HEADER SIGNALING PROTEIN 11-MAR-03 1OR6 TITLE CRYSTAL STRUCTURE OF HEMAT SENSOR DOMAIN FROM B.SUBTILIS IN TITLE 2 THE UNLIGANDED FORM COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEME-BASED AEROTACTIC TRANSDUCER HEMAT; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS; SOURCE 3 ORGANISM_COMMON: BACTERIA; SOURCE 4 GENE: YHFV; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET29 KEYWDS GLOBIN FOLD EXPDTA X-RAY DIFFRACTION AUTHOR W.ZHANG,G.N.PHILLIPS JR. REVDAT 1 23-SEP-03 1OR6 0 JRNL AUTH W.ZHANG,G.N.PHILLIPS JRNL TITL STRUCTURE OF THE OXYGEN SENSOR IN BACILLUS JRNL TITL 2 SUBTILIS: SIGNAL TRANSDUCTION OF CHEMOTAXIS BY JRNL TITL 3 CONTROL OF SYMMETRY. JRNL REF STRUCTURE V. 11 1097 2003 JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.71 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.71 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.74 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.3 REMARK 3 NUMBER OF REFLECTIONS : 15592 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) : 0.208 REMARK 3 FREE R VALUE : 0.329 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.300 REMARK 3 FREE R VALUE TEST SET COUNT : 1457 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.71 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.81 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 57.70 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 937 REMARK 3 BIN R VALUE (WORKING SET) : 0.2930 REMARK 3 BIN FREE R VALUE : 0.4090 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.00 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 82 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.045 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2621 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 86 REMARK 3 SOLVENT ATOMS : 185 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 15.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.10 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -4.21000 REMARK 3 B22 (A**2) : -6.51000 REMARK 3 B33 (A**2) : 10.72000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.33 REMARK 3 ESD FROM SIGMAA (A) : 0.42 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.57 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.68 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.10 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.00 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.94 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.360 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.350 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 1.930 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.060 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.38 REMARK 3 BSOL : 58.93 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 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : HEME_H1234.PARAM REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER.TOP REMARK 3 TOPOLOGY FILE 3 : HEME.TOP REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1OR6 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 RCSB018587. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-APR-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 14-BM-C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : SI 111 CHANNEL 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 : 15592 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.710 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.09800 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) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80 REMARK 200 COMPLETENESS FOR SHELL (%) : 74.