[Scop | Full Entry | Seq (local cached copy) | More Options ]
HEADER OXYGEN STORAGE/TRANSPORT 15-JUN-00 1F5P TITLE 2.9 ANGSTROM CRYSTAL STRUCTURE OF LAMPREY HEMOGLOBIN THAT TITLE 2 HAS BEEN EXPOSED TO CARBON MONOXIDE. COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN V; COMPND 3 CHAIN: A, B, C, D, E, F SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PETROMYZON MARINUS; SOURCE 3 ORGANISM_COMMON: SEA LAMPREY KEYWDS CRYSTALLINE LIGAND TRANSITIONS, HEMOGLOBIN, HEME, LAMPREY EXPDTA X-RAY DIFFRACTION AUTHOR H.A.HEASLET,W.E.ROYER JR. REVDAT 3 01-APR-03 1F5P 1 JRNL REVDAT 2 22-AUG-01 1F5P 1 JRNL REVDAT 1 28-JUN-00 1F5P 0 JRNL AUTH H.A.HEASLET,W.E.ROYER JR. JRNL TITL CRYSTALLINE LIGAND TRANSITIONS IN LAMPREY JRNL TITL 2 HEMOGLOBIN. STRUCTURAL EVIDENCE FOR THE REGULATION JRNL TITL 3 OF OXYGEN AFFINITY. JRNL REF J.BIOL.CHEM. V. 276 26230 2001 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH H.A.HEASLET,W.E.ROYER JR. REMARK 1 TITL THE 2.7 ANGSTROM CRYSTAL STRUCTURE OF REMARK 1 TITL 2 DEOXYGENTATED HEMOGLOBIN FROM THE SEA LAMPREY REMARK 1 TITL 3 (PETROMYZON MARINUS): STRUCTURAL BASIS FOR A REMARK 1 TITL 4 LOWERED OXYGEN AFFINITY AND BOHR EFFECT. REMARK 1 REF STRUCTURE (LONDON) V. 7 517 1999 REMARK 1 REFN ASTM STRUE6 UK ISSN 0969-2126 REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 0.9 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) : 2.90 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) (%) : 75.6 REMARK 3 NUMBER OF REFLECTIONS : 19804 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) : 0.206 REMARK 3 FREE R VALUE : 0.256 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1803 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 : 6884 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 270 REMARK 3 SOLVENT ATOMS : 6 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL 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) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.59 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : 1.06 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 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : 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: SIMULATED ANNEALING, POWELL REMARK 3 MINIMIZATION, GROUP B-FACTOR AND GROUP OCCUPANCY REFINEMENTS REMARK 3 USING TIGHT NON-CRYSTALLOGRAPHIC SYMMETRY RESTRAINTS (WA=200) REMARK 3 ON THE PROTEIN EXCEPT FOR RESIDUE 73. REMARK 4 REMARK 4 1F5P 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 RCSB011274. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-MAR-2000 REMARK 200 TEMPERATURE (KELVIN) : 296.0 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 : RIGAKU IV REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19804 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 75.6 REMARK 200 DATA REDUNDANCY : 3.010 REMARK 200 R MERGE (I) : 0.10900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.4000 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) : 3.