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HEADER METAL BINDING PROTEIN 12-JAN-99 3LHB TITLE THE 2.7 ANGSTROM CRYSTAL STRUCTURE OF DEOXYGENATED TITLE 2 HEMOGLOBIN FROM THE SEA LAMPREY (PETROMYZON MARINUS) COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (HEMOGLOBIN); COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PETROMYZON MARINUS; SOURCE 3 ORGANISM_COMMON: SEA LAMPREY; SOURCE 4 CELL: RED BLOOD CELL; SOURCE 5 CELLULAR_LOCATION: CYTOPLASM; SOURCE 6 OTHER_DETAILS: COMPONENT FIVE(5) OF SIX(6) HEMOGLOBINS SOURCE 7 ISOLATED FROM P.MARINUS. KEYWDS HEMOGLOBIN, OXYGEN TRANSPORT, BOHR EFFECT EXPDTA X-RAY DIFFRACTION AUTHOR H.A.HEASLET,W.E.ROYER JR. REVDAT 3 24-AUG-04 3LHB 1 TITLE JRNL REMARK LINK REVDAT 3 2 1 SITE KEYWDS MASTER AUTHOR REVDAT 2 22-DEC-99 3LHB 4 HEADER COMPND REMARK JRNL REVDAT 2 2 4 ATOM SOURCE SEQRES REVDAT 1 20-JAN-99 3LHB 0 JRNL AUTH H.A.HEASLET,W.E.ROYER JR. JRNL TITL THE 2.7 A CRYSTAL STRUCTURE OF DEOXYGENATED JRNL TITL 2 HEMOGLOBIN FROM THE SEA LAMPREY (PETROMYZON JRNL TITL 3 MARINUS): STRUCTURAL BASIS FOR A LOWERED OXYGEN JRNL TITL 4 AFFINITY AND BOHR EFFECT. JRNL REF STRUCTURE FOLD.DES. V. 7 517 1999 JRNL REFN ASTM FODEFH UK ISSN 0969-2126 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.B.HONZATKO,W.A.HENDRICKSON,W.E.LOVE REMARK 1 TITL REFINEMENT OF A MOLCULAR MODEL FOR LAMPREY REMARK 1 TITL 2 HEMOGLOBIN FROM PETROMYZON MARINUS REMARK 1 REF J.MOL.BIOL. V. 184 147 1985 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REFERENCE 2 REMARK 1 AUTH W.A.HENDRICKSON,W.E.LOVE REMARK 1 TITL STRUCTURE OF LAMPREY HEMOGLOBIN REMARK 1 REF NATURE NEW BIOL. V. 232 197 1971 REMARK 1 REFN ASTM NNBYA7 UK ISSN 0369-4887 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00 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) (%) : 94.7 REMARK 3 NUMBER OF REFLECTIONS : 49184 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) : 0.195 REMARK 3 FREE R VALUE : 0.232 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 11.400 REMARK 3 FREE R VALUE TEST SET COUNT : 5599 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 : 8 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.80 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.20 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3678 REMARK 3 BIN R VALUE (WORKING SET) : 0.2870 REMARK 3 BIN FREE R VALUE : 0.3290 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.90 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 449 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 : 13728 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 516 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.50 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) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 1.36 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : 1.26 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : GROUP THERMAL FACTORS 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 : RESTRAINTS REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : 1.5 ; 300 REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO REMARK 3 PARAMETER FILE 2 : PARAM19X.HEME REMARK 3 PARAMETER FILE 3 : PARAM19.SOL REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : TOPH19X.HEME REMARK 3 TOPOLOGY FILE 3 : TOPH19.SOL REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3LHB 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 (2007-03-18) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB008056. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-DEC-1997 REMARK 200 TEMPERATURE (KELVIN) : 293.1 REMARK 200 PH : 6.80 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 : RIGAKU RU200 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.54 REMARK 200 MONOCHROMATOR : GRAPHITE REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49184 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 10.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7 REMARK 200 DATA REDUNDANCY : 3.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.07600 REMARK 200 FOR THE DATA SET : 12.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80 REMARK 200 COMPLETENESS FOR SHELL (%) : 87.2 REMARK 200 DATA REDUNDANCY IN SHELL : 3.00 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.42200 REMARK 200 FOR SHELL : 2.700 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: 2LHB REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.8 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 107.58000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 12CHAIN(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 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 BIOMOLECULE: 3 REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F 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 BIOMOLECULE: 4 REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H 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 BIOMOLECULE: 5 REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J 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 BIOMOLECULE: 6 REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L 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 LYS B 56 NH1 ARG C 20 2.18 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 88 CB MET A 88 CG -0.043 REMARK 500 MET A 88 CG MET A 88 SD -0.041 REMARK 500 MET A 94 SD MET A 94 CE -0.048 REMARK 500 MET A 140 SD MET A 140 CE 0.045 REMARK 500 PRO B 1 CG PRO B 1 CD 0.040 REMARK 500 ILE B 2 CG1 ILE B 2 CD1 -0.051 REMARK 500 MET B 94 SD MET B 94 CE -0.041 REMARK 500 MET B 96 SD MET B 96 CE -0.049 REMARK 500 MET B 138 SD MET B 138 CE -0.074 REMARK 500 MET C 138 SD MET C 138 CE -0.040 REMARK 500 MET E 88 SD MET E 88 CE -0.051 REMARK 500 MET E 140 SD MET E 140 CE -0.046 REMARK 500 MET F 94 SD MET F 94 CE -0.050 REMARK 500 MET G 88 SD MET G 88 CE -0.043 REMARK 500 MET G 138 SD MET G 138 CE -0.054 REMARK 500 MET I 94 SD MET I 94 CE -0.076 REMARK 500 MET L 94 SD MET L 94 CE -0.042 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 LYS A 107 N - CA - C ANGL. DEV. = 6.9 DEGREES REMARK 500 LYS B 107 N - CA - C ANGL. DEV. = 6.3 DEGREES REMARK 500 LEU D 58 CA - CB - CG ANGL. DEV. = 6.6 DEGREES REMARK 500 LYS D 107 N - CA - C ANGL. DEV. = 6.6 DEGREES REMARK 500 LYS E 107 N - CA - C ANGL. DEV. = 6.5 DEGREES REMARK 500 LYS F 107 N - CA - C ANGL. DEV. = 6.5 DEGREES REMARK 500 SER G 108 N - CA - C ANGL. DEV. = 6.6 DEGREES REMARK 500 LYS H 107 N - CA - C ANGL. DEV. = 6.8 DEGREES REMARK 500 LYS I 107 N - CA - C ANGL. DEV. = 6.5 DEGREES REMARK 500 LYS J 107 N - CA - C ANGL. DEV. = 6.3 DEGREES REMARK 500 LYS K 107 N - CA - C ANGL. DEV. = 6.5 DEGREES REMARK 500 LYS L 107 N - CA - C ANGL. DEV. = 6.5 DEGREES REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: FE1 REMARK 800 SITE_DESCRIPTION: HIS 73 IS THE PROXIMAL HISTIDINE AND HIS 105 REMARK 800 IS THE DISTAL HISTIDINE REMARK 800 SITE_IDENTIFIER: FE2 REMARK 800 SITE_DESCRIPTION: HIS 73 IS THE PROXIMAL HISTIDINE AND HIS REMARK 800 105 