   ANGL. DEV. =  21.9 DEGREES
REMARK 500    ALA A  22   N   -  CA  -  CB  ANGL. DEV. = -17.4 DEGREES
REMARK 500    HIS A  24   N   -  CA  -  CB  ANGL. DEV. = -14.4 DEGREES
REMARK 500    GLN A  26   CB  -  CA  -  C   ANGL. DEV. =  19.3 DEGREES
REMARK 500    ASP A  27   CB  -  CA  -  C   ANGL. DEV. =  20.4 DEGREES
REMARK 500    ASP A  27   N   -  CA  -  CB  ANGL. DEV. = -12.4 DEGREES
REMARK 500    ASP A  27   CB  -  CG  -  OD1 ANGL. DEV. =   7.6 DEGREES
REMARK 500    LEU A  29   CB  -  CA  -  C   ANGL. DEV. =  18.5 DEGREES
REMARK 500    ILE A  30   CB  -  CA  -  C   ANGL. DEV. =  16.7 DEGREES
REMARK 500    PHE A  33   CB  -  CG  -  CD1 ANGL. DEV. =  -4.5 DEGREES
REMARK 500    HIS A  36   N   -  CA  -  CB  ANGL. DEV. = -12.9 DEGREES
REMARK 500    GLU A  38   N   -  CA  -  CB  ANGL. DEV. = -13.0 DEGREES
REMARK 500    GLU A  38   OE1 -  CD  -  OE2 ANGL. DEV. =   7.8 DEGREES
REMARK 500    LEU A  40   CB  -  CA  -  C   ANGL. DEV. = -15.0 DEGREES
REMARK 500    GLU A  41   OE1 -  CD  -  OE2 ANGL. DEV. =   8.3 DEGREES
REMARK 500    LYS A  42   CB  -  CA  -  C   ANGL. DEV. = -20.2 DEGREES
REMARK 500    PHE A  43   N   -  CA  -  CB  ANGL. DEV. = -16.8 DEGREES
REMARK 500    ASP A  44   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES
REMARK 500    ARG A  45   N   -  CA  -  CB  ANGL. DEV. =  16.4 DEGREES
REMARK 500    LYS A  47   N   -  CA  -  CB  ANGL. DEV. =  15.3 DEGREES
REMARK 500    LYS A  50   N   -  CA  -  CB  ANGL. DEV. =  11.6 DEGREES
REMARK 500    GLU A  52   CB  -  CA  -  C   ANGL. DEV. = -15.8 DEGREES
REMARK 500    ALA A  53   N   -  CA  -  CB  ANGL. DEV. =  10.0 DEGREES
REMARK 500    LYS A  56   CB  -  CA  -  C   ANGL. DEV. = -14.0 DEGREES
REMARK 500    ALA A  57   CB  -  CA  -  C   ANGL. DEV. = -13.5 DEGREES
REMARK 500    ALA A  57   N   -  CA  -  CB  ANGL. DEV. =  13.6 DEGREES
REMARK 500    SER A  58   CB  -  CA  -  C   ANGL. DEV. = -15.7 DEGREES
REMARK 500    GLU A  59   OE1 -  CD  -  OE2 ANGL. DEV. =   7.9 DEGREES
REMARK 500    ASP A  60   CB  -  CG  -  OD1 ANGL. DEV. =   8.8 DEGREES
REMARK 500    ASP A  60   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS     110 ANGLE DEVIATIONS.
