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HEADER OXYGEN STORAGE/TRANSPORT 17-JUN-01 1JEB TITLE CHIMERIC HUMAN/MOUSE CARBONMONOXY HEMOGLOBIN (HUMAN ZETA2 / TITLE 2 MOUSE BETA2) COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN ZETA CHAIN; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEMOGLOBIN BETA-SINGLE CHAIN; COMPND 7 CHAIN: B, D; COMPND 8 SYNONYM: B SINGLE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 GENE: HBZ; SOURCE 5 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: MOUSE; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BALB/C; SOURCE 8 OTHER_DETAILS: TRANSGENIC-KNOCKOUT MOUSE EXPRESSING SOURCE 9 CHIMERIC HUMAN ZETA / MOUSE BETA-SINGLE HEMOGLOBIN; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 12 ORGANISM_COMMON: MOUSE; SOURCE 13 OTHER_DETAILS: TRANSGENIC-KNOCKOUT MOUSE EXPRESSING SOURCE 14 CHIMERIC HUMAN ZETA / MOUSE BETA-SINGLE HEMOGLOBIN KEYWDS OXYGEN TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR R.D.KIDD,J.E.RUSSELL,N.J.WATMOUGH,E.N.BAKER,T.BRITTAIN REVDAT 2 01-APR-03 1JEB 1 JRNL REVDAT 1 23-JAN-02 1JEB 0 JRNL AUTH R.D.KIDD,J.E.RUSSELL,N.J.WATMOUGH,E.N.BAKER, JRNL AUTH 2 T.BRITTAIN JRNL TITL THE ROLE OF BETA CHAINS IN THE CONTROL OF THE JRNL TITL 2 HEMOGLOBIN OXYGEN BINDING FUNCTION: CHIMERIC JRNL TITL 3 HUMAN/MOUSE PROTEINS, STRUCTURE, AND FUNCTION. JRNL REF BIOCHEMISTRY V. 40 15669 2001 JRNL REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 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) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00 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) (%) : 95.3 REMARK 3 NUMBER OF REFLECTIONS : 41201 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) : 0.216 REMARK 3 FREE R VALUE : 0.249 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100 REMARK 3 FREE R VALUE TEST SET COUNT : 4162 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) : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.80 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5704 REMARK 3 BIN R VALUE (WORKING SET) : 0.3790 REMARK 3 BIN FREE R VALUE : 0.3950 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.50 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 671 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4374 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 180 REMARK 3 SOLVENT ATOMS : 234 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 23.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.10 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 4.04000 REMARK 3 B22 (A**2) : 4.04000 REMARK 3 B33 (A**2) : -8.08000 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) : 0.38 REMARK 3 ESD FROM SIGMAA (A) : 0.40 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) : 0.42 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.43 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 1.20 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 16.20 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.08 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC 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 : 39.53 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_XPLOR.PAR REMARK 3 PARAMETER FILE 3 : CMO_XPLOR.PAR REMARK 3 PARAMETER FILE 4 : ACE_XPLOR.PAR REMARK 3 PARAMETER FILE 5 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 6 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : HEM_XPLOR.TOP REMARK 3 TOPOLOGY FILE 3 : CMO_XPLOR.TOP REMARK 3 TOPOLOGY FILE 4 : ACE_XPLOR.TOP REMARK 3 TOPOLOGY FILE 5 : WATER_REP.TOP REMARK 3 TOPOLOGY FILE 6 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1JEB 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 RCSB. REMARK 100 THE RCSB ID CODE IS RCSB013676. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-FEB-2001 REMARK 200 TEMPERATURE (KELVIN) : 110.0 REMARK 200 PH : 8.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL9-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.00 REMARK 200 MONOCHROMATOR : SI 111 CHANNEL REMARK 200 OPTICS : MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ADSC, DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43348 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 4.400 REMARK 200 R MERGE (I) : 0.05300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 3.90 REMARK 200 R MERGE FOR SHELL (I) : 0.46500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: CNS REMARK 200 STARTING MODEL: PDB ENTRY 1BBB REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: BICINE/NAOH, MEPEG 550, PH 8.5, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,1/2+Z REMARK 290 3555 -Y,X,1/4+Z REMARK 290 4555 Y,-X,3/4+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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.26150 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 26.13075 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 78.39225 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 LYS B 144 REMARK 465 TYR B 145 REMARK 465 HIS B 146 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 OH TYR D 41 O HOH 219 2.18 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 MET C 13 SD MET C 13 CE 0.040 REMARK 500 ALA C 123 CA ALA C 123 CB 0.039 REMARK 500 HIS D 146 CB HIS D 146 CG 0.043 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. =-11.9 DEGREES REMARK 500 THR B 4 N - CA - C ANGL. DEV. = -6.3 DEGREES REMARK 500 PRO B 36 N - CA - C ANGL. DEV. = 7.4 DEGREES REMARK 500 ASP B 94 N - CA - C ANGL. DEV. = 6.7 DEGREES REMARK 500 ASP C 47 N - CA - C ANGL. DEV. =-12.1 DEGREES REMARK 500 LEU C 83 N - CA - C ANGL. DEV. = 6.6 DEGREES REMARK 500 ASN D 19 N - CA - C ANGL. DEV. = -9.2 DEGREES REMARK 500 TYR D 35 N - CA - C ANGL. DEV. = -7.8 DEGREES REMARK 500 PRO D 36 N - CA - C ANGL. DEV. = 7.8 DEGREES REMARK 500 LYS D 95 N - CA - C ANGL. DEV. = 6.4 DEGREES REMARK 500 LEU D 118 N - CA - C ANGL. DEV. = 7.3 DEGREES REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 TYR D 145 -117.78 78.19 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 230 DISTANCE = 5.53 ANGSTROMS REMARK 525 HOH 340 DISTANCE = 6.04 ANGSTROMS REMARK 525 HOH 405 DISTANCE = 5.69 ANGSTROMS REMARK 525 HOH 427 DISTANCE = 6.34 ANGSTROMS DBREF 1JEB A 1 141 UNP P02008 HBAZ_HUMAN 1 141 DBREF 1JEB C 1 141 UNP P02008 HBAZ_HUMAN 1 141 DBREF 1JEB B 1 146 UNP P02088 HBB1_MOUSE 1 146 DBREF 1JEB D 1 146 UNP P02088 HBB1_MOUSE 1 146 SEQRES 1 A 141 SER LEU THR LYS THR GLU ARG THR ILE ILE VAL SER MET SEQRES 2 A 141 TRP ALA LYS ILE SER THR GLN ALA ASP THR ILE GLY THR SEQRES 3 A 141 GLU THR LEU GLU ARG LEU PHE LEU SER HIS PRO GLN THR SEQRES 4 A 141 LYS THR TYR PHE PRO HIS PHE ASP LEU HIS PRO GLY SER SEQRES 5 A 141 ALA GLN LEU ARG ALA HIS GLY SER LYS VAL VAL ALA ALA SEQRES 6 A 141 VAL GLY ASP ALA VAL LYS SER ILE ASP ASP ILE GLY GLY SEQRES 7 A 141 ALA LEU SER LYS LEU SER GLU LEU HIS ALA TYR ILE 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 ARG PHE PRO ALA ASP PHE SEQRES 10 A 141 THR ALA GLU ALA HIS ALA ALA TRP ASP LYS PHE LEU SER SEQRES 11 A 141 VAL VAL SER SER VAL LEU THR GLU LYS TYR ARG SEQRES 1 B 146 VAL HIS LEU THR ASP ALA GLU LYS ALA ALA VAL SER GLY SEQRES 2 B 146 LEU TRP GLY LYS VAL ASN ALA ASP GLU 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 TYR PHE ASP SER