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HEADER OXYGEN STORAGE/TRANSPORT 05-OCT-00 1G0A TITLE CARBONMONOXY LIGANDED BOVINE HEMOGLOBIN PH 8.5 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN ALPHA CHAIN; COMPND 3 CHAIN: A, C; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: HEMOGLOBIN BETA CHAIN; COMPND 6 CHAIN: B, D SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: BOVINE; SOURCE 4 TISSUE: BLOOD; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 7 ORGANISM_COMMON: BOVINE; SOURCE 8 TISSUE: BLOOD KEYWDS BOVINE, HEMOGLOBIN, LIGANDED, CARBONMONOXY, PROTOPORPHYRIN KEYWDS 2 IX EXPDTA X-RAY DIFFRACTION AUTHOR T.C.MUESER,P.H.ROGERS,A.ARNONE REVDAT 1 27-DEC-00 1G0A 0 JRNL AUTH T.C.MUESER,P.H.ROGERS,A.ARNONE JRNL TITL INTERFACE SLIDING AS ILLUSTRATED BY THE MULTIPLE JRNL TITL 2 QUATERNARY STRUCTURES OF LIGANDED HEMOGLOBIN. JRNL REF BIOCHEMISTRY V. 39 15353 2000 JRNL REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.04 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PROLSQ REMARK 3 AUTHORS : KONNERT,HENDRICKSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.04 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4 REMARK 3 NUMBER OF REFLECTIONS : 36902 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : 0.189 REMARK 3 R VALUE (WORKING SET) : 0.189 REMARK 3 FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA. REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL REMARK 3 FREE R VALUE (NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 37869 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4386 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 180 REMARK 3 SOLVENT ATOMS : 145 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 29.20 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 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : 0.009 ; NULL REMARK 3 ANGLE DISTANCE (A) : 0.023 ; NULL REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : NULL ; NULL REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : NULL ; NULL REMARK 3 STAGGERED (DEGREES) : NULL ; NULL REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1G0A 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 RCSB012072. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-JAN-1992 REMARK 200 TEMPERATURE (KELVIN) : 298.0 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 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 : AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : SDMS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SDMS REMARK 200 DATA SCALING SOFTWARE : SDMS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38330 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.040 REMARK 200 RESOLUTION RANGE LOW (A) : 35.530 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2 REMARK 200 DATA REDUNDANCY : 7.950 REMARK 200 R MERGE (I) : 0.06700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20 REMARK 200 COMPLETENESS FOR SHELL (%) : 86.4 REMARK 200 DATA REDUNDANCY IN SHELL : 3.10 REMARK 200 R MERGE FOR SHELL (I) : 0.19700 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: MERLOT REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.04 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM TAPS, AMMONIUM SULPHATE, REMARK 280 POTASSIUM CHLORIDE, POLYETHYLENE GLYCOL 3350, PH 8.5, VAPOR REMARK 280 DIFFUSION, HANGING DROP, 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 36.90000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.55000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.70000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 31.55000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.90000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.70000 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 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HIS A 45 O HOH 65 2564 1.62 REMARK 500 C HIS A 45 O HOH 65 2564 1.63 REMARK 500 OD2 ASP B 52 O HOH 84 4556 2.10 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 102 DISTANCE = 5.95 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1G08 RELATED DB: PDB REMARK 900 CARBONMONOXY LIGANDED BOVINE HEMOGLOBIN PH 5.0 REMARK 900 RELATED ID: 1G09 RELATED DB: PDB REMARK 900 CARBONMONOXY LIGANDED BOVINE HEMOGLOBIN PH 7.2 REMARK 900 RELATED ID: 1G0B RELATED DB: PDB REMARK 900 CARBONMONOXY LIGANDED EQUINE HEMOGLOBIN PH 8.5 DBREF 1G0A A 1 141 UNP P01966 HBA_BOVIN 1 141 DBREF 1G0A C 1 141 UNP P01966 HBA_BOVIN 1 141 DBREF 1G0A B 2 146 UNP P02070 HBB_BOVIN 1 145 DBREF 1G0A D 2 146 UNP P02070 HBB_BOVIN 1 145 SEQRES 1 A 141 VAL LEU SER ALA ALA ASP LYS GLY ASN VAL LYS ALA ALA SEQRES 2 A 141 TRP GLY LYS VAL GLY GLY