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 79.1 REMARK 200 DATA REDUNDANCY IN SHELL : 9.70 REMARK 200 R MERGE FOR SHELL (I) : 0.37600 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 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.23 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 4K, 170MM PHOSPHATE REMARK 280 BUFFER, PH 6.8, SMALL TUBES, TEMPERATURE 296K 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 41.25000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.55000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.10000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.55000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.25000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.10000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 6 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 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 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 BIOMOLECULE: 3 REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 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 NE2 GLN A 110 NE2 GLN C 110 1455 1.95 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 GLN A 63 CD GLN A 63 NE2 -0.077 REMARK 500 MET A 88 SD MET A 88 CE -0.048 REMARK 500 MET A 94 SD MET A 94 CE 0.067 REMARK 500 GLN B 63 CD GLN B 63 NE2 -0.077 REMARK 500 MET B 94 SD MET B 94 CE -0.078 REMARK 500 GLN C 63 CD GLN C 63 NE2 -0.078 REMARK 500 GLN D 63 CD GLN D 63 NE2 -0.075 REMARK 500 GLN E 63 CD GLN E 63 NE2 -0.075 REMARK 500 MET E 88 SD MET E 88 CE -0.084 REMARK 500 GLN F 63 CD GLN F 63 NE2 -0.079 REMARK 500 HIS F 73 CA HIS F 73 C 0.049 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 LYS A 107 N - CA - C ANGL. DEV. = 6.8 DEGREES REMARK 500 LYS B 107 N - CA - C ANGL. DEV. = 7.7 DEGREES REMARK 500 LYS C 107 N - CA - C ANGL. DEV. = 6.9 DEGREES REMARK 500 LYS D 107 N - CA - C ANGL. DEV. = 6.9 DEGREES REMARK 500 LYS F 107 N - CA - C ANGL. DEV. = 7.7 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1F5O RELATED DB: PDB REMARK 900 2.9 ANGSTROM CRYSTAL STRUCTURE OF DEOXYGENATED LAMPREY REMARK 900 HEMOGLOBIN V IN THE SPACE GROUP P2(1)2(1)2(1) REMARK 900 RELATED ID: 3LHB RELATED DB: PDB REMARK 900 2.7 ANGSTROM CRYSTAL STRUCTURE OF DEOXYGENTATED LAMPREY REMARK 900 HEMOGLOBIN V IN THE SPACE GROUP P2(1) WITH TWELVE MONOMERS REMARK 900 IN THE ASSYMETRIC UNIT. REMARK 900 RELATED ID: 2LHB RELATED DB: PDB REMARK 900 REFINEMENT OF A MOLECULAR MODEL FOR LAMPREY HEMOGLOBIN FROM REMARK 900 PETROMYZON MARINUS. DBREF 1F5P A 1 149 UNP P02208 GLB5_PETMA 2 150 DBREF 1F5P B 1 149 UNP P02208 GLB5_PETMA 2 150 DBREF 1F5P C 1 149 UNP