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HEADER OXYGEN STORAGE/TRANSPORT 26-OCT-99 1D8U TITLE CRYSTAL STRUCTURE OF NON-SYMBIOTIC PLANT HEMOGLOBIN FROM TITLE 2 RICE COMPND MOL_ID: 1; COMPND 2 MOLECULE: NON-SYMBIOTIC HEMOGLOBIN; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ORYZA SATIVA; SOURCE 3 ORGANISM_COMMON: RICE; SOURCE 4 ORGAN: ROOT; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A KEYWDS GLOBIN, BIS-HISTIDYL, HEME PROTEIN, OXYGEN STORAGE/TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR M.HARGROVE,E.A.BRUCKER,B.STEC,J.S.OLSON,G.N.PHILLIPS JR. REVDAT 2 01-APR-03 1D8U 1 JRNL REVDAT 1 10-JAN-01 1D8U 0 JRNL AUTH M.S.HARGROVE,E.A.BRUCKER,B.STEC,G.SARATH, JRNL AUTH 2 R.ARREDONDO-PETER,R.V.KLUCAS,J.S.OLSON, JRNL AUTH 3 G.N.PHILLIPS JR. JRNL TITL CRYSTAL STRUCTURE OF A NONSYMBIOTIC PLANT JRNL TITL 2 HEMOGLOBIN. JRNL REF STRUCTURE FOLD.DES. V. 8 1005 2000 JRNL REFN ASTM FODEFH UK ISSN 1359-0278 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.35 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1, CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.8 REMARK 3 NUMBER OF REFLECTIONS : 19025 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : 1 SET RANDOM REMARK 3 R VALUE (WORKING SET) : 0.208 REMARK 3 FREE R VALUE : 0.261 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1879 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 : 2576 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 86 REMARK 3 SOLVENT ATOMS : 203 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 27.20 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 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) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 2.11 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 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1D8U COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB009898. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-AUG-1997 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.80 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X4A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.74 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : FUJI REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19025 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 87.8 REMARK 200 DATA REDUNDANCY : 8.060 REMARK 200 R MERGE (I) : 0.70000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42 REMARK 200 COMPLETENESS FOR SHELL (%) : 0.7 REMARK 200 DATA REDUNDANCY IN SHELL : 3.40 REMARK 200 R MERGE FOR SHELL (I) : 0.27100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: PHASES REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 64.71 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.49 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM PHOSPHATE, SUCROSE, REMARK 280 POTASSIUM PHOSPHATE, PH 7.8, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 22K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,1/3+Z REMARK 290 3555 -X+Y,-X,2/3+Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,2/3-Z REMARK 290 6555 -X,-X+Y,1/3-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 18.50000 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 37.00000 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 37.00000 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 18.50000 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 2 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 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 0 REMARK 465 MET B 0 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),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 MET A 137 SD MET A 137 CE -0.076 REMARK 500 MET A 142 CG MET A 142 SD -0.077 REMARK 500 MET A 161 SD MET A 161 CE 0.055 REMARK 500 MET B 80 SD MET B 80 CE 0.070 REMARK 500 MET B 142 CG MET B 142 SD -0.060 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 A 13 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 GLU A 132 