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HEADER OXYGEN STORAGE/TRANSPORT 08-AUG-00 1GCV TITLE DEOXY FORM HEMOGLOBIN FROM MUSTELUS GRISEUS COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN; COMPND 3 CHAIN: A, C; COMPND 4 FRAGMENT: ALPHA CHAIN; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEMOGLOBIN; COMPND 7 CHAIN: B, D; COMPND 8 FRAGMENT: BETA CHAIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUSTELUS GRISEUS; SOURCE 3 ORGANISM_COMMON: HOUNDSHARK; SOURCE 4 TISSUE: BLOOD; SOURCE 5 CELL: RED BLOOD CELL; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUSTELUS GRISEUS; SOURCE 8 ORGANISM_COMMON: HOUNDSHARK; SOURCE 9 TISSUE: BLOOD; SOURCE 10 CELL: RED BLOOD CELL KEYWDS HEMOGLOBIN,DEOXY FORM EXPDTA X-RAY DIFFRACTION AUTHOR Y.NAOI,K.T.CHONG,K.YOSHIMATSU,G.MIYAZAKI,J.R.H.TAME, AUTHOR 2 S.Y.PARK,S.I.ADACHI,H.MORIMOTO REVDAT 5 01-APR-03 1GCV 1 JRNL REVDAT 4 28-JAN-03 1GCV 1 REMARK REVDAT 3 25-APR-00 1GCV 1 REMARK REVDAT 2 11-APR-00 1GCV 1 JRNL REVDAT 1 31-AUG-00 1GCV 0 JRNL AUTH Y.NAOI,K.T.CHONG,K.YOSHIMATSU,G.MIYAZAKI,J.R.TAME, JRNL AUTH 2 S.Y.PARK,S.ADACHI,H.MORIMOTO JRNL TITL THE FUNCTIONAL SIMILARITY AND STRUCTURAL DIVERSITY JRNL TITL 2 OF HUMAN AND CARTILAGINOUS FISH HEMOGLOBINS. JRNL REF J.MOL.BIOL. V. 307 259 2001 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.00 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) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 39340 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.181 REMARK 3 FREE R VALUE : 0.223 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2078 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4402 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 172 REMARK 3 SOLVENT ATOMS : 148 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 27.17 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL 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) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.15 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : 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 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 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1GCV 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 PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB005038. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-NOV-1999 REMARK 200 TEMPERATURE (KELVIN) : 298.0 REMARK 200 PH : 6.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL44B2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.6 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 180156 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8 REMARK 200 DATA REDUNDANCY : 4.300 REMARK 200 R MERGE (I) : 0.04400 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) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1 REMARK 200 DATA REDUNDANCY IN SHELL : 4.50 REMARK 200 R MERGE FOR SHELL (I) : 0.16600 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: NULL REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.50 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, AMMONIUM REMARK 280 PHOSPHATE, HYDRO SULFIDE, PH 6.5, SMALL TUBES, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -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 45.27500 REMARK 290 SMTRY3 2 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 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, B, C, D 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 