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HEADER OXYGEN STORAGE/TRANSPORT 13-JUL-05 2AA1 TITLE CRYSTAL STRUCTURE OF THE CATHODIC HEMOGLOBIN ISOLATED FROM TITLE 2 THE ANTARCTIC FISH TREMATOMUS NEWNESI COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN ALPHA-1 CHAIN; COMPND 3 CHAIN: A, C; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: HEMOGLOBIN BETA-C CHAIN; COMPND 6 CHAIN: B, D SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: TREMATOMUS NEWNESI; SOURCE 3 ORGANISM_COMMON: DUSKY NOTOTHEN; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: TREMATOMUS NEWNESI; SOURCE 6 ORGANISM_COMMON: DUSKY NOTOTHEN KEYWDS HEMOGLOBIN, ROOT EFFECT, COOPERATIVITY, ANTARCTIC FISH EXPDTA X-RAY DIFFRACTION AUTHOR L.MAZZARELLA,G.BONOMI,M.C.LUBRANO,A.MERLINO,A.RICCIO, AUTHOR 2 A.VERGARA,L.VITAGLIANO,C.VERDE,G.DI PRISCO REVDAT 2 24-JAN-06 2AA1 1 JRNL REVDAT 1 02-AUG-05 2AA1 0 JRNL AUTH L.MAZZARELLA,G.BONOMI,M.C.LUBRANO,A.MERLINO, JRNL AUTH 2 A.RICCIO,A.VERGARA,L.VITAGLIANO,C.VERDE,G.DI PRISCO JRNL TITL MINIMAL STRUCTURAL REQUIREMENTS FOR ROOT EFFECT: JRNL TITL 2 CRYSTAL STRUCTURE OF THE CATHODIC HEMOGLOBIN JRNL TITL 3 ISOLATED FROM THE ANTARCTIC FISH TREMATOMUS NEWNESI JRNL REF PROTEINS V. 62 316 2006 JRNL REFN ASTM PSFGEY US ISSN 0887-3585 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH L.MAZZARELLA,R.D'AVINO,G.DI PRISCO,C.SAVINO, REMARK 1 AUTH 2 L.VITAGLIANO,P.C.E.MOODY,A.ZAGARI REMARK 1 TITL CRYSTAL STRUCTURE OF TREMATOMUS NEWNESI REMARK 1 TITL 2 HAEMOGLOBIN RE-OPENS THE ROOT EFFECT QUESTION REMARK 1 REF J.MOL.BIOL. V. 287 897 1999 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 51907 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) : 0.186 REMARK 3 FREE R VALUE : 0.220 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 4603 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 : 4540 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 172 REMARK 3 SOLVENT ATOMS : 369 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) : NULL REMARK 3 BOND ANGLES (DEGREES) : NULL REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL 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 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: NULL REMARK 4 REMARK 4 2AA1 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 RCSB033672. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-APR-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.20 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-4 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9393 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 : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL 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) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88 REMARK 200 COMPLETENESS FOR SHELL (%) : 77.0 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: 1HBH REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.10 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 9-12%(W/V) PEG 6000, PHOSPHATE REMARK 280 BUFFER, PH 6.