P02208 GLB5_PETMA 2 150 DBREF 1F5P D 1 149 UNP P02208 GLB5_PETMA 2 150 DBREF 1F5P E 1 149 UNP P02208 GLB5_PETMA 2 150 DBREF 1F5P F 1 149 UNP P02208 GLB5_PETMA 2 150 SEQADV 1F5P THR A 29 UNP P02208 ASN 30 SEE REMARK 999 SEQADV 1F5P ALA A 86 UNP P02208 VAL 87 SEE REMARK 999 SEQADV 1F5P THR B 29 UNP P02208 ASN 30 SEE REMARK 999 SEQADV 1F5P ALA B 86 UNP P02208 VAL 87 SEE REMARK 999 SEQADV 1F5P THR C 29 UNP P02208 ASN 30 SEE REMARK 999 SEQADV 1F5P ALA C 86 UNP P02208 VAL 87 SEE REMARK 999 SEQADV 1F5P THR D 29 UNP P02208 ASN 30 SEE REMARK 999 SEQADV 1F5P ALA D 86 UNP P02208 VAL 87 SEE REMARK 999 SEQADV 1F5P THR E 29 UNP P02208 ASN 30 SEE REMARK 999 SEQADV 1F5P ALA E 86 UNP P02208 VAL 87 SEE REMARK 999 SEQADV 1F5P THR F 29 UNP P02208 ASN 30 SEE REMARK 999 SEQADV 1F5P ALA F 86 UNP P02208 VAL 87 SEE REMARK 999 SEQRES 1 A 149 PRO ILE VAL ASP THR GLY SER VAL ALA PRO LEU SER ALA SEQRES 2 A 149 ALA GLU LYS THR LYS ILE ARG SER ALA TRP ALA PRO VAL SEQRES 3 A 149 TYR SER THR TYR GLU THR SER GLY VAL ASP ILE LEU VAL SEQRES 4 A 149 LYS PHE PHE THR SER THR PRO ALA ALA GLN GLU PHE PHE SEQRES 5 A 149 PRO LYS PHE LYS GLY LEU THR THR ALA ASP GLN LEU LYS SEQRES 6 A 149 LYS SER ALA ASP VAL ARG TRP HIS ALA GLU ARG ILE ILE SEQRES 7 A 149 ASN ALA VAL ASN ASP ALA VAL ALA SER MET ASP ASP THR SEQRES 8 A 149 GLU LYS MET SER MET LYS LEU ARG ASP LEU SER GLY LYS SEQRES 9 A 149 HIS ALA LYS SER PHE GLN VAL ASP PRO GLN TYR PHE LYS SEQRES 10 A 149 VAL LEU ALA ALA VAL ILE ALA ASP THR VAL ALA ALA GLY SEQRES 11 A 149 ASP ALA GLY PHE GLU LYS LEU MET SER MET ILE CYS ILE SEQRES 12 A 149 LEU LEU ARG SER ALA TYR SEQRES 1 B 149 PRO ILE VAL ASP THR GLY SER VAL ALA PRO LEU SER ALA SEQRES 2 B 149 ALA GLU LYS THR LYS ILE ARG SER ALA TRP ALA PRO VAL SEQRES 3 B 149 TYR SER THR TYR GLU THR SER GLY VAL ASP ILE LEU VAL SEQRES 4 B 149 LYS PHE PHE THR SER THR PRO ALA ALA GLN GLU PHE PHE SEQRES 5 B 149 PRO LYS PHE LYS GLY LEU THR THR ALA ASP GLN LEU LYS SEQRES 6 B 149 LYS SER ALA ASP VAL ARG TRP HIS ALA GLU ARG ILE ILE SEQRES 7 B 149 ASN ALA VAL ASN ASP ALA VAL ALA SER MET ASP ASP THR SEQRES 8 B 149 GLU LYS MET SER MET LYS LEU ARG ASP LEU SER GLY LYS SEQRES 9 B 149 HIS ALA LYS SER PHE GLN VAL ASP PRO GLN TYR PHE LYS SEQRES 10 B 149 VAL LEU ALA ALA VAL ILE ALA ASP THR VAL ALA ALA GLY SEQRES 11 B 149 ASP ALA GLY PHE GLU LYS LEU MET SER MET ILE CYS ILE SEQRES 12 B 149 LEU LEU ARG SER ALA TYR SEQRES 1 C 149 PRO ILE VAL ASP THR GLY SER VAL ALA PRO LEU SER ALA SEQRES 2 C 149 ALA GLU LYS THR LYS ILE ARG SER ALA TRP ALA PRO VAL SEQRES 3 C 149 TYR SER THR TYR GLU THR SER GLY VAL ASP ILE LEU VAL SEQRES 4 C 149 LYS PHE PHE THR SER THR PRO ALA ALA GLN GLU PHE PHE SEQRES 5 C 149 PRO LYS PHE LYS GLY LEU THR THR ALA ASP GLN LEU LYS SEQRES 6 C 149 LYS SER ALA ASP VAL ARG TRP HIS ALA GLU ARG ILE ILE SEQRES 7 C 149 ASN