HEADER OXYGEN TRANSPORT 11-NOV-03 1URV TITLE CRYSTAL STRUCTURE OF CYTOGLOBIN: THE FOURTH GLOBIN TYPE TITLE 2 DISCOVERED IN MAN DISPLAYS HEME HEXA-COORDINATION COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYTOGLOBIN; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: HISTOGLOBIN, HGB, STELLATE CELL ACTIVATION- COMPND 5 ASSOCIATED-PROTEIN, CYGB, STAP; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI KEYWDS GLOBIN, CYTOGLOBIN, HISTOGLOBIN, HEME, HEXA-COORDINATION, KEYWDS 2 PROTEIN, OXYGEN TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR D.DE SANCTIS,S.DEWILDE,A.PESCE,L.MOENS,P.ASCENZI,T.HANKELN, AUTHOR 2 T.BURMESTER,M.BOLOGNESI REVDAT 2 23-DEC-04 1URV 1 SOURCE REVDAT 1 15-DEC-04 1URV 0 JRNL AUTH D.DE SANCTIS,S.DEWILDE,A.PESCE,L.MOENS,P.ASCENZI, JRNL AUTH 2 T.HANKELN,T.BURMESTER,M.BOLOGNESI JRNL TITL CRYSTAL STRUCTURE OF CYTOGLOBIN: THE FOURTH GLOBIN JRNL TITL 2 TYPE DISCOVERED IN MAN DISPLAYS HEME JRNL TITL 3 HEXA-COORDINATION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 22020 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) : 0.222 REMARK 3 R VALUE (WORKING SET) : 0.219 REMARK 3 FREE R VALUE : 0.265 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1190 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2554 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 112 REMARK 3 SOLVENT ATOMS : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.44 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.13000 REMARK 3 B22 (A**2) : -0.06000 REMARK 3 B33 (A**2) : 0.19000 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): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.191 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 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : NULL ; NULL REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : NULL ; NULL REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : NULL ; NULL REMARK 3 STAGGERED (DEGREES) : NULL ; NULL REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 1URV 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 3.102 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI . REMARK 100 THE EBI ID CODE IS EBI-13938 . REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-AUG-2003 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 5.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.934 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 : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 341899 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 7.000 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: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER 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 (%): 39.42 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.0 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 24.47000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.45650 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.21450 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.45650 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.47000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.21450 