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HEADER OXYGEN TRANSPORT 05-FEB-96 1SPG TITLE CARBONMONOXY HEMOGLOBIN FROM THE TELEOST FISH LEIOSTOMUS TITLE 2 XANTHURUS COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: SPOT HEMOGLOBIN, SPOTHBCO; COMPND 5 OTHER_DETAILS: R-STATE, CARBONMONOXY BOUND ROOT EFFECT COMPND 6 HEMOGLOBIN; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: HEMOGLOBIN; COMPND 9 CHAIN: B; COMPND 10 SYNONYM: SPOT HEMOGLOBIN, SPOTHBCO; COMPND 11 OTHER_DETAILS: R-STATE, CARBONMONOXY BOUND ROOT EFFECT COMPND 12 HEMOGLOBIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LEIOSTOMUS XANTHURUS; SOURCE 3 ORGANISM_COMMON: SPOT; SOURCE 4 TISSUE: BLOOD; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: LEIOSTOMUS XANTHURUS; SOURCE 7 ORGANISM_COMMON: SPOT; SOURCE 8 TISSUE: BLOOD KEYWDS CARBON MONOXIDE, R-STATE, LEIOSTOMUS XANTHURUS, TELEOST KEYWDS 2 FISH, ROOT EFFECT, GLOBIN, OXYGEN TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR S.E.MYLVAGANAM,E.D.GETZOFF REVDAT 1 12-MAR-97 1SPG 0 JRNL AUTH S.E.MYLVAGANAM,C.BONAVENTURA,J.BONAVENTURA, JRNL AUTH 2 E.D.GETZOFF JRNL TITL STRUCTURAL BASIS FOR THE ROOT EFFECT IN JRNL TITL 2 HAEMOGLOBIN. JRNL REF NAT.STRUCT.BIOL. V. 3 275 1996 JRNL REFN ASTM NSBIEW US ISSN 1072-8368 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.BONAVENTURA,B.SULLIVAN,J.BONAVENTURA REMARK 1 TITL SPOT HEMOGLOBIN. STUDIES ON THE ROOT EFFECT REMARK 1 TITL 2 HEMOGLOBIN OF A MARINE TELEOST REMARK 1 REF J.BIOL.CHEM. V. 251 1871 1976 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 2 REMARK 2 RESOLUTION. 1.95 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) : 1.95 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 65.4 REMARK 3 NUMBER OF REFLECTIONS : 13623 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.191 REMARK 3 FREE R VALUE : 0.245 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000 REMARK 3 FREE R VALUE TEST SET COUNT : NULL 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 : 2253 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 90 REMARK 3 SOLVENT ATOMS : 175 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.60 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) : 0.012 REMARK 3 BOND ANGLES (DEGREES) : 1.69 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.30 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.76 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 1SPG 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 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-NOV-1993 REMARK 200 TEMPERATURE (KELVIN) : 293.1 REMARK 200 PH : 7.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : ELLIOT GX-21 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NI FILTER REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : MULTIWIRE AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : SIEMENS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XENGEN REMARK 200 DATA SCALING SOFTWARE : XENGEN REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16125 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950 REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 76.0 REMARK 200 DATA REDUNDANCY : 2.000 REMARK 200 R MERGE (I) : 0.04000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 26.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07 REMARK 200 COMPLETENESS FOR SHELL (%) : 38.0 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: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: INITIAL PHASES FROM THE REMARK 200 ISOMORPHOUS PHOSPHATE BOUND SPOT R-STATE HEMOGLOBIN (S. REMARK 200 MYLVAGANAM AND E. GETZOFF, UNPUBLISHED) REMARK 200 SOFTWARE USED: X-PLOR 3.1 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 40.