HEADER OXIDOREDUCTASE 15-AUG-01 1JRX
TITLE CRYSTAL STRUCTURE OF ARG402ALA MUTANT FLAVOCYTOCHROME C3 FROM
TITLE 2 SHEWANELLA FRIGIDIMARINA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLAVOCYTOCHROME C;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: FUMARATE REDUCTASE FLAVOPROTEIN SUBUNIT;
COMPND 5 EC: 1.3.99.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SHEWANELLA FRIGIDIMARINA;
SOURCE 3 ORGANISM_TAXID: 56812;
SOURCE 4 GENE: FCC;
SOURCE 5 EXPRESSION_SYSTEM: SHEWANELLA FRIGIDIMARINA NCIMB 400;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 318167;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: NCIMB400;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMMB503EH
KEYWDS FUMARATE REDUCTASE, MUTANT, FLAVOCYTOCHROME, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.G.MOWAT,R.MOYSEY,C.S.MILES,D.LEYS,M.K.DOHERTY,P.TAYLOR,
AUTHOR 2 M.D.WALKINSHAW,G.A.REID,S.K.CHAPMAN
REVDAT 5 15-NOV-23 1JRX 1 ATOM
REVDAT 4 16-AUG-23 1JRX 1 REMARK
REVDAT 3 27-OCT-21 1JRX 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1JRX 1 VERSN
REVDAT 1 02-NOV-01 1JRX 0
JRNL AUTH C.G.MOWAT,R.MOYSEY,C.S.MILES,D.LEYS,M.K.DOHERTY,P.TAYLOR,
JRNL AUTH 2 M.D.WALKINSHAW,G.A.REID,S.K.CHAPMAN
JRNL TITL KINETIC AND CRYSTALLOGRAPHIC ANALYSIS OF THE KEY ACTIVE SITE
JRNL TITL 2 ACID/BASE ARGININE IN A SOLUBLE FUMARATE REDUCTASE.
JRNL REF BIOCHEMISTRY V. 40 12292 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11591148
JRNL DOI 10.1021/BI011360H
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 3 NUMBER OF REFLECTIONS : 65029
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 + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 3468
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8411
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 468
REMARK 3 SOLVENT ATOMS : 1676
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.00
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.014 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 3.100 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JRX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-01.
REMARK 100 THE DEPOSITION ID IS D_1000014118.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : DARESBURY
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 : 74263
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.20100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1QJD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, TRISHCL, SODIUM CHLORIDE,
REMARK 280 SODIUM FUMARATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP AT 277K
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,Y+1/2,-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 42.96500
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 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 LYS A 569
REMARK 465 LYS A 570
REMARK 465 ASN A 571
REMARK 465 LYS B 569
REMARK 465 LYS B 570
REMARK 465 ASN B 571
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 LYS A 476 CG CD CE NZ
REMARK 470 GLU B 23 CD OE1 OE2
REMARK 470 GLU B 481 CG CD OE1 OE2
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 DISTANCE
REMARK 500 O2' FAD B 2805 O HOH B 3035 2.11
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 176 N TRP A 176 CA -0.120
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 15 CB - CG - OD1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 LYS A 110 CD - CE - NZ ANGL. DEV. = 14.2 DEGREES
REMARK 500 LYS A 112 CA - CB - CG ANGL. DEV. = 26.7 DEGREES
