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HEADER OXYGEN TRANSPORT 11-APR-98 1A9W TITLE HUMAN EMBRYONIC GOWER II CARBONMONOXY HEMOGLOBIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN (ALPHA CHAIN); COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: HUMAN GOWER II EMBRYONIC HEMOGLOBIN; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HEMOGLOBIN (BETA CHAIN); COMPND 8 CHAIN: E, F; COMPND 9 ENGINEERED: YES; COMPND 10 OTHER_DETAILS: HUMAN GOWER II EMBRYONIC HEMOGLOBIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE; SOURCE 5 EXPRESSION_SYSTEM_STRAIN: GSY112; SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PRMAE389; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE; SOURCE 11 EXPRESSION_SYSTEM_STRAIN: GSY112; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PRMAE389 KEYWDS OXYGEN TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR A.J.SUTHERLAND-SMITH,H.M.BAKER,O.M.HOFMANN,T.BRITTAIN, AUTHOR 2 E.N.BAKER REVDAT 1 17-JUN-98 1A9W 0 JRNL AUTH A.J.SUTHERLAND-SMITH,H.M.BAKER,O.M.HOFMANN, JRNL AUTH 2 T.BRITTAIN,E.N.BAKER JRNL TITL CRYSTAL STRUCTURE OF A HUMAN EMBRYONIC JRNL TITL 2 HAEMOGLOBIN: THE CARBONMONOXY FORM OF GOWER II JRNL TITL 3 (ALPHA2 EPSILON2) HAEMOGLOBIN AT 2.9 A RESOLUTION. JRNL REF J.MOL.BIOL. V. 280 475 1998 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000.000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.9 REMARK 3 NUMBER OF REFLECTIONS : 14598 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) : 0.185 REMARK 3 FREE R VALUE : 0.232 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200 REMARK 3 FREE R VALUE TEST SET COUNT : 1485 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 8 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.03 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 76.30 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1232 REMARK 3 BIN R VALUE (WORKING SET) : 0.2940 REMARK 3 BIN FREE R VALUE : 0.3540 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 137 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.030 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4234 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 180 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 61.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.30 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.20000 REMARK 3 B22 (A**2) : -1.20000 REMARK 3 B33 (A**2) : 2.83000 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 COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : 0.35 REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.006 REMARK 3 BOND ANGLES (DEGREES) : 1.20 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.50 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.10 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : ONE B FOR MAIN CHAIN ATOM B FOR SIDE REMARK 3 CHAIN ATOMS 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 NCS MODEL : RESTRAINTS REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : 0.015 ; 1000 REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 GROUP 2 POSITIONAL (A) : 0.048 ; 1000 REMARK 3 GROUP 2 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO REMARK 3 PARAMETER FILE 2 : HEM.PRO REMARK 3 PARAMETER FILE 3 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : HEM.TOP REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: TNT-5E ALSO USED REMARK 4 REMARK 4 1A9W 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 