HIS ALA ALA 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 ALA LYS VAL ALA ALA ALA SEQRES 6 A 141 LEU THR LYS ALA VAL GLU HIS LEU ASP ASP LEU PRO GLY SEQRES 7 A 141 ALA LEU SER GLU 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 SER SEQRES 9 A 141 LEU LEU VAL THR LEU ALA SER HIS LEU PRO SER ASP PHE SEQRES 10 A 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA SEQRES 11 A 141 ASN VAL SER THR VAL LEU THR SER LYS TYR ARG SEQRES 1 B 145 MET LEU THR ALA GLU GLU LYS ALA ALA VAL THR ALA PHE SEQRES 2 B 145 TRP GLY LYS VAL LYS VAL ASP GLU VAL GLY GLY GLU ALA SEQRES 3 B 145 LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN ARG SEQRES 4 B 145 PHE PHE GLU SER PHE GLY ASP LEU SER THR ALA ASP ALA SEQRES 5 B 145 VAL MET ASN ASN PRO LYS VAL LYS ALA HIS GLY LYS LYS SEQRES 6 B 145 VAL LEU ASP SER PHE SER ASN GLY MET LYS HIS LEU ASP SEQRES 7 B 145 ASP LEU LYS GLY THR PHE ALA ALA LEU SER GLU LEU HIS SEQRES 8 B 145 CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE LYS LEU SEQRES 9 B 145 LEU GLY ASN VAL LEU VAL VAL VAL LEU ALA ARG ASN PHE SEQRES 10 B 145 GLY LYS GLU PHE THR PRO VAL LEU GLN ALA ASP PHE GLN SEQRES 11 B 145 LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS ARG SEQRES 12 B 145 TYR HIS SEQRES 1 C 141 VAL LEU SER ALA ALA ASP LYS GLY ASN VAL LYS ALA ALA SEQRES 2 C 141 TRP GLY LYS VAL GLY GLY HIS ALA ALA 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 ALA LYS VAL ALA ALA ALA SEQRES 6 C 141 LEU THR LYS ALA VAL GLU HIS LEU ASP ASP LEU PRO GLY SEQRES 7 C 141 ALA LEU SER GLU 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 SER SEQRES 9 C 141 LEU LEU VAL THR LEU ALA SER HIS LEU PRO SER ASP PHE SEQRES 10 C 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA SEQRES 11 C 141 ASN VAL SER THR VAL LEU THR SER LYS TYR ARG SEQRES 1 D 145 MET LEU THR ALA GLU GLU LYS ALA ALA VAL THR ALA PHE SEQRES 2 D 145 TRP GLY LYS VAL LYS VAL ASP GLU VAL GLY GLY GLU ALA SEQRES 3 D 145 LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN ARG SEQRES 4 D 145 PHE PHE GLU SER PHE GLY ASP LEU SER THR ALA ASP ALA SEQRES 5 D 145 VAL MET ASN ASN PRO LYS VAL LYS ALA HIS GLY LYS LYS SEQRES 6 D 145 VAL LEU ASP SER PHE SER ASN GLY MET LYS HIS LEU ASP SEQRES 7 D 145 ASP LEU LYS GLY THR PHE ALA ALA LEU SER GLU LEU HIS SEQRES 8 D 145 CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE LYS LEU SEQRES 9 D 145 LEU GLY ASN VAL LEU VAL VAL VAL LEU ALA ARG ASN PHE SEQRES 10 D 145 GLY LYS GLU PHE THR PRO VAL LEU GLN ALA ASP PHE GLN SEQRES 11 D 145 LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS ARG SEQRES 12 D 145 TYR HIS HET HEM A 142 43 HET CMO A 143 2 HET HEM B 147 43 HET CMO B 148 2 HET HEM C 142 43 HET CMO C 143 2 HET HEM D 147 43 HET CMO D 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) FORMUL 13 HOH *145(H2 O) HELIX 1 1 SER A 3 GLY A 18 1 16 HELIX 2 2 HIS A 20 PHE A 36 1 17 HELIX 3 3 PRO A 37 PHE A 43 5 7 HELIX 4 4 SER A 52 HIS A 72 1 21 HELIX 5 5 ASP A 75 SER A 81 1 7 HELIX 6 6 LEU A 80 ALA A 88 1 9 HELIX 7 7 PRO A 95 LEU A 113 1 19 HELIX 8 8 THR A 118 THR A 137 1 20 HELIX 9 9 THR B 4 GLY B 16 1 13 HELIX 10 10 LYS B 19 TYR B 35 1 17 HELIX 11 11 PRO B 36 GLU B 43 5 8 HELIX 12 12 PHE B 42 GLY B 46 5 5 HELIX 13 13 THR B 50 ASN B 57 1 8 HELIX 14 14 ASN B 57 HIS B 77 1 21 HELIX 15 15 ASP B 80 PHE B 85 1 6 HELIX 16 16 PHE B 85 LYS B 95 1 11 HELIX 17 17 PRO B 100 GLY B 119 1 20 HELIX 18 18 LYS B 120 PHE B 122 5 3 HELIX 19 19 THR B 123 ALA B 142 1 20 HELIX 20 20 HIS B 143 TYR B 145 5 3 HELIX 21 21 SER C 3 GLY C 18 1 16 HELIX 22 22 HIS C 20 PHE C 36 1 17 HELIX 23 23 PRO C 37 PHE C 43 5 7 HELIX 24 24 SER C 52 HIS C 72 1 21 HELIX 25 25 ASP C 75 LEU C 80 1 6 HELIX 26 26 LEU C 80 HIS C 89 1 10 HELIX 27 27 PRO C 95 LEU C 113 1 19 HELIX 28 28 THR C 118 THR C 137 1 20 HELIX 29 29 THR D 4 GLY D 16 1 13 HELIX 30 30 LYS D 19 TYR D 35 1 17 HELIX 31 31 PRO D 36 GLU D 43 5 8 HELIX 32 32 PHE D 42 GLY D 46 5 5 HELIX 33 33 THR D 50 ASN D 57 1 8 HELIX 34 34 ASN D 57 MET D 75 1 19 HELIX 35 35 ASP D 80 PHE D 85 1 6 HELIX 36 36 PHE D 85 LYS D 95 1 11 HELIX 37 37 PRO D 100 GLY D 119 1 20 HELIX 38 38 LYS D 120 PHE D 122 5 3 HELIX 39 39 THR D 123 ALA D 142 1 20 HELIX 40 40 HIS D 143 TYR D 145 5 3 LINK FE HEM A 142 NE2 HIS A 87 LINK FE HEM A 142 C CMO A 143 LINK FE HEM B 147 NE2 HIS B 92 LINK FE HEM B 147 C CMO B 148 LINK FE HEM C 142 NE2 HIS C 87 LINK FE HEM C 142 C CMO C 143 LINK FE HEM D 147 NE2 HIS D 92 LINK FE HEM D 147 C CMO D 148 CRYST1 73.800 131.400 63.100 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 0.013550 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007610 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015848 0.00000