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HEADER OXIDOREDUCTASE 13-FEB-02 1GVH TITLE THE X-RAY STRUCTURE OF FERRIC ESCHERICHIA COLI TITLE 2 FLAVOHEMOGLOBIN REVEALS AN UNESPECTED GEOMETRY OF THE TITLE 3 DISTAL HEME POCKET COMPND MOL_ID: 1; COMPND 2 MOLECULE: FLAVOHEMOPROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: FLAVOHEMOGLOBIN, DIHYDROPTERIDINE REDUCTASE, COMPND 5 HEMOGLOBIN-LIKE PROTEIN, DIHYDROPTERIDINE REDUCTASE, COMPND 6 FERRISIDEROPHORE REDUCTASE B, NITRIC OXIDE DIOXYGENASE, COMPND 7 NOD; COMPND 8 EC: 1.6.99.7 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI KEYWDS OXIDOREDUCTASE, NADP, HEME, FLAVOPROTEIN, FAD, IRON TRANSPOR EXPDTA X-RAY DIFFRACTION AUTHOR A.ILARI,K.A.JOHNSON,A.BONAMORE,A.FARINA,A.BOFFI REVDAT 2 01-APR-03 1GVH 1 JRNL REVDAT 1 06-AUG-02 1GVH 0 JRNL AUTH A.ILARI,A.BONAMORE,A.FARINA,K.A.JOHNSON,A.BOFFI JRNL TITL THE X-RAY STRUCTURE OF FERRIC ESCHERICHIA COLI JRNL TITL 2 FLAVOHEMOGLOBIN REVEALS AN UNEXPECTED GEOMETRY OF JRNL TITL 3 THE DISTAL HEME POCKET. JRNL REF J.BIOL.CHEM. V. 277 23725 2002 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.19 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) : 2.19 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00 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) (%) : 99.4 REMARK 3 NUMBER OF REFLECTIONS : 22443 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.187 REMARK 3 FREE R VALUE : 0.247 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL 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 : 3097 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 99 REMARK 3 SOLVENT ATOMS : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.80 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.40 REMARK 3 IMPROPER ANGLES (DEGREES) : 4.19 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 : PROLSQ.PROT REMARK 3 PARAMETER FILE 2 : PARAM19X.HEME REMARK 3 PARAMETER FILE 3 : PARAM.FAD REMARK 3 PARAMETER FILE 4 : PARAM19.SOLV REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPH19X_HEME.PRO REMARK 3 TOPOLOGY FILE 2 : TOPOL.FAD REMARK 3 TOPOLOGY FILE 3 : TOPH19.SOL REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1GVH 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 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI . REMARK 100 THE EBI ID CODE IS EBI-9427 . REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 5.10 REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ELETTRA REMARK 200 BEAMLINE : 5.2R REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22448 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190 REMARK 200 RESOLUTION RANGE LOW (A) : 25.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 11.000 REMARK 200 R MERGE (I) : 0.09000 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: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR 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 (%): 48.46 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.1 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 -X,-Y,Z REMARK 290 5555 Y,-X+Y,Z REMARK 290 6555 X-Y,X,Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z REMARK 290 10555 -Y,-X,-Z REMARK 290 11555 -X+Y,Y,-Z REMARK 290 12555 X,X-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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 