IS THE DISTAL HISTIDINE REMARK 800 SITE_IDENTIFIER: FE3 REMARK 800 SITE_DESCRIPTION: HIS 73 IS THE PROXIMAL HISTIDINE AND HIS REMARK 800 105 IS THE DISTAL HISTIDINE REMARK 800 SITE_IDENTIFIER: FE4 REMARK 800 SITE_DESCRIPTION: HIS 73 IS THE PROXIMAL HISTIDINE AND HIS REMARK 800 105 IS THE DISTAL HISTIDINE REMARK 800 SITE_IDENTIFIER: FE5 REMARK 800 SITE_DESCRIPTION: HIS 73 IS THE PROXIMAL HISTIDINE AND HIS REMARK 800 105 IS THE DISTAL HISTIDINE REMARK 800 SITE_IDENTIFIER: FE6 REMARK 800 SITE_DESCRIPTION: HIS 73 IS THE PROXIMAL HISTIDINE AND HIS REMARK 800 105 IS THE DISTAL HISTIDINE REMARK 800 SITE_IDENTIFIER: FE7 REMARK 800 SITE_DESCRIPTION: HIS 73 IS THE PROXIMAL HISTIDINE AND HIS REMARK 800 105 IS THE DISTAL HISTIDINE REMARK 800 SITE_IDENTIFIER: FE8 REMARK 800 SITE_DESCRIPTION: HIS 73 IS THE PROXIMAL HISTIDINE AND HIS REMARK 800 105 IS THE DISTAL HISTIDINE REMARK 800 SITE_IDENTIFIER: FE9 REMARK 800 SITE_DESCRIPTION: HIS 73 IS THE PROXIMAL HISTIDINE AND HIS REMARK 800 105 IS THE DISTAL HISTIDINE REMARK 800 SITE_IDENTIFIER: F10 REMARK 800 SITE_DESCRIPTION: HIS 73 IS THE PROXIMAL HISTIDINE AND HIS REMARK 800 105 IS THE DISTAL HISTIDINE REMARK 800 SITE_IDENTIFIER: F11 REMARK 800 SITE_DESCRIPTION: HIS 73 IS THE PROXIMAL HISTIDINE AND HIS REMARK 800 105 IS THE DISTAL HISTIDINE REMARK 800 SITE_IDENTIFIER: F12 REMARK 800 SITE_DESCRIPTION: HIS 73 IS THE PROXIMAL HISTIDINE AND HIS REMARK 800 105 IS THE DISTAL HISTIDINE DBREF 3LHB A 1 149 UNP P02208 GLB5_PETMA 1 149 DBREF 3LHB B 1 149 UNP P02208 GLB5_PETMA 1 149 DBREF 3LHB C 1 149 UNP P02208 GLB5_PETMA 1 149 DBREF 3LHB D 1 149 UNP P02208 GLB5_PETMA 1 149 DBREF 3LHB E 1 149 UNP P02208 GLB5_PETMA 1 149 DBREF 3LHB F 1 149 UNP P02208 GLB5_PETMA 1 149 DBREF 3LHB G 1 149 UNP P02208 GLB5_PETMA 1 149 DBREF 3LHB H 1 149 UNP P02208 GLB5_PETMA 1 149 DBREF 3LHB I 1 149 UNP P02208 GLB5_PETMA 1 149 DBREF 3LHB J 1 149 UNP P02208 GLB5_PETMA 1 149 DBREF 3LHB K 1 149 UNP P02208 GLB5_PETMA 1 149 DBREF 3LHB L 1 149 UNP P02208 GLB5_PETMA 1 149 SEQADV 3LHB GLU A 63 UNP P02208 GLN 63 CONFLICT SEQADV 3LHB ASP A 82 UNP P02208 ASN 82 CONFLICT SEQADV 3LHB ASN A 100 UNP P02208 ASP 100 CONFLICT SEQADV 3LHB GLU A 114 UNP P02208 GLN 114 CONFLICT SEQADV 3LHB GLU B 63 UNP P02208 GLN 63 CONFLICT SEQADV 3LHB ASP B 82 UNP P02208 ASN 82 CONFLICT SEQADV 3LHB ASN B 100 UNP P02208 ASP 100 CONFLICT SEQADV 3LHB GLU B 114 UNP P02208 GLN 114 CONFLICT SEQADV 3LHB GLU C 63 UNP P02208 GLN 63 CONFLICT SEQADV 3LHB ASP C 82 UNP P02208 ASN 82 CONFLICT SEQADV 3LHB ASN C 100 UNP P02208 ASP 100 CONFLICT SEQADV 3LHB GLU C 114 UNP P02208 GLN 114 CONFLICT SEQADV 3LHB GLU D 63 UNP P02208 GLN 63 CONFLICT SEQADV 3LHB ASP D 82 UNP P02208 ASN 82 CONFLICT SEQADV 3LHB ASN D 100 UNP P02208 ASP 100 CONFLICT SEQADV 3LHB GLU D 114 UNP P02208 GLN 114 CONFLICT SEQADV 3LHB GLU E 63 UNP P02208 GLN 63 CONFLICT SEQADV 3LHB ASP E 82 UNP P02208 ASN 82 CONFLICT SEQADV 3LHB ASN E 100 UNP P02208 ASP 100 CONFLICT SEQADV 3LHB GLU E 114 UNP P02208 GLN 114 CONFLICT SEQADV 3LHB GLU F 63 UNP P02208 GLN 63 CONFLICT SEQADV 3LHB ASP F 82 UNP P02208 ASN 82 CONFLICT SEQADV 3LHB ASN F 100 UNP P02208 ASP 100 CONFLICT SEQADV 3LHB GLU F 114 UNP P02208 GLN 114 CONFLICT SEQADV 3LHB GLU G 63 UNP P02208 GLN 63 CONFLICT SEQADV 3LHB ASP G 82 UNP P02208 ASN 82 CONFLICT SEQADV 3LHB ASN G 100 UNP P02208 ASP 100 CONFLICT SEQADV 3LHB GLU G 114 UNP P02208 GLN 114 CONFLICT SEQADV 3LHB GLU H 63 UNP P02208 GLN 63 CONFLICT SEQADV 3LHB ASP H 82 UNP P02208 ASN 82 CONFLICT