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : OCT-1994 REMARK 200 TEMPERATURE (KELVIN) : 287.0 REMARK 200 PH : 8.50 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/MSC RU-H2R REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : GRAPHITE(002) REMARK 200 OPTICS : 0.3 MM COLLIMATOR REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : R-AXIS IIC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : CCP4 (AGROVATA, ROTAVATA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14645 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.900 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9 REMARK 200 DATA REDUNDANCY : 5.900 REMARK 200 R MERGE (I) : 0.09100 REMARK 200 R SYM (I) : 0.09100 REMARK 200 FOR THE DATA SET : 7.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.97 REMARK 200 COMPLETENESS FOR SHELL (%) : 76.3 REMARK 200 DATA REDUNDANCY IN SHELL : 4.50 REMARK 200 R MERGE FOR SHELL (I) : 0.37000 REMARK 200 R SYM FOR SHELL (I) : 0.37000 REMARK 200 FOR SHELL : 1.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE, TFFC REMARK 200 STARTING MODEL: PDB ENTRY 1BBB REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 21% REMARK 280 MME-PEG 5000, 0.2M TAPS/ KOH, PH 8.5, 2MM DITHIONITE. THEN REMARK 280 MICROSEEDING AND MACROSEEDING USED TO INCREASE CRYSTAL SIZE, REMARK 280 MICROSEEDING AND MACROSEEDING USED TO INCREASE CRYSTAL SIZE REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,1/2+Z REMARK 290 3555 1/2-Y,1/2+X,3/4+Z REMARK 290 4555 1/2+Y,1/2-X,1/4+Z REMARK 290 5555 1/2-X,1/2+Y,3/4-Z REMARK 290 6555 1/2+X,1/2-Y,1/4-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,1/2-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 160.45000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.40000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.40000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 240.67500 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.40000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.40000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 80.22500 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.40000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.40000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 240.67500 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.40000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.40000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 80.22500 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 160.45000 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 4 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, E, C, F 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 HIS E 146 REMARK 465 HIS F 146 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU A 23 CG CD OE1 OE2 REMARK 470 HIS A 50 CG ND1 CD2 CE1 NE2 REMARK 470 LYS A 56 CG CD CE NZ REMARK 470 LYS A 60 CG CD CE NZ REMARK 470 ASN A 78 CG OD1 ND2 REMARK 470 ARG A 141 CG CD NE CZ NH1 NH2 REMARK 470 HIS E 2 CG ND1 CD2 CE1 NE2 REMARK 470 GLU E 22 CG CD OE1 OE2 REMARK 470 LYS E 59 CG CD CE NZ REMARK 470 LYS E 61 CG CD CE NZ REMARK 470 LYS E 65 CD CE NZ REMARK 470 LYS E 76 CG CD CE NZ REMARK 470 LYS E 82 CG CD CE NZ REMARK 470 LYS E 87 CG CD CE NZ REMARK 470 GLU E 90 CG CD OE1 OE2 REMARK 470 LYS E 95 CG CD CE NZ REMARK 470 LYS E 120 CG CD CE NZ REMARK 470 GLU E 121 CG CD OE1 OE2 REMARK 470 HIS E 143 CG ND1 CD2 CE1 NE2 REMARK 470 GLU C 23 CG CD