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HEADER OXYGEN STORAGE/TRANSPORT 28-MAR-02 1LA6 TITLE THE CRYSTAL STRUCTURE OF TREMATOMUS NEWNESI HEMOGLOBIN IN A TITLE 2 PARTIAL HEMICHROME STATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN ALPHA-1 CHAIN; COMPND 3 CHAIN: A; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: HEMOGLOBIN BETA-1/2 CHAIN; COMPND 6 CHAIN: B SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: TREMATOMUS NEWNESI; SOURCE 3 ORGANISM_COMMON: ANTARCTIC FISH; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: TREMATOMUS NEWNESI; SOURCE 6 ORGANISM_COMMON: ANTARCTIC FISH KEYWDS HEMICHROME, BISHISTIDINE COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR A.RICCIO,L.VITAGLIANO,G.DI PRISCO,A.ZAGARI,L.MAZZARELLA REVDAT 1 31-JUL-02 1LA6 0 JRNL AUTH A.RICCIO,L.VITAGLIANO,G.DI PRISCO,A.ZAGARI, JRNL AUTH 2 L.MAZZARELLA JRNL TITL THE CRYSTAL STRUCTURE OF A TETRAMERIC HEMOGLOBIN JRNL TITL 2 IN A PARTIAL HEMICHROME STATE JRNL REF PROC.NATL.ACAD.SCI.USA V. 99 9801 2002 JRNL REFN ASTM PNASA6 US ISSN 0027-8424 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.RICCIO,L.VITAGLIANO,G.DI PRISCO,A.ZAGARI, REMARK 1 AUTH 2 L.MAZZARELLA REMARK 1 TITL LIGANDED AND UNLIGANDED FORMS OF ANTARCTIC FISH REMARK 1 TITL 2 HAEMOGLOBINS IN POLYETHYLENE GLYCOL: REMARK 1 TITL 3 CRYSTALLIZATION OF AN R-STATE HAEMICHROME REMARK 1 TITL 4 INTERMEDIATE REMARK 1 REF ACTA CRYSTALLOGR. V. 57 1144 2001 REMARK 1 REFN ASTM ACCRA9 DK ISSN 0365-110X REMARK 1 REFERENCE 2 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. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.00 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 : 23191 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) : 0.179 REMARK 3 FREE R VALUE : 0.212 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2280 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 : 2154 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 88 REMARK 3 SOLVENT ATOMS : 71 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) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.45 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.70 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.44 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC 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 1LA6 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 RCSB015788. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-MAR-2000 REMARK 200 TEMPERATURE (KELVIN) : 293.0 REMARK 200 PH : 7.60 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 : ENRAF-NONIUS FR571 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : MIRRORS REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MACSCIENCE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27020 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 12.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.8 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.07700 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) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15 REMARK 200 COMPLETENESS FOR SHELL (%) : 87.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.35000 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: X-PLOR REMARK 200 STARTING MODEL: PDB ENTRY 1T1N REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.68 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: MPEG 5000, SODIUM ACETATE, PH 7.6, REMARK 280 FREE INTERFACE DIFFUSION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 1/2+X,1/2+Y,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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 44.92650 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.09500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 44.92650 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 44.09500 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 2 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 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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 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 SER B 43 REMARK 465 GLY B 44 REMARK 465 PHE B 45 REMARK 465 GLY B 46 REMARK 465 ASN B 47 REMARK 465 LEU B 48 REMARK 465 TYR B 49 REMARK 465 ASN B 50 REMARK 465 ALA B 51 REMARK 465 GLU B 52 REMARK 465 GLY B 53 REMARK 465 GLN 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 CZ ARG A 11 O HOH 201 1.21 REMARK 500 NH1 ARG A 11 O HOH 201 1.23 REMARK 500 NH2 ARG A 11 O HOH 201 1.37 REMARK 500 FE HEM A 143 C CMO 144 1.86 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 A 82 SD MET A 82 CE 0.059 REMARK 500 MET B 18 SD MET B 18 CE -0.062 REMARK 500 MET B 78 SD MET B 78 CE -0.053 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 TYR A 90 N - CA - C ANGL. DEV. = 7.7 DEGREES REMARK 500 MET A 113 N - CA - C ANGL. DEV. = 7.6 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1T1N RELATED DB: PDB REMARK 900 PDB-ID 1T1N CONTAINS THE SAME PROTEIN FULLY COMPLEXED WITH REMARK 900 CO DBREF 1LA6 A 1 142 UNP P45718 HBA1_TRENE 1 142 DBREF 1LA6 B 1 146 UNP P45720 HBB_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 LYS GLU ARG SER ILE ILE SER ASP SEQRES 2 B 146 ILE PHE SER HIS MET ASP TYR ASP ASP ILE GLY PRO LYS SEQRES 3 B 146 ALA LEU SER ARG CYS LEU VAL VAL TYR PRO TRP THR GLN SEQRES 4 B 146 ARG TYR PHE SER GLY PHE GLY ASN LEU TYR ASN ALA GLU SEQRES 5 B 146 GLY ILE MET SER ASN ALA ASN VAL ALA ALA HIS GLY ILE SEQRES 6 B 146 LYS VAL LEU HIS GLY LEU ASP ARG GLY MET LYS ASN MET SEQRES 7 B 146 ASP ASN ILE ALA ASP ALA TYR THR ASP LEU SER THR LEU SEQRES 8 B 146 HIS SER GLU LYS LEU HIS VAL ASP PRO ASP ASN PHE LYS SEQRES 9 B 146 LEU LEU SER ASP CYS ILE THR ILE VAL LEU ALA ALA LYS SEQRES 10 B 146 MET GLY HIS ALA PHE THR ALA GLU THR GLN GLY ALA PHE SEQRES 11 B 146 GLN LYS PHE LEU ALA ALA VAL VAL SER ALA LEU GLY LYS SEQRES 12 B 146 GLN TYR HIS HET ACE A 0 3 HET HEM A 143 43 HET CMO 144 2 HET HEM B 147 43 HETNAM ACE ACETYL GROUP HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM CMO CARBON MONOXIDE HETSYN HEM HEME FORMUL 3 ACE C2 H4 O FORMUL 4 HEM 2(C34 H32 FE N4 O4) FORMUL 5 CMO C O FORMUL 7 HOH *69(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 TYR A 90 1 10 HELIX 7 7 ASP A 95 SER A 97 5 3 HELIX 8 8 ASN A 98 PHE A 114 1 17 HELIX 9 9 THR A 119 GLU A 139 1 21 HELIX 10 10 ARG A 140 ARG A 142 5 3 HELIX 11 11 THR B 4 HIS B 17 1 14 HELIX 12 12 ASP B 19 TYR B 35 1 17 HELIX 13 13 PRO B 36 PHE B 42 5 7 HELIX 14 14 ASN B 57 ASN B 77 1 21 HELIX 15 15 ASN B 80 TYR B 85 1 6 HELIX 16 16 TYR B 85 LYS B 95 1 11 HELIX 17 17 PRO B 100 GLY B 119 1 20 HELIX 18 18 HIS B 120 PHE B 122 5 3 HELIX 19 19 THR B 123 LYS B 143 1 21 LINK FE HEM B 147 NE2 HIS B 92 LINK FE HEM B 147 NE2 HIS B 63 LINK FE HEM A 143 NE2 HIS A 88 LINK C ACE A 0 N SER A 1 CRYST1 89.853 88.190 55.142 90.00 97.79 90.00 C 1 2 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 0.011130 0.000000 0.001520 0.00000 SCALE2 0.000000 0.011340 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018300 0.00000