SEQADV 3LHB ASN H 100 UNP P02208 ASP 100 CONFLICT SEQADV 3LHB GLU H 114 UNP P02208 GLN 114 CONFLICT SEQADV 3LHB GLU I 63 UNP P02208 GLN 63 CONFLICT SEQADV 3LHB ASP I 82 UNP P02208 ASN 82 CONFLICT SEQADV 3LHB ASN I 100 UNP P02208 ASP 100 CONFLICT SEQADV 3LHB GLU I 114 UNP P02208 GLN 114 CONFLICT SEQADV 3LHB GLU J 63 UNP P02208 GLN 63 CONFLICT SEQADV 3LHB ASP J 82 UNP P02208 ASN 82 CONFLICT SEQADV 3LHB ASN J 100 UNP P02208 ASP 100 CONFLICT SEQADV 3LHB GLU J 114 UNP P02208 GLN 114 CONFLICT SEQADV 3LHB GLU K 63 UNP P02208 GLN 63 CONFLICT SEQADV 3LHB ASP K 82 UNP P02208 ASN 82 CONFLICT SEQADV 3LHB ASN K 100 UNP P02208 ASP 100 CONFLICT SEQADV 3LHB GLU K 114 UNP P02208 GLN 114 CONFLICT SEQADV 3LHB GLU L 63 UNP P02208 GLN 63 CONFLICT SEQADV 3LHB ASP L 82 UNP P02208 ASN 82 CONFLICT SEQADV 3LHB ASN L 100 UNP P02208 ASP 100 CONFLICT SEQADV 3LHB GLU L 114 UNP P02208 GLN 114 CONFLICT SEQRES 1 A 149 PRO ILE VAL ASP THR GLY SER VAL ALA PRO LEU SER ALA SEQRES 2 A 149 ALA GLU LYS THR LYS ILE ARG SER ALA TRP ALA PRO VAL SEQRES 3 A 149 TYR SER THR TYR GLU THR SER GLY VAL ASP ILE LEU VAL SEQRES 4 A 149 LYS PHE PHE THR SER THR PRO ALA ALA GLN GLU PHE PHE SEQRES 5 A 149 PRO LYS PHE LYS GLY LEU THR THR ALA ASP GLU LEU LYS SEQRES 6 A 149 LYS SER ALA ASP VAL ARG TRP HIS ALA GLU ARG ILE ILE SEQRES 7 A 149 ASN ALA VAL ASP ASP ALA VAL ALA SER MET ASP ASP THR SEQRES 8 A 149 GLU LYS MET SER MET LYS LEU ARG ASN LEU SER GLY LYS SEQRES 9 A 149 HIS ALA LYS SER PHE GLN VAL ASP PRO GLU TYR PHE LYS SEQRES 10 A 149 VAL LEU ALA ALA VAL ILE ALA ASP THR VAL ALA ALA GLY SEQRES 11 A 149 ASP ALA GLY PHE GLU LYS LEU MET SER MET ILE CYS ILE SEQRES 12 A 149 LEU LEU ARG SER ALA TYR SEQRES 1 B 149 PRO ILE VAL ASP THR GLY SER VAL ALA PRO LEU SER ALA SEQRES 2 B 149 ALA GLU LYS THR LYS ILE ARG SER ALA TRP ALA PRO VAL SEQRES 3 B 149 TYR SER THR TYR GLU THR SER GLY VAL ASP ILE LEU VAL SEQRES 4 B 149 LYS PHE PHE THR SER THR PRO ALA ALA GLN GLU PHE PHE SEQRES 5 B 149 PRO LYS PHE LYS GLY LEU THR THR ALA ASP GLU LEU LYS SEQRES 6 B 149 LYS SER ALA ASP VAL ARG TRP HIS ALA GLU ARG ILE ILE SEQRES 7 B 149 ASN ALA VAL ASP ASP ALA VAL ALA SER MET ASP ASP THR SEQRES 8 B 149 GLU LYS MET SER MET LYS LEU ARG ASN LEU SER GLY LYS SEQRES 9 B 149 HIS ALA LYS SER PHE GLN VAL ASP PRO GLU TYR PHE LYS SEQRES 10 B 149 VAL LEU ALA ALA VAL ILE ALA ASP THR VAL ALA ALA GLY SEQRES 11 B 149 ASP ALA GLY PHE GLU LYS LEU MET SER MET ILE CYS ILE SEQRES 12 B 149 LEU LEU ARG SER ALA TYR SEQRES 1 C 149 PRO ILE VAL ASP THR GLY SER VAL ALA PRO LEU SER ALA SEQRES 2 C 149 ALA GLU LYS THR LYS ILE ARG SER ALA TRP ALA PRO VAL SEQRES 3 C 149 TYR SER THR TYR GLU THR SER GLY VAL ASP ILE LEU VAL SEQRES 4 C 149 LYS PHE PHE THR SER THR PRO ALA ALA GLN GLU PHE PHE SEQRES 5 C 149 PRO LYS PHE LYS GLY LEU THR THR ALA ASP GLU LEU LYS SEQRES 6 C 149 LYS SER ALA ASP VAL ARG TRP HIS ALA GLU ARG ILE ILE SEQRES 7 C 149 ASN ALA VAL ASP ASP ALA VAL ALA SER MET ASP ASP THR SEQRES 8 C 149 GLU LYS MET SER MET LYS LEU ARG ASN LEU SER GLY LYS SEQRES 9 C 149 HIS ALA LYS SER PHE GLN VAL ASP PRO GLU TYR PHE LYS SEQRES 10 C 149 VAL LEU ALA ALA VAL ILE ALA ASP THR VAL ALA ALA GLY SEQRES 11 C 149 ASP ALA GLY PHE GLU LYS LEU MET SER MET ILE CYS ILE SEQRES 12 C 149 LEU LEU ARG SER ALA TYR SEQRES 1 D 149 PRO ILE VAL ASP THR GLY SER VAL ALA PRO LEU SER ALA SEQRES 2 D 149 ALA GLU LYS THR LYS ILE ARG SER ALA TRP ALA PRO VAL SEQRES 3 D 149 TYR SER THR TYR GLU THR SER GLY VAL ASP ILE LEU VAL SEQRES 4 D 149 LYS PHE PHE THR SER THR