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 1 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 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 5 0.500000 0.866025 0.000000 0.00000 REMARK 350 BIOMT2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 350 BIOMT2 6 0.866025 0.500000 0.000000 0.00000 REMARK 350 BIOMT3 6 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 350 BIOMT2 7 0.866025 0.500000 0.000000 0.00000 REMARK 350 BIOMT3 7 0.000000 0.000000 -1.000000 213.84000 REMARK 350 BIOMT1 8 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 8 0.000000 0.000000 -1.000000 213.84000 REMARK 350 BIOMT1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 350 BIOMT2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 350 BIOMT3 9 0.000000 0.000000 -1.000000 213.84000 REMARK 350 BIOMT1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 350 BIOMT2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 10 0.000000 0.000000 -1.000000 213.84000 REMARK 350 BIOMT1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 11 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 11 0.000000 0.000000 -1.000000 213.84000 REMARK 350 BIOMT1 12 0.500000 0.866025 0.000000 0.00000 REMARK 350 BIOMT2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 12 0.000000 0.000000 -1.000000 213.84000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: Z 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 HOH Z 57 O HOH Z 58 2.17 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 TRP A 120 CG TRP A 120 CD2 -0.071 REMARK 500 TRP A 149 CG TRP A 149 CD2 -0.069 REMARK 500 TRP A 192 CG TRP A 192 CD2 -0.075 REMARK 500 TRP A 323 CG TRP A 323 CD2 -0.070 REMARK 500 HIS A 393 CG HIS A 393 CD2 0.130 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 396 N - CA - CB ANGL. DEV. = 12.4 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 Z 3 DISTANCE = 6.21 ANGSTROMS REMARK 525 HOH Z 39 DISTANCE = 5.32 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR CHAIN A DBREF 1GVH A 1 396 UNP P24232 HMP_ECOLI 1 396 SEQRES 1 A 396 MET LEU ASP ALA GLN THR ILE ALA THR VAL LYS ALA THR SEQRES 2 A 396 ILE PRO LEU LEU VAL GLU THR GLY PRO LYS LEU THR ALA SEQRES 3 A 396 HIS PHE TYR ASP ARG MET PHE THR HIS ASN PRO GLU LEU SEQRES 4 A 396 LYS GLU ILE PHE ASN MET SER ASN GLN ARG ASN GLY ASP SEQRES 5 A 396 GLN ARG GLU ALA LEU PHE ASN ALA ILE ALA ALA TYR ALA SEQRES 6 A 396 SER ASN ILE GLU ASN LEU PRO ALA LEU LEU PRO ALA VAL SEQRES 7 A 396 GLU LYS ILE ALA GLN LYS HIS THR SER PHE GLN ILE LYS SEQRES 8 A 396 PRO GLU GLN TYR ASN ILE VAL GLY GLU HIS LEU LEU ALA SEQRES 9 A 396 THR LEU ASP GLU MET PHE SER PRO GLY GLN GLU VAL LEU SEQRES 10 A 396 ASP ALA TRP GLY LYS ALA TYR GLY VAL LEU ALA ASN VAL SEQRES 11 A 396 PHE ILE ASN ARG GLU ALA GLU ILE TYR ASN GLU ASN ALA SEQRES 12 A 396 SER LYS ALA GLY GLY TRP GLU GLY THR ARG ASP PHE ARG SEQRES 13 A 396 ILE VAL ALA LYS THR PRO ARG SER ALA LEU ILE THR SER SEQRES 14 A 396 PHE GLU LEU GLU PRO VAL ASP GLY GLY ALA VAL ALA GLU SEQRES 15 A 396 TYR ARG PRO GLY GLN TYR LEU GLY VAL TRP LEU LYS PRO SEQRES 16 A 396 GLU GLY PHE PRO HIS GLN GLU ILE ARG GLN TYR SER LEU SEQRES 17 A 396 THR ARG LYS PRO ASP GLY LYS GLY TYR ARG ILE ALA VAL SEQRES 18 A 396 LYS ARG GLU GLU GLY GLY GLN VAL SER ASN TRP LEU HIS SEQRES 19 A 396 ASN HIS ALA ASN VAL GLY ASP VAL VAL LYS LEU VAL ALA SEQRES 20 A 396 PRO ALA