REMARK 500 ARG A 115 NE - CZ - NH2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ALA A 175 N - CA - CB ANGL. DEV. = 12.6 DEGREES
REMARK 500 TRP A 176 C - N - CA ANGL. DEV. = 54.8 DEGREES
REMARK 500 TRP A 176 N - CA - CB ANGL. DEV. = 13.6 DEGREES
REMARK 500 ASP A 218 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP A 221 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A 246 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 273 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG A 277 NE - CZ - NH2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 ASP A 284 CB - CG - OD1 ANGL. DEV. = 8.9 DEGREES
REMARK 500 LYS A 286 CA - CB - CG ANGL. DEV. = 16.5 DEGREES
REMARK 500 LEU A 293 CA - CB - CG ANGL. DEV. = 25.0 DEGREES
REMARK 500 ARG A 322 NH1 - CZ - NH2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG A 322 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 322 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ASP A 327 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP A 347 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 TYR A 361 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 381 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 426 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 467 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 482 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG A 487 CD - NE - CZ ANGL. DEV. = 14.8 DEGREES
REMARK 500 ARG A 487 NE - CZ - NH1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG A 487 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 MET A 511 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 ASP A 552 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 LYS A 566 CA - CB - CG ANGL. DEV. = 16.0 DEGREES
REMARK 500 TYR A 567 O - C - N ANGL. DEV. = -10.4 DEGREES
REMARK 500 SER A 568 C - N - CA ANGL. DEV. = 25.5 DEGREES
REMARK 500 HIS B 8 CE1 - NE2 - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 CYS B 39 CA - CB - SG ANGL. DEV. = -11.2 DEGREES
REMARK 500 LYS B 112 CA - CB - CG ANGL. DEV. = 13.5 DEGREES
REMARK 500 ARG B 115 NE - CZ - NH1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ASP B 125 CB - CG - OD1 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ALA B 175 CB - CA - C ANGL. DEV. = -11.5 DEGREES
REMARK 500 ALA B 175 N - CA - CB ANGL. DEV. = 10.6 DEGREES
REMARK 500 TRP B 176 C - N - CA ANGL. DEV. = 32.2 DEGREES
REMARK 500 TRP B 176 N - CA - CB ANGL. DEV. = 25.7 DEGREES
REMARK 500 ASP B 218 CB - CG - OD2 ANGL. DEV. = -11.2 DEGREES
REMARK 500 ASP B 221 CB - CG - OD2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG B 246 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 268 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG B 273 NH1 - CZ - NH2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ARG B 273 NE - CZ - NH1 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ARG B 277 NE - CZ - NH2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 LYS B 286 N - CA - CB ANGL. DEV. = 11.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 67 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 11 25.04 -141.08
REMARK 500 THR A 42 178.02 -57.04
REMARK 500 ALA A 59 76.46 -150.48
REMARK 500 SER A 113 23.89 -72.39
REMARK 500 GLU A 114 -38.92 -159.15
REMARK 500 ALA A 169 -63.85 -122.03
REMARK 500 ARG A 243 13.96 -150.69
REMARK 500 THR A 248 136.10 -38.47
REMARK 500 ASP A 284 -167.38 -79.46
REMARK 500 PHE A 395 -1.38 -148.72
REMARK 500 ASP A 422 -169.61 -118.08