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 HIS A 87 CG HIS A 87 CD2 0.037 REMARK 500 HIS A 87 NE2 HIS A 87 CD2 0.038 REMARK 500 HIS B 53 CG HIS B 53 CD2 0.043 REMARK 500 HIS B 82 CG HIS B 82 CD2 0.041 REMARK 500 HIS C 58 CG HIS C 58 CD2 0.047 REMARK 500 HIS C 87 CG HIS C 87 CD2 0.042 REMARK 500 HIS C 87 NE2 HIS C 87 CD2 0.037 REMARK 500 HIS D 53 CG HIS D 53 CD2 0.046 REMARK 500 HIS D 82 CG HIS D 82 CD2 0.039 REMARK 500 ILE D 131 CA ILE D 131 CB 0.037 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 HIS A 58 CB - CG - CD2 ANGL. DEV. = -7.7 DEGREES REMARK 500 HIS A 58 CG - CD2 - NE2 ANGL. DEV. = -7.4 DEGREES REMARK 500 HIS A 87 ND1 - CG - CD2 ANGL. DEV. = 6.8 DEGREES REMARK 500 HIS A 87 CG - CD2 - NE2 ANGL. DEV. = -7.1 DEGREES REMARK 500 SER A 137 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 THR B 4 N - CA - C ANGL. DEV. = -8.5 DEGREES REMARK 500 HIS B 53 CA - CB - CG ANGL. DEV. = -8.0 DEGREES REMARK 500 HIS B 53 CB - CG - CD2 ANGL. DEV. = -7.1 DEGREES REMARK 500 HIS B 53 CG - CD2 - NE2 ANGL. DEV. = -6.7 DEGREES REMARK 500 HIS B 82 ND1 - CG - CD2 ANGL. DEV. = 7.2 DEGREES REMARK 500 HIS B 82 CG - ND1 - CE1 ANGL. DEV. = -7.3 DEGREES REMARK 500 HIS C 58 CB - CG - CD2 ANGL. DEV. = -7.9 DEGREES REMARK 500 HIS C 58 ND1 - CG - CD2 ANGL. DEV. = 7.0 DEGREES REMARK 500 HIS C 58 CG - ND1 - CE1 ANGL. DEV. = -6.6 DEGREES REMARK 500 HIS C 58 CG - CD2 - NE2 ANGL. DEV. = -7.2 DEGREES REMARK 500 SER C 137 N - CA - C ANGL. DEV. = 6.9 DEGREES REMARK 500 PRO D 36 N - CA - C ANGL. DEV. = 7.7 DEGREES REMARK 500 THR D 46 N - CA - C ANGL. DEV. = 7.4 DEGREES REMARK 500 HIS D 53 CB - CG - CD2 ANGL. DEV. = -6.8 DEGREES REMARK 500 ASP D 84 N - CA - C ANGL. DEV. = 8.1 DEGREES REMARK 500 LYS D 133 N - CA - C ANGL. DEV. = 6.8 DEGREES REMARK 500 GLN D 134 N - CA - C ANGL. DEV. = 7.2 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 LYS D 109 -118.81 43.61 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 1136 DISTANCE = 5.65 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1GCW RELATED DB: PDB REMARK 900 1GCW CONTAINS THE CARBON MONOXIDE BOUND FORM OF HEMOGLOBIN. DBREF 1GCV A 1 140 UNP Q9YGW2 HBA_MUSGR 1 140 DBREF 1GCV B 1 136 UNP Q9YGW1 HBB_MUSGR 1 136 DBREF 1GCV C 1 140 UNP Q9YGW2 HBA_MUSGR 1 140 DBREF 1GCV D 1 136 UNP Q9YGW1 HBB_MUSGR 1 136 SEQRES 1 A 140 ALA PHE THR ALA CYS GLU LYS GLN THR ILE GLY LYS ILE SEQRES 2 A 140 ALA GLN VAL LEU ALA LYS SER PRO GLU ALA TYR GLY ALA SEQRES 3 A 140 GLU CYS LEU ALA ARG LEU PHE VAL THR HIS PRO GLY SER SEQRES 4 A 140 LYS SER TYR PHE GLU TYR LYS ASP TYR SER ALA ALA GLY SEQRES 5 A 140 ALA LYS VAL GLN VAL HIS GLY GLY LYS VAL ILE ARG ALA SEQRES 6 A 140 VAL VAL LYS ALA ALA GLU HIS VAL ASP ASP LEU HIS SER SEQRES 7 A 140 HIS LEU GLU THR LEU ALA LEU THR HIS GLY LYS LYS LEU SEQRES 8 A 140 LEU VAL ASP PRO GLN ASN PHE PRO MET LEU SER GLU CYS SEQRES 9 A 140 ILE ILE VAL THR LEU ALA THR HIS LEU THR GLU PHE SER SEQRES 10 A 140 PRO ASP THR HIS CYS ALA VAL ASP LYS LEU LEU SER ALA SEQRES 11 A 140 ILE CYS GLN GLU LEU SER SER ARG TYR ARG SEQRES 1 B 136 VAL HIS TRP THR GLN GLU GLU ARG ASP GLU ILE SER LYS SEQRES 2 B 136 THR PHE GLN GLY THR ASP MET LYS THR VAL VAL THR GLN SEQRES 3 B 136 ALA LEU ASP ARG MET PHE LYS VAL TYR PRO TRP THR ASN SEQRES 4 B 136 ARG TYR PHE GLN LYS ARG THR ASP PHE ARG SER SER ILE SEQRES 5 B 136 HIS ALA GLY ILE VAL VAL GLY ALA LEU GLN ASP ALA VAL SEQRES 6 B 136 LYS HIS MET ASP ASP VAL LYS THR LEU PHE LYS ASP LEU SEQRES 7 B 136 SER LYS LYS HIS ALA ASP ASP LEU HIS VAL ASP PRO GLY SEQRES 8 B 136 