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HEADER OXYGEN STORAGE/TRANSPORT 13-JUL-00 1FAW TITLE GRAYLAG GOOSE HEMOGLOBIN (OXY FORM) COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN (ALPHA SUBUNIT); COMPND 3 CHAIN: A, C; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: HEMOGLOBIN (BETA SUBUNIT); COMPND 6 CHAIN: B, D SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ANSER ANSER; SOURCE 3 ORGANISM_COMMON: GRAYLAG GOOSE; SOURCE 4 TISSUE: BLOOD; SOURCE 5 CELL: ERYTHROCYTES; SOURCE 6 CELLULAR_LOCATION: CYTOPLASM; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: ANSER ANSER; SOURCE 9 ORGANISM_COMMON: GRAYLAG GOOSE; SOURCE 10 TISSUE: BLOOD; SOURCE 11 CELL: ERYTHROCYTES; SOURCE 12 CELLULAR_LOCATION: CYTOPLASM KEYWDS OXYGEN TRANSPORT, HEME, RESPIRATORY PROTEIN, ERYTHROCYTE EXPDTA X-RAY DIFFRACTION AUTHOR Y.-H.LIANG,X.-Z.LIU,S.-H.LIU,G.-Y.LU REVDAT 2 01-APR-03 1FAW 1 JRNL REVDAT 1 05-DEC-01 1FAW 0 JRNL AUTH Y.H.LIANG,X.Z.LIU,S.H.LIU,G.Y.LU JRNL TITL THE STRUCTURE OF GREYLAG GOOSE OXY HAEMOGLOBIN: JRNL TITL 2 THE ROLES OF FOUR MUTATIONS COMPARED WITH JRNL TITL 3 BAR-HEADED GOOSE HAEMOGLOBIN. JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 57 1850 2001 JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.09 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 0.5 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.09 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.30 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1092327.870 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.7 REMARK 3 NUMBER OF REFLECTIONS : 11543 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) : 0.176 REMARK 3 FREE R VALUE : 0.220 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.900 REMARK 3 FREE R VALUE TEST SET COUNT : 1022 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.09 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.28 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.80 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1648 REMARK 3 BIN R VALUE (WORKING SET) : 0.2660 REMARK 3 BIN FREE R VALUE : 0.3030 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.30 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 190 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4470 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) : 37.20 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.90 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.96000 REMARK 3 B22 (A**2) : -3.44000 REMARK 3 B33 (A**2) : 2.49000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -3.33000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29 REMARK 3 ESD FROM SIGMAA (A) : 0.43 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.37 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.48 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 1.60 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.60 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.15 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : GROUP 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 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.31 REMARK 3 BSOL : 28.82 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 : PROTEIN_REP.PA REMARK 3 PARAMETER FILE 2 : WATER_REP.PARA REMARK 3 PARAMETER FILE 3 : PARAM19X.HEME REMARK 3 PARAMETER FILE 4 : LIGAND.PARAM REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER.TOP REMARK 3 TOPOLOGY FILE 3 : TOPH19X.HEME REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1FAW 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 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB011443. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-JAN-1997 REMARK 200 TEMPERATURE (KELVIN) : 291.0 REMARK 200 PH : 6.80 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 RU200 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12746 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 200 DATA REDUNDANCY : 4.400 REMARK 200 R MERGE (I) : 0.11300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.07 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0 REMARK 200 DATA REDUNDANCY IN SHELL : 2.30 REMARK 200 R MERGE FOR SHELL (I) : 0.33400 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: CNS 0.5 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.56 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, POTASSIUM PHOSPHATE, PH REMARK 280 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K 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 40.31200 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 0.057 REMARK 500 HIS C 87 CG HIS C 87 CD2 0.057 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. =-13.8 DEGREES REMARK 500 LEU A 48 N - CA - C ANGL. DEV. = 7.4 DEGREES REMARK 500 HIS B 92 CA - CB - CG ANGL. DEV. = -9.0 DEGREES REMARK 500 PHE B 103 N - CA - C ANGL. DEV. = -7.5 DEGREES REMARK 500 ASP C 47 N - CA - C ANGL. DEV. =-13.8 DEGREES REMARK 500 LEU C 48 N - CA - C ANGL. DEV. = 7.4 DEGREES REMARK 500 HIS D 92 CA - CB - CG ANGL. DEV. = -9.0 DEGREES REMARK 500 PHE D 103 N - CA - C ANGL. DEV. = -7.5 DEGREES DBREF 1FAW A 1 141 UNP P01989 HBA_ANSAN 1 141 DBREF 1FAW B 1 146 UNP P02117 HBB_ANSAN 1 146 DBREF 1FAW C 1 141 UNP P01989 HBA_ANSAN 1 141 DBREF 1FAW D 1 146 UNP P02117 HBB_ANSAN 1 146 SEQRES 1 A 141 VAL LEU SER ALA ALA ASP LYS THR ASN VAL LYS GLY VAL SEQRES 2 A 141 PHE SER LYS ILE GLY GLY HIS ALA GLU GLU TYR GLY ALA SEQRES 3 A 141 GLU THR LEU GLU ARG MET PHE THR ALA TYR PRO GLN THR SEQRES 4 A 141 LYS THR TYR PHE PRO HIS PHE ASP LEU GLN HIS GLY SER SEQRES 5 A 141 ALA GLN ILE LYS ALA HIS GLY LYS LYS VAL ALA ALA ALA SEQRES 6 A 141 LEU VAL GLU ALA VAL ASN HIS ILE ASP ASP ILE ALA GLY SEQRES 7 A 141 ALA LEU SER LYS LEU SER ASP LEU HIS ALA GLN LYS LEU SEQRES 8 A 141 ARG VAL ASP PRO VAL ASN PHE LYS PHE LEU GLY HIS CYS SEQRES 9 A 141 PHE LEU VAL VAL VAL ALA ILE HIS HIS PRO SER ALA LEU SEQRES 10 A 141 THR PRO GLU VAL HIS ALA SER LEU ASP LYS PHE LEU CYS SEQRES 11 A 141 ALA VAL GLY THR VAL LEU THR ALA LYS TYR ARG SEQRES 1 B 146 VAL HIS TRP SER ALA GLU GLU LYS GLN LEU ILE THR GLY SEQRES 2 B 146 LEU TRP GLY LYS VAL ASN VAL ALA ASP CYS GLY ALA GLU SEQRES 3 B 146 ALA LEU ALA ARG LEU LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 B 146 ARG PHE PHE SER SER PHE GLY ASN LEU SER SER PRO THR SEQRES 5 B 146 ALA ILE LEU GLY ASN PRO MET VAL ARG ALA HIS GLY LYS SEQRES 6 B 146 LYS VAL LEU THR SER PHE GLY ASP ALA VAL LYS ASN LEU SEQRES 7 B 146 ASP ASN ILE LYS ASN THR PHE ALA GLN LEU SER GLU LEU SEQRES 8 B 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG SEQRES 9 B 146 LEU LEU GLY ASP ILE LEU ILE ILE VAL LEU ALA ALA HIS SEQRES 10 B 146 PHE ALA LYS GLU PHE THR PRO GLU CYS GLN ALA ALA TRP SEQRES 11 B 146 GLN LYS LEU VAL ARG VAL VAL ALA HIS ALA LEU ALA ARG SEQRES 12 B 146 LYS TYR HIS SEQRES 1 C 141 VAL LEU SER ALA ALA ASP LYS THR ASN VAL LYS GLY VAL SEQRES 2 C 141 PHE SER LYS ILE GLY GLY HIS ALA GLU GLU TYR GLY ALA SEQRES 3 C 141 GLU THR LEU GLU ARG MET PHE THR ALA TYR PRO GLN THR SEQRES 4 C 141 LYS THR TYR PHE PRO HIS PHE ASP LEU GLN HIS GLY