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HEADER LIPID BINDING PROTEIN 12-AUG-99 1CQX TITLE CRYSTAL STRUCTURE OF THE FLAVOHEMOGLOBIN FROM ALCALIGENES TITLE 2 EUTROPHUS AT 1.75 A RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: FLAVOHEMOPROTEIN; COMPND 3 CHAIN: A, B SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RALSTONIA EUTROPHA; SOURCE 3 ORGANISM_COMMON: BACTERIA KEYWDS GLOBIN FOLD, SIX-STRANDED ANTIPARALLEL BETA SHEET, HELIX- KEYWDS 2 FLANKED FIVE-STRANDED PARALLEL BETA SHEET, LIPID BINDING KEYWDS 3 PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR U.ERMLER,R.A.SIDDIQUI,R.CRAMM,B.FRIEDRICH REVDAT 4 02-MAY-06 1CQX 1 JRNL REMARK DBREF MASTER REVDAT 3 05-JUL-00 1CQX 1 COMPND SOURCE REMARK HETNAM REVDAT 2 10-NOV-99 1CQX 1 COMPND JRNL REMARK REVDAT 1 31-AUG-99 1CQX 0 JRNL AUTH U.ERMLER,R.A.SIDDIQUI,R.CRAMM,B.FRIEDRICH JRNL TITL CRYSTAL STRUCTURE OF THE FLAVOHEMOGLOBIN FROM JRNL TITL 2 ALCALIGENES EUTROPHUS AT 1.75 A RESOLUTION. JRNL REF EMBO J. V. 14 6067 1995 JRNL REFN ASTM EMJODG UK ISSN 0261-4189 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH G.OLLESCH,A.KAUNZINGER,D.JUCHELKA, REMARK 1 AUTH 2 M.SCHUBERT-ZSILAVECZ,U.ERMLER REMARK 1 TITL PHOSPHOLIPID BOUND TO THE FLAVOHEMOPROTEIN FROM REMARK 1 TITL 2 ALCALIGENES EUTROPHUS REMARK 1 REF EUR.J.BIOCHEM. V. 262 396 1999 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 REMARK 2 REMARK 2 RESOLUTION. 1.75 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 29433623.090 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.7 REMARK 3 NUMBER OF REFLECTIONS : 80753 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) : 0.182 REMARK 3 FREE R VALUE : 0.215 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 4066 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.75 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.86 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 56.90 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8162 REMARK 3 BIN R VALUE (WORKING SET) : 0.2570 REMARK 3 BIN FREE R VALUE : 0.2540 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 433 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6316 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 283 REMARK 3 SOLVENT ATOMS : 581 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 19.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.70 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.84000 REMARK 3 B22 (A**2) : -0.58000 REMARK 3 B33 (A**2) : -0.26000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.53000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20 REMARK 3 ESD FROM SIGMAA (A) : 0.19 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) : 0.22 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.16 