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HEADER OXYGEN STORAGE/TRANSPORT 16-SEP-01 1JZL TITLE CRYSTAL STRUCTURE OF SAPHARCA INAEQUIVALVIS HBI, I114M TITLE 2 MUTANT LIGATED TO CARBON MONOXIDE. COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLOBIN I - ARK SHELL; 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: W3110LACIQL8; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCS-26 KEYWDS INVERTEBRATE, HEMOGLOBIN, ALLOSTERY, COOPERATIVITY, OXYGEN- KEYWDS 2 BINDING, OXYGEN-TRANSPORT, HEME PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.E.KNAPP,Q.H.GIBSON,L.CUSHING,W.E.ROYER JR. REVDAT 1 19-DEC-01 1JZL 0 JRNL AUTH J.E.KNAPP,Q.H.GIBSON,L.CUSHING,W.E.ROYER JR. JRNL TITL RESTRICTING THE LIGAND-LINKED HEME MOVEMENT IN JRNL TITL 2 SCAPHARCA DIMERIC HEMOGLOBIN REVEALS TIGHT JRNL TITL 3 COUPLING BETWEEN DISTAL AND PROXIMAL CONTRIBUTIONS JRNL TITL 4 TO COOPERATIVITY. JRNL REF BIOCHEMISTRY V. 40 14795 2001 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 1 REFERENCE 2 REMARK 1 AUTH W.E.ROYER JR. REMARK 1 TITL HIGH RESOLUTION CRYSTALLOGRAPHIC ANALYSIS OF REMARK 1 TITL 2 CO-OPERATIVE DIMERIC HEMOGLOBIN. REMARK 1 REF J.MOL.BIOL. V. 235 657 1994 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. 1.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 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) : 28.62 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1139634.690 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.3 REMARK 3 NUMBER OF REFLECTIONS : 40765 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) : 0.215 REMARK 3 FREE R VALUE : 0.236 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100 REMARK 3 FREE R VALUE TEST SET COUNT : 4098 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004 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) (%) : 41.20 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1716 REMARK 3 BIN R VALUE (WORKING SET) : 0.2910 REMARK 3 BIN FREE R VALUE : 0.3180 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.20 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 173 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2240 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 90 REMARK 3 SOLVENT ATOMS : 165 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 20.40 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.90 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.65000 REMARK 3 B22 (A**2) : 1.50000 REMARK 3 B33 (A**2) : -2.15000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.09000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20 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) : 0.22 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.14 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 1.10 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.00 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.12 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 0.720 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.120 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 0.130 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 0.220 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.38 REMARK 3 BSOL : 56.39 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 1JZL 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 RCSB014373. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-FEB-2000; 16-FEB-2000 REMARK 200 TEMPERATURE (KELVIN) : 296; 296 REMARK 200 PH : 7.50 REMARK 200 NUMBER OF CRYSTALS USED : 2 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N; N REMARK 200 RADIATION SOURCE : ROTATING ANODE; ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200; RIGAKU RU200 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418; 1.5418 REMARK 200 MONOCHROMATOR : YALE MIRRORS; YALE MIRRORS REMARK 200 OPTICS : YALE MIRRORS; YALE MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE; IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC; RIGAKU REMARK 200 RAXIS IIC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40783 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 88.1 REMARK 200 DATA REDUNDANCY : 3.000 REMARK 200 R MERGE (I) : 0.06600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.6000 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 (%) : 39.9 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.23500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: CNS REMARK 200 STARTING MODEL: 3SDH REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 45.69 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1-2.3M PHOSPHATE BUFFER, PH 7.5, REMARK 280 MICROBATCH, TEMPERATURE 296K 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 46.55500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.98500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.55500 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 21.98500 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 -0.049 REMARK 500 MET B 114 SD MET B 114 CE 0.054 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. = 7.6 DEGREES REMARK 500 ASP B 28 N - CA - C ANGL. DEV. = -6.6 DEGREES REMARK 500 ALA B 76 N - CA - C ANGL. DEV. = -7.0 DEGREES REMARK 500 ASN B 126 N - CA - C ANGL. DEV. = 6.9 DEGREES REMARK 500 PHE B 127 N - CA - C ANGL. DEV. = -7.3 DEGREES REMARK 500 GLY B 128 N - CA - C ANGL. DEV. = 7.9 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1JWN RELATED DB: PDB REMARK 900 1JWN IS 1HBI, I114F MUTATION, CO-LIGATED STRUCTURE. REMARK 900 RELATED ID: 1JZK RELATED DB: PDB REMARK 900 1JZK IS HBI, I114F MUTATION, DEOXY STRUCTURE. REMARK 900 RELATED ID: 3SDH RELATED DB: PDB REMARK 900 3SDH IS WILD TYPE HBI, CO-LIGATED STRUCTURE. REMARK 900 RELATED ID: 4SDH RELATED DB: PDB REMARK 900 4SDH IS WILD TYPE HBI, DEOXY STRUCTURE. REMARK 900 RELATED ID: 1HBI RELATED DB: PDB REMARK 900 1HBI IS WILD TYPE HBI, OXYGENATED STRUCTURE. REMARK 900 RELATED ID: 3HBI RELATED DB: PDB REMARK 900 3HBI IS HBI, F97L MUTANT, CO-LIGATED STRUCTURE. DBREF 1JZL A 1 146 UNP P02213 GLB1_SCAIN 1 146 DBREF 1JZL B 1 146 UNP P02213 GLB1_SCAIN 1 146 SEQADV 1JZL MET A 114 UNP P02213 ILE 114 ENGINEERED SEQADV 1JZL MET B 114 UNP P02213 ILE 114 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 ASN 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 PHE ALA VAL ASN HIS ILE THR ARG SEQRES 9 A 146 LYS ILE SER ALA ALA GLU PHE GLY LYS MET 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 ASN 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 PHE ALA VAL ASN HIS ILE THR ARG SEQRES 9 B 146 LYS ILE SER ALA ALA GLU PHE GLY LYS MET 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 *165(H2 O) HELIX 1 1 SER A 2 GLN A 9 1 8 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 ASN 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 MET A 114 SER A 124 1 11 HELIX 10 10 GLY A 128 ALA A 145 1 18 HELIX 11 11 SER B 2 LEU B 10 1 9 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 ASN 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 MET 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 93.110 43.970 83.440 90.00 122.01 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 0.010740 0.000000 0.006714 0.00000 SCALE2 0.000000 0.022743 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014134 0.00000