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, Y, Z 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 2 REMARK 465 LYS A 3 REMARK 465 VAL A 4 REMARK 465 PRO A 5 REMARK 465 GLY A 6 REMARK 465 GLU A 7 REMARK 465 MET A 8 REMARK 465 GLU A 9 REMARK 465 ILE A 10 REMARK 465 GLU A 11 REMARK 465 ARG A 12 REMARK 465 ARG A 13 REMARK 465 GLU A 14 REMARK 465 ARG A 15 REMARK 465 SER A 16 REMARK 465 GLU A 17 REMARK 465 VAL A 172 REMARK 465 GLN A 173 REMARK 465 GLN A 174 REMARK 465 VAL A 175 REMARK 465 PRO A 176 REMARK 465 ASN A 177 REMARK 465 ALA A 178 REMARK 465 THR A 179 REMARK 465 THR A 180 REMARK 465 PRO A 181 REMARK 465 PRO A 182 REMARK 465 ALA A 183 REMARK 465 THR A 184 REMARK 465 LEU A 185 REMARK 465 PRO A 186 REMARK 465 SER A 187 REMARK 465 SER A 188 REMARK 465 GLY A 189 REMARK 465 PRO A 190 REMARK 465 MET B 1 REMARK 465 GLU B 2 REMARK 465 LYS B 3 REMARK 465 VAL B 4 REMARK 465 PRO B 5 REMARK 465 GLY B 6 REMARK 465 GLU B 7 REMARK 465 MET B 8 REMARK 465 GLU B 9 REMARK 465 ILE B 10 REMARK 465 GLU B 11 REMARK 465 ARG B 12 REMARK 465 ARG B 13 REMARK 465 GLU B 14 REMARK 465 ARG B 15 REMARK 465 SER B 16 REMARK 465 GLU B 17 REMARK 465 VAL B 172 REMARK 465 GLN B 173 REMARK 465 GLN B 174 REMARK 465 VAL B 175 REMARK 465 PRO B 176 REMARK 465 ASN B 177 REMARK 465 ALA B 178 REMARK 465 THR B 179 REMARK 465 THR B 180 REMARK 465 PRO B 181 REMARK 465 PRO B 182 REMARK 465 ALA B 183 REMARK 465 THR B 184 REMARK 465 LEU B 185 REMARK 465 PRO B 186 REMARK 465 SER B 187 REMARK 465 SER B 188 REMARK 465 GLY B 189 REMARK 465 PRO B 190 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 LYS A 25 CG LYS A 25 CD -0.412 REMARK 500 MET A 30 SD MET A 30 CE -0.131 REMARK 500 ARG A 48 CG ARG A 48 CD -0.109 REMARK 500 GLU A 146 CB GLU A 146 CG 0.231 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 LYS A 25 CB - CG - CD ANGL. DEV. = 30.9 DEGREES REMARK 500 LYS A 25 CG - CD - CE ANGL. DEV. = 13.1 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 SER B 141 -44.36 143.04 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 SITE_DESCRIPTION: FC6 BINDING SITE FOR CHAIN B DBREF 1URV A 1 190 UNP Q8WWM9 CYGB_HUMAN 1 190 DBREF 1URV B 1 190 UNP Q8WWM9 CYGB_HUMAN 1 190 SEQADV 1URV SER A 38 UNP Q8WWM9 CYS 38 ENGINEERED MUTATION SEQADV 1URV SER A 83 UNP Q8WWM9 CYS 83 ENGINEERED MUTATION SEQADV 1URV SER B 38 UNP Q8WWM9 CYS 38 ENGINEERED MUTATION SEQADV 1URV SER B 83 UNP Q8WWM9 CYS 83 ENGINEERED MUTATION SEQRES 1 A 190 MET GLU LYS VAL PRO GLY GLU MET GLU ILE GLU ARG ARG SEQRES 2 A 190 GLU ARG SER GLU GLU LEU SER GLU ALA GLU ARG LYS ALA SEQRES 3 A 190 VAL GLN ALA MET TRP ALA ARG LEU TYR ALA ASN SER GLU SEQRES 4 A 190 ASP VAL GLY VAL ALA ILE LEU VAL ARG PHE PHE VAL ASN SEQRES 5 A 190 PHE PRO SER ALA LYS GLN TYR PHE SER GLN PHE LYS HIS SEQRES 6 A 190 MET GLU ASP PRO LEU GLU MET GLU ARG SER PRO GLN LEU SEQRES 7 A 190 ARG LYS HIS ALA SER ARG VAL MET GLY ALA LEU ASN THR SEQRES 8 A 190 VAL VAL GLU ASN LEU HIS ASP PRO ASP LYS VAL SER SER SEQRES 9 A 190 VAL LEU ALA LEU VAL GLY LYS ALA HIS ALA LEU LYS HIS SEQRES 10 A 190 LYS VAL GLU PRO VAL TYR PHE LYS ILE LEU