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K 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 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: 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 31 CB ARG A 31 CG -0.043 REMARK 500 MET C 82 SD MET C 82 CE 0.040 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 ILE A 17 N - CA - C ANGL. DEV. = 7.2 DEGREES REMARK 500 TYR A 90 N - CA - C ANGL. DEV. = 6.8 DEGREES REMARK 500 TYR A 141 N - CA - C ANGL. DEV. = 8.2 DEGREES REMARK 500 GLU B 19 N - CA - C ANGL. DEV. = -7.2 DEGREES REMARK 500 TYR B 20 N - CA - C ANGL. DEV. = 6.6 DEGREES REMARK 500 TYR B 49 N - CA - C ANGL. DEV. = 6.9 DEGREES REMARK 500 GLU B 94 N - CA - C ANGL. DEV. = 8.9 DEGREES REMARK 500 PHE B 118 N - CA - C ANGL. DEV. = 6.7 DEGREES REMARK 500 ILE C 17 N - CA - C ANGL. DEV. = 7.6 DEGREES REMARK 500 TYR C 90 N - CA - C ANGL. DEV. = 6.8 DEGREES REMARK 500 TYR C 141 N - CA - C ANGL. DEV. = 7.2 DEGREES REMARK 500 GLU D 19 N - CA - C ANGL. DEV. = -7.7 DEGREES REMARK 500 TYR D 20 N - CA - C ANGL. DEV. = 7.4 DEGREES REMARK 500 GLU D 94 N - CA - C ANGL. DEV. = 8.3 DEGREES REMARK 500 LEU D 106 CA - CB - CG ANGL. DEV. = 6.8 DEGREES REMARK 500 PHE D 118 N - CA - C ANGL. DEV. = 6.7 DEGREES REMARK 500 LYS D 143 N - CA - C ANGL. DEV. = 7.4 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 1206 DISTANCE = 11.86 ANGSTROMS REMARK 525 HOH 1251 DISTANCE = 7.61 ANGSTROMS REMARK 525 HOH 1292 DISTANCE = 11.82 ANGSTROMS REMARK 525 HOH 1341 DISTANCE = 9.17 ANGSTROMS DBREF 2AA1 A 1 142 UNP P45718 HBA1_TRENE 1 142 DBREF 2AA1 C 1 142 UNP P45718 HBA1_TRENE 1 142 DBREF 2AA1 B 1 146 UNP P45721 HBBC_TRENE 1 146 DBREF 2AA1 D 1 146 UNP P45721 HBBC_TRENE 1 146 SEQRES 1 A 142 SER LEU SER ASP LYS ASP LYS ALA ALA VAL ARG ALA LEU SEQRES 2 A 142 TRP SER LYS ILE GLY LYS SER SER ASP ALA ILE GLY ASN SEQRES 3 A 142 ASP ALA LEU SER ARG MET ILE VAL VAL TYR PRO GLN THR SEQRES 4 A 142 LYS ILE TYR PHE SER HIS TRP PRO ASP VAL THR PRO GLY SEQRES 5 A 142 SER PRO ASN ILE LYS ALA HIS GLY LYS LYS VAL MET GLY SEQRES 6 A 142 GLY ILE ALA LEU ALA VAL SER LYS ILE ASP ASP LEU LYS SEQRES 7 A 142 THR GLY LEU MET GLU LEU SER GLU GLN HIS ALA TYR LYS SEQRES 8 A 142 LEU ARG VAL ASP PRO SER ASN PHE LYS ILE LEU ASN HIS SEQRES 9 A 142 CYS ILE LEU VAL VAL ILE SER THR MET PHE PRO LYS GLU SEQRES 10 A 142 PHE THR PRO GLU ALA HIS VAL SER LEU ASP LYS PHE LEU SEQRES 11 A 142 SER GLY VAL ALA LEU ALA LEU ALA GLU ARG TYR ARG SEQRES 1 B 146 VAL GLU TRP THR ASP PHE GLU ARG ALA THR ILE LYS ASP SEQRES 2 B 146 ILE PHE SER LYS LEU GLU TYR ASP VAL VAL GLY PRO ALA SEQRES 3 B 146 THR LEU ALA ARG CYS LEU VAL VAL TYR PRO TRP THR GLN SEQRES 4 B 146 ARG TYR PHE GLY LYS PHE GLY ASN LEU TYR ASN ALA ALA SEQRES 5 B 146 ALA ILE ALA GLN ASN ALA MET VAL SER LYS HIS GLY THR SEQRES 6 B 146 THR ILE LEU ASN GLY LEU ASP ARG ALA VAL LYS ASN MET SEQRES 7 B 146 ASP ASP ILE THR ASN THR TYR ALA GLU LEU SER VAL LEU SEQRES 8 B 146 HIS SER GLU LYS LEU HIS VAL ASP PRO ASP ASN PHE LYS SEQRES 9 B 146 LEU LEU ALA ASP CYS LEU THR ILE VAL VAL ALA ALA ARG SEQRES 10 B 146 PHE GLY SER ALA PHE THR GLY GLU VAL GLN ALA ALA PHE SEQRES 11 B 146 GLN LYS PHE MET ALA VAL VAL VAL SER SER LEU GLY LYS SEQRES 12 B 146 GLN TYR ARG SEQRES 1 C 142 SER LEU SER ASP LYS ASP LYS ALA ALA VAL ARG ALA LEU SEQRES 2 C 142 TRP SER LYS ILE GLY LYS SER SER ASP ALA ILE GLY ASN SEQRES 3 C 142 ASP ALA