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HEADER OXYGEN STORAGE/TRANSPORT 08-AUG-00 1GCW TITLE CO FORM HEMOGLOBIN FROM MUSTELUS GRISEUS COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (HEMOGLOBIN); COMPND 3 CHAIN: A, C; COMPND 4 FRAGMENT: ALPHA CHAIN; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: PROTEIN (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, CARBON MONOXIDE BOUND 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 4 01-APR-03 1GCW 1 JRNL REVDAT 3 28-JAN-03 1GCW 1 REMARK REVDAT 2 11-APR-01 1GCW 1 JRNL REVDAT 1 06-SEP-00 1GCW 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) : 30.00 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 : 37342 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) : 0.199 REMARK 3 FREE R VALUE : 0.255 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1963 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 : 4268 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 172 REMARK 3 SOLVENT ATOMS : 63 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 37229.00 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) : 1.09 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 1GCW 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 (2007-05-01) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB005039. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 298.0 REMARK 200 PH : 7.00 REMARK 200 NUMBER OF CRYSTALS USED : 3 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PHOTON FACTORY REMARK 200 BEAMLINE : BL-18B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : FUJI REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 255405 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 100.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.5 REMARK 200 DATA REDUNDANCY : 6.500 REMARK 200 R MERGE (I) : 0.07500 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) : 2.07 REMARK 200 COMPLETENESS FOR SHELL (%) : 66.4 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.26500 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 (%): 50.24 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG2000, SODIUM PHOSPHATE, HYDRO REMARK 280 SULFIDE, PH 7.00, SMALL TUBES, TEMPERATURE 298K 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 33.35000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.41500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.22500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.41500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.35000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.22500 REMARK 290 SMTRY3 4 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 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 LYS B 44 REMARK 465 ARG B 45 REMARK 465 THR B 46 REMARK 465 ASP B 47 REMARK 465 GLN B 134 REMARK 465 TYR B 135 REMARK 465 LYS D 44 REMARK 465 ARG D 45 REMARK 465 THR D 46 REMARK 465 ASP D 47 REMARK 465 GLN D 134 REMARK 465 TYR D 135 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 58 CG HIS A 58 CD2 0.059 REMARK 500 MET B 31 SD MET B 31 CE -0.097 REMARK 500 PHE B 48 N PHE B 48 CA 0.043 REMARK 500 HIS B 53 CG HIS B 53 CD2 0.042 REMARK 500 HIS B 82 CG HIS B 82 CD2 0.063 REMARK 500 HIS B 82 NE2 HIS B 82 CD2 0.048 REMARK 500 HIS C 58 CG HIS C 58 CD2 0.053 REMARK 500 HIS C 87 CG HIS C 87 CD2 0.048 REMARK 500 PHE D 48 N PHE D 48 CA 0.041 REMARK 500 HIS D 82 CG HIS D 82 CD2 0.047 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 CA - CB - CG ANGL. DEV. = -9.2 DEGREES REMARK 500 HIS A 58 ND1 - CG - CD2 ANGL. DEV. = 7.6 DEGREES REMARK 500 HIS A 58 CG - ND1 - CE1 ANGL. DEV. = -8.8 DEGREES REMARK 500 HIS A 58 ND1 - CE1 - NE2 ANGL. DEV. = 7.1 DEGREES REMARK 500 HIS A 58 CG - CD2 - NE2 ANGL. DEV. = -7.5 DEGREES REMARK 500 HIS A 87 ND1 - CG - CD2 ANGL. DEV. = 6.9 DEGREES REMARK 500 HIS A 87 CG - ND1 - CE1 ANGL. DEV. = -7.0 DEGREES REMARK 500 HIS A 112 N - CA - C ANGL. DEV. = 8.2 DEGREES REMARK 500 HIS B 53 CA - CB - CG ANGL. DEV. = -7.5 DEGREES REMARK 500 HIS B 82 ND1 - CE1 - NE2 ANGL. DEV. = 