OE1 OE2 REMARK 470 GLU C 30 CG CD OE1 OE2 REMARK 470 HIS C 50 CG ND1 CD2 CE1 NE2 REMARK 470 LYS C 56 CG CD CE NZ REMARK 470 LYS C 60 CG CD CE NZ REMARK 470 ASN C 78 CG OD1 ND2 REMARK 470 ARG C 141 CG CD NE CZ NH1 NH2 REMARK 470 HIS F 2 CG ND1 CD2 CE1 NE2 REMARK 470 GLU F 6 CG CD OE1 OE2 REMARK 470 GLU F 22 CG CD OE1 OE2 REMARK 470 LYS F 76 CD CE NZ REMARK 470 ASN F 80 CG OD1 ND2 REMARK 470 LYS F 82 CG CD CE NZ REMARK 470 LYS F 87 CG CD CE NZ REMARK 470 LYS F 95 CG CD CE NZ REMARK 470 LYS F 120 CD CE NZ REMARK 470 HIS F 143 CG ND1 CD2 CE1 NE2 REMARK 470 LYS F 144 CG CD CE NZ 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 32 SD MET A 32 CE -0.044 REMARK 500 MET E 18 SD MET E 18 CE 0.050 REMARK 500 LYS E 65 CB LYS E 65 CG -0.105 REMARK 500 MET F 18 SD MET F 18 CE 0.056 REMARK 500 LYS F 76 CB LYS F 76 CG -0.103 REMARK 500 PRO F 100 CB PRO F 100 CG -0.044 REMARK 500 LYS F 120 CB LYS F 120 CG -0.106 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 ASP A 47 N - CA - C ANGL. DEV. =-11.6 DEGREES REMARK 500 HIS A 50 N - CA - C ANGL. DEV. = 7.7 DEGREES REMARK 500 MET E 18 N - CA - C ANGL. DEV. = 11.3 DEGREES REMARK 500 PRO E 36 N - CA - C ANGL. DEV. = 7.2 DEGREES REMARK 500 PRO E 36 C - N - CA ANGL. DEV. = 7.3 DEGREES REMARK 500 ASP C 47 N - CA - C ANGL. DEV. =-11.8 DEGREES REMARK 500 HIS C 50 N - CA - C ANGL. DEV. = 7.8 DEGREES REMARK 500 MET F 18 N - CA - C ANGL. DEV. = 11.2 DEGREES REMARK 500 ASP F 43 N - CA - CB ANGL. DEV. = -7.8 DEGREES DBREF 1A9W A 1 141 UNP P69905 HBA_HUMAN 1 141 DBREF 1A9W E 1 146 UNP P02100 HBE_HUMAN 1 146 DBREF 1A9W C 1 141 UNP P69905 HBA_HUMAN 1 141 DBREF 1A9W F 1 146 UNP P02100 HBE_HUMAN 1 146 SEQRES 1 A 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA SEQRES 2 A 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA SEQRES 3 A 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR SEQRES 4 A 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER SEQRES 5 A 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA SEQRES 6 A 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN SEQRES 7 A 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU SEQRES 8 A 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS SEQRES 9 A 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE SEQRES 10 A 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA SEQRES 11 A 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG SEQRES 1 E 146 VAL HIS PHE THR ALA GLU GLU LYS ALA ALA VAL THR SER SEQRES 2 E 146 LEU TRP SER LYS MET ASN VAL GLU GLU ALA GLY GLY GLU SEQRES 3 E 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN SEQRES 4 E 146 ARG PHE PHE ASP SER PHE GLY ASN LEU SER SER PRO SER SEQRES 5 E 146 ALA ILE LEU GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS SEQRES 6 E 146 LYS VAL LEU THR SER PHE GLY ASP ALA ILE LYS ASN MET SEQRES 7 E 146 ASP ASN LEU LYS PRO ALA PHE ALA LYS LEU SER GLU LEU SEQRES 8 E 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE LYS SEQRES 9 E 146 LEU LEU GLY ASN VAL MET VAL ILE ILE LEU ALA THR HIS SEQRES 10 E 146 PHE GLY LYS GLU PHE THR PRO GLU VAL GLN ALA ALA TRP SEQRES 11 E 146 GLN LYS LEU VAL SER ALA VAL ALA ILE ALA LEU ALA HIS SEQRES 12 E 146 LYS TYR HIS SEQRES 1 C 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA SEQRES 2 C 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA SEQRES 3 C 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR SEQRES 4 C 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER SEQRES 5 C 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA SEQRES 6 C 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN SEQRES 7 C 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU SEQRES 8 C 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS SEQRES 9 C 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE SEQRES 10 C 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA SEQRES 11 C 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG SEQRES 1 F 146 VAL HIS PHE THR ALA GLU GLU LYS ALA ALA VAL THR SER SEQRES 2 F 146 LEU TRP SER LYS MET ASN VAL GLU GLU ALA GLY GLY GLU SEQRES 3 F 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN SEQRES 4 F 146 ARG PHE PHE ASP SER PHE GLY ASN LEU SER SER PRO SER SEQRES 5 F 146 ALA ILE LEU GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS SEQRES 6 F 146 LYS VAL LEU THR SER PHE GLY ASP ALA ILE LYS ASN MET SEQRES 7 F 146 ASP ASN LEU LYS PRO ALA PHE ALA LYS LEU SER GLU LEU SEQRES 8 F 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE LYS SEQRES 9 F 146 LEU LEU GLY ASN VAL MET VAL ILE ILE LEU ALA THR HIS SEQRES 10 F 146 PHE GLY LYS GLU PHE THR PRO GLU VAL GLN ALA ALA TRP SEQRES 11 F 146 GLN LYS LEU VAL SER ALA VAL ALA ILE ALA LEU ALA HIS SEQRES 12 F 146 LYS TYR HIS HET HEM A 142 43 HET CMO A 143 2 HET HEM E 147 43 HET CMO E 148 2 HET HEM C 142 43 HET CMO C 143 2 HET HEM F 147 43 HET CMO F 148 2 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM CMO CARBON MONOXIDE HETSYN HEM HEME FORMUL 5 HEM 4(C34 H32 FE N4 O4) FORMUL 6 CMO 4(C O) HELIX 1 1 PRO A 4 SER A 35 1 32 HELIX 2 2 PRO A 37 TYR A 42 5 6 HELIX 3 3 ALA A 53 ALA A 71 1 19 HELIX 4 4 MET A 76 ALA A 79 1 4 HELIX 5 5 SER A 81 ALA A 88 1 8 HELIX 6 6 PRO A 95 HIS A 112 5 18 HELIX 7 7 PRO A 119 LEU A 136 1 18 HELIX 8 8 ALA E 5 SER E 16 1 12 HELIX 9 9 GLU E 22 VAL E 34 1 13 HELIX 10 10 PRO E 36 ARG E 40 5 5 HELIX 11 11 ASP E 43 PHE E 45 5 3 HELIX 12 12 PRO E 51 GLY E 56 1 6 HELIX 13 13 PRO E 58 ASN E 77 1 20 HELIX 14 14 ALA E 86 CYS E 93 1 8 HELIX 15 15 PRO E 100 GLU E 121 5 22 HELIX 16 16 PRO E 124 LEU E 141 1 18 HELIX 17 17 PRO C 4 SER C 35 1 32 HELIX 18 18 PRO C 37 TYR C 42 5 6 HELIX 19 19 ALA C 53 ALA C 71 1 19 HELIX 20 20 MET C 76 ALA C 79 1 4 HELIX 21 21 SER C 81 ALA C 88 1 8 HELIX 22 22 PRO C 95 HIS C 112 5 18 HELIX 23 23 PRO C 119 LEU C 136 1 18 HELIX 24 24 ALA F 5 SER F 16 1 12 HELIX 25 25 GLU F 22 VAL F 34 1 13 HELIX 26 26 PRO F 36 ARG F 40 5 5 HELIX 27 27 ASP F 43 PHE F 45 5 3 HELIX 28 28 PRO F 51 GLY F 56 1 6 HELIX 29 29 PRO F 58 ASN F 77 1 20 HELIX 30 30 ALA F 86 CYS F 93 1 8 HELIX 31 31 PRO F 100 GLU F 121 5 22 HELIX 32 32 PRO F 124 LEU F 141 1 18 LINK FE HEM A 142 NE2 HIS A 87 LINK FE HEM A 142 C CMO A 143 LINK FE HEM E 147 NE2 HIS E 92 LINK FE HEM E 147 C CMO E 148 LINK FE HEM C 142 NE2 HIS C 87 LINK FE HEM C 142 C CMO C 143 LINK FE HEM F 147 NE2 HIS F 92 LINK FE HEM F 147 C CMO F 148 CRYST1 62.800 62.800 320.900 90.00 90.00 90.00 P 43 21 2 16 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 0.015924 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015924 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003116 0.00000 MTRIX1 1 -0.244910 -0.873480 -0.420780 64.31423 1 MTRIX2 1 -0.875860 0.013200 0.482380 8.04574 1 MTRIX3 1 -0.415790 0.486690 -0.768280 99.26502 1 MTRIX1 2 -0.229300 -0.879660 -0.416670 63.93441 1 MTRIX2 2 -0.890430 0.016670 0.454810 9.52063 1 MTRIX3 2 -0.393130 0.475310 -0.787100 100.20728 1