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HEADER OXYGEN STORAGE/TRANSPORT 22-JAN-04 1S61 TITLE CRYSTAL STRUCTURE OF "TRUNCATED" HEMOGLOBIN N (HBN) FROM TITLE 2 MYCOBACTERIUM TUBERCULOSIS, SOAKED WITH BUTYL-ISOCYANIDE 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,A.PESCE,Y.OUELLET,S.DEWILDE,J.FRIEDMAN,P.ASCENZI, AUTHOR 2 M.GUERTIN,M.BOLOGNESI REVDAT 1 29-JUN-04 1S61 0 JRNL AUTH M.MILANI,A.PESCE,Y.OUELLET,S.DEWILDE,J.FRIEDMAN, JRNL AUTH 2 P.ASCENZI,M.GUERTIN,M.BOLOGNESI JRNL TITL HEME-LIGAND TUNNELING IN GROUP I TRUNCATED JRNL TITL 2 HEMOGLOBINS JRNL REF J.BIOL.CHEM. V. 279 21520 2004 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.1.24 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) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 91.5 REMARK 3 NUMBER OF REFLECTIONS : 12993 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) : 0.197 REMARK 3 R VALUE (WORKING SET) : 0.194 REMARK 3 FREE R VALUE : 0.251 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 691 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW : 2.15 REMARK 3 REFLECTION IN BIN (WORKING SET) : 898 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2320 REMARK 3 BIN FREE R VALUE SET COUNT : 58 REMARK 3 BIN FREE R VALUE : 0.3170 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 2245 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.22 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.78000 REMARK 3 B22 (A**2) : 3.60000 REMARK 3 B33 (A**2) : -2.82000 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): 0.308 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.227 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 : 0.945 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2116 ; 0.012 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): 1953 ; 0.000 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2901 ; 1.335 ; 2.094 REMARK 3 BOND ANGLES OTHERS (DEGREES): 4486 ; 3.553 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 267 ; 5.194 ; 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): 317 ; 0.065 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2342 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 410 ; 0.005 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 648 ; 0.387 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2109 ; 0.308 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): 1020 ; 0.108 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 104 ; 0.224 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 4 ; 0.499 ; 0.200 REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 17 ; 0.299 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 99 ; 0.339 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.233 ; 0.200 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): 1319 ; 0.607 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2107 ; 1.115 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 797 ; 1.828 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 794 ; 2.872 ; 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 1S61 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 RCSB021411. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-DEC-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.70 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.933 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD 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 : 14957 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 (%) : NULL REMARK 200 DATA REDUNDANCY : NULL 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: MOLECULAR REPLACEMENT 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 (%): 40.13 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PHOSPHATE, PH 7.7, VAPOR DIFFUSION, REMARK 280 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 21.76700 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.89250 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.71600 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.89250 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.76700 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.71600 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 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 345 FE HEM B 144 1.71 REMARK 500 C CYN 245 FE HEC A 144 1.88 REMARK 500 NH2 ARG A 84 O HOH 28 1.96 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 ILE A 115 CG1 ILE A 115 CD1 -0.074 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 GLN A 82 OE1 - CD - NE2 ANGL. DEV. = -9.3 DEGREES REMARK 500 GLN A 82 CG - CD - NE2 ANGL. DEV. = 10.3 DEGREES REMARK 500 THR B 133 C - N - CA ANGL. DEV. = -9.3 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1S56 RELATED DB: PDB REMARK 900 RELATED ID: 1IDR RELATED DB: PDB REMARK 900 RELATED ID: 1RTE RELATED DB: PDB DBREF 1S61 A 1 136 UNP P0A592 GLBN_MYCTU 1 136 DBREF 1S61 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 245 2 HET CYN 345 2 HET PO4 301 5 HET PO4 302 5 HET PO4 303 5 HET PO4 304 5 HET K 401 1 HET HEC A 144 43 HET HEM B 144 44 HET NBN 201 6 HETNAM CYN CYANIDE ION HETNAM PO4 PHOSPHATE ION HETNAM K POTASSIUM ION HETNAM HEC HEME C HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM NBN N-BUTYL ISOCYANIDE HETSYN HEM HEME FORMUL 3 CYN 2(C N 1-) FORMUL 5 PO4 4(O4 P 3-) FORMUL 9 K K 1+ FORMUL 10 HEC C34 H34 FE N4 O4 FORMUL 11 HEM C34 H32 FE N4 O4 FORMUL 12 NBN C5 H9 N FORMUL 13 HOH *128(H2 O) HELIX 1 1 GLY A 2 LYS A 9 1 8 HELIX 2 2 SER A 14 GLY A 20 1 7 HELIX 3 3 GLY A 21 ALA A 38 1 18 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 FE HEC A 144 NE2 HIS A 81 LINK FE HEM B 144 NE2 HIS B 81 CRYST1 43.534 61.432 91.785 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 0.022971 0.000000 0.000000 0.00000 SCALE2 0.000000 0.016278 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010895 0.00000