SER GLY VAL SEQRES 11 A 190 ILE LEU GLU VAL VAL ALA GLU GLU PHE ALA SER ASP PHE SEQRES 12 A 190 PRO PRO GLU THR GLN ARG ALA TRP ALA LYS LEU ARG GLY SEQRES 13 A 190 LEU ILE TYR SER HIS VAL THR ALA ALA TYR LYS GLU VAL SEQRES 14 A 190 GLY TRP VAL GLN GLN VAL PRO ASN ALA THR THR PRO PRO SEQRES 15 A 190 ALA THR LEU PRO SER SER GLY PRO SEQRES 1 B 190 MET GLU LYS VAL PRO GLY GLU MET GLU ILE GLU ARG ARG SEQRES 2 B 190 GLU ARG SER GLU GLU LEU SER GLU ALA GLU ARG LYS ALA SEQRES 3 B 190 VAL GLN ALA MET TRP ALA ARG LEU TYR ALA ASN SER GLU SEQRES 4 B 190 ASP VAL GLY VAL ALA ILE LEU VAL ARG PHE PHE VAL ASN SEQRES 5 B 190 PHE PRO SER ALA LYS GLN TYR PHE SER GLN PHE LYS HIS SEQRES 6 B 190 MET GLU ASP PRO LEU GLU MET GLU ARG SER PRO GLN LEU SEQRES 7 B 190 ARG LYS HIS ALA SER ARG VAL MET GLY ALA LEU ASN THR SEQRES 8 B 190 VAL VAL GLU ASN LEU HIS ASP PRO ASP LYS VAL SER SER SEQRES 9 B 190 VAL LEU ALA LEU VAL GLY LYS ALA HIS ALA LEU LYS HIS SEQRES 10 B 190 LYS VAL GLU PRO VAL TYR PHE LYS ILE LEU SER GLY VAL SEQRES 11 B 190 ILE LEU GLU VAL VAL ALA GLU GLU PHE ALA SER ASP PHE SEQRES 12 B 190 PRO PRO GLU THR GLN ARG ALA TRP ALA LYS LEU ARG GLY SEQRES 13 B 190 LEU ILE TYR SER HIS VAL THR ALA ALA TYR LYS GLU VAL SEQRES 14 B 190 GLY TRP VAL GLN GLN VAL PRO ASN ALA THR THR PRO PRO SEQRES 15 B 190 ALA THR LEU PRO SER SER GLY PRO HET HEM A1172 43 HET FC6 A1173 13 HET HEM B1172 43 HET FC6 B1173 13 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM FC6 HEXACYANOFERRATE(3-) HETSYN HEM HEME HETSYN FC6 FERRI(III)HEXACYANIDE FORMUL 3 HEM 2(C34 H32 FE N4 O4) FORMUL 4 FC6 2(C6 FE N6) FORMUL 7 HOH *98(H2 O) HELIX 1 1 SER A 20 ALA A 36 1 17 HELIX 2 2 ASN A 37 PHE A 53 1 17 HELIX 3 3 PRO A 54 PHE A 60 5 7 HELIX 4 4 ASP A 68 SER A 75 1 8 HELIX 5 5 SER A 75 ASN A 95 1 21 HELIX 6 6 ASP A 98 LYS A 116 1 19 HELIX 7 7 PRO A 121 PHE A 139 1 19 HELIX 8 8 ALA A 140 PHE A 143 5 4 HELIX 9 9 PRO A 144 VAL A 169 1 26 HELIX 10 10 SER B 20 ASN B 37 1 18 HELIX 11 11 ASN B 37 PHE B 53 1 17 HELIX 12 12 PHE B 53 GLN B 58 1 6 HELIX 13 13 ASP B 68 SER B 75 1 8 HELIX 14 14 SER B 75 ASN B 95 1 21 HELIX 15 15 ASP B 98 LYS B 116 1 19 HELIX 16 16 PRO B 121 PHE B 139 1 19 HELIX 17 17 PRO B 144 VAL B 169 1 26 LINK FE HEM A1172 NE2 HIS A 113 LINK FE HEM A1172 NE2 HIS A 81 LINK FE HEM B1172 NE2AHIS B 81 LINK FE HEM B1172 NE2 HIS B 113 SITE 1 AC1 11 TYR A 59 PHE A 60 GLN A 77 HIS A 81 SITE 2 AC1 11 ARG A 84 ALA A 112 HIS A 113 HIS A 117 SITE 3 AC1 11 PHE A 124 HOH Z 33 HOH Z 55 SITE 1 AC2 16 GLU A 138 PHE A 139 ALA A 140 SER A 141 SITE 2 AC2 16 TYR B 59 PHE B 60 GLN B 62 HIS B 81 SITE 3 AC2 16 ARG B 84 ALA B 88 HIS B 113 HIS B 117 SITE 4 AC2 16 TYR B 123 PHE B 124 LEU B 127 HOH Z 48 SITE 1 AC3 9 LYS A 125 ARG A 155 GLY A 156 TYR A 159 SITE 2 AC3 9 PHE B 53 PRO B 54 SER B 55 HOH Z 44 SITE 3 AC3 9 HOH Z 57 SITE 1 AC4 7 PHE A 53 PRO A 54 SER A 55 LYS B 125 SITE 2 AC4 7 ARG B 155 GLY B 156 TYR B 159 CRYST1 48.940 70.429 100.913 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 0.020433 -0.000001 -0.000001 0.00000 SCALE2 0.000000 0.014199 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009910 0.00000