ALA VAL ASN ASP ALA VAL ALA SER MET ASP ASP THR SEQRES 8 C 149 GLU LYS MET SER MET LYS LEU ARG ASP LEU SER GLY LYS SEQRES 9 C 149 HIS ALA LYS SER PHE GLN VAL ASP PRO GLN TYR PHE LYS SEQRES 10 C 149 VAL LEU ALA ALA VAL ILE ALA ASP THR VAL ALA ALA GLY SEQRES 11 C 149 ASP ALA GLY PHE GLU LYS LEU MET SER MET ILE CYS ILE SEQRES 12 C 149 LEU LEU ARG SER ALA TYR SEQRES 1 D 149 PRO ILE VAL ASP THR GLY SER VAL ALA PRO LEU SER ALA SEQRES 2 D 149 ALA GLU LYS THR LYS ILE ARG SER ALA TRP ALA PRO VAL SEQRES 3 D 149 TYR SER THR TYR GLU THR SER GLY VAL ASP ILE LEU VAL SEQRES 4 D 149 LYS PHE PHE THR SER THR PRO ALA ALA GLN GLU PHE PHE SEQRES 5 D 149 PRO LYS PHE LYS GLY LEU THR THR ALA ASP GLN LEU LYS SEQRES 6 D 149 LYS SER ALA ASP VAL ARG TRP HIS ALA GLU ARG ILE ILE SEQRES 7 D 149 ASN ALA VAL ASN ASP ALA VAL ALA SER MET ASP ASP THR SEQRES 8 D 149 GLU LYS MET SER MET LYS LEU ARG ASP LEU SER GLY LYS SEQRES 9 D 149 HIS ALA LYS SER PHE GLN VAL ASP PRO GLN TYR PHE LYS SEQRES 10 D 149 VAL LEU ALA ALA VAL ILE ALA ASP THR VAL ALA ALA GLY SEQRES 11 D 149 ASP ALA GLY PHE GLU LYS LEU MET SER MET ILE CYS ILE SEQRES 12 D 149 LEU LEU ARG SER ALA TYR SEQRES 1 E 149 PRO ILE VAL ASP THR GLY SER VAL ALA PRO LEU SER ALA SEQRES 2 E 149 ALA GLU LYS THR LYS ILE ARG SER ALA TRP ALA PRO VAL SEQRES 3 E 149 TYR SER THR TYR GLU THR SER GLY VAL ASP ILE LEU VAL SEQRES 4 E 149 LYS PHE PHE THR SER THR PRO ALA ALA GLN GLU PHE PHE SEQRES 5 E 149 PRO LYS PHE LYS GLY LEU THR THR ALA ASP GLN LEU LYS SEQRES 6 E 149 LYS SER ALA ASP VAL ARG TRP HIS ALA GLU ARG ILE ILE SEQRES 7 E 149 ASN ALA VAL ASN ASP ALA VAL ALA SER MET ASP ASP THR SEQRES 8 E 149 GLU LYS MET SER MET LYS LEU ARG ASP LEU SER GLY LYS SEQRES 9 E 149 HIS ALA LYS SER PHE GLN VAL ASP PRO GLN TYR PHE LYS SEQRES 10 E 149 VAL LEU ALA ALA VAL ILE ALA ASP THR VAL ALA ALA GLY SEQRES 11 E 149 ASP ALA GLY PHE GLU LYS LEU MET SER MET ILE CYS ILE SEQRES 12 E 149 LEU LEU ARG SER ALA TYR SEQRES 1 F 149 PRO ILE VAL ASP THR GLY SER VAL ALA PRO LEU SER ALA SEQRES 2 F 149 ALA GLU LYS THR LYS ILE ARG SER ALA TRP ALA PRO VAL SEQRES 3 F 149 TYR SER THR TYR GLU THR SER GLY VAL ASP ILE LEU VAL SEQRES 4 F 149 LYS PHE PHE THR SER THR PRO ALA ALA GLN GLU PHE PHE SEQRES 5 F 149 PRO LYS PHE LYS GLY LEU THR THR ALA ASP GLN LEU LYS SEQRES 6 F 149 LYS SER ALA ASP VAL ARG TRP HIS ALA GLU ARG ILE ILE SEQRES 7 F 149 ASN ALA VAL ASN ASP ALA VAL ALA SER MET ASP ASP THR SEQRES 8 F 149 GLU LYS MET SER MET LYS LEU ARG ASP LEU SER GLY LYS SEQRES 9 F 149 HIS ALA LYS SER PHE GLN VAL ASP PRO GLN TYR PHE LYS SEQRES 10 F 149 VAL LEU ALA ALA VAL ILE ALA ASP THR VAL ALA ALA GLY SEQRES 11 F 149 ASP ALA GLY PHE GLU LYS LEU MET SER MET ILE CYS ILE SEQRES 12 F 149 LEU LEU ARG SER ALA TYR HET HEM A 150 43 HET CMO A 151 2 HET HEM B 150 43 HET CMO B 151 2 HET HEM C 150 43 HET CMO C 151 2 