PRO ALA ALA GLN GLU PHE PHE SEQRES 5 D 149 PRO LYS PHE LYS GLY LEU THR THR ALA ASP GLU LEU LYS SEQRES 6 D 149 LYS SER ALA ASP VAL ARG TRP HIS ALA GLU ARG ILE ILE SEQRES 7 D 149 ASN ALA VAL ASP ASP ALA VAL ALA SER MET ASP ASP THR SEQRES 8 D 149 GLU LYS MET SER MET LYS LEU ARG ASN LEU SER GLY LYS SEQRES 9 D 149 HIS ALA LYS SER PHE GLN VAL ASP PRO GLU TYR PHE LYS SEQRES 10 D 149 VAL LEU ALA ALA VAL ILE ALA ASP THR VAL ALA ALA GLY SEQRES 11 D 149 ASP ALA GLY PHE GLU LYS LEU MET SER MET ILE CYS ILE SEQRES 12 D 149 LEU LEU ARG SER ALA TYR SEQRES 1 E 149 PRO ILE VAL ASP THR GLY SER VAL ALA PRO LEU SER ALA SEQRES 2 E 149 ALA GLU LYS THR LYS ILE ARG SER ALA TRP ALA PRO VAL SEQRES 3 E 149 TYR SER THR TYR GLU THR SER GLY VAL ASP ILE LEU VAL SEQRES 4 E 149 LYS PHE PHE THR SER THR PRO ALA ALA GLN GLU PHE PHE SEQRES 5 E 149 PRO LYS PHE LYS GLY LEU THR THR ALA ASP GLU LEU LYS SEQRES 6 E 149 LYS SER ALA ASP VAL ARG TRP HIS ALA GLU ARG ILE ILE SEQRES 7 E 149 ASN ALA VAL ASP ASP ALA VAL ALA SER MET ASP ASP THR SEQRES 8 E 149 GLU LYS MET SER MET LYS LEU ARG ASN LEU SER GLY LYS SEQRES 9 E 149 HIS ALA LYS SER PHE GLN VAL ASP PRO GLU TYR PHE LYS SEQRES 10 E 149 VAL LEU ALA ALA VAL ILE ALA ASP THR VAL ALA ALA GLY SEQRES 11 E 149 ASP ALA GLY PHE GLU LYS LEU MET SER MET ILE CYS ILE SEQRES 12 E 149 LEU LEU ARG SER ALA TYR SEQRES 1 F 149 PRO ILE VAL ASP THR GLY SER VAL ALA PRO LEU SER ALA SEQRES 2 F 149 ALA GLU LYS THR LYS ILE ARG SER ALA TRP ALA PRO VAL SEQRES 3 F 149 TYR SER THR TYR GLU THR SER GLY VAL ASP ILE LEU VAL SEQRES 4 F 149 LYS PHE PHE THR SER THR PRO ALA ALA GLN GLU PHE PHE SEQRES 5 F 149 PRO LYS PHE LYS GLY LEU THR THR ALA ASP GLU LEU LYS SEQRES 6 F 149 LYS SER ALA ASP VAL ARG TRP HIS ALA GLU ARG ILE ILE SEQRES 7 F 149 ASN ALA VAL ASP ASP ALA VAL ALA SER MET ASP ASP THR SEQRES 8 F 149 GLU LYS MET SER MET LYS LEU ARG ASN LEU SER GLY LYS SEQRES 9 F 149 HIS ALA LYS SER PHE GLN VAL ASP PRO GLU TYR PHE LYS SEQRES 10 F 149 VAL LEU ALA ALA VAL ILE ALA ASP THR VAL ALA ALA GLY SEQRES 11 F 149 ASP ALA GLY PHE GLU LYS LEU MET SER MET ILE CYS ILE SEQRES 12 F 149 LEU LEU ARG SER ALA TYR SEQRES 1 G 149 PRO ILE VAL ASP THR GLY SER VAL ALA PRO LEU SER ALA SEQRES 2 G 149 ALA GLU LYS THR LYS ILE ARG SER ALA TRP ALA PRO VAL SEQRES 3 G 149 TYR SER THR TYR GLU THR SER GLY VAL ASP ILE LEU VAL SEQRES 4 G 149 LYS PHE PHE THR SER THR PRO ALA ALA GLN GLU PHE PHE SEQRES 5 G 149 PRO LYS PHE LYS GLY LEU THR THR ALA ASP GLU LEU LYS SEQRES 6 G 149 LYS SER ALA ASP VAL ARG TRP HIS ALA GLU ARG ILE ILE SEQRES 7 G 149 ASN ALA VAL ASP ASP ALA VAL ALA SER MET ASP ASP THR SEQRES 8 G 149 GLU LYS MET SER MET LYS LEU ARG ASN LEU SER GLY LYS SEQRES 9 G 149 HIS ALA LYS SER PHE GLN VAL ASP PRO GLU TYR PHE LYS SEQRES 10 G 149 VAL LEU ALA ALA VAL ILE ALA ASP THR VAL ALA ALA GLY SEQRES 11 G 149 ASP ALA GLY PHE GLU LYS LEU MET SER MET ILE CYS ILE SEQRES 12 G 149 LEU LEU ARG SER ALA TYR SEQRES 1 H 149 PRO ILE VAL ASP THR GLY SER VAL ALA PRO LEU SER ALA SEQRES 2 H 149 ALA GLU LYS THR LYS ILE ARG SER ALA TRP ALA PRO VAL SEQRES 3 H 149 TYR SER THR TYR GLU THR SER GLY VAL ASP ILE LEU VAL SEQRES 4 H 149 LYS PHE PHE THR SER THR PRO ALA ALA GLN GLU PHE PHE SEQRES 5 H 149 PRO LYS PHE LYS GLY LEU THR THR ALA ASP GLU LEU LYS SEQRES 6 H 149 LYS SER ALA ASP VAL ARG TRP HIS ALA GLU ARG ILE ILE SEQRES 7 H 149 ASN ALA VAL ASP ASP ALA VAL ALA SER MET ASP ASP THR SEQRES 8 H 149 GLU LYS MET SER MET LYS LEU ARG ASN LEU SER GLY LYS SEQRES 9 H 149 HIS ALA LYS SER PHE GLN VAL ASP PRO