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HEADER OXYGEN STORAGE/TRANSPORT 27-FEB-04 1SI4 TITLE CRYSTAL STRUCTURE OF HUMAN HEMOGLOBIN A2 (IN R2 STATE) AT TITLE 2 2.2 A RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN ALPHA CHAIN; COMPND 3 CHAIN: A, C; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: HEMOGLOBIN DELTA CHAIN; COMPND 6 CHAIN: B, D SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 TISSUE: BETA THALASSEMIA MINOR BLOOD; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 7 ORGANISM_COMMON: HUMAN; SOURCE 8 TISSUE: BETA THALASSEMIA MINOR BLOOD KEYWDS HEMOGLOBIN A2, BETA THALASSEMIA, OXYGEN TRANSPORT, KEYWDS 2 ANTISICKLING EFFECT EXPDTA X-RAY DIFFRACTION AUTHOR U.SEN,J.DASGUPTA,D.CHOUDHURY,P.DATTA,A.CHAKRABARTI, AUTHOR 2 S.B.CHAKRABARTY,A.CHAKRABARTY,J.K.DATTAGUPTA REVDAT 1 26-OCT-04 1SI4 0 JRNL AUTH U.SEN,J.DASGUPTA,D.CHOUDHURY,P.DATTA,A.CHAKRABARTI, JRNL AUTH 2 S.B.CHAKRABARTY,A.CHAKRABARTY,J.K.DATTAGUPTA JRNL TITL CRYSTAL STRUCTURES OF HBA2 AND HBE AND MODELING OF JRNL TITL 2 HEMOGLOBIN DELTA4: INTERPRETATION OF THE THERMAL JRNL TITL 3 STABILITY AND THE ANTISICKLING EFFECT OF HBA2 AND JRNL TITL 4 IDENTIFICATION OF THE FERROCYANIDE BINDING SITE IN JRNL TITL 5 HB. JRNL REF BIOCHEMISTRY V. 43 12477 2004 JRNL REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.DASGUPTA,U.SEN,D.CHOUDHURY,P.DATTA,A.CHAKRABARTI, REMARK 1 AUTH 2 S.B.CHAKRABARTY,A.CHAKRABARTY,J.K.DATTAGUPTA REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY STRUCTURAL REMARK 1 TITL 2 STUDIES OF HEMOGLOBIN A2 AND HEMOGLOBIN E, REMARK 1 TITL 3 ISOLATED FROM THE BLOOD SAMPLES OF REMARK 1 TITL 4 BETA-THALASSEMIC PATIENTS REMARK 1 REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 303 619 2003 REMARK 1 REFN ASTM BBRCA9 US ISSN 0006-291X REMARK 2 REMARK 2 RESOLUTION. 2.20 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.96 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2074348.930 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.9 REMARK 3 NUMBER OF REFLECTIONS : 28343 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) : 0.218 REMARK 3 FREE R VALUE : 0.258 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1452 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) : 2.20 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.40 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4479 REMARK 3 BIN R VALUE (WORKING SET) : 0.3160 REMARK 3 BIN FREE R VALUE : 0.3450 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 239 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 : 4379 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 180 REMARK 3 SOLVENT ATOMS : 663 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 24.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.60 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -8.91000 REMARK 3 B22 (A**2) : 10.92000 REMARK 3 B33 (A**2) : -2.00000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28 REMARK 3 ESD FROM SIGMAA (A) : 0.33 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) : 0.35 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.41 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.40 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.70 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.98 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) : 3.700 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.810 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 4.550 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.810 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.29 REMARK 3 BSOL : 55.00 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.PARAM REMARK 3 PARAMETER FILE 2 : HEM.PARAM REMARK 3 PARAMETER FILE 3 : ION.PARAM REMARK 3 PARAMETER FILE 4 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 5 : CN.PARAM REMARK 3 PARAMETER FILE 6 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : HEM.TOP REMARK 3 TOPOLOGY FILE 3 : ION.TOP REMARK 3 TOPOLOGY FILE 4 : WATER_REP.TOP REMARK 3 TOPOLOGY FILE 5 : CN.TOP REMARK 3 TOPOLOGY FILE 6 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1SI4 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 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB021727. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-MAY-2003 REMARK 200 TEMPERATURE (KELVIN) : 100.0 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 : GRAPHITE REMARK 200 OPTICS : OSMIC 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 : 28343 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 REMARK 200 RESOLUTION RANGE LOW (A) : 15.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.06900 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) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: PDB CODE: 1SHR REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 45.12 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, GLYCEROL, PH 8.5, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K 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 30.22500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.29750 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.09300 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.29750 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.22500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.09300 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 56 CG CD CE NZ REMARK 470 LYS B 8 CG CD CE NZ REMARK 470 SER D 86 OG 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 OE1 GLU D 90 NZ LYS D 144 2.09 REMARK 500 NE2 HIS A 72 O HOH 1228 2.11 REMARK 500 OD1 ASP C 75 ND2 ASN C 78 2.15 REMARK 500 O HOH 1209 O HOH 1635 2.15 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 ARG A 92 CB ARG A 92 CG 0.076 REMARK 500 ARG A 92 CG ARG A 92 CD 0.068 REMARK 500 GLN B 87 CA GLN B 87 CB 0.063 REMARK 500 ALA C 63 CA ALA C 63 CB -0.057 REMARK 500 MET C 76 SD MET C 76 CE -0.055 REMARK 500 HIS D 2 CA HIS D 2 C -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. = -9.9 DEGREES REMARK 500 ARG A 92 CB - CG - CD ANGL. DEV. = 9.7 DEGREES REMARK 500 ASP B 94 N - CA - C ANGL. DEV. = 9.7 DEGREES REMARK 500 PHE B 118 N - CA - C ANGL. DEV. = 8.8 DEGREES REMARK 500 GLY B 119 N - CA - C ANGL. DEV. = 10.2 DEGREES REMARK 500 ALA C 13 N - CA - C ANGL. DEV. = 9.0 DEGREES REMARK 500 GLU C 23 N - CA - C ANGL. DEV. =-17.6 DEGREES REMARK 500 PRO C 37 N - CA - C ANGL. DEV. = 9.0 DEGREES REMARK 500 ASP C 47 N - CA - C ANGL. DEV. =-10.2 DEGREES REMARK 500 LEU D 3 N - CA - C ANGL. DEV. =-12.0 DEGREES REMARK 500 GLY D 119 N - CA - C ANGL. DEV. = 9.0 DEGREES 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 1004 DISTANCE = 5.02 ANGSTROMS REMARK 525 HOH 1131 DISTANCE = 5.57 ANGSTROMS REMARK 525 HOH 1196 DISTANCE = 6.57 ANGSTROMS REMARK 525 HOH 1210 DISTANCE = 5.24 ANGSTROMS REMARK 525 HOH 1243 DISTANCE = 5.05 ANGSTROMS REMARK 525 HOH 1304 DISTANCE = 6.49 ANGSTROMS REMARK 525 HOH 1385 DISTANCE = 7.21 ANGSTROMS REMARK 525 HOH 1469 DISTANCE = 5.16 ANGSTROMS REMARK 525 HOH 1483 DISTANCE = 8.17 ANGSTROMS REMARK 525 HOH 1488 DISTANCE = 6.26 ANGSTROMS REMARK 525 HOH 1491 DISTANCE = 7.84 ANGSTROMS REMARK 525 HOH 1494 DISTANCE = 6.31 ANGSTROMS REMARK 525 HOH 1512 DISTANCE = 6.89 ANGSTROMS REMARK 525 HOH 1530 DISTANCE = 7.11 ANGSTROMS REMARK 525 HOH 1533 DISTANCE = 7.62 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1SHR RELATED DB: PDB REMARK 900 FERROCYANIDE BOUND HEMOGLOBIN A2 AT 1.88A RESOLUTION DBREF 1SI4 A 1 141 UNP P69905 HBA_HUMAN 1 141 DBREF 1SI4 B 1 146 UNP P02042 HBD_HUMAN 1 146 DBREF 1SI4 C 1 141 UNP P69905 HBA_HUMAN 1 141 DBREF 1SI4 D 1 146 UNP P02042 HBD_HUMAN 1 146 SEQRES 1 A 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA SEQRES 2 A 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY 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 LYS LYS VAL ALA ASP ALA SEQRES 6 A 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN SEQRES 7 A 141 ALA LEU SER ALA 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 CYS SEQRES 9 A 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE SEQRES 10 A 