HET HEM D 150 43 HET CMO D 151 2 HET HEM E 150 43 HET CMO E 151 2 HET HEM F 150 43 HET CMO F 151 2 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM CMO CARBON MONOXIDE HETSYN HEM HEME FORMUL 7 HEM 6(C34 H32 FE N4 O4) FORMUL 8 CMO 6(C O) FORMUL 19 HOH *6(H2 O) HELIX 1 1 SER A 12 SER A 28 1 17 HELIX 2 2 THR A 29 THR A 45 1 17 HELIX 3 3 PRO A 46 LYS A 56 5 11 HELIX 4 4 THR A 60 LYS A 65 1 6 HELIX 5 5 SER A 67 MET A 88 1 22 HELIX 6 6 ASP A 90 SER A 108 1 19 HELIX 7 7 ASP A 112 GLN A 114 5 3 HELIX 8 8 TYR A 115 ALA A 129 1 15 HELIX 9 9 ASP A 131 ARG A 146 1 16 HELIX 10 10 SER B 12 SER B 28 1 17 HELIX 11 11 THR B 29 THR B 45 1 17 HELIX 12 12 PRO B 46 LYS B 56 5 11 HELIX 13 13 THR B 60 LYS B 65 1 6 HELIX 14 14 SER B 67 MET B 88 1 22 HELIX 15 15 ASP B 90 SER B 108 1 19 HELIX 16 16 ASP B 112 GLN B 114 5 3 HELIX 17 17 TYR B 115 ALA B 129 1 15 HELIX 18 18 ASP B 131 ARG B 146 1 16 HELIX 19 19 SER C 12 SER C 28 1 17 HELIX 20 20 THR C 29 THR C 45 1 17 HELIX 21 21 PRO C 46 LYS C 56 5 11 HELIX 22 22 THR C 60 LYS C 65 1 6 HELIX 23 23 SER C 67 MET C 88 1 22 HELIX 24 24 ASP C 90 SER C 108 1 19 HELIX 25 25 ASP C 112 GLN C 114 5 3 HELIX 26 26 TYR C 115 ALA C 129 1 15 HELIX 27 27 ASP C 131 ARG C 146 1 16 HELIX 28 28 SER D 12 SER D 28 1 17 HELIX 29 29 THR D 29 THR D 45 1 17 HELIX 30 30 PRO D 46 LYS D 56 5 11 HELIX 31 31 THR D 60 LYS D 65 1 6 HELIX 32 32 SER D 67 MET D 88 1 22 HELIX 33 33 ASP D 90 SER D 108 1 19 HELIX 34 34 ASP D 112 GLN D 114 5 3 HELIX 35 35 TYR D 115 ALA D 129 1 15 HELIX 36 36 ASP D 131 ARG D 146 1 16 HELIX 37 37 SER E 12 SER E 28 1 17 HELIX 38 38 THR E 29 THR E 45 1 17 HELIX 39 39 PRO E 46 LYS E 56 5 11 HELIX 40 40 THR E 60 LYS E 65 1 6 HELIX 41 41 SER E 67 SER E 87 1 21 HELIX 42 42 ASP E 90 SER E 108 1 19 HELIX 43 43 ASP E 112 GLN E 114 5 3 HELIX 44 44 TYR E 115 ALA E 129 1 15 HELIX 45 45 ASP E 131 ARG E 146 1 16 HELIX 46 46 SER F 12 SER F 28 1 17 HELIX 47 47 THR F 29 THR F 45 1 17 HELIX 48 48 PRO F 46 LYS F 56 5 11 HELIX 49 49 THR F 60 LYS F 65 1 6 HELIX 50 50 SER F 67 SER F 87 1 21 HELIX 51 51 ASP F 90 SER F 108 1 19 HELIX 52 52 ASP F 112 GLN F 114 5 3 HELIX 53 53 TYR F 115 ALA F 129 1 15 HELIX 54 54 ASP F 131 ARG F 146 1 16 LINK FE HEM A 150 NE2 HIS A 105 LINK FE HEM A 150 C CMO A 151 LINK FE HEM B 150 NE2 HIS B 105 LINK FE HEM B 150 C CMO B 151 LINK FE HEM C 150 NE2 HIS C 105 LINK FE HEM C 150 C CMO C 151 LINK FE HEM D 150 NE2 HIS D 105 LINK FE HEM D 150 C CMO D 151 LINK FE HEM E 150 NE2 HIS E 105 LINK FE HEM E 150 C CMO E 151 LINK FE HEM F 150 NE2 HIS F 105 LINK FE HEM F 150 C CMO F 151 CRYST1 82.500 96.200 145.100 90.00 90.00 90.00 P 21 21 21 24 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 0.012121 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010395 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006892 0.00000