SER PHE HIS LEU LEU THR ASP CYS ILE ILE VAL GLU LEU SEQRES 9 B 136 ALA TYR LEU ARG LYS ASP CYS PHE THR PRO HIS ILE GLN SEQRES 10 B 136 GLY ILE TRP ASP LYS PHE PHE GLU VAL VAL ILE ASP ALA SEQRES 11 B 136 ILE SER LYS GLN TYR HIS SEQRES 1 C 140 ALA PHE THR ALA CYS GLU LYS GLN THR ILE GLY LYS ILE SEQRES 2 C 140 ALA GLN VAL LEU ALA LYS SER PRO GLU ALA TYR GLY ALA SEQRES 3 C 140 GLU CYS LEU ALA ARG LEU PHE VAL THR HIS PRO GLY SER SEQRES 4 C 140 LYS SER TYR PHE GLU TYR LYS ASP TYR SER ALA ALA GLY SEQRES 5 C 140 ALA LYS VAL GLN VAL HIS GLY GLY LYS VAL ILE ARG ALA SEQRES 6 C 140 VAL VAL LYS ALA ALA GLU HIS VAL ASP ASP LEU HIS SER SEQRES 7 C 140 HIS LEU GLU THR LEU ALA LEU THR HIS GLY LYS LYS LEU SEQRES 8 C 140 LEU VAL ASP PRO GLN ASN PHE PRO MET LEU SER GLU CYS SEQRES 9 C 140 ILE ILE VAL THR LEU ALA THR HIS LEU THR GLU PHE SER SEQRES 10 C 140 PRO ASP THR HIS CYS ALA VAL ASP LYS LEU LEU SER ALA SEQRES 11 C 140 ILE CYS GLN GLU LEU SER SER ARG TYR ARG SEQRES 1 D 136 VAL HIS TRP THR GLN GLU GLU ARG ASP GLU ILE SER LYS SEQRES 2 D 136 THR PHE GLN GLY THR ASP MET LYS THR VAL VAL THR GLN SEQRES 3 D 136 ALA LEU ASP ARG MET PHE LYS VAL TYR PRO TRP THR ASN SEQRES 4 D 136 ARG TYR PHE GLN LYS ARG THR ASP PHE ARG SER SER ILE SEQRES 5 D 136 HIS ALA GLY ILE VAL VAL GLY ALA LEU GLN ASP ALA VAL SEQRES 6 D 136 LYS HIS MET ASP ASP VAL LYS THR LEU PHE LYS ASP LEU SEQRES 7 D 136 SER LYS LYS HIS ALA ASP ASP LEU HIS VAL ASP PRO GLY SEQRES 8 D 136 SER PHE HIS LEU LEU THR ASP CYS ILE ILE VAL GLU LEU SEQRES 9 D 136 ALA TYR LEU ARG LYS ASP CYS PHE THR PRO HIS ILE GLN SEQRES 10 D 136 GLY ILE TRP ASP LYS PHE PHE GLU VAL VAL ILE ASP ALA SEQRES 11 D 136 ILE SER LYS GLN TYR HIS HET HEM A 141 43 HET HEM B 137 43 HET HEM C 141 43 HET HEM D 137 43 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 5 HEM 4(C34 H32 FE N4 O4) FORMUL 9 HOH *148(H2 O) HELIX 1 1 THR A 3 SER A 20 1 18 HELIX 2 2 SER A 20 HIS A 36 1 17 HELIX 3 3 PRO A 37 PHE A 43 5 7 HELIX 4 4 GLY A 52 HIS A 72 1 21 HELIX 5 5 ASP A 75 LEU A 80 1 6 HELIX 6 6 LEU A 80 LYS A 90 1 11 HELIX 7 7 ASP A 94 GLN A 96 5 3 HELIX 8 8 ASN A 97 LEU A 113 1 17 HELIX 9 9 SER A 117 SER A 136 1 20 HELIX 10 10 THR B 4 THR B 18 1 15 HELIX 11 11 ASP B 19 TYR B 35 1 17 HELIX 12 12 PRO B 36 PHE B 42 5 7 HELIX 13 13 ARG B 49 HIS B 67 1 19 HELIX 14 14 ASP B 70 PHE B 75 1 6 HELIX 15 15 PHE B 75 ASP B 85 1 11 HELIX 16 16 ASP B 89 GLY B 91 5 3 HELIX 17 17 SER B 92 LYS B 109 1 18 HELIX 18 18 ASP B 110 PHE B 112 5 3 HELIX 19 19 THR B 113 LYS B 133 1 21 HELIX 20 20 THR C 3 ALA C 18 1 16 HELIX 21 21 SER C 20 HIS C 36 1 17 HELIX 22 22 PRO C 37 PHE C 43 5 7 HELIX 23 23 GLY C 52 HIS C 72 1 21 HELIX 24 24 ASP C 75 LEU C 80 1 6 HELIX 25 25 LEU C 80 LYS C 90 1 11 HELIX 26 26 GLN C 96 LEU C 113 1 18 HELIX 27 27 SER C 117 SER C 136 1 20 HELIX 28 28 THR D 4 THR D 18 1 15 HELIX 29 29 ASP D 19 TYR D 35 1 17 HELIX 30 30 PRO D 36 PHE D 42 5 7 HELIX 31 31 ARG D 49 HIS D 67 1 19 HELIX 32 32 ASP D 70 PHE D 75 1 6 HELIX 33 33 PHE D 75 ASP D 85 1 11 HELIX 34 34 ASP D 89 GLY D 91 5 3 HELIX 35 35 SER D 92 LYS D 109 1 18 HELIX 36 36 ASP D 110 PHE D 112 5 3 HELIX 37 37 THR D 113 LYS D 133 1 21 LINK FE HEM A 141 NE2 HIS A 87 LINK FE HEM B 137 NE2 HIS B 82 LINK FE HEM C 141 NE2 HIS C 87 LINK FE HEM D 137 NE2 HIS D 82 CRYST1 57.680 90.550 61.450 90.00 98.45 90.00 P 1 21 1 4 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 0.017337 0.000000 0.002576 0.00000 SCALE2 0.000000 0.011044 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016452 0.00000