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PDBsum entry 1lhb

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Oxygen transport PDB id
1lhb
Jmol
Contents
Protein chain
148 a.a.
Ligands
HEM
HEADER    OXYGEN TRANSPORT                        01-MAR-73   1LHB
OBSLTE     21-JAN-86 1LHB      2LHB
TITLE     CRYSTAL STRUCTURE ANALYSIS OF SEA LAMPREY HEMOGLOBIN AT 2
TITLE    2 ANGSTROMS RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE:;
COMPND   3 CHAIN: NULL;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1
KEYWDS    OXYGEN TRANSPORT
EXPDTA    X-RAY DIFFRACTION
AUTHOR    W.A.HENDRICKSON,W.E.LOVE,J.KARLE
REVDAT  14   21-JAN-86 1LHB    3       OBSLTE
REVDAT  13   04-MAR-85 1LHB    1       SEQRES
REVDAT  12   17-FEB-84 1LHB    1       REMARK
REVDAT  11   30-SEP-83 1LHB    1       REVDAT
REVDAT  10   07-MAR-83 1LHB    3       ATOM
REVDAT   9   14-SEP-81 1LHB    1       REMARK
REVDAT   8   31-DEC-80 1LHB    1       REMARK
REVDAT   7   10-JUL-80 1LHB    3       ATOM
REVDAT   6   07-APR-80 1LHB    3       ATOM
REVDAT   5   19-SEP-78 1LHB    2       CONECT
REVDAT   4   20-JUL-78 1LHB    2       CONECT
REVDAT   3   01-NOV-77 1LHB    1       AUTHOR JRNL   REMARK FORMUL
REVDAT   2   09-SEP-77 1LHB    3       REMARK HETATM
REVDAT   1   06-JAN-77 1LHB    0
JRNL        AUTH   W.A.HENDRICKSON,W.E.LOVE,J.KARLE
JRNL        TITL   CRYSTAL STRUCTURE ANALYSIS OF SEA LAMPREY
JRNL        TITL 2 HEMOGLOBIN AT 2 ANGSTROMS RESOLUTION
JRNL        REF    J.MOL.BIOL.                   V.  74   331 1973
JRNL        REFN   ASTM JMOBAK  UK ISSN 0022-2836
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   W.A.HENDRICKSON,W.E.LOVE
REMARK   1  TITL   STRUCTURE OF LAMPREY HAEMOGLOBIN
REMARK   1  REF    NATURE NEW BIOL.              V. 232   197 1971
REMARK   1  REFN   ASTM NNBYA7  UK ISSN 0369-4887
REMARK   1 REFERENCE 2
REMARK   1  EDIT   R.J.FELDMANN
REMARK   1  REF    ATLAS OF MACROMOLECULAR                 36 1976
REMARK   1  REF  2 STRUCTURE ON MICROFICHE
REMARK   1  PUBL   TRACOR JITCO INC.,ROCKVILLE,MD.
REMARK   1  REFN                   ISBN 0-917934-01-6
REMARK   1 REFERENCE 3
REMARK   1  EDIT   M.O.DAYHOFF
REMARK   1  REF    ATLAS OF PROTEIN SEQUENCE     V.   5   222 1976
REMARK   1  REF  2 AND STRUCTURE,SUPPLEMENT 2
REMARK   1  PUBL   NATIONAL BIOMEDICAL RESEARCH FOUNDATION, SILVER
REMARK   1  PUBL 2 SPRING,MD.
