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HEADER SIGNALING PROTEIN 11-MAR-03 1OR4 TITLE CRYSTAL STRUCTURE OF HEMAT SENSOR DOMAIN FROM B.SUBTILIS IN TITLE 2 THE CYANO-LIGANDED 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: BL21DE3; 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 1OR4 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. 2.15 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : SHELXL-97 REMARK 3 AUTHORS : G.M.SHELDRICK REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.98 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 CROSS-VALIDATION METHOD : FREE R REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF). REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.197 REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.197 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.258 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 4.300 REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1379 REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 31839 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.178 REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.178 REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.230 REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 4.300 REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 1155 REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 26903 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2666 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 90 REMARK 3 SOLVENT ATOMS : 204 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2901.50 REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00 REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 4 REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 12286 REMARK 3 NUMBER OF RESTRAINTS : 12870 REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 ANGLE DISTANCES (A) : 0.025 REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.005 REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.024 REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.033 REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.040 REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.006 REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.002 REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.108 REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: NULL REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : NULL REMARK 3 SPECIAL CASE: NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT APPLIED REMARK 3 TO HEME GROUP ONLY REMARK 4 REMARK 4 1OR4 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 3.101 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB018585. 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; M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : SI 111 CHANNEL; 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 : 31839 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150 REMARK 200 RESOLUTION RANGE LOW (A) : 100.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL 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) : 2.15 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23 REMARK 200 COMPLETENESS FOR SHELL (%) : 83.7 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: MAD; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD REMARK 200 SOFTWARE USED: SOLVE, XTALVIEW REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 35.90 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92 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 24.99700 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.97200 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.05850 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.97200 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.99700 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.05850 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 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 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 GLU A 10 CG CD OE1 OE2 REMARK 470 LYS A 22 CG CD CE NZ REMARK 470 LYS A 30 CG CD CE NZ REMARK 470 LYS B 30 CG CD CE NZ REMARK 470 HIS B 75 CG ND1 CD2 CE1 NE2 REMARK 470 ARG B 125 CG CD NE CZ NH1 NH2 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 HOH 3 O HOH 121 1.91 REMARK 500 OD1 ASP B 85 O HOH 15 2.18 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH 8 O HOH 156 4565 1.99 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 ASP A 74 CA - CB - CG ANGL. DEV. = 13.7 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 13 DISTANCE = 7.73 ANGSTROMS REMARK 525 HOH 39 DISTANCE = 5.40 ANGSTROMS REMARK 525 HOH 60 DISTANCE = 6.75 ANGSTROMS REMARK 525 HOH 122 DISTANCE = 5.17 ANGSTROMS REMARK 525 HOH 176 DISTANCE = 7.57 ANGSTROMS REMARK 525 HOH 179 DISTANCE = 5.07 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1OR6 RELATED DB: PDB DBREF 1OR4 A 1 178 UNP O07621 HEMAT_BACSU 1 178 DBREF 1OR4 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 CYN A 181 2 HET CYN B 181 2 HET HEM A 180 43 HET HEM B 180 43 HETNAM CYN CYANIDE ION HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 3 CYN 2(C N 1-) FORMUL 5 HEM 2(C34 H32 FE N4 O4) FORMUL 7 HOH *204(H2 O) HELIX 1 1 SER A 17 LYS A 22 5 6 HELIX 2 2 THR A 28 LYS A 30 5 3 HELIX 3 3 HIS A 31 VAL A 41 1 11 HELIX 4 4 GLY A 44 ASP A 74 1 31 HELIX 5 5 GLU A 76 SER A 87 1 12 HELIX 6 6 SER A 88 MET A 103 1 16 HELIX 7 7 ASP A 110 ILE A 126 1 17 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 THR B 28 LYS B 30 5 3 HELIX 11 11 HIS B 31 ARG B 42 1 12 HELIX 12 12 GLY B 44 ASN B 61 1 18 HELIX 13 13 ASN B 61 ASP B 74 1 14 HELIX 14 14 GLU B 76 SER B 87 1 12 HELIX 15 15 SER B 88 PHE B 104 1 17 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 GLU B 178 1 25 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 A 180 C CYN A 181 LINK FE HEM B 180 NE2 HIS B 123 LINK FE HEM B 180 C CYN B 181 CISPEP 1 LEU A 177 GLU A 178 0 -5.54 CRYST1 49.994 80.117 85.944 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 0.020002 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012482 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011635 0.00000