GLY ASP PHE PHE MET ALA VAL ALA ASP ASP THR SEQRES 21 A 396 PRO VAL THR LEU ILE SER ALA GLY VAL GLY GLN THR PRO SEQRES 22 A 396 MET LEU ALA MET LEU ASP THR LEU ALA LYS ALA GLY HIS SEQRES 23 A 396 THR ALA GLN VAL ASN TRP PHE HIS ALA ALA GLU ASN GLY SEQRES 24 A 396 ASP VAL HIS ALA PHE ALA ASP GLU VAL LYS GLU LEU GLY SEQRES 25 A 396 GLN SER LEU PRO ARG PHE THR ALA HIS THR TRP TYR ARG SEQRES 26 A 396 GLN PRO SER GLU ALA ASP ARG ALA LYS GLY GLN PHE ASP SEQRES 27 A 396 SER GLU GLY LEU MET ASP LEU SER LYS LEU GLU GLY ALA SEQRES 28 A 396 PHE SER ASP PRO THR MET GLN PHE TYR LEU CYS GLY PRO SEQRES 29 A 396 VAL GLY PHE MET GLN PHE THR ALA LYS GLN LEU VAL ASP SEQRES 30 A 396 LEU GLY VAL LYS GLN GLU ASN ILE HIS TYR GLU CYS PHE SEQRES 31 A 396 GLY PRO HIS LYS VAL LEU HET NA A1399 1 HET NA A1400 1 HET CL A1401 1 HET FAD A1397 53 HET HEM A1398 43 HETNAM NA SODIUM ION HETNAM CL CHLORIDE ION HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 2 NA 2(NA 1+) FORMUL 4 CL CL 1- FORMUL 5 FAD C27 H33 N9 O15 P2 FORMUL 6 HEM C34 H32 FE N4 O4 FORMUL 7 HOH *191(H2 O) HELIX 1 1 ASP A 3 GLU A 19 1 17 HELIX 2 2 THR A 20 ASN A 36 1 17 HELIX 3 3 PRO A 37 ILE A 42 5 6 HELIX 4 4 GLY A 51 SER A 66 1 16 HELIX 5 5 ASN A 67 ALA A 73 5 7 HELIX 6 6 LEU A 74 PHE A 88 1 15 HELIX 7 7 LYS A 91 SER A 111 1 21 HELIX 8 8 GLY A 113 LYS A 145 1 33 HELIX 9 9 GLY A 227 HIS A 236 1 10 HELIX 10 10 GLN A 271 ALA A 284 1 14 HELIX 11 11 PHE A 304 SER A 314 1 11 HELIX 12 12 SER A 328 GLY A 335 1 8 HELIX 13 13 ASP A 344 LEU A 348 5 5 HELIX 14 14 PRO A 364 LEU A 378 1 15 HELIX 15 15 LYS A 381 GLU A 383 5 3 SHEET 1 AA 6 GLU A 202 SER A 207 0 SHEET 2 AA 6 TYR A 188 LEU A 193 -1 O LEU A 189 N TYR A 206 SHEET 3 AA 6 VAL A 242 ALA A 249 -1 O LYS A 244 N TRP A 192 SHEET 4 AA 6 THR A 152 PRO A 162 -1 O ARG A 153 N LEU A 245 SHEET 5 AA 6 ILE A 167 PRO A 174 -1 O SER A 169 N THR A 161 SHEET 6 AA 6 TYR A 217 LYS A 222 -1 O TYR A 217 N LEU A 172 SHEET 1 AB 6 SER A 339 GLU A 340 0 SHEET 2 AB 6 PHE A 318 TYR A 324 1 O THR A 322 N SER A 339 SHEET 3 AB 6 VAL A 290 ALA A 296 1 O VAL A 290 N THR A 319 SHEET 4 AB 6 VAL A 262 ALA A 267 1 O VAL A 262 N ASN A 291 SHEET 5 AB 6 GLN A 358 CYS A 362 1 O GLN A 358 N THR A 263 SHEET 6 AB 6 ILE A 385 GLU A 388 1 O HIS A 386 N LEU A 361 LINK FE HEM A1398 NE2 HIS A 85 LINK NA NA A1399 O GLN A 201 LINK NA NA A1399 O LYS A 40 LINK NA NA A1399 OE1 GLU A 202 LINK NA NA A1399 O PHE A 43 SITE 1 AC1 24 ASN A 44 SER A 46 GLN A 48 ASN A 50 SITE 2 AC1 24 TYR A 188 ARG A 204 GLN A 205 TYR A 206 SITE 3 AC1 24 SER A 207 ALA A 220 LYS A 222 GLU A 224 SITE 4 AC1 24 GLU A 225 GLY A 227 GLN A 228 SER A 230 SITE 5 AC1 24 THR A 272 GLU A 388 PHE A 390 HOH Z 96 SITE 6 AC1 24 HOH Z 104 HOH Z 187 HOH Z 188 HOH Z 189 SITE 1 AC2 19 LEU A 39 ASN A 44 GLN A 53 ALA A 56 SITE 2 AC2 19 LEU A 57 ALA A 60 ILE A 61 ILE A 81 SITE 3 AC2 19 LYS A 84 HIS A 85 PHE A 88 ILE A 90 SITE 4 AC2 19 GLN A 94 TYR A 95 LEU A 127 PRO A 392 SITE 5 AC2 19 HIS A 393 HOH Z 190 HOH Z 191 SITE 1 AC3 4 LYS A 40 PHE A 43 GLN A 201 GLU A 202 SITE 1 AC4 5 GLN A 271 HIS A 294 HIS A 302 ALA A 303 SITE 2 AC4 5 HOH Z 138 CRYST1 164.860 164.860 53.460 90.00 90.00 120.00 P 6 2 2 12 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 0.006066 0.003502 0.000000 0.00000 SCALE2 0.000000 0.007004 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018705 0.00000