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 1.80 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.60 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.53 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) : 1.300 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.180 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 24.200; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 16.250; 2.500 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.PA REMARK 3 PARAMETER FILE 2 : FAHE.PARA REMARK 3 PARAMETER FILE 3 : WATER_REP.PARA REMARK 3 PARAMETER FILE 4 : ION.PARAM REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : FAHELI.TOP REMARK 3 TOPOLOGY FILE 3 : WATER.TOP REMARK 3 TOPOLOGY FILE 4 : ION.TOP REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1CQX 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 RCSB009502. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-DEC-1993 REMARK 200 TEMPERATURE (KELVIN) : 277.0 REMARK 200 PH : 6.30 REMARK 200 NUMBER OF CRYSTALS USED : 2 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : MPG/DESY, HAMBURG REMARK 200 BEAMLINE : BW6 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 : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (AGROVATA, ROTAVATA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 196672 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 90.5 REMARK 200 DATA REDUNDANCY : 2.400 REMARK 200 R MERGE (I) : 0.05200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84 REMARK 200 COMPLETENESS FOR SHELL (%) : 62.7 REMARK 200 DATA REDUNDANCY IN SHELL : 1.40 REMARK 200 R MERGE FOR SHELL (I) : 0.15100 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: NULL REMARK 200 SOFTWARE USED: MLPHARE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.07 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: TRIS, POTASSIUM REMARK 280 CHLORIDE, DTT, PLUS PRECIPITANT; PRECIPITANT: PEG 3350, SODIUM REMARK 280 CHLORIDE, SODIUM CITRATE, PH 6.3, VAPOR DIFFUSION, HANGING REMARK 280 DROP, TEMPERATURE 281K 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 42.90000 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 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 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: 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 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 75 SD MET A 75 CE 0.049 REMARK 500 MET A 136 SD MET A 136 CE -0.047 REMARK 500 PRO A 164 CB PRO A 164 CG 0.041 REMARK 500 PRO A 292 CB PRO A 292 CG 0.050 REMARK 500 ASN A 323 CG ASN A 323 ND2 -0.074 REMARK 500 MET B 1 SD MET B 1 CE -0.044 REMARK 500 MET B 136 SD MET B 136 CE -0.047 REMARK 500 PRO B 280 CB PRO B 280 CG 0.113 REMARK 500 PRO B 361 CB PRO B 361 CG 0.041 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 