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HEADER OXYGEN STORAGE/TRANSPORT 29-AUG-05 2AV0 TITLE F97L WITH CO BOUND COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLOBIN I; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: DIMERIC HEMOGLOBIN, HBI; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SCAPHARCA INAEQUIVALVIS; SOURCE 3 ORGANISM_COMMON: ARK CLAM; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: W3110LACIQ L8; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCS-26 KEYWDS OXYGEN TRANSPORT, OXYGEN BINDING, ALLOSTERIC, HEMOGLOBIN EXPDTA X-RAY DIFFRACTION AUTHOR J.E.KNAPP,M.A.BONHAM,Q.H.GIBSON,J.C.NICHOLS,W.E.ROYER JR. REVDAT 1 28-MAR-06 2AV0 0 SPRSDE 28-MAR-06 2AV0 3HBI JRNL AUTH J.E.KNAPP,M.A.BONHAM,Q.H.GIBSON,J.C.NICHOLS, JRNL AUTH 2 W.E.ROYER JR. JRNL TITL RESIDUE F4 PLAYS A KEY ROLE IN MODULATING OXYGEN JRNL TITL 2 AFFINITY AND COOPERATIVITY IN SCAPHARCA DIMERIC JRNL TITL 3 HEMOGLOBIN JRNL REF BIOCHEMISTRY V. 44 14419 2005 JRNL REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.PARDANANI,Q.H.GIBSON,G.COLOTTI,W.E.ROYER JR. REMARK 1 TITL MUTATION OF RESIDUE PHE97 TO LEU DISRUPTS THE REMARK 1 TITL 2 CENTRAL ALLOSTERIC PATHWAY IN SCAPHARCA DIMERIC REMARK 1 TITL 3 HEMOGLOBIN REMARK 1 REF J.BIOL.CHEM. V. 272 13171 1997 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 2 REMARK 2 RESOLUTION. 1.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 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 : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.43 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1489678.850 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.7 REMARK 3 NUMBER OF REFLECTIONS : 40594 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.189 REMARK 3 FREE R VALUE : 0.206 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2033 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.55 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 54.90 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2406 REMARK 3 BIN R VALUE (WORKING SET) : 0.2980 REMARK 3 BIN FREE R VALUE : 0.2960 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 123 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2226 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 90 REMARK 3 SOLVENT ATOMS : 222 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 20.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.30 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.27000 REMARK 3 B22 (A**2) : 2.56000 REMARK 3 B33 (A**2) : -2.29000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.79000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.17 REMARK 3 ESD FROM SIGMAA (A) : 0.15 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.18 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.17 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.006 REMARK 3 BOND ANGLES (DEGREES) : 1.10 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.10 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.99 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : INIDIVIDUAL 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 : FLAT MODEL REMARK 3 KSOL : 0.34 REMARK 3 BSOL : 69.78 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 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : PARAM19X.HEME REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER.TOP REMARK 3 TOPOLOGY FILE 3 : TOPH19X.HEME REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2AV0 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 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB034345. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-APR-1995 REMARK 200 TEMPERATURE (KELVIN) : 298.0 REMARK 200 PH : 7.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : GRAPHITE REMARK 200 OPTICS : COLLIMATOR REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40594 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 87.8 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.05520 REMARK 200 R SYM (I) : 0.05520 REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55 REMARK 200 COMPLETENESS FOR SHELL (%) : 54.7 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: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: PDB ENTRY 3SDH REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 44.60 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PHOSPHATE, PH 7.5, SMALL TUBES, REMARK 280 TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 