LEU SER ARG MET ILE VAL VAL TYR PRO GLN THR SEQRES 4 C 142 LYS ILE TYR PHE SER HIS TRP PRO ASP VAL THR PRO GLY SEQRES 5 C 142 SER PRO ASN ILE LYS ALA HIS GLY LYS LYS VAL MET GLY SEQRES 6 C 142 GLY ILE ALA LEU ALA VAL SER LYS ILE ASP ASP LEU LYS SEQRES 7 C 142 THR GLY LEU MET GLU LEU SER GLU GLN HIS ALA TYR LYS SEQRES 8 C 142 LEU ARG VAL ASP PRO SER ASN PHE LYS ILE LEU ASN HIS SEQRES 9 C 142 CYS ILE LEU VAL VAL ILE SER THR MET PHE PRO LYS GLU SEQRES 10 C 142 PHE THR PRO GLU ALA HIS VAL SER LEU ASP LYS PHE LEU SEQRES 11 C 142 SER GLY VAL ALA LEU ALA LEU ALA GLU ARG TYR ARG SEQRES 1 D 146 VAL GLU TRP THR ASP PHE GLU ARG ALA THR ILE LYS ASP SEQRES 2 D 146 ILE PHE SER LYS LEU GLU TYR ASP VAL VAL GLY PRO ALA SEQRES 3 D 146 THR LEU ALA ARG CYS LEU VAL VAL TYR PRO TRP THR GLN SEQRES 4 D 146 ARG TYR PHE GLY LYS PHE GLY ASN LEU TYR ASN ALA ALA SEQRES 5 D 146 ALA ILE ALA GLN ASN ALA MET VAL SER LYS HIS GLY THR SEQRES 6 D 146 THR ILE LEU ASN GLY LEU ASP ARG ALA VAL LYS ASN MET SEQRES 7 D 146 ASP ASP ILE THR ASN THR TYR ALA GLU LEU SER VAL LEU SEQRES 8 D 146 HIS SER GLU LYS LEU HIS VAL ASP PRO ASP ASN PHE LYS SEQRES 9 D 146 LEU LEU ALA ASP CYS LEU THR ILE VAL VAL ALA ALA ARG SEQRES 10 D 146 PHE GLY SER ALA PHE THR GLY GLU VAL GLN ALA ALA PHE SEQRES 11 D 146 GLN LYS PHE MET ALA VAL VAL VAL SER SER LEU GLY LYS SEQRES 12 D 146 GLN TYR ARG HET ACE A 0 3 HET ACE C 0 3 HET HEM A 200 43 HET HEM B 400 43 HET HEM C 600 43 HET HEM D 800 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 *369(H2 O) HELIX 1 1 SER A 3 GLY A 18 1 16 HELIX 2 2 SER A 20 TYR A 36 1 17 HELIX 3 3 PRO A 37 SER A 44 5 8 HELIX 4 4 SER A 53 LYS A 73 1 21 HELIX 5 5 ASP A 76 LEU A 81 1 6 HELIX 6 6 LEU A 81 LYS A 91 1 11 HELIX 7 7 PRO A 96 PHE A 114 1 19 HELIX 8 8 THR A 119 ALA A 138 1 20 HELIX 9 9 THR B 4 LEU B 18 1 15 HELIX 10 10 GLU B 19 TYR B 35 1 17 HELIX 11 11 PRO B 36 GLY B 46 5 11 HELIX 12 12 ASN B 50 ASN B 57 1 8 HELIX 13 13 ASN B 57 GLY B 70 1 14 HELIX 14 14 LEU B 71 ASN B 77 1 7 HELIX 15 15 ASP B 80 LYS B 95 1 16 HELIX 16 16 PRO B 100 GLY B 119 1 20 HELIX 17 17 SER B 120 PHE B 122 5 3 HELIX 18 18 THR B 123 LYS B 143 1 21 HELIX 19 19 SER C 3 GLY C 18 1 16 HELIX 20 20 SER C 20 TYR C 36 1 17 HELIX 21 21 PRO C 37 SER C 44 5 8 HELIX 22 22 SER C 53 LYS C 73 1 21 HELIX 23 23 ASP C 76 LEU C 81 1 6 HELIX 24 24 LEU C 81 LYS C 91 1 11 HELIX 25 25 PRO C 96 PHE C 114 1 19 HELIX 26 26 THR C 119 GLU C 139 1 21 HELIX 27 27 THR D 4 LEU D 18 1 15 HELIX 28 28 GLU D 19 TYR D 35 1 17 HELIX 29 29 PRO D 36 PHE D 42 5 7 HELIX 30 30 ASN D 50 ASN D 57 1 8 HELIX 31 31 ASN D 57 GLY D 70 1 14 HELIX 32 32 LEU D 71 ASN D 77 1 7 HELIX 33 33 ASP D 80 TYR D 85 1 6 HELIX 34 34 TYR D 85 LYS D 95 1 11 HELIX 35 35 PRO D 100 GLY D 119 1 20 HELIX 36 36 SER D 120 PHE D 122 5 3 HELIX 37 37 THR D 123 LYS D 143 1 21 LINK NE2 HIS A 88 FE HEM A 200 LINK NE2 HIS B 92 FE HEM B 400 LINK NE2 HIS C 88 FE HEM C 600 LINK NE2 HIS D 92 FE HEM D 800 LINK C ACE A 0 N SER A 1 LINK C ACE C 0 N SER C 1 CRYST1 58.097 60.801 61.232 80.73 81.36 62.01 P 1 2 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 0.017210 -0.009150 -0.001670 0.00000 SCALE2 0.000000 0.018630 -0.001940 0.00000 SCALE3 0.000000 0.000000 0.016610 0.00000