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    SER A   3      150.06    -49.57
REMARK 500    ALA A  15      -35.44    -39.68
REMARK 500    ASP A  27      -75.10    -39.32
REMARK 500    LEU A  49      109.62    -50.79
REMARK 500    LYS A  62      -76.57    -41.69
REMARK 500    LEU A  76      -70.64    -48.91
REMARK 500    LYS A  77      -23.21    -39.01
REMARK 500    LYS A  79       47.57     38.43
REMARK 500    HIS A  81       57.68    -91.01
REMARK 500    LYS A  87      -71.82    -44.80
REMARK 500    LYS A  96      -62.54   -137.99
REMARK 500    PHE A 106      -73.07    -44.55
REMARK 500    GLU A 109      -71.45    -67.32
REMARK 500    SER A 117      -52.98    -29.18
REMARK 500    LYS A 147      -70.97    -40.90
REMARK 500    GLU A 148      -61.93    -27.00
REMARK 500    GLN A 152       77.69     87.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500   M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500     GLN A   8       168.5                     ALPHA-CARBON
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 155  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  93   NE2
REMARK 620 2  OH A 154   O   167.9
REMARK 620 N                    1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: HMB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: HEM BINDING SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OH A 154
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 155
DBREF  1MBN A    1   153  UNP    P02185   MYG_PHYCA        1    153
SEQRES   1 A  153  VAL LEU SER GLU GLY GLU TRP GLN LEU VAL LEU HIS VAL
SEQRES   2 A  153  TRP ALA LYS VAL GLU ALA ASP VAL ALA GLY HIS GLY GLN
SEQRES   3 A  153  ASP ILE LEU ILE ARG LEU PHE LYS SER HIS PRO GLU THR
SEQRES   4 A  153  LEU GLU LYS PHE ASP ARG PHE LYS HIS LEU LYS THR GLU
SEQRES   5 A  153  ALA GLU MET LYS ALA SER GLU ASP LEU LYS LYS HIS GLY
SEQRES   6 A  153  VAL THR VAL LEU THR ALA LEU GLY ALA ILE LEU LYS LYS
SEQRES   7 A  153  LYS GLY HIS HIS GLU ALA GLU LEU LYS PRO LEU ALA GLN
SEQRES   8 A  153  SER HIS ALA THR LYS HIS LYS ILE PRO ILE LYS TYR LEU
SEQRES   9 A  153  GLU PHE ILE SER GLU ALA ILE ILE HIS VAL LEU HIS SER
SEQRES  10 A  153  ARG HIS PRO GLY ASP PHE GLY ALA ASP ALA GLN GLY ALA
SEQRES  11 A  153  MET ASN LYS ALA LEU GLU LEU PHE ARG LYS ASP ILE ALA
SEQRES  12 A  153  ALA LYS TYR LYS GLU LEU GLY TYR GLN GLY
HET     OH  A 154       1
HET    HEM  A 155      43
HETNAM      OH HYDROXIDE ION
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN     HEM HEME
FORMUL   2   OH    H O 1-
FORMUL   3  HEM    C34 H32 FE N4 O4
HELIX    1   A SER A    3  GLU A   18  1N=3.63,PHI=1.73,H=1.50            16
HELIX    2   B ASP A   20  SER A   35  1N=3.72,PHI=1.69,H=1.47            16
HELIX    3   C HIS A   36  LYS A   42  1SHORT IRREGULAR HELIX              7
HELIX    4   D THR A   51  ALA A   57  1N=3.63,PHI=1.73,H=1.45             7
HELIX    5   E SER A   58  LYS A   77  1BENT ABOUT 7 DEG. AT THR (67)     20
HELIX    6   F LEU A   86  ALA A   94  1N=3.70,PHI=1.70,H=1.46             9
HELIX    7   G PRO A  100  ARG A  118  1N=3.59,PHI=1.75,H=1.53            19
HELIX    8   H ALA A  125  GLU A  148  1N=3.63,PHI=1.73,H=1.49            24
LINK         NE2 HIS A  93                FE   HEM A 155     1555   1555  2.19
LINK         O    OH A 154                FE   HEM A 155     1555   1555  2.15
SITE     1 HMB  9 PHE A  43  ARG A  45  HIS A  64  VAL A  68
SITE     2 HMB  9 ALA A  71  HIS A  93  HIS A  97  LEU A 104
SITE     3 HMB  9 ILE A 107
SITE     1 AC1  3 PHE A  43  HIS A  64  HEM A 155
SITE     1 AC2 10 PHE A  43  ARG A  45  LEU A  89  SER A  92
SITE     2 AC2 10 HIS A  93  HIS A  97  ILE A  99  TYR A 103
SITE     3 AC2 10 PHE A 138   OH A 154
CRYST1   64.500   30.900   34.700  90.00 106.00  90.00 P 1 21 1      2
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      0.015504  0.000000  0.004446        0.00000
SCALE2      0.000000  0.032362  0.000000        0.00000
SCALE3      0.000000  0.000000  0.029980        0.00000
      
PROCHECK
Go to PROCHECK summary
 References