REMARK   1  REFN                   ISSN 0-912466-05-7
REMARK   2
REMARK   2 RESOLUTION. NULL 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) : NULL
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            : 1137
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 45
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 1LHB COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK   5
REMARK   5 1LHB CORRECTION. REFORMAT HEADER INFORMATION TO MEET NEW
REMARK   5 1LHB SPECIFICATIONS. 1LHB ADD FORMUL RECORDS. 1LHB 01-NOV-
REMARK   5 77. 1LHB
REMARK   6
REMARK   6 1LHB CORRECTION. FIX TWO CONECT RECORDS. 20-JUL-78. 1LHB
REMARK   7
REMARK   7 1LHB CORRECTION. FIX CONECT RECORD. 19-SEP-78. 1LHB
REMARK   8
REMARK   8 1LHB CORRECTION. STANDARDIZE NOMENCLATURE TO FOLLOW IUPAC-
REMARK   8 IUB 1LHB RECOMMENDATIONS. INTERCHANGE CD1 AND CD2 FOR
REMARK   8 LEUCINES 1LHB 11, 38, 58, 64, 100, 118, 136, 137, 143, 144.
REMARK   8 INTERCHANGE 1LHB CG1 AND CG2 FOR VALINES 3, 8, 26, 35, 39,
REMARK   8 70, 81, 85, 110, 1LHB 117, 121, 126. 07-APR-80. 1LHB
REMARK   9
REMARK   9 1LHB CORRECTION. FIX ATOM NUMBER FOR ATOM 531. 10-JUL-80.
REMARK   9 1LHB
REMARK  10
REMARK  10 1LHB CORRECTION. STANDARDIZE FORMAT OF REMARK 2. 31-DEC-80.
REMARK  10 1LHB
REMARK  11
REMARK  11 1LHB CORRECTION. CORRECT JOURNAL NAME FOR REFERENCE 1. 1LHB
REMARK  11 14-SEP-81. 1LHB
REMARK  12
REMARK  12 1LHB CORRECTION. CORRECT ATOM NAME FOR ATOM 1037. 07-MAR-
REMARK  12 83. 1LHB
REMARK  13
REMARK  13 1LHB CORRECTION. INSERT REVDAT RECORDS. 30-SEP-83. 1LHB
REMARK  14
REMARK  14 1LHB CORRECTION. CORRECT ISSN FOR REFERENCE 1. 17-FEB-84.
REMARK  14 1LHB
REMARK  15
REMARK  15 1LHB CORRECTION. CORRECT NUMBER OF SEQRES RECORD. 04-MAR-
REMARK  15 85. 1LHB
REMARK  16
REMARK  16 1LHB CORRECTION. THIS ENTRY IS OBSOLETE. 21-JAN-86. 1LHB
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   (%): 41.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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   1/2-X,-Y,1/2+Z
REMARK 290       3555   -X,1/2+Y,1/2-Z
REMARK 290       4555   1/2+X,1/2-Y,-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       22.28500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       15.67000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.31000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       15.67000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.28500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.31000
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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
REMARK 500   CG2  VAL     110     CBC  HEM       1              1.53
REMARK 500   NE2  HIS     104    FE    HEM       1              1.67
REMARK 500   NZ   LYS      16     OD1  ASP      89              1.72
REMARK 500   CE   LYS      16     OD1  ASP      89              1.79
REMARK 500   O    LEU     137     CG2  ILE     140              1.82
REMARK 500   CB   SER     101     O    LEU     144              1.92
REMARK 500   O    THR      43     N    THR      45              2.04
REMARK 500   O    LEU     100     CB   HIS     104              2.06
REMARK 500   O    THR      45     N    ALA      48              2.07
REMARK 500   O    ALA     123     O    ALA     127              2.07
REMARK 500   O    THR      43     CD   PRO      46              2.08
REMARK 500   O    ASP      36     CE   LYS      40              2.09
REMARK 500   O    PHE      42     N    PRO      46              2.11
REMARK 500   CE1  PHE      42     CD1  PHE      52              2.15
REMARK 500   O    GLU      92     N    MET      94              2.15