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5 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 44.80000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.80000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 44.80000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.80000 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 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 ARG A 143 O REMARK 470 HIS B 147 O 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 GLU A 23 CB - CG - CD ANGL. DEV. = 18.3 DEGREES REMARK 500 GLY A 47 N - CA - C ANGL. DEV. = 13.5 DEGREES REMARK 500 GLN A 48 CB - CG - CD ANGL. DEV. = 13.8 DEGREES REMARK 500 ASP A 49 N - CA - C ANGL. DEV. = 11.3 DEGREES REMARK 500 ASP A 49 C - N - CA ANGL. DEV. =-11.5 DEGREES REMARK 500 LEU A 50 N - CA - C ANGL. DEV. = 11.8 DEGREES REMARK 500 GLN A 53 CB - CG - CD ANGL. DEV. = 19.7 DEGREES REMARK 500 GLN A 84 CB - CG - CD ANGL. DEV. = 14.3 DEGREES REMARK 500 GLU A 87 CB - CG - CD ANGL. DEV. = 14.8 DEGREES REMARK 500 GLU A 140 CB - CG - CD ANGL. DEV. = 14.8 DEGREES REMARK 500 GLU B 22 CB - CG - CD ANGL. DEV. = 11.3 DEGREES REMARK 500 GLN B 26 CB - CG - CD ANGL. DEV. = 13.7 DEGREES REMARK 500 GLU B 126 CB - CG - CD ANGL. DEV. = 16.6 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 220 DISTANCE = 8.75 ANGSTROMS REMARK 525 HOH 237 DISTANCE = 13.72 ANGSTROMS REMARK 525 HOH 265 DISTANCE = 6.47 ANGSTROMS REMARK 525 HOH 273 DISTANCE = 6.40 ANGSTROMS REMARK 525 HOH 317 DISTANCE = 7.84 ANGSTROMS REMARK 525 HOH 325 DISTANCE = 11.55 ANGSTROMS REMARK 525 HOH 362 DISTANCE = 6.71 ANGSTROMS REMARK 525 HOH 376 DISTANCE = 7.35 ANGSTROMS REMARK 525 HOH 407 DISTANCE = 8.90 ANGSTROMS REMARK 525 HOH 408 DISTANCE = 6.01 ANGSTROMS REMARK 525 HOH 438 DISTANCE = 6.88 ANGSTROMS REMARK 525 HOH 439 DISTANCE = 5.91 ANGSTROMS REMARK 525 HOH 440 DISTANCE = 5.85 ANGSTROMS REMARK 525 HOH 445 DISTANCE = 5.65 ANGSTROMS REMARK 525 HOH 447 DISTANCE = 5.39 ANGSTROMS REMARK 525 HOH 452 DISTANCE = 7.25 ANGSTROMS REMARK 525 HOH 478 DISTANCE = 5.09 ANGSTROMS REMARK 525 HOH 480 DISTANCE = 5.26 ANGSTROMS REMARK 525 HOH 486 DISTANCE = 7.09 ANGSTROMS REMARK 525 HOH 487 DISTANCE = 5.76 ANGSTROMS REMARK 525 HOH 490 DISTANCE = 8.81 ANGSTROMS REMARK 525 HOH 501 DISTANCE = 5.08 ANGSTROMS DBREF 1SPG A 1 143 UNP P56250 HBA_LEIXA 1 143 DBREF 1SPG B 1 147 UNP P56251 HBB_LEIXA 1 147 SEQRES 1 A 143 SER LEU SER ALA THR ASP LYS ALA ARG VAL LYS ALA LEU SEQRES 2 A 143 TRP ASP LYS ILE GLU GLY LYS SER ALA GLU LEU GLY ALA SEQRES 3 A 143 GLU ALA LEU GLY ARG MET LEU VAL SER PHE PRO GLN THR SEQRES 4 A 143 LYS ILE TYR PHE SER GLU TRP GLY GLN ASP LEU GLY PRO SEQRES 5 A 143 GLN THR PRO GLN VAL ARG ASN HIS GLY ALA VAL ILE MET SEQRES 6 A 143 ALA ALA VAL GLY LYS ALA VAL LYS SER ILE ASP ASN LEU SEQRES 7 A 143 VAL GLY GLY LEU SER GLN LEU SER GLU LEU HIS ALA PHE SEQRES 8 A 143 LYS LEU ARG VAL ASP PRO ALA ASN PHE LYS ILE LEU ALA SEQRES 9 A 143 HIS ASN ILE ILE LEU VAL ILE SER MET TYR PHE PRO GLY SEQRES 10 A 143 ASP PHE THR PRO GLU VAL HIS LEU SER VAL ASP LYS PHE SEQRES 11 A 143 LEU ALA CYS LEU ALA LEU ALA LEU SER GLU LYS TYR ARG SEQRES 1 B 147 VAL ASP TRP THR ASP ALA GLU ARG ALA ALA ILE LYS ALA SEQRES 2 B 147 LEU TRP GLY LYS ILE ASP VAL GLY GLU ILE GLY PRO GLN SEQRES 3 B 147 ALA LEU SER ARG LEU LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 B 147 ARG HIS PHE LYS GLY PHE GLY ASN ILE SER THR ASN ALA SEQRES 5 B 147 ALA ILE LEU GLY ASN ALA LYS VAL ALA GLU HIS GLY LYS SEQRES 6 B 147 THR VAL MET GLY GLY LEU ASP ARG ALA VAL GLN ASN MET SEQRES 7 B 147 ASP ASN ILE LYS ASN VAL TYR LYS GLN LEU SER ILE LYS SEQRES 8 B 147 HIS SER GLU LYS ILE HIS VAL ASP PRO ASP ASN PHE ARG SEQRES 9 B 147 LEU LEU GLY GLU ILE ILE THR MET CYS VAL GLY ALA LYS SEQRES 10 B 147 PHE GLY PRO SER ALA PHE THR PRO GLU ILE HIS GLU ALA SEQRES 11 B 147 TRP GLN LYS PHE LEU ALA VAL VAL VAL SER ALA LEU GLY SEQRES 12 B 147 ARG GLN TYR HIS HET ACE A 0 3 HET HEM A 144 43 HET CMO A 145 2 HET HEM B 148 43 HET CMO B 149 2 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 2(C O) FORMUL 8 HOH *175(H2 O) HELIX 1 AA SER A 3 GLU A 18 1 16 HELIX 2 BA LYS A 20 SER A 35 1 16 HELIX 3 CA PHE A 36 TYR A 42 1 7 HELIX 4 EA THR A 54 LYS A 73 1 20 HELIX 5 FA LEU A 82 ALA A 90 1 9 HELIX 6 GA ASP A 96 TYR A 114 1 19 HELIX 7 HA PRO A 121 GLU A 140 1 20 HELIX 8 AB THR B 4 ILE B 18 1 15 HELIX 9 BB VAL B 20 VAL B 34 1 15 HELIX 10 CB TYR B 35 HIS B 41 1 7 HELIX 11 DB THR B 50 GLY B 56 1 7 HELIX 12 EB ASN B 57 GLN B 76 1 20 HELIX 13 FB TYR B 85 SER B 93 1 9 HELIX 14 GB ASP B 99 LYS B 117 1 19 HELIX 15 HB THR B 124 ARG B 144 1 21 LINK C ACE A 0 N SER A 1 LINK C CMO A 145 FE HEM A 144 LINK FE HEM A 144 NE2 HIS A 89 LINK C CMO B 149 FE HEM B 148 LINK FE HEM B 148 NE2 HIS B 92 CRYST1 89.600 75.600 69.700 90.00 141.90 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 0.011161 0.000000 0.014234 0.00000 SCALE2 0.000000 0.013228 0.000000 0.00000 SCALE3 0.000000 0.000000 0.023252 0.00000