SER SEQRES 5 C 141 ALA GLN ILE LYS ALA HIS GLY LYS LYS VAL ALA ALA ALA SEQRES 6 C 141 LEU VAL GLU ALA VAL ASN HIS ILE ASP ASP ILE ALA GLY SEQRES 7 C 141 ALA LEU SER LYS LEU SER ASP LEU HIS ALA GLN LYS LEU SEQRES 8 C 141 ARG VAL ASP PRO VAL ASN PHE LYS PHE LEU GLY HIS CYS SEQRES 9 C 141 PHE LEU VAL VAL VAL ALA ILE HIS HIS PRO SER ALA LEU SEQRES 10 C 141 THR PRO GLU VAL HIS ALA SER LEU ASP LYS PHE LEU CYS SEQRES 11 C 141 ALA VAL GLY THR VAL LEU THR ALA LYS TYR ARG SEQRES 1 D 146 VAL HIS TRP SER ALA GLU GLU LYS GLN LEU ILE THR GLY SEQRES 2 D 146 LEU TRP GLY LYS VAL ASN VAL ALA ASP CYS GLY ALA GLU SEQRES 3 D 146 ALA LEU ALA ARG LEU LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 D 146 ARG PHE PHE SER SER PHE GLY ASN LEU SER SER PRO THR SEQRES 5 D 146 ALA ILE LEU GLY ASN PRO MET VAL ARG ALA HIS GLY LYS SEQRES 6 D 146 LYS VAL LEU THR SER PHE GLY ASP ALA VAL LYS ASN LEU SEQRES 7 D 146 ASP ASN ILE LYS ASN THR PHE ALA GLN LEU SER GLU LEU SEQRES 8 D 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG SEQRES 9 D 146 LEU LEU GLY ASP ILE LEU ILE ILE VAL LEU ALA ALA HIS SEQRES 10 D 146 PHE ALA LYS GLU PHE THR PRO GLU CYS GLN ALA ALA TRP SEQRES 11 D 146 GLN LYS LEU VAL ARG VAL VAL ALA HIS ALA LEU ALA ARG SEQRES 12 D 146 LYS TYR HIS HET HEM A 150 43 HET OXY A 151 2 HET HEM B 150 43 HET OXY B 151 2 HET HEM C 150 43 HET OXY C 151 2 HET HEM D 150 43 HET OXY D 151 2 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM OXY OXYGEN MOLECULE HETSYN HEM HEME FORMUL 5 HEM 4(C34 H32 FE N4 O4) FORMUL 6 OXY 4(O2) HELIX 1 1 SER A 3 LYS A 16 1 14 HELIX 2 2 ILE A 17 GLY A 19 5 3 HELIX 3 3 HIS A 20 TYR A 36 1 17 HELIX 4 4 PRO A 37 PHE A 43 5 7 HELIX 5 5 SER A 52 ASN A 71 1 20 HELIX 6 6 HIS A 72 ILE A 76 5 5 HELIX 7 7 LEU A 80 GLN A 89 1 10 HELIX 8 8 PRO A 95 HIS A 113 1 19 HELIX 9 9 PRO A 114 LEU A 117 5 4 HELIX 10 10 THR A 118 THR A 137 1 20 HELIX 11 11 ALA A 138 ARG A 141 5 4 HELIX 12 12 SER B 4 GLY B 16 1 13 HELIX 13 13 ASN B 19 TYR B 35 1 17 HELIX 14 14 PRO B 36 SER B 43 5 8 HELIX 15 15 PHE B 42 GLY B 46 5 5 HELIX 16 16 SER B 50 ASN B 57 1 8 HELIX 17 17 ASN B 57 ASN B 77 1 21 HELIX 18 18 ASN B 80 PHE B 85 1 6 HELIX 19 19 PHE B 85 ASP B 94 1 10 HELIX 20 20 PRO B 100 ALA B 119 1 20 HELIX 21 21 LYS B 120 PHE B 122 5 3 HELIX 22 22 THR B 123 ALA B 142 1 20 HELIX 23 23 SER C 3 LYS C 16 1 14 HELIX 24 24 ILE C 17 GLY C 19 5 3 HELIX 25 25 HIS C 20 TYR C 36 1 17 HELIX 26 26 PRO C 37 PHE C 43 5 7 HELIX 27 27 SER C 52 ASN C 71 1 20 HELIX 28 28 HIS C 72 ILE C 76 5 5 HELIX 29 29 LEU C 80 GLN C 89 1 10 HELIX 30 30 PRO C 95 HIS C 113 1 19 HELIX 31 31 PRO C 114 LEU C 117 5 4 HELIX 32 32 THR C 118 THR C 137 1 20 HELIX 33 33 ALA C 138 ARG C 141 5 4 HELIX 34 34 SER D 4 GLY D 16 1 13 HELIX 35 35 ASN D 19 TYR D 35 1 17 HELIX 36 36 PRO D 36 SER D 43 5 8 HELIX 37 37 PHE D 42 GLY D 46 5 5 HELIX 38 38 SER D 50 ASN D 57 1 8 HELIX 39 39 ASN D 57 ASN D 77 1 21 HELIX 40 40 ASN D 80 PHE D 85 1 6 HELIX 41 41 PHE D 85 ASP D 94 1 10 HELIX 42 42 PRO D 100 ALA D 119 1 20 HELIX 43 43 LYS D 120 PHE D 122 5 3 HELIX 44 44 THR D 123 ALA D 142 1 20 LINK FE HEM A 150 O1 OXY A 151 LINK FE HEM B 150 O1 OXY B 151 LINK FE HEM C 150 O1 OXY C 151 LINK FE HEM D 150 O1 OXY D 151 LINK FE HEM A 150 NE2 HIS A 87 LINK FE HEM B 150 NE2 HIS B 92 LINK FE HEM C 150 NE2 HIS C 87 LINK FE HEM D 150 NE2 HIS D 92 CRYST1 57.552 80.624 72.571 90.00 102.75 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 0.017376 0.000000 0.003931 0.00000 SCALE2 0.000000 0.012403 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014128 0.00000