[Scop | Full Entry | Seq (local cached copy) | More Options ]
HEADER OXYGEN STORAGE/TRANSPORT 07-JAN-01 1HV4 TITLE CRYSTAL STRUCTURE ANALYSIS OF BAR-HEAD GOOSE HEMOGLOBIN TITLE 2 (DEOXY FORM) COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN ALPHA-A CHAIN; COMPND 3 CHAIN: A, C, E, G; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: HEMOGLOBIN BETA CHAIN; COMPND 6 CHAIN: B, D, F, H SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ANSER INDICUS; SOURCE 3 ORGANISM_COMMON: BAR-HEADED GOOSE; SOURCE 4 TISSUE: BLOOD; SOURCE 5 CELL: ERYTHROCYTES; SOURCE 6 CELLULAR_LOCATION: CYTOPLASM; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: ANSER INDICUS; SOURCE 9 ORGANISM_COMMON: BAR-HEADED GOOSE; SOURCE 10 TISSUE: BLOOD; SOURCE 11 CELL: ERYTHROCYTES; SOURCE 12 CELLULAR_LOCATION: CYTOPLASM KEYWDS ALLOSTERIC MECHANISM, OXYGEN TRANSPORT, HEME, RESPIRATORY KEYWDS 2 PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR Y.LIANG,Z.HUA,X.LIANG,Q.XU,G.LU REVDAT 2 31-OCT-01 1HV4 1 AUTHOR JRNL REVDAT 1 17-JAN-01 1HV4 0 JRNL AUTH Y.LIANG,Z.HUA,X.LIANG,Q.XU,G.LU JRNL TITL THE CRYSTAL STRUCTURE OF BAR-HEADED GOOSE JRNL TITL 2 HEMOGLOBIN IN DEOXY FORM: THE ALLOSTERIC MECHANISM JRNL TITL 3 OF A HEMOGLOBIN SPECIES WITH HIGH OXYGEN AFFINITY. JRNL REF J.MOL.BIOL. V. 313 123 2001 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 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) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.89 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 63263.600 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.0 REMARK 3 NUMBER OF REFLECTIONS : 27148 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) : 0.197 REMARK 3 FREE R VALUE : 0.243 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2752 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005 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) : 2.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 68.00 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3268 REMARK 3 BIN R VALUE (WORKING SET) : 0.2850 REMARK 3 BIN FREE R VALUE : 0.3290 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.60 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 389 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 8944 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 344 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 28.40 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.70 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.95000 REMARK 3 B22 (A**2) : -5.21000 REMARK 3 B33 (A**2) : 6.16000 REMARK 3 B12 (A**2) : 1.41000 REMARK 3 B13 (A**2) : -2.33000 REMARK 3 B23 (A**2) : -0.53000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30 REMARK 3 ESD FROM SIGMAA (A) : 0.44 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) : 0.38 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.55 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.014 REMARK 3 BOND ANGLES (DEGREES) : 1.60 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.80 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.25 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED 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 : 0.30 REMARK 3 BSOL : 30.63 REMARK 3 REMARK 3 NCS MODEL : CONSTR 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.PARAM REMARK 3 PARAMETER FILE 2 : PARAM19X.HEME-USE REMARK 3 PARAMETER FILE 3 : PARAM19.SOL REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : TOPH19X.HEME-USE REMARK 3 TOPOLOGY FILE 3 : TOPH19.SOL REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1HV4 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 RCSB012606. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-MAY-1995 REMARK 200 TEMPERATURE (KELVIN) : 291.0 REMARK 200 PH : 7.20 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 RU300 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 : SIMENS X-200 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IPC REMARK 200 DATA SCALING SOFTWARE : XENGEN REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30654 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.570 REMARK 200 RESOLUTION RANGE LOW (A) : 36.890 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 67.4 REMARK 200 DATA REDUNDANCY : 1.900 REMARK 200 R MERGE (I) : 0.06100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.57 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.73 REMARK 200 COMPLETENESS FOR SHELL (%) : 24.0 REMARK 200 DATA REDUNDANCY IN SHELL : 1.14 REMARK 200 R MERGE FOR SHELL (I) : 0.14600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 4.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: PDB ENTRY 1A4F REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.99 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, POTASSIUM PHOSPHATE , PH REMARK 280 7.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 8 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 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H 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 IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI REMARK 500 O ALA D 142 N LYS D 144 2.06 REMARK 500 O ALA F 142 N LYS F 144 2.06 REMARK 500 O ALA H 142 N LYS H 144 2.07 REMARK 500 O ALA B 142 N LYS B 144 2.08 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 CYS A 130 CB CYS A 130 SG 0.056 REMARK 500 MET B 59 SD MET B 59 CE 0.078 REMARK 500 MET C 32 SD MET C 32 CE -0.081 REMARK 500 CYS C 130 CB CYS C 130 SG 0.075 REMARK 500 CYS E 130 CB CYS E 130 SG 0.065 REMARK 500 MET F 59 SD MET F 59 CE 0.092 REMARK 500 CYS G 130 CB CYS G 130 SG 0.073 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. = -9.8 DEGREES REMARK 500 THR A 137 N - CA - C ANGL. DEV. = -8.0 DEGREES REMARK 500 VAL B 18 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 ASN B 19 N - CA - C ANGL. DEV. = -8.1 DEGREES REMARK 500 LEU B 48 N - CA - C ANGL. DEV. =-10.6 DEGREES REMARK 500 ASP C 47 N - CA - C ANGL. DEV. = -9.5 DEGREES REMARK 500 THR C 137 N - CA - C ANGL. DEV. = -8.0 DEGREES REMARK 500 VAL D 18 N - CA - C ANGL. DEV. = 8.2 DEGREES REMARK 500 LEU D 48 N - CA - C ANGL. DEV. =-10.3 DEGREES REMARK 500 ASP E 47 N - CA - C ANGL. DEV. = -9.6 DEGREES REMARK 500 VAL F 18 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 LEU F 48 N - CA - C ANGL. DEV. =-10.6 DEGREES REMARK 500 ASP G 47 N - CA - C ANGL. DEV. = -9.5 DEGREES REMARK 500 THR G 137 N - CA - C ANGL. DEV. = -8.1 DEGREES REMARK 500 VAL H 18 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 LEU H 48 N - CA - C ANGL. DEV. =-10.1 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1A4F RELATED DB: PDB REMARK 900 BAR-HEADED GOOSE HB (OXY FORM) REMARK 900 RELATED ID: 1C40 RELATED DB: PDB REMARK 900 BAR-HEADED GOOSE HB (AQUOMET FORM) DBREF 1HV4 A 1 141 UNP P01990 HBA_ANSIN 1 141 DBREF 1HV4 C 1 141 UNP P01990 HBA_ANSIN 1 141 DBREF 