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 GLU B 132 N - CA - C ANGL. DEV. = 8.8 DEGREES REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 20 DISTANCE = 8.45 ANGSTROMS REMARK 525 HOH 22 DISTANCE = 5.35 ANGSTROMS REMARK 525 HOH 23 DISTANCE = 6.87 ANGSTROMS REMARK 525 HOH 26 DISTANCE = 7.12 ANGSTROMS REMARK 525 HOH 70 DISTANCE = 6.02 ANGSTROMS REMARK 525 HOH 92 DISTANCE = 5.61 ANGSTROMS REMARK 525 HOH 99 DISTANCE = 5.64 ANGSTROMS REMARK 525 HOH 105 DISTANCE = 6.02 ANGSTROMS REMARK 525 HOH 118 DISTANCE = 6.34 ANGSTROMS REMARK 525 HOH 131 DISTANCE = 5.79 ANGSTROMS REMARK 525 HOH 135 DISTANCE = 5.10 ANGSTROMS REMARK 525 HOH 136 DISTANCE = 7.81 ANGSTROMS REMARK 525 HOH 149 DISTANCE = 6.14 ANGSTROMS REMARK 525 HOH 162 DISTANCE = 5.51 ANGSTROMS REMARK 525 HOH 164 DISTANCE = 5.00 ANGSTROMS REMARK 525 HOH 167 DISTANCE = 5.08 ANGSTROMS REMARK 525 HOH 179 DISTANCE = 5.53 ANGSTROMS REMARK 525 HOH 180 DISTANCE = 8.07 ANGSTROMS REMARK 525 HOH 182 DISTANCE = 5.30 ANGSTROMS REMARK 525 HOH 183 DISTANCE = 5.73 ANGSTROMS REMARK 525 HOH 195 DISTANCE = 5.66 ANGSTROMS REMARK 525 HOH 200 DISTANCE = 6.35 ANGSTROMS DBREF 1D8U A 0 165 UNP O04986 HBL1_ORYSA 1 166 DBREF 1D8U B 0 165 UNP O04986 HBL1_ORYSA 1 166 SEQRES 1 A 166 MET ALA LEU VAL GLU ASP ASN ASN ALA VAL ALA VAL SER SEQRES 2 A 166 PHE SER GLU GLU GLN GLU ALA LEU VAL LEU LYS SER TRP SEQRES 3 A 166 ALA ILE LEU LYS LYS ASP SER ALA ASN ILE ALA LEU ARG SEQRES 4 A 166 PHE PHE LEU LYS ILE PHE GLU VAL ALA PRO SER ALA SER SEQRES 5 A 166 GLN MET PHE SER PHE LEU ARG ASN SER ASP VAL PRO LEU SEQRES 6 A 166 GLU LYS ASN PRO LYS LEU LYS THR HIS ALA MET SER VAL SEQRES 7 A 166 PHE VAL MET THR CYS GLU ALA ALA ALA GLN LEU ARG LYS SEQRES 8 A 166 ALA GLY LYS VAL THR VAL ARG ASP THR THR LEU LYS ARG SEQRES 9 A 166 LEU GLY ALA THR HIS LEU LYS TYR GLY VAL GLY ASP ALA SEQRES 10 A 166 HIS PHE GLU VAL VAL LYS PHE ALA LEU LEU ASP THR ILE SEQRES 11 A 166 LYS GLU GLU VAL PRO ALA ASP MET TRP SER PRO ALA MET SEQRES 12 A 166 LYS SER ALA TRP SER GLU ALA TYR ASP HIS LEU VAL ALA SEQRES 13 A 166 ALA ILE LYS GLN GLU MET LYS PRO ALA GLU SEQRES 1 B 166 MET ALA LEU VAL GLU ASP ASN ASN ALA VAL ALA VAL SER SEQRES 2 B 166 PHE SER GLU GLU GLN GLU ALA LEU VAL LEU LYS SER TRP SEQRES 3 B 166 ALA ILE LEU LYS LYS ASP SER ALA ASN ILE ALA LEU ARG SEQRES 4 B 166 PHE PHE LEU LYS ILE PHE GLU VAL ALA PRO SER ALA SER SEQRES 5 B 166 GLN MET PHE SER PHE LEU ARG ASN SER ASP VAL PRO LEU SEQRES 6 B 166 GLU LYS ASN PRO LYS LEU LYS THR HIS ALA MET SER VAL SEQRES 7 B 166 PHE VAL MET THR CYS GLU ALA ALA ALA GLN LEU ARG LYS SEQRES 8 B 166 ALA GLY LYS VAL THR VAL ARG ASP THR THR LEU LYS ARG SEQRES 9 B 166 LEU GLY ALA THR HIS LEU LYS TYR GLY VAL GLY ASP ALA SEQRES 10 B 166 HIS PHE GLU VAL VAL LYS PHE ALA LEU LEU ASP THR ILE SEQRES 11 B 166 LYS GLU GLU VAL PRO ALA ASP MET TRP SER PRO ALA MET SEQRES 12 B 166 LYS SER ALA TRP SER GLU ALA TYR ASP HIS LEU VAL ALA SEQRES 13 B 166 ALA ILE LYS GLN GLU MET LYS PRO ALA GLU HET HEM A 166 43 HET HEM B 166 43 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 3 HEM 2(C34 H32 FE N4 O4) FORMUL 5 HOH *203(H2 O) HELIX 1 1 SER A 14 LYS A 30 1 17 HELIX 2 2 ASP A 31 ALA A 47 1 17 HELIX 3 3 ALA A 47 GLN A 52 1 6 HELIX 4 4 PRO A 63 LYS A 66 5 4 HELIX 5 5 ASN A 67 GLY A 92 1 26 HELIX 6 6 ARG A 97 TYR A 111 1 15 HELIX 7 7 GLY A 114 VAL A 133 1 20 HELIX 8 8 SER A 139 GLU A 160 1 22 HELIX 9 9 SER B 14 LYS B 30 1 17 HELIX 10 10 ASP B 31 ALA B 47 1 17 HELIX 11 11 ALA B 47 GLN B 52 1 6 HELIX 12 12 ASN B 67 GLY B 92 1 26 HELIX 13 13 ARG B 97 TYR B 111 1 15 HELIX 14 14 GLY B 114 VAL B 133 1 20 HELIX 15 15 SER B 139 GLU B 160 1 22 LINK NE2 HIS A 73 FE HEM A 166 LINK NE2 HIS A 108 FE HEM A 166 LINK NE2 HIS B 73 FE HEM B 166 LINK NE2 HIS B 108 FE HEM B 166 CRYST1 126.800 126.800 55.500 90.00 90.00 120.00 P 31 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 0.007886 0.004553 0.000000 0.00000 SCALE2 0.000000 0.009106 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018018 0.00000