GLU TYR PHE LYS SEQRES 10 H 149 VAL LEU ALA ALA VAL ILE ALA ASP THR VAL ALA ALA GLY SEQRES 11 H 149 ASP ALA GLY PHE GLU LYS LEU MET SER MET ILE CYS ILE SEQRES 12 H 149 LEU LEU ARG SER ALA TYR SEQRES 1 I 149 PRO ILE VAL ASP THR GLY SER VAL ALA PRO LEU SER ALA SEQRES 2 I 149 ALA GLU LYS THR LYS ILE ARG SER ALA TRP ALA PRO VAL SEQRES 3 I 149 TYR SER THR TYR GLU THR SER GLY VAL ASP ILE LEU VAL SEQRES 4 I 149 LYS PHE PHE THR SER THR PRO ALA ALA GLN GLU PHE PHE SEQRES 5 I 149 PRO LYS PHE LYS GLY LEU THR THR ALA ASP GLU LEU LYS SEQRES 6 I 149 LYS SER ALA ASP VAL ARG TRP HIS ALA GLU ARG ILE ILE SEQRES 7 I 149 ASN ALA VAL ASP ASP ALA VAL ALA SER MET ASP ASP THR SEQRES 8 I 149 GLU LYS MET SER MET LYS LEU ARG ASN LEU SER GLY LYS SEQRES 9 I 149 HIS ALA LYS SER PHE GLN VAL ASP PRO GLU TYR PHE LYS SEQRES 10 I 149 VAL LEU ALA ALA VAL ILE ALA ASP THR VAL ALA ALA GLY SEQRES 11 I 149 ASP ALA GLY PHE GLU LYS LEU MET SER MET ILE CYS ILE SEQRES 12 I 149 LEU LEU ARG SER ALA TYR SEQRES 1 J 149 PRO ILE VAL ASP THR GLY SER VAL ALA PRO LEU SER ALA SEQRES 2 J 149 ALA GLU LYS THR LYS ILE ARG SER ALA TRP ALA PRO VAL SEQRES 3 J 149 TYR SER THR TYR GLU THR SER GLY VAL ASP ILE LEU VAL SEQRES 4 J 149 LYS PHE PHE THR SER THR PRO ALA ALA GLN GLU PHE PHE SEQRES 5 J 149 PRO LYS PHE LYS GLY LEU THR THR ALA ASP GLU LEU LYS SEQRES 6 J 149 LYS SER ALA ASP VAL ARG TRP HIS ALA GLU ARG ILE ILE SEQRES 7 J 149 ASN ALA VAL ASP ASP ALA VAL ALA SER MET ASP ASP THR SEQRES 8 J 149 GLU LYS MET SER MET LYS LEU ARG ASN LEU SER GLY LYS SEQRES 9 J 149 HIS ALA LYS SER PHE GLN VAL ASP PRO GLU TYR PHE LYS SEQRES 10 J 149 VAL LEU ALA ALA VAL ILE ALA ASP THR VAL ALA ALA GLY SEQRES 11 J 149 ASP ALA GLY PHE GLU LYS LEU MET SER MET ILE CYS ILE SEQRES 12 J 149 LEU LEU ARG SER ALA TYR SEQRES 1 K 149 PRO ILE VAL ASP THR GLY SER VAL ALA PRO LEU SER ALA SEQRES 2 K 149 ALA GLU LYS THR LYS ILE ARG SER ALA TRP ALA PRO VAL SEQRES 3 K 149 TYR SER THR TYR GLU THR SER GLY VAL ASP ILE LEU VAL SEQRES 4 K 149 LYS PHE PHE THR SER THR PRO ALA ALA GLN GLU PHE PHE SEQRES 5 K 149 PRO LYS PHE LYS GLY LEU THR THR ALA ASP GLU LEU LYS SEQRES 6 K 149 LYS SER ALA ASP VAL ARG TRP HIS ALA GLU ARG ILE ILE SEQRES 7 K 149 ASN ALA VAL ASP ASP ALA VAL ALA SER MET ASP ASP THR SEQRES 8 K 149 GLU LYS MET SER MET LYS LEU ARG ASN LEU SER GLY LYS SEQRES 9 K 149 HIS ALA LYS SER PHE GLN VAL ASP PRO GLU TYR PHE LYS SEQRES 10 K 149 VAL LEU ALA ALA VAL ILE ALA ASP THR VAL ALA ALA GLY SEQRES 11 K 149 ASP ALA GLY PHE GLU LYS LEU MET SER MET ILE CYS ILE SEQRES 12 K 149 LEU LEU ARG SER ALA TYR SEQRES 1 L 149 PRO ILE VAL ASP THR GLY SER VAL ALA PRO LEU SER ALA SEQRES 2 L 149 ALA GLU LYS THR LYS ILE ARG SER ALA TRP ALA PRO VAL SEQRES 3 L 149 TYR SER THR TYR GLU THR SER GLY VAL ASP ILE LEU VAL SEQRES 4 L 149 LYS PHE PHE THR SER THR PRO ALA ALA GLN GLU PHE PHE SEQRES 5 L 149 PRO LYS PHE LYS GLY LEU THR THR ALA ASP GLU LEU LYS SEQRES 6 L 149 LYS SER ALA ASP VAL ARG TRP HIS ALA GLU ARG ILE ILE SEQRES 7 L 149 ASN ALA VAL ASP ASP ALA VAL ALA SER MET ASP ASP THR SEQRES 8 L 149 GLU LYS MET SER MET LYS LEU ARG ASN LEU SER GLY LYS SEQRES 9 L 149 HIS ALA LYS SER PHE GLN VAL ASP PRO GLU TYR PHE LYS SEQRES 10 L 149 VAL LEU ALA ALA VAL ILE ALA ASP THR VAL ALA ALA GLY SEQRES 11 L 149 ASP ALA GLY PHE GLU LYS LEU MET SER MET ILE CYS ILE SEQRES 12 L 149 LEU LEU ARG SER ALA TYR HET HEM A 150 43 HET HEM B 150 43 HET HEM C 150 43 HET HEM D 150 43 HET HEM E 150 43 HET HEM F 150 43 HET HEM G 150 43 HET HEM H 150 43 HET HEM I 150 43 