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HEADER OXYGEN STORAGE/TRANSPORT 19-NOV-03 1V4X TITLE CRYSTAL STRUCTURE OF BLUEFIN TUNA HEMOGLOBIN DEOXY FORM AT TITLE 2 PH5.0 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: THUNNUS THYNNUS; SOURCE 3 ORGANISM_COMMON: BLUEFIN TUNA; SOURCE 4 TISSUE: RED CELL; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: THUNNUS THYNNUS; SOURCE 7 ORGANISM_COMMON: BLUEFIN TUNA; SOURCE 8 TISSUE: RED CELL KEYWDS OXYGEN TRANSPORT, HEME, RESPIRATORY PROTEIN, ERYTHROCYTE, KEYWDS 2 ROOT EFFECT, SWIM BLADDER EXPDTA X-RAY DIFFRACTION AUTHOR T.YOKOYAMA,K.T.CHONG,Y.MIYAZAKI,T.NAKATSUKASA,S.UNZAI, AUTHOR 2 G.MIYAZAKI,H.MORIMOTO,R.H.T.JEREMY,S.Y.PARK REVDAT 1 06-JUL-04 1V4X 0 JRNL AUTH T.YOKOYAMA,K.T.CHONG,G.MIYAZAKI,H.MORIMOTO, JRNL AUTH 2 D.T.SHIH,S.UNZAI,J.R.TAME,S.Y.PARK JRNL TITL NOVEL MECHANISMS OF PH SENSITIVITY IN TUNA JRNL TITL 2 HEMOGLOBIN: A STRUCTURAL EXPLANATION OF THE ROOT JRNL TITL 3 EFFECT JRNL REF J.BIOL.CHEM. V. 279 28632 2004 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.1.22 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.73 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 60051 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 + TEST SET) : 0.206 REMARK 3 R VALUE (WORKING SET) : 0.204 REMARK 3 FREE R VALUE : 0.250 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 3197 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 1.60 REMARK 3 BIN RESOLUTION RANGE LOW : 1.64 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3416 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.3510 REMARK 3 BIN FREE R VALUE SET COUNT : 184 REMARK 3 BIN FREE R VALUE : 0.3860 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 4916 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.76 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.00000 REMARK 3 B22 (A**2) : -0.78000 REMARK 3 B33 (A**2) : -0.36000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.81000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.116 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.117 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.189 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4764 ; 0.018 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6504 ; 1.748 ; 2.065 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 574 ; 5.545 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 704 ; 0.116 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3562 ; 0.008 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2385 ; 0.209 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 259 ; 0.144 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 33 ; 0.159 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.159 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2878 ; 0.958 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4612 ; 1.608 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1886 ; 2.781 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1892 ; 4.185 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 0 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1V4X 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 PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB006210. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 5.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL40B2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63648 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 88.4 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.07300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66 REMARK 200 COMPLETENESS FOR SHELL (%) : 72.7 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.33100 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: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.72 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000, SODIUM PHOSPHATE, REMARK 280 MAGNESIUM CHLORIDE, PH 5.0, BATCH METHOD, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 30.26850 REMARK 290 SMTRY3 2 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 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 HOH 139 O HOH 256 2.16 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 450 SD MET C 450 CE 0.121 REMARK 500 ILE D 611 CB ILE D 611 CG2 0.112 REMARK 500 ILE D 705 CB ILE D 705 CG2 -0.117 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 LEU B 306 CB - CG - CD2 ANGL. DEV. = 12.0 DEGREES REMARK 500 LEU C 488 CA - CB - CG