REMARK 500 ASN A 490 31.84 -154.58
REMARK 500 HIS A 504 -39.59 -131.75
REMARK 500 ASN B 26 174.67 179.87
REMARK 500 GLU B 114 -57.76 121.59
REMARK 500 SER B 134 44.61 -101.75
REMARK 500 ALA B 169 -54.22 -131.45
REMARK 500 TRP B 176 64.88 167.91
REMARK 500 THR B 248 134.55 -37.18
REMARK 500 PHE B 395 -0.19 -150.18
REMARK 500 ASP B 422 -160.66 -117.08
REMARK 500 PRO B 442 151.21 -48.28
REMARK 500 ASN B 490 13.31 -146.12
REMARK 500 HIS B 504 -39.38 -140.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA B 175 TRP B 176 100.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLU B 158 -11.25
REMARK 500 ALA B 175 16.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 802 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 8 NE2
REMARK 620 2 HEM A 802 NA 100.3
REMARK 620 3 HEM A 802 NB 90.0 90.6
REMARK 620 4 HEM A 802 NC 85.3 174.2 87.7
REMARK 620 5 HEM A 802 ND 92.5 90.8 176.8 90.6
REMARK 620 6 HIS A 40 NE2 174.3 85.2 91.0 89.2 86.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 801 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 HEM A 801 NA 91.2
REMARK 620 3 HEM A 801 NB 85.7 88.6
REMARK 620 4 HEM A 801 NC 82.3 173.1 88.7
REMARK 620 5 HEM A 801 ND 86.3 89.0 171.7 92.7
REMARK 620 6 HIS A 75 NE2 179.5 89.0 94.7 97.5 93.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 803 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 58 NE2
REMARK 620 2 HEM A 803 NA 90.2
REMARK 620 3 HEM A 803 NB 88.0 90.1
REMARK 620 4 HEM A 803 NC 88.9 178.8 89.1
REMARK 620 5 HEM A 803 ND 92.5 87.7 177.8 93.2
REMARK 620 6 HIS A 72 NE2 174.3 87.7 86.7 93.1 92.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 804 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 61 NE2
REMARK 620 2 HEM A 804 NA 88.3
REMARK 620 3 HEM A 804 NB 93.2 90.7
REMARK 620 4 HEM A 804 NC 89.6 177.9 89.1
REMARK 620 5 HEM A 804 ND 87.6 88.7 178.9 91.5
REMARK 620 6 HIS A 86 NE2 177.1 89.0 85.8 93.1 93.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1810 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 506 O
REMARK 620 2 GLY A 508 O 85.3
REMARK 620 3 GLU A 534 O 99.1 102.6
REMARK 620 4 THR A 536 O 168.8 88.1 91.1
REMARK 620 5 HOH A1811 O 89.0 156.7 100.6 93.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 802 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 8 NE2
REMARK 620 2 HEM B 802 NA 90.6
REMARK 620 3 HEM B 802 NB 94.5 91.4
REMARK 620 4 HEM B 802 NC 88.8 179.3 89.1
REMARK 620 5 HEM B 802 ND 86.4 88.3 179.0 91.2
REMARK 620 6 HIS B 40 NE2 174.7 85.8 89.5 94.7 89.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 801 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 18 NE2
REMARK 620 2 HEM B 801 NA 87.5
REMARK 620 3 HEM B 801 NB 86.4 87.9
REMARK 620 4 HEM B 801 NC 90.4 176.5 89.2
REMARK 620 5 HEM B 801 ND 90.5 90.5 176.6 92.2
REMARK 620 6 HIS B 75 NE2 171.2 84.1 90.8 97.9 91.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 803 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 58 NE2
REMARK 620 2 HEM B 803 NA 92.4
REMARK 620 3 HEM B 803 NB 97.9 89.7
REMARK 620 4 HEM B 803 NC 92.9 174.6 89.1
REMARK 620 5 HEM B 803 ND 88.0 87.1 173.4 93.5
REMARK 620 6 HIS B 72 NE2 174.6 85.7 87.1 89.0 86.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 804 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 61 NE2
REMARK 620 2 HEM B 804 NA 94.5
REMARK 620 3 HEM B 804 NB 88.3 88.2
REMARK 620 4 HEM B 804 NC 87.0 177.8 90.3
REMARK 620 5 HEM B 804 ND 92.6 90.9 178.8 90.6
