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HEADER OXYGEN STORAGE/TRANSPORT 10-DEC-03 1RTE TITLE X-RAY STRUCTURE OF CYANIDE DERIVATIVE OF TRUNCATED TITLE 2 HEMOGLOBIN N (TRHBN) FROM MYCOBACTERIUM TUBERCULOSIS COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN-LIKE PROTEIN HBN; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: FLAVOHEMOGLOBIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS; SOURCE 3 GENE: GLBN, RV1542C, MT1594, MTCY48.23, MB1569C; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA KEYWDS TRUNCATED HEMOGLOBIN EXPDTA X-RAY DIFFRACTION AUTHOR M.MILANI,M.GUERTIN,A.BOFFI,G.ANTONINI,A.BOCEDI,M.MATTU, AUTHOR 2 M.BOLOGNESI,P.ASCENZI REVDAT 1 27-JUL-04 1RTE 0 JRNL AUTH M.MILANI,Y.OUELLET,H.OUELLET,M.GUERTIN,A.BOFFI, JRNL AUTH 2 G.ANTONINI,A.BOCEDI,M.MATTU,M.BOLOGNESI,P.ASCENZI JRNL TITL CYANIDE BINDING TO TRUNCATED HEMOGLOBINS: A JRNL TITL 2 CRYSTALLOGRAPHIC AND KINETIC STUDY JRNL REF BIOCHEMISTRY V. 43 5213 2004 JRNL REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.1.19 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.30 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 16560 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 + TEST SET) : 0.182 REMARK 3 R VALUE (WORKING SET) : 0.179 REMARK 3 FREE R VALUE : 0.237 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 879 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 2.00 REMARK 3 BIN RESOLUTION RANGE LOW : 2.05 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1204 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.1920 REMARK 3 BIN FREE R VALUE SET COUNT : 45 REMARK 3 BIN FREE R VALUE : 0.2880 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 2329 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.89 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.62000 REMARK 3 B22 (A**2) : 0.08000 REMARK 3 B33 (A**2) : 0.55000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.205 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.180 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2145 ; 0.012 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): 1933 ; 0.000 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2946 ; 1.331 ; 2.094 REMARK 3 BOND ANGLES OTHERS (DEGREES): 4454 ; 3.699 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 269 ; 5.160 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 313 ; 0.068 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2391 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 418 ; 0.006 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 625 ; 0.396 ; 0.300 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2118 ; 0.307 ; 0.300 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): 967 ; 0.104 ; 0.500 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 238 ; 0.223 ; 0.500 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.588 ; 0.500 REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 23 ; 0.264 ; 0.300 REMARK 3 SYMMETRY VDW OTHERS (A): 97 ; 0.350 ; 0.300 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 46 ; 0.312 ; 0.500 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1308 ; 0.670 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2096 ; 1.215 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 837 ; 1.847 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 850 ; 2.956 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 0 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 1RTE 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 RCSB021024. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.93 REMARK 200 MONOCHROMATOR : DIAMOND (111), GE(220) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17605 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 4.000 REMARK 200 R MERGE (I) : 0.13700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6 REMARK 200 DATA REDUNDANCY IN SHELL : 4.00 REMARK 200 R MERGE FOR SHELL (I) : 0.23600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 4.