6.8 DEGREES REMARK 500 LEU B 107 CA - CB - CG ANGL. DEV. = 6.8 DEGREES REMARK 500 HIS C 58 CA - CB - CG ANGL. DEV. = -7.4 DEGREES REMARK 500 HIS C 87 ND1 - CG - CD2 ANGL. DEV. = 7.2 DEGREES REMARK 500 HIS C 87 CG - ND1 - CE1 ANGL. DEV. = -8.1 DEGREES REMARK 500 HIS C 87 ND1 - CE1 - NE2 ANGL. DEV. = 6.8 DEGREES REMARK 500 HIS D 53 CA - CB - CG ANGL. DEV. = -7.5 DEGREES REMARK 500 HIS D 53 CB - CG - CD2 ANGL. DEV. = -6.7 DEGREES REMARK 500 HIS D 53 CG - CD2 - NE2 ANGL. DEV. = -6.8 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1GCV RELATED DB: PDB REMARK 900 1GCV CONTAINS THE DEOXY FORM OF HEMOGLOBIN. DBREF 1GCW A 1 140 UNP Q9YGW2 HBA_MUSGR 1 140 DBREF 1GCW B 1 136 UNP Q9YGW1 HBB_MUSGR 1 136 DBREF 1GCW C 1 140 UNP Q9YGW2 HBA_MUSGR 1 140 DBREF 1GCW 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 135 VAL HIS TRP THR GLN GLU GLU ARG ASP GLU ILE SER LYS SEQRES 2 B 135 THR PHE GLN GLY THR ASP MET LYS THR VAL VAL THR GLN SEQRES 3 B 135 ALA LEU ASP ARG MET PHE LYS VAL TYR PRO TRP THR ASN SEQRES 4 B 135 ARG TYR PHE GLN LYS ARG THR ASP PHE ARG SER SER ILE SEQRES 5 B 135 HIS ALA GLY ILE VAL VAL GLY ALA LEU GLN ASP ALA VAL SEQRES 6 B 135 LYS HIS MET ASP ASP VAL LYS THR LEU PHE LYS ASP LEU SEQRES 7 B 135 SER LYS LYS HIS ALA ASP ASP LEU HIS VAL ASP PRO GLY SEQRES 8 B 135 SER PHE HIS LEU LEU THR ASP CYS ILE ILE VAL GLU LEU SEQRES 9 B 135 ALA TYR LEU ARG LYS ASP CYS PHE THR PRO HIS ILE GLN SEQRES 10 B 135 GLY ILE TRP ASP LYS PHE PHE GLU VAL VAL ILE ASP ALA SEQRES 11 B 135 ILE SER LYS GLN TYR 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 135 VAL HIS TRP THR GLN GLU GLU ARG ASP GLU ILE SER LYS SEQRES 2 D 135 THR PHE GLN GLY THR ASP MET LYS THR VAL VAL THR GLN SEQRES 3 D 135 ALA LEU ASP ARG MET PHE LYS VAL TYR PRO TRP THR ASN SEQRES 4 D 135 ARG TYR PHE GLN LYS ARG THR ASP PHE ARG SER SER ILE SEQRES 5 D 135 HIS ALA GLY ILE VAL VAL GLY ALA LEU GLN ASP ALA VAL SEQRES 6 D 135 LYS HIS MET ASP ASP VAL LYS THR LEU PHE LYS ASP LEU SEQRES 7 D 135 SER LYS LYS HIS ALA ASP ASP LEU HIS VAL ASP PRO GLY SEQRES 8 D 135 SER PHE HIS LEU LEU THR ASP CYS ILE ILE VAL GLU LEU SEQRES 9 D 135 ALA TYR LEU ARG LYS ASP CYS PHE THR PRO HIS ILE GLN SEQRES 10 D 135 GLY ILE TRP ASP LYS PHE PHE GLU VAL VAL ILE ASP ALA SEQRES 11 D 135 ILE SER LYS GLN TYR HET HEM A 141 43 HET CMO A 142 2 HET HEM B 134 43 HET CMO B 135 2 HET HEM C 141 43 HET CMO C 142 2 HET HEM D 134 43 HET CMO D 135 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) FORMUL 13 HOH *63(H2 O) HELIX 1 1 CYS A 5 SER A 20 1 16 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 GLU A 71 1 20 HELIX 5 5 HIS A 72 ASP A 74 5 3 HELIX 6 6 ASP A 75 LEU A 80 1 6 HELIX 7 7 LEU A 80 LYS A 89 1 10 HELIX 8 8 GLN A 96 LEU A 113 1 18 HELIX 9 9 SER A 117 LEU A 135 1 19 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 GLN B 43 5 8 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 84 1 10 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 SER B 132 1 20 HELIX 20 20 THR C 3 SER C 20 1 18 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 GLU C 71 1 20 HELIX 24 24 HIS C 72 ASP C 74 5 3 HELIX 25 25 ASP C 75 LEU C 80 1 6 HELIX 26 26 LEU C 80 GLY C 88 1 9 HELIX 27 27 GLN C 96 LEU C 113 1 18 HELIX 28 28 SER C 117 SER C 136 1 20 HELIX 29 29 THR D 4 THR D 18 1 15 HELIX 30 30 ASP D 19 TYR D 35 1 17 HELIX 31 31 PRO D 36 GLN D 43 5 8 HELIX 32 32 ARG D 49 HIS D 67 1 19 HELIX 33 33 ASP D 70 PHE D 75 1 6 HELIX 34 34 PHE D 75 ASP D 85 1 11 HELIX 35 35 SER D 92 ARG D 108 1 17 HELIX 36 36 LYS D 109 PHE D 112 5 4 HELIX 37 37 THR D 113 ALA D 130 1 18 LINK FE HEM A 141 NE2 HIS A 87 LINK FE HEM A 141 C CMO A 142 LINK FE HEM B 134 NE2 HIS B 82 LINK FE HEM B 134 C CMO B 135 LINK FE HEM C 141 NE2 HIS C 87 LINK FE HEM C 141 C CMO C 142 LINK FE HEM D 134 NE2 HIS D 82 LINK FE HEM D 134 C CMO D 135 CRYST1 66.700 80.450 114.830 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 0.014993 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012430 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008709 0.00000