HET HEM J 150 43 HET HEM K 150 43 HET HEM L 150 43 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 13 HEM 12(C34 H32 FE N4 O4) HELIX 1 1 SER A 12 THR A 29 1 18 HELIX 2 2 THR A 29 THR A 45 1 17 HELIX 3 3 PRO A 46 LYS A 56 5 11 HELIX 4 4 THR A 60 SER A 67 1 8 HELIX 5 5 SER A 67 SER A 87 1 21 HELIX 6 6 ASP A 90 SER A 108 1 19 HELIX 7 7 ASP A 112 GLU A 114 5 3 HELIX 8 8 TYR A 115 ALA A 129 1 15 HELIX 9 9 ASP A 131 SER A 147 1 17 HELIX 10 10 SER B 12 THR B 29 1 18 HELIX 11 11 THR B 29 THR B 45 1 17 HELIX 12 12 PRO B 46 PHE B 52 5 7 HELIX 13 13 PHE B 52 LYS B 56 5 5 HELIX 14 14 THR B 60 SER B 67 1 8 HELIX 15 15 SER B 67 SER B 87 1 21 HELIX 16 16 ASP B 90 SER B 108 1 19 HELIX 17 17 ASP B 112 GLU B 114 5 3 HELIX 18 18 TYR B 115 ALA B 129 1 15 HELIX 19 19 ASP B 131 SER B 147 1 17 HELIX 20 20 SER C 12 THR C 29 1 18 HELIX 21 21 THR C 29 THR C 45 1 17 HELIX 22 22 PRO C 46 PHE C 52 5 7 HELIX 23 23 PHE C 52 LYS C 56 5 5 HELIX 24 24 THR C 60 SER C 67 1 8 HELIX 25 25 SER C 67 SER C 87 1 21 HELIX 26 26 ASP C 90 SER C 108 1 19 HELIX 27 27 ASP C 112 GLU C 114 5 3 HELIX 28 28 TYR C 115 ALA C 129 1 15 HELIX 29 29 ASP C 131 ARG C 146 1 16 HELIX 30 30 SER D 12 THR D 29 1 18 HELIX 31 31 THR D 29 THR D 45 1 17 HELIX 32 32 PRO D 46 LYS D 56 5 11 HELIX 33 33 THR D 60 SER D 67 1 8 HELIX 34 34 SER D 67 SER D 87 1 21 HELIX 35 35 ASP D 90 SER D 108 1 19 HELIX 36 36 ASP D 112 GLU D 114 5 3 HELIX 37 37 TYR D 115 ALA D 129 1 15 HELIX 38 38 ASP D 131 ARG D 146 1 16 HELIX 39 39 SER E 12 THR E 29 1 18 HELIX 40 40 THR E 29 THR E 45 1 17 HELIX 41 41 PRO E 46 PHE E 52 5 7 HELIX 42 42 PHE E 52 LYS E 56 5 5 HELIX 43 43 THR E 60 SER E 67 1 8 HELIX 44 44 SER E 67 SER E 87 1 21 HELIX 45 45 ASP E 90 SER E 108 1 19 HELIX 46 46 ASP E 112 GLU E 114 5 3 HELIX 47 47 TYR E 115 ALA E 129 1 15 HELIX 48 48 ASP E 131 ARG E 146 1 16 HELIX 49 49 SER F 12 THR F 29 1 18 HELIX 50 50 THR F 29 THR F 45 1 17 HELIX 51 51 PRO F 46 PHE F 52 5 7 HELIX 52 52 PHE F 52 LYS F 56 5 5 HELIX 53 53 THR F 60 SER F 67 1 8 HELIX 54 54 SER F 67 SER F 87 1 21 HELIX 55 55 ASP F 90 SER F 108 1 19 HELIX 56 56 ASP F 112 GLU F 114 5 3 HELIX 57 57 TYR F 115 ALA F 129 1 15 HELIX 58 58 ASP F 131 SER F 147 1 17 HELIX 59 59 SER G 12 THR G 29 1 18 HELIX 60 60 THR G 29 THR G 45 1 17 HELIX 61 61 PRO G 46 PHE G 52 5 7 HELIX 62 62 PHE G 52 LYS G 56 5 5 HELIX 63 63 THR G 60 SER G 67 1 8 HELIX 64 64 SER G 67 SER G 87 1 21 HELIX 65 65 ASP G 90 SER G 108 1 19 HELIX 66 66 ASP G 112 GLU G 114 5 3 HELIX 67 67 TYR G 115 ALA G 129 1 15 HELIX 68 68 ASP G 131 SER G 147 1 17 HELIX 69 69 SER H 12 THR H 29 1 18 HELIX 70 70 THR H 29 THR H 45 1 17 HELIX 71 71 PRO H 46 LYS H 56 5 11 HELIX 72 72 THR H 60 SER H 67 1 8 HELIX 73 73 SER H 67 SER H 87 1 21 HELIX 74 74 ASP H 90 SER H 108 1 19 HELIX 75 75 ASP H 112 GLU H 114 5 3 HELIX 76 76 TYR H 115 ALA H 129 1 15 HELIX 77 77 ASP H 131 SER H 147 1 17 HELIX 78 78 SER I 12 THR I 29 1 18 HELIX 79 79 THR I 29 THR I 45 1 17 HELIX 80 80 PRO I 46 PHE I 52 5 7 HELIX 81 81 PHE I 52 LYS I 56 5 5 HELIX 82 82 THR I 60 LYS I 66 1 7 HELIX 83 83 SER I 67 SER I 87 1 21 HELIX 84 84 ASP I 90 SER I 108 1 19 HELIX 85 85 ASP I 112 GLU I 114 5 3 HELIX 86 86 TYR I 115 ALA I 129 1 15 HELIX 87 87 ASP I 131 SER I 147 1 17 HELIX 88 88 SER J 12 THR J 29 1 18 HELIX 89 89 THR J 29 THR J 45 1 17 HELIX 90 90 PRO J 46 PHE J 52 5 7 HELIX 91 91 PHE J 52 LYS J 56 5 5 HELIX 92 92 THR J 60 SER J 67 1 8 HELIX 93 93 SER J 67 SER J 87 1 21 HELIX 94 94 ASP J 90 SER J 108 1 19 HELIX 95 95 ASP J 112 GLU