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HEADER OXYGEN TRANSPORT 21-JUN-96 1OUU TITLE CARBONMONOXY TROUT HEMOGLOBIN I COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN I; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 OTHER_DETAILS: CARBONMONOXY; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: HEMOGLOBIN I; COMPND 9 CHAIN: B, D; COMPND 10 ENGINEERED: YES; COMPND 11 MUTATION: YES; COMPND 12 OTHER_DETAILS: CARBONMONOXY SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ONCORHYNCHUS MYKISS; SOURCE 3 ORGANISM_COMMON: TROUT; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: ONCORHYNCHUS MYKISS; SOURCE 6 ORGANISM_COMMON: TROUT; SOURCE 7 TISSUE: BLOOD KEYWDS HEME, OXYGEN TRANSPORT, RESPIRATORY PROTEIN, ERYTHROCYTE EXPDTA X-RAY DIFFRACTION AUTHOR J.TAME,J.WILSON REVDAT 1 11-JAN-97 1OUU 0 JRNL AUTH J.R.TAME,J.C.WILSON,R.E.WEBER JRNL TITL THE CRYSTAL STRUCTURES OF TROUT HB I IN THE DEOXY JRNL TITL 2 AND CARBONMONOXY FORMS. JRNL REF J.MOL.BIOL. V. 259 749 1996 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PROLSQ REMARK 3 AUTHORS : KONNERT,HENDRICKSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 16338 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 + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.162 REMARK 3 FREE R VALUE : 0.286 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA. REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1620 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.286 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL 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 : 163 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.40 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) : 0.25 REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : 0.014 ; 0.025 REMARK 3 ANGLE DISTANCE (A) : 0.033 ; 0.035 REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.038 ; 0.050 REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.112 ; 0.130 REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : 0.199 ; 0.300 REMARK 3 MULTIPLE TORSION (A) : 0.273 ; 0.300 REMARK 3 H-BOND (X...Y) (A) : 0.187 ; 0.300 REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : 2.194 ; 3.000 REMARK 3 STAGGERED (DEGREES) : 22.636; 20.000 REMARK 3 TRANSVERSE (DEGREES) : 34.315; 30.000 REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 3.010 ; 4.000 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.539 ; 6.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 7.200 ; 8.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 9.433 ; 10.000 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1OUU 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 : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : MULTIWIRE AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : SIEMENS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22054 REMARK 200 RESOLUTION RANGE HIGH (A) : NULL 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 (%) : 74.1 REMARK 200 DATA REDUNDANCY : 1.400 REMARK 200 R MERGE (I) : 0.06500 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) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL 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: NULL REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-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 32.60000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.45000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.90000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.45000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.60000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.90000 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 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 N SER C 1 O ACE C 0 2.14 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 VAL D 48 C - N - CA ANGL. DEV. = 20.4 DEGREES REMARK 500 LEU D 110 CA - CB - CG ANGL. DEV. = 18.8 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 141 DISTANCE = 5.93 ANGSTROMS REMARK 525 HOH 149 DISTANCE = 6.04 ANGSTROMS REMARK 525 HOH 155 DISTANCE = 5.38 ANGSTROMS DBREF 1OUU A 1 141 UNP P02019 HBA1_ONCMY 1 143 DBREF 1OUU B 1 146 UNP P02142 HBB1_ONCMY 1 146 DBREF 1OUU C 1 141 UNP P02019 HBA1_ONCMY 1 143 DBREF 1OUU D 1 146 UNP P02142 HBB1_ONCMY 1 146 SEQADV 1OUU A UNP P02019 ASP 32 DELETION SEQADV 1OUU A UNP P02019 LYS 33 DELETION SEQADV 1OUU C UNP P02019 ASP 32 DELETION SEQADV 1OUU C UNP P02019 LYS 33 DELETION SEQRES 1 A 142 SER LEU THR ALA LYS ASP LYS SER VAL VAL LYS ALA PHE SEQRES 2 A 142 TRP GLY LYS ILE SER GLY LYS ALA ASP VAL VAL GLY ALA SEQRES 3 A 142 GLU ALA LEU GLY ARG MET LEU THR ALA TYR PRO GLN THR SEQRES 4 A 142 LYS THR TYR PHE SER HIS TRP ALA ASP LEU SER PRO GLY SEQRES 5 A 142 SER GLY PRO VAL LYS LYS HIS GLY GLY ILE ILE MET GLY SEQRES 6 A 142 ALA ILE GLY LYS ALA VAL GLY LEU MET ASP ASP LEU VAL SEQRES 7 A 142 GLY GLY MET SER ALA LEU SER ASP LEU HIS ALA PHE LYS SEQRES 8 A 142 LEU ARG VAL ASP PRO GLY ASN PHE LYS ILE LEU SER HIS SEQRES 9 A 142 ASN ILE LEU VAL THR LEU ALA ILE HIS PHE PRO SER ASP SEQRES 10 A 142 PHE THR PRO GLU VAL HIS ILE ALA VAL ASP LYS PHE LEU SEQRES 11 A 142 ALA ALA VAL SER ALA ALA LEU ALA ASP LYS TYR ARG SEQRES 1 B 146 VAL GLU TRP THR ASP ALA GLU LYS SER THR ILE SER ALA SEQRES 2 B 146 VAL TRP GLY LYS VAL ASN ILE ASP GLU ILE GLY PRO LEU SEQRES 3 B 146 ALA LEU ALA ARG VAL LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 B 146 ARG TYR PHE GLY SER PHE GLY ASN VAL SER THR PRO ALA SEQRES 5 B 146 ALA ILE MET GLY ASN PRO LYS VAL ALA ALA HIS GLY LYS SEQRES 6 B 146 VAL VAL CYS GLY ALA LEU ASP LYS ALA VAL LYS ASN MET SEQRES 7 B 146 GLY ASN ILE LEU ALA THR TYR LYS SER LEU SER GLU THR SEQRES 8 B 146 HIS ALA ASN LYS LEU PHE VAL ASP PRO ASP ASN PHE ARG SEQRES 9 B 146 VAL LEU ALA ASP VAL LEU THR ILE VAL ILE ALA ALA LYS SEQRES 10 B 146 PHE GLY ALA SER PHE THR PRO GLU ILE GLN ALA THR TRP SEQRES 11 B 146 GLN LYS PHE MET LYS VAL VAL VAL ALA ALA MET GLY SER SEQRES 12 B 146 ARG TYR PHE SEQRES 1 C 142 SER LEU THR ALA LYS ASP LYS SER VAL VAL LYS ALA PHE SEQRES 2 C 142 TRP GLY LYS ILE SER GLY LYS ALA ASP VAL VAL GLY ALA SEQRES 3 C 142 GLU ALA LEU GLY ARG MET LEU THR ALA TYR PRO GLN THR SEQRES 4 C 142 LYS THR TYR PHE SER HIS TRP ALA ASP LEU SER PRO GLY SEQRES 5 C 142 SER GLY PRO VAL LYS LYS HIS GLY GLY ILE ILE MET GLY SEQRES 6 C 142 ALA ILE GLY LYS ALA VAL GLY LEU MET ASP ASP LEU VAL SEQRES 7 C 142 GLY GLY MET SER ALA LEU SER ASP LEU HIS ALA PHE LYS SEQRES 8 C 142 LEU ARG VAL ASP PRO