1HV4 E 1 141 UNP P01990 HBA_ANSIN 1 141 DBREF 1HV4 G 1 141 UNP P01990 HBA_ANSIN 1 141 DBREF 1HV4 B 1 146 UNP P02118 HBB_ANSIN 1 146 DBREF 1HV4 D 1 146 UNP P02118 HBB_ANSIN 1 146 DBREF 1HV4 F 1 146 UNP P02118 HBB_ANSIN 1 146 DBREF 1HV4 H 1 146 UNP P02118 HBB_ANSIN 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 SER 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 VAL 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 ALA 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 ASP 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 SER 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 VAL 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 ALA 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 ASP 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 SEQRES 1 E 141 VAL LEU SER ALA ALA ASP LYS THR ASN VAL LYS GLY VAL SEQRES 2 E 141 PHE SER LYS ILE SER GLY HIS ALA GLU GLU TYR GLY ALA SEQRES 3 E 141 GLU THR LEU GLU ARG MET PHE THR ALA TYR PRO GLN THR SEQRES 4 E 141 LYS THR TYR PHE PRO HIS PHE ASP LEU GLN HIS GLY SER SEQRES 5 E 141 ALA GLN ILE LYS ALA HIS GLY LYS LYS VAL VAL ALA ALA SEQRES 6 E 141 LEU VAL GLU ALA VAL ASN HIS ILE ASP ASP ILE ALA GLY SEQRES 7 E 141 ALA LEU SER LYS LEU SER ASP LEU HIS ALA GLN LYS LEU SEQRES 8 E 141 ARG VAL ASP PRO VAL ASN PHE LYS PHE LEU GLY HIS CYS SEQRES 9 E 141 PHE LEU VAL VAL VAL ALA ILE HIS HIS PRO SER ALA LEU SEQRES 10 E 141 THR ALA GLU VAL HIS ALA SER LEU ASP LYS PHE LEU CYS SEQRES 11 E 141 ALA VAL GLY THR VAL LEU THR ALA LYS TYR ARG SEQRES 1 F 146 VAL HIS TRP SER ALA GLU GLU LYS GLN LEU ILE THR GLY SEQRES 2 F 146 LEU TRP GLY LYS VAL ASN VAL ALA ASP CYS GLY ALA GLU SEQRES 3 F 146 ALA LEU ALA ARG LEU LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 F 146 ARG PHE PHE SER SER PHE GLY ASN LEU SER SER PRO THR SEQRES 5 F 146 ALA ILE LEU GLY ASN PRO MET VAL ARG ALA HIS GLY LYS SEQRES 6 F 146 LYS VAL LEU THR SER PHE GLY ASP ALA VAL LYS ASN LEU SEQRES 7 F 146 ASP ASN ILE LYS ASN THR PHE ALA GLN LEU SER GLU LEU SEQRES 8 F 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG SEQRES 9 F 146 LEU LEU GLY ASP ILE LEU ILE ILE VAL LEU ALA ALA HIS SEQRES 10 F 146 PHE ALA LYS GLU PHE THR PRO ASP CYS GLN ALA ALA TRP SEQRES 11 F 146 GLN LYS LEU VAL ARG VAL VAL ALA HIS ALA LEU ALA ARG SEQRES 12 F 146 LYS TYR HIS SEQRES 1 G 141 VAL LEU SER ALA ALA ASP LYS THR ASN VAL LYS GLY VAL SEQRES 2 G 141 PHE SER LYS ILE SER GLY HIS ALA GLU GLU TYR GLY ALA SEQRES 3 G 141 GLU THR LEU GLU ARG MET PHE THR ALA TYR PRO GLN THR SEQRES 4 G 141 LYS THR TYR PHE PRO HIS PHE ASP LEU GLN HIS GLY SER SEQRES 5 G 141 ALA GLN ILE LYS ALA HIS GLY LYS LYS VAL VAL ALA ALA SEQRES 6 G 141 LEU VAL GLU ALA VAL ASN HIS ILE ASP ASP ILE ALA GLY SEQRES 7 G 141 ALA LEU SER LYS LEU SER ASP LEU HIS ALA GLN LYS LEU SEQRES 8 G 141 ARG VAL ASP PRO VAL ASN PHE LYS PHE LEU GLY HIS CYS SEQRES 9 G 141 PHE LEU VAL VAL VAL ALA ILE HIS HIS PRO SER ALA LEU SEQRES 10 G 141 THR ALA GLU VAL HIS ALA SER LEU ASP LYS PHE LEU CYS SEQRES 11 G 141 ALA VAL GLY THR VAL LEU THR ALA LYS TYR ARG SEQRES 1 H 146 VAL HIS TRP SER ALA GLU GLU LYS GLN LEU ILE THR GLY SEQRES 2 H 146 LEU TRP GLY LYS VAL ASN VAL ALA ASP CYS GLY ALA GLU SEQRES 3 H 146 ALA LEU ALA ARG LEU LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 H 146 ARG PHE PHE SER SER PHE GLY ASN LEU SER SER PRO THR SEQRES 5 H 146 ALA ILE LEU GLY ASN PRO MET VAL ARG ALA HIS GLY LYS SEQRES 6 H 146 LYS VAL LEU