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.21600 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: CNS REMARK 200 STARTING MODEL: PDB ENTRY 1OR4 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 38.90 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, KH2PO4, N-OCTYL-D- REMARK 280 GLUCOSIDE , PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 298K 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 24.72650 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.57300 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.86200 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.57300 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.72650 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.86200 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 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 MET A 1 REMARK 465 LEU A 2 REMARK 465 PHE A 3 REMARK 465 LYS A 4 REMARK 465 LYS A 5 REMARK 465 ASP A 6 REMARK 465 ARG A 7 REMARK 465 LYS A 8 REMARK 465 GLN A 9 REMARK 465 GLU A 10 REMARK 465 MET B 1 REMARK 465 LEU B 2 REMARK 465 PHE B 3 REMARK 465 LYS B 4 REMARK 465 LYS B 5 REMARK 465 ASP B 6 REMARK 465 ARG B 7 REMARK 465 LYS B 8 REMARK 465 GLN B 9 REMARK 465 GLU B 10 REMARK 465 THR B 11 REMARK 465 ALA B 12 REMARK 465 TYR B 13 REMARK 465 PHE B 14 REMARK 465 SER B 15 REMARK 465 ASP B 16 REMARK 465 SER B 17 REMARK 465 ASN B 18 REMARK 465 GLY B 19 REMARK 465 GLN B 20 REMARK 465 GLN B 21 REMARK 465 LYS B 22 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 THR A 11 OG1 CG2 REMARK 470 LYS A 22 CG CD CE NZ REMARK 470 LYS A 30 CG CD CE NZ REMARK 470 ARG A 118 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 30 CG CD CE NZ REMARK 470 LYS B 71 CG CD CE NZ REMARK 470 ARG B 91 CD NE CZ NH1 NH2 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 B 91 CB ARG B 91 CG -0.107 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 LEU A 129 CA - CB - CG ANGL. DEV. = 7.5 DEGREES REMARK 500 THR A 153 N - CA - C ANGL. DEV. = 7.4 DEGREES REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER B 87 -140.56 178.29 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 1 DISTANCE = 8.72 ANGSTROMS REMARK 525 HOH 15 DISTANCE = 6.57 ANGSTROMS REMARK 525 HOH 31 DISTANCE = 5.71 ANGSTROMS REMARK 525 HOH 43 DISTANCE = 6.90 ANGSTROMS REMARK 525 HOH 44 DISTANCE = 7.17 ANGSTROMS REMARK 525 HOH 46 DISTANCE = 6.80 ANGSTROMS REMARK 525 HOH 54 DISTANCE = 5.59 ANGSTROMS REMARK 525 HOH 59 DISTANCE = 5.99 ANGSTROMS REMARK 525 HOH 60 DISTANCE = 8.60 ANGSTROMS REMARK 525 HOH 61 DISTANCE = 5.90 ANGSTROMS REMARK 525 HOH 66 DISTANCE = 6.22 ANGSTROMS REMARK 525 HOH 72 DISTANCE = 5.22 ANGSTROMS REMARK 525 HOH 81 DISTANCE = 5.47 ANGSTROMS REMARK 525 HOH 85 DISTANCE = 6.64 ANGSTROMS REMARK 525 HOH 91 DISTANCE = 5.71 ANGSTROMS REMARK 525 HOH 93 DISTANCE = 5.61 ANGSTROMS REMARK 525 HOH 123 DISTANCE = 5.58 ANGSTROMS REMARK 525 HOH 128 DISTANCE = 9.19 ANGSTROMS REMARK 525 HOH 131 DISTANCE = 8.21 ANGSTROMS REMARK 525 HOH 137 DISTANCE = 6.13 ANGSTROMS REMARK 525 HOH 144 DISTANCE = 8.80 ANGSTROMS REMARK 525 HOH 145 DISTANCE = 5.77 ANGSTROMS REMARK 525 HOH 148 DISTANCE = 5.73 ANGSTROMS REMARK 525 HOH 150 DISTANCE = 6.22 ANGSTROMS REMARK 525 HOH 157 DISTANCE = 6.21 ANGSTROMS REMARK 525 HOH 158 DISTANCE = 6.99 ANGSTROMS REMARK 525 HOH 159 DISTANCE = 6.69 ANGSTROMS REMARK 525 HOH 161 DISTANCE = 6.22 ANGSTROMS REMARK 525 HOH 166 