1/2+X,1/2+Y,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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 46.62500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.99000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.62500 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 21.99000 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 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 PRO A 1 REMARK 465 PRO B 1 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 37 SD MET A 37 CE -0.061 REMARK 500 ASP A 56 CG ASP A 56 OD2 0.076 REMARK 500 ASP B 56 CG ASP B 56 OD2 0.076 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 GLY A 128 N - CA - C ANGL. DEV. = 7.9 DEGREES REMARK 500 ASP B 28 N - CA - C ANGL. DEV. = -6.2 DEGREES REMARK 500 ALA B 76 N - CA - C ANGL. DEV. = -6.4 DEGREES REMARK 500 LEU B 84 N - CA - C ANGL. DEV. = 6.5 DEGREES REMARK 500 ASN B 126 N - CA - C ANGL. DEV. = 6.8 DEGREES REMARK 500 PHE B 127 N - CA - C ANGL. DEV. = -7.4 DEGREES REMARK 500 GLY B 128 N - CA - C ANGL. DEV. = 8.2 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3HBI RELATED DB: PDB REMARK 900 SAME PROTEIN, F97L WITH CO BOUND REMARK 900 RELATED ID: 2HBI RELATED DB: PDB REMARK 900 F97L-NO LIGAND BOUND REMARK 900 RELATED ID: 2AV3 RELATED DB: PDB REMARK 900 RELATED ID: 2AUO RELATED DB: PDB REMARK 900 RELATED ID: 2AUP RELATED DB: PDB REMARK 900 RELATED ID: 2AUQ RELATED DB: PDB REMARK 900 RELATED ID: 2AUR RELATED DB: PDB DBREF 2AV0 A 1 146 UNP P02213 GLB1_SCAIN 1 146 DBREF 2AV0 B 1 146 UNP P02213 GLB1_SCAIN 1 146 SEQADV 2AV0 LEU A 97 UNP P02213 PHE 97 ENGINEERED SEQADV 2AV0 LEU B 97 UNP P02213 PHE 97 ENGINEERED SEQRES 1 A 146 PRO SER VAL TYR ASP ALA ALA ALA GLN LEU THR ALA ASP SEQRES 2 A 146 VAL LYS LYS ASP LEU ARG ASP SER TRP LYS VAL ILE GLY SEQRES 3 A 146 SER ASP LYS LYS GLY ASN GLY VAL ALA LEU MET THR THR SEQRES 4 A 146 LEU PHE ALA ASP ASN GLN GLU THR ILE GLY TYR PHE LYS SEQRES 5 A 146 ARG LEU GLY ASP VAL SER GLN GLY MET ALA ASN ASP LYS SEQRES 6 A 146 LEU ARG GLY HIS SER ILE THR LEU MET TYR ALA LEU GLN SEQRES 7 A 146 ASN PHE ILE ASP GLN LEU ASP ASN PRO ASP ASP LEU VAL SEQRES 8 A 146 CYS VAL VAL GLU LYS LEU ALA VAL ASN HIS ILE THR ARG SEQRES 9 A 146 LYS ILE SER ALA ALA GLU PHE GLY LYS ILE ASN GLY PRO SEQRES 10 A 146 ILE LYS LYS VAL LEU ALA SER LYS ASN PHE GLY ASP LYS SEQRES 11 A 146 TYR ALA ASN ALA TRP ALA LYS LEU VAL ALA VAL VAL GLN SEQRES 12 A 146 ALA ALA LEU SEQRES 1 B 146 PRO SER VAL TYR ASP ALA ALA ALA GLN LEU THR ALA ASP SEQRES 2 B 146 VAL LYS LYS ASP LEU ARG ASP SER TRP LYS VAL ILE GLY SEQRES 3 B 146 SER ASP LYS LYS GLY ASN GLY VAL ALA LEU MET THR THR SEQRES 4 B 146 LEU PHE ALA ASP ASN GLN GLU THR ILE GLY TYR PHE LYS SEQRES 5 B 146 ARG LEU GLY ASP VAL SER GLN GLY MET ALA ASN ASP LYS SEQRES 6 B 146 LEU ARG GLY HIS SER ILE THR LEU MET TYR ALA LEU GLN SEQRES 7 B 146 ASN PHE ILE ASP GLN LEU ASP ASN PRO ASP ASP LEU VAL SEQRES 8 B 146 CYS VAL VAL GLU LYS LEU ALA VAL ASN HIS ILE THR ARG SEQRES 9 B 146 LYS ILE SER ALA ALA GLU PHE GLY LYS ILE ASN GLY PRO SEQRES 10 B 146 ILE LYS LYS VAL LEU ALA SER LYS ASN PHE GLY ASP LYS SEQRES 11 B 146 TYR ALA ASN ALA TRP ALA LYS LEU VAL ALA VAL VAL GLN SEQRES 12 B 146 ALA ALA LEU HET HEM A 147 43 HET HEM B 147 43 HET CMO A 148 2 HET CMO B 148 2 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM CMO CARBON MONOXIDE HETSYN HEM HEME FORMUL 3 HEM 2(C34 H32 FE N4 O4) FORMUL 5 CMO 2(C O) FORMUL 7 HOH *222(H2 O) HELIX 1 1 SER A 2 ALA A 8 1 7 HELIX 2 2 THR A 11 GLY A 26 1 16 HELIX 3 3 ASP A 28 ASN A 44 1 17 HELIX 4 4 GLN A 45 GLY A 55 5 11 HELIX 5 5 ASP A 56 ALA A 62 5 7 HELIX 6 6 ASN A 63 GLN A 83 1 21 HELIX 7 7 ASN A 86 THR A 103 1 18 HELIX 8 8 SER A 107 GLY A 112 1 6 HELIX 9 9 ILE A 114 LYS A 125 1 12 HELIX 10 10 GLY A 128 ALA A 145 1 18 HELIX 11 11 SER B 2 ALA B 8 1 7 HELIX 12 12 THR B 11 GLY B 26 1 16 HELIX 13 13 ASP B 28 ASN B 44 1 17 HELIX 14 14 GLN B 45 GLY B 55 5 11 HELIX 15 15 ASP B 56 ALA B 62 5 7 HELIX 16 16 ASN B 63 GLN B 83 1 21 HELIX 17 17 ASN B 86 THR B 103 1 18 HELIX 18 18 SER B 107 GLY B 112 1 6 HELIX 19 19 ILE B 114 LYS B 125 1 12 HELIX 20 20 GLY B 128 ALA B 144 1 17 LINK FE HEM A 147 C CMO A 148 LINK FE HEM B 147 C CMO B 148 LINK NE2 HIS A 101 FE HEM A 147 LINK NE2 HIS B 101 FE HEM B 147 CRYST1 93.250 43.980 83.500 90.00 122.03 90.00 C 1 2 1 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.010724 0.000000 0.006709 0.00000 SCALE2 0.000000 0.022738 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014127 0.00000