THR SER PHE GLY ASP ALA VAL LYS ASN LEU SEQRES 7 H 146 ASP ASN ILE LYS ASN THR PHE ALA GLN LEU SER GLU LEU SEQRES 8 H 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG SEQRES 9 H 146 LEU LEU GLY ASP ILE LEU ILE ILE VAL LEU ALA ALA HIS SEQRES 10 H 146 PHE ALA LYS GLU PHE THR PRO ASP CYS GLN ALA ALA TRP SEQRES 11 H 146 GLN LYS LEU VAL ARG VAL VAL ALA HIS ALA LEU ALA ARG SEQRES 12 H 146 LYS TYR HIS HET HEM 151 43 HET HEM 152 43 HET HEM 153 43 HET HEM 154 43 HET HEM 155 43 HET HEM 156 43 HET HEM 157 43 HET HEM 158 43 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 9 HEM 8(C34 H32 FE N4 O4) HELIX 1 1 SER A 3 SER A 18 1 16 HELIX 2 2 HIS A 20 TYR 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 GLN A 89 1 10 HELIX 7 7 ASP A 94 HIS A 113 1 20 HELIX 8 8 THR A 118 ALA A 138 1 21 HELIX 9 9 LYS A 139 ARG A 141 5 3 HELIX 10 10 SER B 4 VAL B 18 1 15 HELIX 11 11 ASN B 19 TYR B 35 1 17 HELIX 12 12 PRO B 36 SER B 43 5 8 HELIX 13 13 PHE B 42 GLY B 46 5 5 HELIX 14 14 SER B 50 ASN B 57 1 8 HELIX 15 15 ASN B 57 ASN B 77 1 21 HELIX 16 16 ASN B 80 ASP B 94 1 15 HELIX 17 17 ASP B 99 PHE B 118 1 20 HELIX 18 18 ALA B 119 PHE B 122 5 4 HELIX 19 19 THR B 123 ARG B 143 1 21 HELIX 20 20 SER C 3 SER C 18 1 16 HELIX 21 21 HIS C 20 TYR C 36 1 17 HELIX 22 22 PRO C 37 PHE C 43 5 7 HELIX 23 23 SER C 52 HIS C 72 1 21 HELIX 24 24 ASP C 75 SER C 81 1 7 HELIX 25 25 LEU C 80 GLN C 89 1 10 HELIX 26 26 ASP C 94 HIS C 113 1 20 HELIX 27 27 THR C 118 ALA C 138 1 21 HELIX 28 28 LYS C 139 ARG C 141 5 3 HELIX 29 29 SER D 4 VAL D 18 1 15 HELIX 30 30 ASN D 19 TYR D 35 1 17 HELIX 31 31 PRO D 36 SER D 43 5 8 HELIX 32 32 PHE D 42 GLY D 46 5 5 HELIX 33 33 SER D 50 ASN D 57 1 8 HELIX 34 34 ASN D 57 ASN D 77 1 21 HELIX 35 35 ASN D 80 ASP D 94 1 15 HELIX 36 36 ASP D 99 PHE D 118 1 20 HELIX 37 37 ALA D 119 PHE D 122 5 4 HELIX 38 38 THR D 123 ARG D 143 1 21 HELIX 39 39 SER E 3 SER E 18 1 16 HELIX 40 40 HIS E 20 TYR E 36 1 17 HELIX 41 41 PRO E 37 PHE E 43 5 7 HELIX 42 42 SER E 52 HIS E 72 1 21 HELIX 43 43 ASP E 75 SER E 81 1 7 HELIX 44 44 LEU E 80 GLN E 89 1 10 HELIX 45 45 PRO E 95 HIS E 113 1 19 HELIX 46 46 THR E 118 ALA E 138 1 21 HELIX 47 47 LYS E 139 ARG E 141 5 3 HELIX 48 48 SER F 4 VAL F 18 1 15 HELIX 49 49 ASN F 19 TYR F 35 1 17 HELIX 50 50 PRO F 36 SER F 43 5 8 HELIX 51 51 PHE F 42 GLY F 46 5 5 HELIX 52 52 SER F 50 ASN F 57 1 8 HELIX 53 53 ASN F 57 ASN F 77 1 21 HELIX 54 54 ASN F 80 ASP F 94 1 15 HELIX 55 55 ASP F 99 PHE F 118 1 20 HELIX 56 56 ALA F 119 PHE F 122 5 4 HELIX 57 57 THR F 123 ARG F 143 1 21 HELIX 58 58 SER G 3 SER G 18 1 16 HELIX 59 59 HIS G 20 TYR G 36 1 17 HELIX 60 60 PRO G 37 PHE G 43 5 7 HELIX 61 61 SER G 52 HIS G 72 1 21 HELIX 62 62 ASP G 75 SER G 81 1 7 HELIX 63 63 LEU G 80 GLN G 89 1 10 HELIX 64 64 ASP G 94 HIS G 113 1 20 HELIX 65 65 THR G 118 ALA G 138 1 21 HELIX 66 66 LYS G 139 ARG G 141 5 3 HELIX 67 67 SER H 4 VAL H 18 1 15 HELIX 68 68 ASN H 19 TYR H 35 1 17 HELIX 69 69 PRO H 36 SER H 43 5 8 HELIX 70 70 PHE H 42 GLY H 46 5 5 HELIX 71 71 SER H 50 ASN H 57 1 8 HELIX 72 72 ASN H 57 ASN H 77 1 21 HELIX 73 73 ASN H 80 ASP H 94 1 15 HELIX 74 74 ASP H 99 PHE H 118 1 20 HELIX 75 75 ALA H 119 PHE H 122 5 4 HELIX 76 76 THR H 123 ARG H 143 1 21 CRYST1 70.660 94.100 59.230 71.55 65.10 83.10 P 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 0.014152 -0.001713 -0.006347 0.00000 SCALE2 0.000000 0.010705 -0.003308 0.00000 SCALE3 0.000000 0.000000 0.019482 0.00000