DISTANCE = 5.08 ANGSTROMS REMARK 525 HOH 175 DISTANCE = 5.58 ANGSTROMS REMARK 525 HOH 179 DISTANCE = 6.45 ANGSTROMS REMARK 525 HOH 182 DISTANCE = 6.38 ANGSTROMS REMARK 525 HOH 184 DISTANCE = 5.87 ANGSTROMS REMARK 525 HOH 185 DISTANCE = 7.81 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1OR4 RELATED DB: PDB DBREF 1OR6 A 1 178 UNP O07621 HEMAT_BACSU 1 178 DBREF 1OR6 B 1 178 UNP O07621 HEMAT_BACSU 1 178 SEQRES 1 A 178 MET LEU PHE LYS LYS ASP ARG LYS GLN GLU THR ALA TYR SEQRES 2 A 178 PHE SER ASP SER ASN GLY GLN GLN LYS ASN ARG ILE GLN SEQRES 3 A 178 LEU THR ASN LYS HIS ALA ASP VAL LYS LYS GLN LEU LYS SEQRES 4 A 178 MET VAL ARG LEU GLY ASP ALA GLU LEU TYR VAL LEU GLU SEQRES 5 A 178 GLN LEU GLN PRO LEU ILE GLN GLU ASN ILE VAL ASN ILE SEQRES 6 A 178 VAL ASP ALA PHE TYR LYS ASN LEU ASP HIS GLU SER SER SEQRES 7 A 178 LEU MET ASP ILE ILE ASN ASP HIS SER SER VAL ASP ARG SEQRES 8 A 178 LEU LYS GLN THR LEU LYS ARG HIS ILE GLN GLU MET PHE SEQRES 9 A 178 ALA GLY VAL ILE ASP ASP GLU PHE ILE GLU LYS ARG ASN SEQRES 10 A 178 ARG ILE ALA SER ILE HIS LEU ARG ILE GLY LEU LEU PRO SEQRES 11 A 178 LYS TRP TYR MET GLY ALA PHE GLN GLU LEU LEU LEU SER SEQRES 12 A 178 MET ILE ASP ILE TYR GLU ALA SER ILE THR ASN GLN GLN SEQRES 13 A 178 GLU LEU LEU LYS ALA ILE LYS ALA THR THR LYS ILE LEU SEQRES 14 A 178 ASN LEU GLU GLN GLN LEU VAL LEU GLU SEQRES 1 B 178 MET LEU PHE LYS LYS ASP ARG LYS GLN GLU THR ALA TYR SEQRES 2 B 178 PHE SER ASP SER ASN GLY GLN GLN LYS ASN ARG ILE GLN SEQRES 3 B 178 LEU THR ASN LYS HIS ALA ASP VAL LYS LYS GLN LEU LYS SEQRES 4 B 178 MET VAL ARG LEU GLY ASP ALA GLU LEU TYR VAL LEU GLU SEQRES 5 B 178 GLN LEU GLN PRO LEU ILE GLN GLU ASN ILE VAL ASN ILE SEQRES 6 B 178 VAL ASP ALA PHE TYR LYS ASN LEU ASP HIS GLU SER SER SEQRES 7 B 178 LEU MET ASP ILE ILE ASN ASP HIS SER SER VAL ASP ARG SEQRES 8 B 178 LEU LYS GLN THR LEU LYS ARG HIS ILE GLN GLU MET PHE SEQRES 9 B 178 ALA GLY VAL ILE ASP ASP GLU PHE ILE GLU LYS ARG ASN SEQRES 10 B 178 ARG ILE ALA SER ILE HIS LEU ARG ILE GLY LEU LEU PRO SEQRES 11 B 178 LYS TRP TYR MET GLY ALA PHE GLN GLU LEU LEU LEU SER SEQRES 12 B 178 MET ILE ASP ILE TYR GLU ALA SER ILE THR ASN GLN GLN SEQRES 13 B 178 GLU LEU LEU LYS ALA ILE LYS ALA THR THR LYS ILE LEU SEQRES 14 B 178 ASN LEU GLU GLN GLN LEU VAL LEU GLU HET HEM A 180 43 HET HEM B 180 43 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 3 HEM 2(C34 H32 FE N4 O4) FORMUL 5 HOH *185(H2 O) HELIX 1 1 HIS A 31 VAL A 41 1 11 HELIX 2 2 GLY A 44 GLU A 60 1 17 HELIX 3 3 ASN A 61 ASP A 74 1 14 HELIX 4 4 GLU A 76 SER A 87 1 12 HELIX 5 5 SER A 88 PHE A 104 1 17 HELIX 6 6 ASP A 110 ASN A 117 1 8 HELIX 7 7 ILE A 119 ILE A 126 1 8 HELIX 8 8 LEU A 129 ILE A 152 1 24 HELIX 9 9 ASN A 154 LEU A 177 1 24 HELIX 10 10 HIS B 31 VAL B 41 1 11 HELIX 11 11 GLY B 44 ASN B 61 1 18 HELIX 12 12 ASN B 61 TYR B 70 1 10 HELIX 13 13 ASN B 72 HIS B 75 5 4 HELIX 14 14 GLU B 76 SER B 87 1 12 HELIX 15 15 LEU B 92 MET B 103 1 12 HELIX 16 16 ASP B 110 GLY B 127 1 18 HELIX 17 17 LEU B 129 ILE B 152 1 24 HELIX 18 18 ASN B 154 VAL B 176 1 23 SHEET 1 A 2 ILE A 25 GLN A 26 0 SHEET 2 A 2 ILE A 108 ASP A 109 1 O ILE A 108 N GLN A 26 SHEET 1 B 2 ILE B 25 GLN B 26 0 SHEET 2 B 2 ILE B 108 ASP B 109 1 O ILE B 108 N GLN B 26 LINK FE HEM A 180 NE2 HIS A 123 LINK FE HEM B 180 NE2 HIS B 123 CRYST1 49.453 79.724 85.146 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 0.020221 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012543 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011745 0.00000