GLY ASN PHE LYS ILE LEU SER HIS SEQRES 9 C 142 ASN ILE LEU VAL THR LEU ALA ILE HIS PHE PRO SER ASP SEQRES 10 C 142 PHE THR PRO GLU VAL HIS ILE ALA VAL ASP LYS PHE LEU SEQRES 11 C 142 ALA ALA VAL SER ALA ALA LEU ALA ASP LYS TYR ARG SEQRES 1 D 146 VAL GLU TRP THR ASP ALA GLU LYS SER THR ILE SER ALA SEQRES 2 D 146 VAL TRP GLY LYS VAL ASN ILE ASP GLU ILE GLY PRO LEU SEQRES 3 D 146 ALA LEU ALA ARG VAL LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 D 146 ARG TYR PHE GLY SER PHE GLY ASN VAL SER THR PRO ALA SEQRES 5 D 146 ALA ILE MET GLY ASN PRO LYS VAL ALA ALA HIS GLY LYS SEQRES 6 D 146 VAL VAL CYS GLY ALA LEU ASP LYS ALA VAL LYS ASN MET SEQRES 7 D 146 GLY ASN ILE LEU ALA THR TYR LYS SER LEU SER GLU THR SEQRES 8 D 146 HIS ALA ASN LYS LEU PHE VAL ASP PRO ASP ASN PHE ARG SEQRES 9 D 146 VAL LEU ALA ASP VAL LEU THR ILE VAL ILE ALA ALA LYS SEQRES 10 D 146 PHE GLY ALA SER PHE THR PRO GLU ILE GLN ALA THR TRP SEQRES 11 D 146 GLN LYS PHE MET LYS VAL VAL VAL ALA ALA MET GLY SER SEQRES 12 D 146 ARG TYR PHE HET ACE A 0 3 HET ACE C 0 3 HET HEM A 143 43 HET CMO A 143 2 HET HEM B 148 43 HET CMO B 148 2 HET HEM C 143 43 HET CMO C 143 2 HET HEM D 148 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 *163(H2 O) HELIX 1 1 ALA A 4 ALA A 35 1 32 HELIX 2 2 PRO A 37 PHE A 43 5 7 HELIX 3 3 GLY A 54 GLY A 72 1 19 HELIX 4 4 LEU A 77 GLY A 80 1 4 HELIX 5 5 SER A 82 PHE A 90 1 9 HELIX 6 6 PRO A 96 HIS A 113 5 18 HELIX 7 7 PRO A 120 LEU A 137 1 18 HELIX 8 8 ASP B 5 LYS B 17 1 13 HELIX 9 9 ILE B 20 VAL B 34 1 15 HELIX 10 10 PRO B 36 TYR B 41 5 6 HELIX 11 11 GLY B 43 PHE B 45 5 3 HELIX 12 12 PRO B 51 MET B 55 1 5 HELIX 13 13 PRO B 58 LYS B 76 1 19 HELIX 14 14 ILE B 81 THR B 84 1 4 HELIX 15 15 LYS B 86 ASN B 94 1 9 HELIX 16 16 PRO B 100 SER B 121 5 22 HELIX 17 17 PRO B 124 ARG B 144 1 21 HELIX 18 18 ALA C 4 ALA C 35 1 32 HELIX 19 19 PRO C 37 PHE C 43 5 7 HELIX 20 20 GLY C 54 LEU C 73 1 20 HELIX 21 21 LEU C 77 GLY C 80 1 4 HELIX 22 22 SER C 82 ALA C 89 1 8 HELIX 23 23 PRO C 96 HIS C 113 5 18 HELIX 24 24 PRO C 120 LEU C 137 1 18 HELIX 25 25 ASP C 139 TYR C 141 5 3 HELIX 26 26 ASP D 5 LYS D 17 1 13 HELIX 27 27 ILE D 20 VAL D 34 1 15 HELIX 28 28 PRO D 36 TYR D 41 5 6 HELIX 29 29 PRO D 51 MET D 55 1 5 HELIX 30 30 PRO D 58 LYS D 76 1 19 HELIX 31 31 ILE D 81 THR D 84 1 4 HELIX 32 32 LYS D 86 ASN D 94 1 9 HELIX 33 33 PRO D 100 SER D 121 5 22 HELIX 34 34 PRO D 124 GLY D 142 1 19 LINK C ACE A 0 N SER A 1 LINK FE HEM A 143 NE2 HIS A 88 LINK FE HEM A 143 C CMO A 143 LINK FE HEM B 148 NE2 HIS B 92 LINK FE HEM B 148 C CMO B 148 LINK C ACE C 0 N SER C 1 LINK FE HEM C 143 NE2 HIS C 88 LINK FE HEM C 143 C CMO C 143 LINK FE HEM D 148 NE2 HIS D 92 LINK FE HEM D 148 C CMO D 148 CRYST1 65.200 79.800 122.900 90.00 90.00 90.00 P 21 21 21 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 0.015337 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012531 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008137 0.00000 MTRIX1 1 -0.997150 0.040610 -0.063590 31.13336 1 MTRIX2 1 0.039690 -0.434470 -0.899810 99.73560 1 MTRIX3 1 -0.064170 -0.899770 0.431620 63.99959 1 MTRIX1 2 -0.997530 0.051480 -0.047840 30.20762 1 MTRIX2 2 0.020180 -0.442250 -0.896660 100.33498 1 MTRIX3 2 -0.067320 -0.895410 0.440120 63.57013 1