REMARK 500   CD   LYS      16     OD1  ASP      89              2.16
REMARK 500   CE1  PHE      42     CE1  PHE      52              2.17
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   OE2  GLU     113     CE   LYS     135     4454     0.64
REMARK 500   OE2  GLU     113     NZ   LYS     135     4454     1.06
REMARK 500   OH   TYR      27     NZ   LYS      65     2565     1.61
REMARK 500   CD   LYS      98     OE1  GLU     109     4555     1.61
REMARK 500   CD   GLU     113     CE   LYS     135     4454     1.70
REMARK 500   CE   LYS      98     OE1  GLU     109     4555     1.71
REMARK 500   CD   GLU     113     NZ   LYS     135     4454     1.81
REMARK 500   OE2  GLU     113     CD   LYS     135     4454     1.89
REMARK 500   NZ   LYS      98     OE1  GLU     109     4555     1.94
REMARK 500   NZ   LYS      98     O    PHE     108     4555     1.95
REMARK 500   NZ   LYS      93     NH2  ARG     145     4555     2.07
REMARK 500   NZ   LYS      98     CG   GLU     109     4555     2.13
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    PHE    51   N   -  CA  -  C   ANGL. DEV. = 30.9 DEGREES
REMARK 500    LEU    58   N   -  CA  -  C   ANGL. DEV. =-26.7 DEGREES
REMARK 500    ALA    61   N   -  CA  -  C   ANGL. DEV. =-22.9 DEGREES
REMARK 500    GLY   132   N   -  CA  -  C   ANGL. DEV. =-34.9 DEGREES
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  M RES CSSEQI        PSI       PHI
REMARK 500    ASP    62      -73.08     72.85
REMARK 500    MET    88       64.56    -16.25
REMARK 500    ASP    89       47.97    125.38
REMARK 500    GLU   109     -131.27     82.97
REMARK 500    VAL   110      120.82    125.30
REMARK 500    ASP   130      134.72     88.88
SEQRES   1    148  PRO ILE VAL ASP THR GLY SER VAL ALA PRO LEU SER ALA
SEQRES   2    148  ALA GLU LYS THR LYS ILE ARG SER ALA TRP ALA PRO VAL
SEQRES   3    148  TYR SER ASP TYR GLU THR SER GLY VAL ASP ILE LEU VAL
SEQRES   4    148  LYS PHE PHE THR SER THR PRO ALA ALA GLU GLU PHE PHE
SEQRES   5    148  PRO LYS PHE LYS GLY LEU THR THR ALA ASP GLU LEU LYS
SEQRES   6    148  LYS SER ALA ASP VAL ARG TRP HIS ALA GLU ARG ILE ILE
SEQRES   7    148  ASP ALA VAL ASP ASP ALA VAL ALA SER MET ASP ASP THR
SEQRES   8    148  GLU LYS MET SER SER MET LYS ASP LEU SER GLY LYS HIS
SEQRES   9    148  ALA LYS SER PHE GLU VAL ASP PRO GLU TYR PHE LYS VAL
SEQRES  10    148  LEU ALA ALA VAL ILE ALA ASP THR VAL ALA ALA GLY ASP
SEQRES  11    148  ALA GLY PHE GLU LYS LEU LEU ARG MET ILE CYS ILE LEU
SEQRES  12    148  LEU ARG SER ALA TYR
HET    HEM      1      45
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN     HEM HEME
FORMUL   2  HEM    C34 H32 FE N4 O4
HELIX    1   A SER     12  ASP     29  1                                  18
HELIX    2   B TYR     30  SER     44  1                                  15
HELIX    3   C THR     45  PHE     52  5                                   8
HELIX    4   D ASP     62  LYS     66  1                                   5
HELIX    5   E SER     67  MET     88  1                                  22
HELIX    6   F GLU     92  LYS    106  5TYPE 1 FROM ASN 98 ONWARDS        15
HELIX    7   G ASP    111  ALA    127  1BEGIN WITH 1 TURN OF TYPE 5       17
HELIX    8   H GLY    132  TYR    148  1RESIDUES 146-148 FORM TYPE 5      17
CRYST1   44.570   96.620   31.340  90.00  90.00  90.00 P 21 21 21    4
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      0.022437  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010350  0.000000        0.00000
SCALE3      0.000000  0.000000  0.031908        0.00000
      
PROCHECK
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 References