242 N - CA - C ANGL. DEV. = 9.3 DEGREES REMARK 500 THR A 279 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 PRO A 293 C - N - CA ANGL. DEV. =-15.0 DEGREES REMARK 500 PRO A 293 C - N - CD ANGL. DEV. = 16.8 DEGREES REMARK 500 ARG A 294 N - CA - C ANGL. DEV. = -9.7 DEGREES REMARK 500 VAL A 395 N - CA - C ANGL. DEV. = -9.2 DEGREES REMARK 500 PRO A 398 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 GLY B 229 N - CA - C ANGL. DEV. =-11.8 DEGREES REMARK 500 ASP B 242 N - CA - C ANGL. DEV. = 9.1 DEGREES REMARK 500 VAL B 395 N - CA - C ANGL. DEV. = -9.2 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 736 DISTANCE = 5.17 ANGSTROMS DBREF 1CQX A 1 403 UNP P39662 HMP_ALCEU 1 403 DBREF 1CQX B 1 403 UNP P39662 HMP_ALCEU 1 403 SEQRES 1 A 403 MET LEU THR GLN LYS THR LYS ASP ILE VAL LYS ALA THR SEQRES 2 A 403 ALA PRO VAL LEU ALA GLU HIS GLY TYR ASP ILE ILE LYS SEQRES 3 A 403 CYS PHE TYR GLN ARG MET PHE GLU ALA HIS PRO GLU LEU SEQRES 4 A 403 LYS ASN VAL PHE ASN MET ALA HIS GLN GLU GLN GLY GLN SEQRES 5 A 403 GLN GLN GLN ALA LEU ALA ARG ALA VAL TYR ALA TYR ALA SEQRES 6 A 403 GLU ASN ILE GLU ASP PRO ASN SER LEU MET ALA VAL LEU SEQRES 7 A 403 LYS ASN ILE ALA ASN LYS HIS ALA SER LEU GLY VAL LYS SEQRES 8 A 403 PRO GLU GLN TYR PRO ILE VAL GLY GLU HIS LEU LEU ALA SEQRES 9 A 403 ALA ILE LYS GLU VAL LEU GLY ASN ALA ALA THR ASP ASP SEQRES 10 A 403 ILE ILE SER ALA TRP ALA GLN ALA TYR GLY ASN LEU ALA SEQRES 11 A 403 ASP VAL LEU MET GLY MET GLU SER GLU LEU TYR GLU ARG SEQRES 12 A 403 SER ALA GLU GLN PRO GLY GLY TRP LYS GLY TRP ARG THR SEQRES 13 A 403 PHE VAL ILE ARG GLU LYS ARG PRO GLU SER ASP VAL ILE SEQRES 14 A 403 THR SER PHE ILE LEU GLU PRO ALA ASP GLY GLY PRO VAL SEQRES 15 A 403 VAL ASN PHE GLU PRO GLY GLN TYR THR SER VAL ALA ILE SEQRES 16 A 403 ASP VAL PRO ALA LEU GLY LEU GLN GLN ILE ARG GLN TYR SEQRES 17 A 403 SER LEU SER ASP MET PRO ASN GLY ARG THR TYR ARG ILE SEQRES 18 A 403 SER VAL LYS ARG GLU GLY GLY GLY PRO GLN PRO PRO GLY SEQRES 19 A 403 TYR VAL SER ASN LEU LEU HIS ASP HIS VAL ASN VAL GLY SEQRES 20 A 403 ASP GLN VAL LYS LEU ALA ALA PRO TYR GLY SER PHE HIS SEQRES 21 A 403 ILE ASP VAL ASP ALA LYS THR PRO ILE VAL LEU ILE SER SEQRES 22 A 403 GLY GLY VAL GLY LEU THR PRO MET VAL SER MET LEU LYS SEQRES 23 A 403 VAL ALA LEU GLN ALA PRO PRO ARG GLN VAL VAL PHE VAL SEQRES 24 A 403 HIS GLY ALA ARG ASN SER ALA VAL HIS ALA MET ARG ASP SEQRES 25 A 403 ARG LEU ARG GLU ALA ALA LYS THR TYR GLU ASN LEU ASP SEQRES 26 A 403 LEU PHE VAL PHE TYR ASP GLN PRO LEU PRO GLU ASP VAL SEQRES 27 A 403 GLN GLY ARG ASP TYR ASP TYR PRO GLY LEU VAL ASP VAL SEQRES 28 A 403 LYS GLN ILE GLU LYS SER ILE LEU LEU PRO ASP ALA ASP SEQRES 29 A 403 TYR TYR ILE CYS GLY PRO ILE PRO PHE MET ARG MET GLN SEQRES 30 A 403 HIS ASP ALA LEU LYS ASN