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: EPMR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.04 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 7, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K 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 22.28350 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.64700 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.72150 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.64700 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.28350 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.72150 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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 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 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 1 REMARK 465 GLU A 130 REMARK 465 SER A 131 REMARK 465 THR A 132 REMARK 465 THR A 133 REMARK 465 ALA A 134 REMARK 465 PRO A 135 REMARK 465 VAL A 136 REMARK 465 MET B 1 REMARK 465 GLU B 130 REMARK 465 SER B 131 REMARK 465 THR B 132 REMARK 465 THR B 133 REMARK 465 ALA B 134 REMARK 465 PRO B 135 REMARK 465 VAL B 136 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 C CYN 446 FE HEM B 144 1.70 REMARK 500 C CYN 445 FE HEM A 144 1.84 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 PRO A 71 CA - C - N ANGL. DEV. = 9.2 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 102 DISTANCE = 5.01 ANGSTROMS REMARK 525 HOH 106 DISTANCE = 6.33 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1IDR RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE TRUNCATED-HEMOGLOBIN-N FROM REMARK 900 MYCOBACTERIUM TUBERCULOSIS DBREF 1RTE A 1 136 UNP P0A592 GLBN_MYCTU 1 136 DBREF 1RTE B 1 136 UNP P0A592 GLBN_MYCTU 1 136 SEQRES 1 A 136 MET GLY LEU LEU SER ARG LEU ARG LYS ARG GLU PRO ILE SEQRES 2 A 136 SER ILE TYR ASP LYS ILE GLY GLY HIS GLU ALA ILE GLU SEQRES 3 A 136 VAL VAL VAL GLU ASP PHE TYR VAL ARG VAL LEU ALA ASP SEQRES 4 A 136 ASP GLN LEU SER ALA PHE PHE SER GLY THR ASN MET SER SEQRES 5 A 136 ARG LEU LYS GLY LYS GLN VAL GLU PHE PHE ALA ALA ALA SEQRES 6 A 136 LEU GLY GLY PRO GLU PRO TYR THR GLY ALA PRO MET LYS SEQRES 7 A 136 GLN VAL HIS GLN GLY ARG GLY ILE THR MET HIS HIS PHE SEQRES 8 A 136 SER LEU VAL ALA GLY HIS LEU ALA ASP ALA LEU THR ALA SEQRES 9 A 136 ALA GLY VAL PRO SER GLU THR ILE THR GLU ILE LEU GLY SEQRES 10 A 136 VAL ILE ALA PRO LEU ALA VAL ASP VAL THR SER GLY GLU SEQRES 11 A 136 SER THR THR ALA PRO VAL SEQRES 1 B 136 MET GLY LEU LEU SER ARG LEU ARG LYS ARG GLU PRO ILE SEQRES 2 B 136 SER ILE TYR ASP LYS ILE GLY GLY HIS GLU ALA ILE GLU SEQRES 3 B 136 VAL VAL VAL GLU ASP PHE TYR VAL ARG VAL LEU ALA ASP SEQRES 4 B 136 ASP GLN LEU SER ALA PHE PHE SER GLY THR ASN MET SER SEQRES 5 B 136 ARG LEU LYS GLY LYS GLN VAL GLU PHE PHE ALA ALA ALA SEQRES 6 B 136 LEU GLY GLY PRO GLU PRO TYR THR GLY ALA PRO MET LYS SEQRES 7 B 136 GLN VAL HIS GLN GLY ARG GLY ILE THR MET HIS HIS PHE SEQRES 8 B 136 SER LEU VAL ALA GLY HIS LEU ALA ASP ALA LEU THR ALA SEQRES 9 B 136 ALA GLY VAL PRO SER GLU THR ILE THR GLU ILE LEU GLY SEQRES 10 B 136 VAL ILE ALA PRO LEU ALA VAL ASP VAL THR SER GLY GLU SEQRES 11 B 136 SER THR THR ALA PRO VAL HET CYN 445 2 HET CYN 446 2 HET SO4 301 5 HET SO4 302 5 HET SO4 303 5 HET SO4 304 5 HET SO4 305 5 HET SO4 306 5 HET SO4 307 5 HET SO4 308 5 HET HEM A 144 43 HET HEM B 144 45 HETNAM CYN CYANIDE ION HETNAM SO4 SULFATE ION HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 3 CYN 2(C N 1-) FORMUL 5 SO4 8(O4 S 2-) FORMUL 13 HEM 2(C34 H32 FE N4 O4) FORMUL 15 HOH *207(H2 O) HELIX 1 1 GLY A 2 LYS A 9 1 8 HELIX 2 2 SER A 14 ILE A 19 1 6 HELIX 3 3 GLY A 20 ALA A 38 1 19 HELIX 4 4 LEU A 42 SER A 47 5 6 HELIX 5 5 ASN A 50 LEU A 66 1 17 HELIX 6 6 PRO A 76 GLN A 82 1 7 HELIX 7 7 THR A 87 ALA A 105 1 19 HELIX 8 8 PRO A 108 ALA A 120 1 13 HELIX 9 9 LEU A 122 THR A 127 1 6 HELIX 10 10 GLY B 2 LYS B 9 1 8 HELIX 11 11 SER B 14 GLY B 20 1 7 HELIX 12 12 GLY B 20 ALA B 38 1 19 HELIX 13 13 LEU B 42 SER B 47 5 6 HELIX 14 14 ASN B 50 LEU B 66 1 17 HELIX 15 15 PRO B 76 GLN B 82 1 7 HELIX 16 16 THR B 87 ALA B 105 1 19 HELIX 17 17 PRO B 108 ALA B 120 1 13 HELIX 18 18 LEU B 122 THR B 127 1 6 LINK NE2 HIS B 81 FE HEM B 144 LINK NE2 HIS A 81 FE HEM A 144 CRYST1 44.567 61.443 91.294 90.00 90.00 90.00 P 21 21 21 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 0.022438 0.000000 0.000000 0.00000 SCALE2 0.000000 0.016275 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010954 0.00000