PHE GLY ASP LEU SER SER ALA SER SEQRES 5 B 146 ALA ILE MET GLY ASN ALA LYS VAL LYS ALA HIS GLY LYS SEQRES 6 B 146 LYS VAL ILE THR ALA PHE ASN ASP GLY LEU ASN HIS LEU SEQRES 7 B 146 ASP SER LEU LYS GLY THR PHE ALA SER 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 MET ILE VAL ILE VAL LEU GLY HIS HIS SEQRES 10 B 146 LEU GLY LYS ASP PHE THR PRO ALA ALA GLN ALA ALA PHE SEQRES 11 B 146 GLN LYS VAL VAL ALA GLY VAL ALA ALA ALA LEU ALA HIS SEQRES 12 B 146 LYS TYR HIS SEQRES 1 C 141 SER LEU THR LYS THR GLU ARG THR ILE ILE VAL SER MET SEQRES 2 C 141 TRP ALA LYS ILE SER THR GLN ALA ASP THR ILE GLY THR SEQRES 3 C 141 GLU THR LEU GLU ARG LEU PHE LEU SER HIS PRO GLN THR SEQRES 4 C 141 LYS THR TYR PHE PRO HIS PHE ASP LEU HIS PRO GLY SER SEQRES 5 C 141 ALA GLN LEU ARG ALA HIS GLY SER LYS VAL VAL ALA ALA SEQRES 6 C 141 VAL GLY ASP ALA VAL LYS SER ILE ASP ASP ILE GLY GLY SEQRES 7 C 141 ALA LEU SER LYS LEU SER GLU LEU HIS ALA TYR ILE 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 ARG PHE PRO ALA ASP PHE SEQRES 10 C 141 THR ALA GLU ALA HIS ALA ALA TRP ASP LYS PHE LEU SER SEQRES 11 C 141 VAL VAL SER SER VAL LEU THR GLU LYS TYR ARG SEQRES 1 D 146 VAL HIS LEU THR ASP ALA GLU LYS ALA ALA VAL SER GLY SEQRES 2 D 146 LEU TRP GLY LYS VAL ASN ALA ASP GLU 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 TYR PHE ASP SER PHE GLY ASP LEU SER SER ALA SER SEQRES 5 D 146 ALA ILE MET GLY ASN ALA LYS VAL LYS ALA HIS GLY LYS SEQRES 6 D 146 LYS VAL ILE THR ALA PHE ASN ASP GLY LEU ASN HIS LEU SEQRES 7 D 146 ASP SER LEU LYS GLY THR PHE ALA SER 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 MET ILE VAL ILE VAL LEU GLY HIS HIS SEQRES 10 D 146 LEU GLY LYS ASP PHE THR PRO ALA ALA GLN ALA ALA PHE SEQRES 11 D 146 GLN LYS VAL VAL ALA GLY VAL ALA ALA ALA LEU ALA HIS SEQRES 12 D 146 LYS TYR HIS HET ACE A 0 3 HET ACE C 0 3 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 ACE ACETYL GROUP HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM CMO CARBON MONOXIDE HETSYN HEM HEME FORMUL 5 ACE 2(C2 H4 O) FORMUL 7 HEM 4(C34 H32 FE N4 O4) FORMUL 8 CMO 4(C O) FORMUL 15 HOH *234(H2 O) HELIX 1 1 LYS A 4 SER A 35 1 32 HELIX 2 2 PRO A 37 TYR A 42 1 6 HELIX 3 3 ALA A 53 LYS A 71 5 19 HELIX 4 4 ILE A 76 ALA A 79 1 4 HELIX 5 5 SER A 81 ALA A 88 1 8 HELIX 6 6 PRO A 95 ARG A 112 1 18 HELIX 7 7 ALA A 119 LEU A 136 1 18 HELIX 8 8 THR B 4 VAL B 18 1 15 HELIX 9 9 ASN B 19 VAL B 34 1 16 HELIX 10 10 TYR B 35 TYR B 41 5 7 HELIX 11 11 SER B 50 GLY B 56 1 7 HELIX 12 12 ASN B 57 ASN B 76 1 20 HELIX 13 13 PHE B 85 CYS B 93 1 9 HELIX 14 14 ASP B 99 HIS B 117 1 19 HELIX 15 15 THR B 123 HIS B 143 1 21 HELIX 16 16 LYS C 4 SER C 35 1 32 HELIX 17 17 PRO C 37 TYR C 42 1 6 HELIX 18 18 ALA C 53 LYS C 71 5 19 HELIX 19 19 ILE C 76 ALA C 79 1 4 HELIX 20 20 SER C 81 ALA C 88 1 8 HELIX 21 21 PRO C 95 ARG C 112 1 18 HELIX 22 22 ALA C 119 LEU C 136 1 18 HELIX 23 23 THR D 4 VAL D 18 1 15 HELIX 24 24 ASN D 19 VAL D 34 1 16 HELIX 25 25 TYR D 35 TYR D 41 5 7 HELIX 26 26 SER D 50 GLY D 56 1 7 HELIX 27 27 ASN D 57 ASN D 76 1 20 HELIX 28 28 PHE D 85 CYS D 93 1 9 HELIX 29 29 ASP D 99 HIS D 117 1 19 HELIX 30 30 THR D 123 HIS D 143 1 21 LINK FE HEM A 142 C CMO A 143 LINK FE HEM B 147 C CMO B 148 LINK FE HEM C 142 C CMO C 143 LINK FE HEM D 147 C CMO D 148 LINK FE HEM C 142 NE2 HIS C 87 LINK FE HEM D 147 NE2 HIS D 92 LINK C ACE A 0 N SER A 1 LINK C ACE C 0 N SER C 1 CRYST1 84.921 84.921 104.523 90.00 90.00 90.00 P 41 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 0.011776 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011776 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009567 0.00000