LEU GLY ILE HIS GLU ALA ARG SEQRES 31 A 403 ILE HIS TYR GLU VAL PHE GLY PRO ASP LEU PHE ALA GLU SEQRES 1 B 403 MET LEU THR GLN LYS THR LYS ASP ILE VAL LYS ALA THR SEQRES 2 B 403 ALA PRO VAL LEU ALA GLU HIS GLY TYR ASP ILE ILE LYS SEQRES 3 B 403 CYS PHE TYR GLN ARG MET PHE GLU ALA HIS PRO GLU LEU SEQRES 4 B 403 LYS ASN VAL PHE ASN MET ALA HIS GLN GLU GLN GLY GLN SEQRES 5 B 403 GLN GLN GLN ALA LEU ALA ARG ALA VAL TYR ALA TYR ALA SEQRES 6 B 403 GLU ASN ILE GLU ASP PRO ASN SER LEU MET ALA VAL LEU SEQRES 7 B 403 LYS ASN ILE ALA ASN LYS HIS ALA SER LEU GLY VAL LYS SEQRES 8 B 403 PRO GLU GLN TYR PRO ILE VAL GLY GLU HIS LEU LEU ALA SEQRES 9 B 403 ALA ILE LYS GLU VAL LEU GLY ASN ALA ALA THR ASP ASP SEQRES 10 B 403 ILE ILE SER ALA TRP ALA GLN ALA TYR GLY ASN LEU ALA SEQRES 11 B 403 ASP VAL LEU MET GLY MET GLU SER GLU LEU TYR GLU ARG SEQRES 12 B 403 SER ALA GLU GLN PRO GLY GLY TRP LYS GLY TRP ARG THR SEQRES 13 B 403 PHE VAL ILE ARG GLU LYS ARG PRO GLU SER ASP VAL ILE SEQRES 14 B 403 THR SER PHE ILE LEU GLU PRO ALA ASP GLY GLY PRO VAL SEQRES 15 B 403 VAL ASN PHE GLU PRO GLY GLN TYR THR SER VAL ALA ILE SEQRES 16 B 403 ASP VAL PRO ALA LEU GLY LEU GLN GLN ILE ARG GLN TYR SEQRES 17 B 403 SER LEU SER ASP MET PRO ASN GLY ARG THR TYR ARG ILE SEQRES 18 B 403 SER VAL LYS ARG GLU GLY GLY GLY PRO GLN PRO PRO GLY SEQRES 19 B 403 TYR VAL SER ASN LEU LEU HIS ASP HIS VAL ASN VAL GLY SEQRES 20 B 403 ASP GLN VAL LYS LEU ALA ALA PRO TYR GLY SER PHE HIS SEQRES 21 B 403 ILE ASP VAL ASP ALA LYS THR PRO ILE VAL LEU ILE SER SEQRES 22 B 403 GLY GLY VAL GLY LEU THR PRO MET VAL SER MET LEU LYS SEQRES 23 B 403 VAL ALA LEU GLN ALA PRO PRO ARG GLN VAL VAL PHE VAL SEQRES 24 B 403 HIS GLY ALA ARG ASN SER ALA VAL HIS ALA MET ARG ASP SEQRES 25 B 403 ARG LEU ARG GLU ALA ALA LYS THR TYR GLU ASN LEU ASP SEQRES 26 B 403 LEU PHE VAL PHE TYR ASP GLN PRO LEU PRO GLU ASP VAL SEQRES 27 B 403 GLN GLY ARG ASP TYR ASP TYR PRO GLY LEU VAL ASP VAL SEQRES 28 B 403 LYS GLN ILE GLU LYS SER ILE LEU LEU PRO ASP ALA ASP SEQRES 29 B 403 TYR TYR ILE CYS GLY PRO ILE PRO PHE MET ARG MET GLN SEQRES 30 B 403 HIS ASP ALA LEU LYS ASN LEU GLY ILE HIS GLU ALA ARG SEQRES 31 B 403 ILE HIS TYR GLU VAL PHE GLY PRO ASP LEU PHE ALA GLU HET NA 490 1 HET HEM A 404 43 HET FAD A 405 53 HET DGG A 406 45 HET HEM B 404 43 HET FAD B 405 53 HET DGG B 406 45 HETNAM NA SODIUM ION HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE HETNAM DGG 1-[GLYCEROLYLPHOSPHONYL]-2-[8-(2-HEXYL-CYCLOPROPYL)- HETNAM 2 DGG OCTANAL-1-YL]-3-[HEXADECANAL-1-YL]-GLYCEROL HETSYN HEM HEME FORMUL 3 NA NA 1+ FORMUL 4 HEM 2(C34 H32 FE N4 O4) FORMUL 5 FAD 2(C27 H33 N9 O15 P2) FORMUL 6 DGG 2(C39 H75 O10 P) FORMUL 10 HOH *581(H2 O) HELIX 1 1 THR A 3 ALA A 14 1 12 HELIX 2 2 THR A 13 HIS A 20 1 8 HELIX 3 3 HIS A 20 HIS A 36 1 