ANGL. DEV. = 12.5 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1V4U RELATED DB: PDB REMARK 900 BLUEFIN TUNA CARBONMONOXY-HEMOGLOBIN AT PH7.5, AT 2.00 A REMARK 900 RELATED ID: 1V4W RELATED DB: PDB REMARK 900 BLUEFIN TUNA HEMOGLOBIN DEOXY FORM AT PH7.5, AT 1.70 A DBREF 1V4X A 1 143 UNP Q8AYM0 Q8AYM0_THUTH 2 144 DBREF 1V4X B 201 346 UNP Q8AYM1 Q8AYM1_THUTH 2 147 DBREF 1V4X C 401 543 UNP Q8AYM0 Q8AYM0_THUTH 2 144 DBREF 1V4X D 601 746 UNP Q8AYM1 Q8AYM1_THUTH 2 147 SEQRES 1 A 143 THR THR LEU SER ASP LYS ASP LYS SER THR VAL LYS ALA SEQRES 2 A 143 LEU TRP GLY LYS ILE SER LYS SER ALA ASP ALA ILE GLY SEQRES 3 A 143 ALA ASP ALA LEU GLY ARG MET LEU ALA VAL TYR PRO GLN SEQRES 4 A 143 THR LYS THR TYR PHE SER HIS TRP PRO ASP MET SER PRO SEQRES 5 A 143 GLY SER GLY PRO VAL LYS ALA HIS GLY LYS LYS VAL MET SEQRES 6 A 143 GLY GLY VAL ALA LEU ALA VAL SER LYS ILE ASP ASP LEU SEQRES 7 A 143 THR THR GLY LEU GLY ASP LEU SER GLU LEU HIS ALA PHE SEQRES 8 A 143 LYS MET ARG VAL ASP PRO SER ASN PHE LYS ILE LEU SER SEQRES 9 A 143 HIS CYS ILE LEU VAL VAL VAL ALA LYS MET PHE PRO LYS SEQRES 10 A 143 GLU PHE THR PRO ASP ALA HIS VAL SER LEU ASP LYS PHE SEQRES 11 A 143 LEU ALA SER VAL ALA LEU ALA LEU ALA GLU ARG TYR ARG SEQRES 1 B 146 VAL GLU TRP THR GLN GLN GLU ARG SER ILE ILE ALA GLY SEQRES 2 B 146 ILE PHE ALA ASN LEU ASN TYR GLU ASP ILE GLY PRO LYS SEQRES 3 B 146 ALA LEU ALA ARG CYS LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 B 146 ARG TYR PHE GLY ALA TYR GLY ASP LEU SER THR PRO ASP SEQRES 5 B 146 ALA ILE LYS GLY ASN ALA LYS ILE ALA ALA HIS GLY VAL SEQRES 6 B 146 LYS VAL LEU HIS GLY LEU ASP ARG ALA VAL LYS ASN MET SEQRES 7 B 146 ASP ASN ILE ASN GLU ALA TYR SER GLU LEU SER VAL LEU SEQRES 8 B 146 HIS SER ASP LYS LEU HIS VAL ASP PRO ASP ASN PHE ARG SEQRES 9 B 146 ILE LEU GLY ASP CYS LEU THR VAL VAL ILE ALA ALA ASN SEQRES 10 B 146 LEU GLY ASP ALA PHE THR VAL GLU THR GLN CYS ALA PHE SEQRES 11 B 146 GLN LYS PHE LEU ALA VAL VAL VAL PHE ALA LEU GLY ARG SEQRES 12 B 146 LYS TYR HIS SEQRES 1 C 143 THR THR LEU SER ASP LYS ASP LYS SER THR VAL LYS ALA SEQRES 2 C 143 LEU TRP GLY LYS ILE SER LYS SER ALA ASP ALA ILE GLY SEQRES 3 C 143 ALA ASP ALA LEU GLY ARG MET LEU ALA VAL TYR PRO GLN SEQRES 4 C 143 THR LYS THR TYR PHE SER HIS TRP PRO ASP MET SER PRO SEQRES 5 C 143 GLY SER GLY PRO VAL LYS ALA HIS GLY LYS LYS VAL MET SEQRES 6 C 143 GLY GLY VAL ALA LEU ALA VAL SER LYS ILE ASP ASP LEU SEQRES 7 C 143 THR THR GLY LEU GLY ASP LEU SER GLU LEU HIS ALA PHE SEQRES 8 C 143 LYS MET ARG VAL ASP PRO SER ASN PHE LYS ILE LEU SER SEQRES 9 C 143 HIS CYS ILE LEU VAL VAL VAL ALA LYS MET PHE PRO LYS SEQRES 10 C 143 GLU PHE THR PRO ASP ALA HIS VAL SER LEU ASP LYS PHE SEQRES 11 C 143 LEU ALA SER VAL ALA LEU ALA LEU ALA GLU ARG TYR ARG SEQRES 1 D 146 VAL GLU TRP THR GLN GLN GLU ARG SER ILE ILE ALA GLY SEQRES 2 D 146 ILE PHE ALA ASN LEU ASN TYR GLU ASP ILE GLY PRO LYS SEQRES 3 D 146 ALA LEU ALA ARG CYS LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 D 146 ARG TYR PHE GLY ALA TYR GLY ASP LEU SER THR PRO ASP SEQRES 5 D 146 ALA ILE LYS GLY ASN ALA LYS ILE ALA ALA HIS GLY VAL SEQRES 6 D 146 LYS VAL LEU HIS GLY LEU ASP ARG ALA VAL LYS ASN MET SEQRES 7 D 146 ASP ASN ILE ASN GLU ALA TYR SER GLU LEU SER VAL LEU SEQRES 8 D 146 HIS SER ASP LYS LEU HIS VAL ASP PRO ASP ASN PHE ARG SEQRES 9 D 146 ILE LEU GLY ASP CYS LEU THR VAL VAL ILE ALA ALA ASN SEQRES 10 D 146 LEU GLY ASP ALA PHE THR VAL GLU THR GLN CYS ALA PHE SEQRES 11 D 146 GLN LYS PHE LEU ALA VAL VAL VAL PHE ALA LEU GLY ARG SEQRES 12 D 146 LYS TYR HIS HET ACE A 0 3 HET ACE C 0 3 HET HEM A 144 43 HET HEM B 347 43 HET HEM C 544 43 HET HEM D 747 43 HETNAM ACE ACETYL GROUP HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 5 ACE 2(C2 H4 O) FORMUL 7 HEM 4(C34 H32 FE N4 O4) FORMUL 11 HOH *282(H2 O) HELIX 1 1 SER A 4 SER A 19 1 16 HELIX 2 2 SER A 21 TYR A 37 1 17 HELIX 3 3 PRO A 38 PHE A 44 5 7 HELIX 4 4 SER A 54 LYS A 74 1 21 HELIX 5 5 ASP A 77 LEU A 82 1 6 HELIX 6 6 LEU A 82 LYS A 92 1 11 HELIX 7 7 PRO A 97 PHE A 115 1 19 HELIX 8 8 THR A 120 GLU A 140 1 21 LINK FE HEM A 144 NE2 HIS A 89 LINK FE HEM B 347 NE2 HIS B 292 LINK FE HEM C 544 NE2 HIS C 489 LINK FE HEM D 747 NE2 HIS D 692 LINK C ACE A 0 N THR A 1 LINK C ACE C 0 N THR C 401 CRYST1 56.979 60.537 80.640 90.00 95.12 90.00 P 1 21 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 0.017550 0.000000 0.001573 0.00000 SCALE2 0.000000 0.016519 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012450 0.00000