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA SEQRES 11 A 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG SEQRES 1 B 146 VAL HIS LEU THR PRO GLU GLU LYS THR ALA VAL ASN ALA SEQRES 2 B 146 LEU TRP GLY LYS VAL ASN VAL ASP ALA VAL GLY GLY GLU SEQRES 3 B 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN SEQRES 4 B 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER SER PRO ASP SEQRES 5 B 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS SEQRES 6 B 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU SEQRES 7 B 146 ASP ASN LEU LYS GLY THR PHE SER 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 ASN VAL LEU VAL CYS VAL LEU ALA ARG ASN SEQRES 10 B 146 PHE GLY LYS GLU PHE THR PRO GLN MET GLN ALA ALA TYR SEQRES 11 B 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS SEQRES 12 B 146 LYS TYR HIS SEQRES 1 C 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA SEQRES 2 C 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY 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 LYS LYS VAL ALA ASP ALA SEQRES 6 C 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN SEQRES 7 C 141 ALA LEU SER ALA 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 CYS SEQRES 9 C 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE SEQRES 10 C 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA SEQRES 11 C 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG SEQRES 1 D 146 VAL HIS LEU THR PRO GLU GLU LYS THR ALA VAL ASN ALA SEQRES 2 D 146 LEU TRP GLY LYS VAL ASN VAL ASP ALA VAL GLY GLY GLU SEQRES 3 D 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN SEQRES 4 D 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER SER PRO ASP SEQRES 5 D 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS SEQRES 6 D 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU SEQRES 7 D 146 ASP ASN LEU LYS GLY THR PHE SER 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 ASN VAL LEU VAL CYS VAL LEU ALA ARG ASN SEQRES 10 D 146 PHE GLY LYS GLU PHE THR PRO GLN MET GLN ALA ALA TYR SEQRES 11 D 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS SEQRES 12 D 146 LYS TYR HIS HET CYN A 143 2 HET CYN B 148 2 HET CYN C 143 2 HET CYN D 148 2 HET HEM A 142 43 HET HEM B 147 43 HET HEM C 142 43 HET HEM D 147 43 HETNAM CYN CYANIDE ION HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 5 CYN 4(C N 1-) FORMUL 9 HEM 4(C34 H32 FE N4 O4) FORMUL 13 HOH *663(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 LYS A 90 1 16 HELIX 6 6 PRO A 95 LEU A 113 1 19 HELIX 7 7 THR A 118 THR A 137 1 20 HELIX 8 8 THR B 4 GLY B 16 1 13 HELIX 9 9 ALA B 22 TYR B 35 1 14 HELIX 10 10 PRO B 36 GLU B 43 5 8 HELIX 11 11 SER B 50 ASN B 57 1 8 HELIX 12 12 ASN B 57 ALA B 76 1 20 HELIX 13 13 ASN B 80 PHE B 85 1 6 HELIX 14 14 PHE B 85 LYS B 95 1 11 HELIX 15 15 PRO B 100 GLY B 119 1 20 HELIX 16 16 LYS B 120 PHE B 122 5 3 HELIX 17 17 THR B 123 HIS B 143 1 21 HELIX 18 18 LYS B 144 HIS B 146 5 3 HELIX 19 19 SER C 3 TRP C 14 1 12 HELIX 20 20 GLU C 23 PHE C 36 1 14 HELIX 21 21 PRO C 37 PHE C 43 5 7 HELIX 22 22 SER C 52 HIS C 72 1 21 HELIX 23 23 ASP C 75 LEU C 80 1 6 HELIX 24 24 LEU C 80 ALA C 88 1 9 HELIX 25 25 PRO C 95 LEU C 113 1 19 HELIX 26 26 THR C 118 SER C 138 1 21 HELIX 27 27 THR D 4 GLY D 16 1 13 HELIX 28 28 ALA D 22 TYR D 35 1 14 HELIX 29 29 PRO D 36 GLU D 43 5 8 HELIX 30 30 SER D 50 ASN D 57 1 8 HELIX 31 31 ASN D 57 ALA D 76 1 20 HELIX 32 32 ASN D 80 PHE D 85 1 6 HELIX 33 33 PHE D 85 LYS D 95 1 11 HELIX 34 34 PRO D 100 GLY D 119 1 20 HELIX 35 35 LYS D 120 PHE D 122 5 3 HELIX 36 36 THR D 123 ALA D 142 1 20 LINK FE HEM A 142 NE2 HIS A 87 LINK FE HEM B 147 NE2 HIS B 92 LINK FE HEM C 142 NE2 HIS C 87 LINK FE HEM D 147 NE2 HIS D 92 LINK FE HEM A 142 C CYN A 143 LINK FE HEM B 147 C CYN B 148 LINK FE HEM C 142 C CYN C 143 LINK FE HEM D 147 C CYN D 148 CRYST1 60.450 88.186 104.595 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 0.016543 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011340 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009561 0.00000