J 114 5 3 HELIX 96 96 TYR J 115 ALA J 129 1 15 HELIX 97 97 ASP J 131 ARG J 146 1 16 HELIX 98 98 SER K 12 THR K 29 1 18 HELIX 99 99 THR K 29 THR K 45 1 17 HELIX 100 100 PRO K 46 PHE K 52 5 7 HELIX 101 101 PHE K 52 LYS K 56 5 5 HELIX 102 102 THR K 60 SER K 67 1 8 HELIX 103 103 SER K 67 SER K 87 1 21 HELIX 104 104 ASP K 90 SER K 108 1 19 HELIX 105 105 ASP K 112 GLU K 114 5 3 HELIX 106 106 TYR K 115 ALA K 129 1 15 HELIX 107 107 ASP K 131 SER K 147 1 17 HELIX 108 108 SER L 12 THR L 29 1 18 HELIX 109 109 THR L 29 THR L 45 1 17 HELIX 110 110 PRO L 46 PHE L 52 5 7 HELIX 111 111 PHE L 52 LYS L 56 5 5 HELIX 112 112 THR L 60 SER L 67 1 8 HELIX 113 113 SER L 67 SER L 87 1 21 HELIX 114 114 ASP L 90 SER L 108 1 19 HELIX 115 115 ASP L 112 GLU L 114 5 3 HELIX 116 116 TYR L 115 ALA L 129 1 15 HELIX 117 117 ASP L 131 SER L 147 1 17 LINK FE HEM B 150 NE2 HIS B 105 LINK NE2 HIS E 105 FE HEM E 150 LINK NE2 HIS C 105 FE HEM C 150 LINK FE HEM F 150 NE2 HIS F 105 LINK FE HEM D 150 NE2 HIS D 105 LINK NE2 HIS A 105 FE HEM A 150 LINK NE2 HIS K 105 FE HEM K 150 LINK FE HEM H 150 NE2 HIS H 105 LINK FE HEM L 150 NE2 HIS L 105 LINK NE2 HIS J 105 FE HEM J 150 LINK FE HEM G 150 NE2 HIS G 105 LINK FE HEM I 150 NE2 HIS I 105 SITE 1 FE1 2 HIS A 73 HIS A 105 SITE 1 FE2 2 HIS B 73 HIS B 105 SITE 1 FE3 2 HIS C 73 HIS C 105 SITE 1 FE4 2 HIS D 73 HIS D 105 SITE 1 FE5 2 HIS E 73 HIS E 105 SITE 1 FE6 2 HIS F 73 HIS F 105 SITE 1 FE7 2 HIS G 73 HIS G 105 SITE 1 FE8 2 HIS H 73 HIS H 105 SITE 1 FE9 2 HIS I 73 HIS I 105 SITE 1 F10 2 HIS J 73 HIS J 105 SITE 1 F11 2 HIS K 73 HIS K 105 SITE 1 F12 2 HIS L 73 HIS L 105 CRYST1 59.630 215.160 75.390 90.00 95.80 90.00 P 1 21 1 24 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 0.016770 0.000000 0.001703 0.00000 SCALE2 0.000000 0.004648 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013333 0.00000 MTRIX1 1 -0.995624 0.071172 0.060553 44.14900 1 MTRIX2 1 0.092939 0.821627 0.562398 32.98880 1 MTRIX3 1 -0.009724 0.565565 -0.824646 -112.23650 1 MTRIX1 2 0.952872 -0.196594 0.231054 20.23010 1 MTRIX2 2 -0.267964 -0.902493 0.337198 395.72040 1 MTRIX3 2 0.142233 -0.383220 -0.912640 114.43380 1 MTRIX1 3 -0.961494 0.110635 -0.251572 58.08690 1 MTRIX2 3 -0.063347 -0.979960 -0.188854 424.65649 1 MTRIX3 3 -0.267425 -0.165646 0.949234 10.87740 1 MTRIX1 4 0.927905 -0.366844 -0.066476 55.01010 1 MTRIX2 4 -0.053753 0.044804 -0.997549 272.76321 1 MTRIX3 4 0.368923 0.929203 0.021855 -176.16580 1 MTRIX1 5 -0.931105 0.364485 -0.013948 10.34830 1 MTRIX2 5 0.220629 0.532340 -0.817274 162.90961 1 MTRIX3 5 -0.290459 -0.764045 -0.576081 188.41440 1 MTRIX1 6 -0.995444 0.013278 0.094423 52.24950 1 MTRIX2 6 0.095093 0.211133 0.972821 151.72000 1 MTRIX3 6 -0.007018 0.977367 -0.211434 -160.73880 1 MTRIX1 7 0.999983 0.004353 0.003770 2.02040 1 MTRIX2 7 -0.005747 0.712798 0.701346 72.99750 1 MTRIX3 7 0.000366 -0.701356 0.712811 110.00270 1 MTRIX1 8 -0.945881 0.034753 -0.322647 39.62290 1 MTRIX2 8 0.278728 -0.422176 -0.862600 271.63251 1 MTRIX3 8 -0.166192 -0.905847 0.389642 132.26770 1 MTRIX1 9 0.962645 -0.081954 0.258065 26.50620 1 MTRIX2 9 0.072196 -0.840901 -0.536352 332.02689 1 MTRIX3 9 0.260964 0.534948 -0.803573 -71.21180 1 MTRIX1 10 -0.922132 -0.317125 -0.221596 84.10030 1 MTRIX2 10 0.043958 -0.654958 0.754386 270.78159 1 MTRIX3 10 -0.384371 0.685902 0.617898 -111.49340 1 MTRIX1 11 0.921119 0.276786 0.273732 -21.09910 1 MTRIX2 11 -0.231941 -0.174512 0.956948 198.57980 1 MTRIX3 11 0.312639 -0.944952 -0.096548 134.24940 1