17 HELIX 4 4 PRO A 37 VAL A 42 5 6 HELIX 5 5 GLU A 49 ILE A 68 1 20 HELIX 6 6 ASP A 70 GLY A 89 1 20 HELIX 7 7 LYS A 91 GLU A 93 5 3 HELIX 8 8 GLN A 94 GLY A 111 1 18 HELIX 9 9 ASN A 112 ALA A 114 5 3 HELIX 10 10 THR A 115 GLU A 146 1 32 HELIX 11 11 GLY A 234 VAL A 244 1 11 HELIX 12 12 GLY A 277 LEU A 289 1 13 HELIX 13 13 HIS A 308 TYR A 321 1 14 HELIX 14 14 ASP A 350 GLN A 353 5 4 HELIX 15 15 ILE A 354 LEU A 359 1 6 HELIX 16 16 PRO A 370 LEU A 384 1 15 HELIX 17 17 HIS A 387 ALA A 389 5 3 HELIX 18 18 THR B 3 ALA B 14 1 12 HELIX 19 19 THR B 13 HIS B 20 1 8 HELIX 20 20 HIS B 20 HIS B 36 1 17 HELIX 21 21 PRO B 37 VAL B 42 5 6 HELIX 22 22 GLU B 49 ILE B 68 1 20 HELIX 23 23 ASP B 70 GLY B 89 1 20 HELIX 24 24 LYS B 91 GLU B 93 5 3 HELIX 25 25 GLN B 94 GLY B 111 1 18 HELIX 26 26 ASN B 112 ALA B 114 5 3 HELIX 27 27 THR B 115 GLN B 147 1 33 HELIX 28 28 GLY B 234 VAL B 244 1 11 HELIX 29 29 GLY B 277 LEU B 289 1 13 HELIX 30 30 HIS B 308 TYR B 321 1 14 HELIX 31 31 ILE B 354 LEU B 359 1 6 HELIX 32 32 PRO B 370 ASN B 383 1 14 HELIX 33 33 HIS B 387 ALA B 389 5 3 SHEET 1 A 6 GLN A 203 SER A 209 0 SHEET 2 A 6 TYR A 190 ASP A 196 -1 O THR A 191 N TYR A 208 SHEET 3 A 6 GLN A 249 LEU A 252 -1 O LYS A 251 N ALA A 194 SHEET 4 A 6 ARG A 155 PRO A 164 -1 O ARG A 155 N LEU A 252 SHEET 5 A 6 ILE A 169 PRO A 176 -1 N SER A 171 O ARG A 163 SHEET 6 A 6 TYR A 219 LYS A 224 -1 O TYR A 219 N LEU A 174 SHEET 1 B 6 TYR A 345 PRO A 346 0 SHEET 2 B 6 LEU A 324 TYR A 330 1 O VAL A 328 N TYR A 345 SHEET 3 B 6 VAL A 296 ALA A 302 1 O VAL A 296 N ASP A 325 SHEET 4 B 6 ILE A 269 SER A 273 1 O ILE A 269 N VAL A 297 SHEET 5 B 6 ASP A 364 CYS A 368 1 O ASP A 364 N VAL A 270 SHEET 6 B 6 ILE A 391 TYR A 393 1 N HIS A 392 O TYR A 365 SHEET 1 C 6 GLN B 203 SER B 209 0 SHEET 2 C 6 TYR B 190 ASP B 196 -1 O THR B 191 N TYR B 208 SHEET 3 C 6 GLN B 249 LEU B 252 -1 O LYS B 251 N ALA B 194 SHEET 4 C 6 ARG B 155 PRO B 164 -1 O ARG B 155 N LEU B 252 SHEET 5 C 6 ILE B 169 PRO B 176 -1 N SER B 171 O ARG B 163 SHEET 6 C 6 TYR B 219 LYS B 224 -1 O TYR B 219 N LEU B 174 SHEET 1 D 6 TYR B 345 PRO B 346 0 SHEET 2 D 6 LEU B 324 TYR B 330 1 O VAL B 328 N TYR B 345 SHEET 3 D 6 VAL B 296 ALA B 302 1 O VAL B 296 N ASP B 325 SHEET 4 D 6 ILE B 269 SER B 273 1 O ILE B 269 N VAL B 297 SHEET 5 D 6 ASP B 364 CYS B 368 1 O ASP B 364 N VAL B 270 SHEET 6 D 6 ILE B 391 TYR B 393 1 O HIS B 392 N ILE B 367 CISPEP 1 THR A 279 PRO A 280 0 -1.68 CISPEP 2 ALA A 291 PRO A 292 0 -2.30 CISPEP 3 THR B 279 PRO B 280 0 -0.18 CISPEP 4 ALA B 291 PRO B 292 0 -1.07 CRYST1 52.200 85.800 103.900 90.00 81.80 90.00 P 1 21 1 4 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 0.019157 0.000000 -0.002761 0.00000 SCALE2 0.000000 0.011655 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009724 0.00000