REMARK 620 6 HIS B 86 NE2 174.4 89.1 87.6 89.3 91.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B2810 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 506 O
REMARK 620 2 GLY B 508 O 85.1
REMARK 620 3 GLU B 534 O 103.1 106.9
REMARK 620 4 THR B 536 O 165.9 88.3 90.8
REMARK 620 5 HOH B3033 O 87.9 155.8 97.3 93.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 2810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 1805
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 2805
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUM A 1806
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUM B 2806
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JRY RELATED DB: PDB
REMARK 900 R402K MUTANT OF THE SAME ENZYME
REMARK 900 RELATED ID: 1JRZ RELATED DB: PDB
REMARK 900 R402Y MUTANT OF THE SAME ENZYME
DBREF 1JRX A 1 571 UNP Q02469 FRDA_SHEFR 26 596
DBREF 1JRX B 1 571 UNP Q02469 FRDA_SHEFR 26 596
SEQADV 1JRX ALA A 402 UNP Q02469 ARG 427 ENGINEERED MUTATION
SEQADV 1JRX ALA B 402 UNP Q02469 ARG 427 ENGINEERED MUTATION
SEQRES 1 A 571 ALA ASP ASN LEU ALA GLU PHE HIS VAL GLN ASN GLN GLU
SEQRES 2 A 571 CYS ASP SER CYS HIS THR PRO ASP GLY GLU LEU SER ASN
SEQRES 3 A 571 ASP SER LEU THR TYR GLU ASN THR GLN CYS VAL SER CYS
SEQRES 4 A 571 HIS GLY THR LEU ALA GLU VAL ALA GLU THR THR LYS HIS
SEQRES 5 A 571 GLU HIS TYR ASN ALA HIS ALA SER HIS PHE PRO GLY GLU
SEQRES 6 A 571 VAL ALA CYS THR SER CYS HIS SER ALA HIS GLU LYS SER
SEQRES 7 A 571 MET VAL TYR CYS ASP SER CYS HIS SER PHE ASP PHE ASN
SEQRES 8 A 571 MET PRO TYR ALA LYS LYS TRP LEU ARG ASP GLU PRO THR
SEQRES 9 A 571 ILE ALA GLU LEU ALA LYS ASP LYS SER GLU ARG GLN ALA
SEQRES 10 A 571 ALA LEU ALA SER ALA PRO HIS ASP THR VAL ASP VAL VAL
SEQRES 11 A 571 VAL VAL GLY SER GLY GLY ALA GLY PHE SER ALA ALA ILE
SEQRES 12 A 571 SER ALA THR ASP SER GLY ALA LYS VAL ILE LEU ILE GLU
SEQRES 13 A 571 LYS GLU PRO VAL ILE GLY GLY ASN ALA LYS LEU ALA ALA
SEQRES 14 A 571 GLY GLY MET ASN ALA ALA TRP THR ASP GLN GLN LYS ALA
SEQRES 15 A 571 LYS LYS ILE THR ASP SER PRO GLU LEU MET PHE GLU ASP
SEQRES 16 A 571 THR MET LYS GLY GLY GLN ASN ILE ASN ASP PRO ALA LEU
SEQRES 17 A 571 VAL LYS VAL LEU SER SER HIS SER LYS ASP SER VAL ASP
SEQRES 18 A 571 TRP MET THR ALA MET GLY ALA ASP LEU THR ASP VAL GLY
SEQRES 19 A 571 MET MET GLY GLY ALA SER VAL ASN ARG ALA HIS ARG PRO
SEQRES 20 A 571 THR GLY GLY ALA GLY VAL GLY ALA HIS VAL VAL GLN VAL
SEQRES 21 A 571 LEU TYR ASP ASN ALA VAL LYS ARG ASN ILE ASP LEU ARG
SEQRES 22 A 571 MET ASN THR ARG GLY ILE GLU VAL LEU LYS ASP ASP LYS
SEQRES 23 A 571 GLY THR VAL LYS GLY ILE LEU VAL LYS GLY MET TYR LYS
SEQRES 24 A 571 GLY TYR TYR TRP VAL LYS ALA ASP ALA VAL ILE LEU ALA
SEQRES 25 A 571 THR GLY GLY PHE ALA LYS ASN ASN GLU ARG VAL ALA LYS
SEQRES 26 A 571 LEU ASP PRO SER LEU LYS GLY PHE ILE SER THR ASN GLN
SEQRES 27 A 571 PRO GLY ALA VAL GLY ASP GLY LEU ASP VAL ALA GLU ASN
SEQRES 28 A 571 ALA GLY GLY ALA LEU LYS ASP MET GLN TYR ILE GLN ALA
SEQRES 29 A 571 HIS PRO THR LEU SER VAL LYS GLY GLY VAL MET VAL THR
SEQRES 30 A 571 GLU ALA VAL ARG GLY ASN GLY ALA ILE LEU VAL ASN ARG
SEQRES 31 A 571 GLU GLY LYS ARG PHE VAL ASN GLU ILE THR THR ALA ASP
SEQRES 32 A 571 LYS ALA SER ALA ALA ILE LEU ALA GLN THR GLY LYS SER
SEQRES 33 A 571 ALA TYR LEU ILE PHE ASP ASP SER VAL ARG LYS SER LEU
SEQRES 34 A 571 SER LYS ILE ASP LYS TYR ILE GLY LEU GLY VAL ALA PRO
SEQRES 35 A 571 THR ALA ASP SER LEU VAL LYS LEU GLY LYS MET GLU GLY
SEQRES 36 A 571 ILE ASP GLY LYS ALA LEU THR GLU THR VAL ALA ARG TYR
SEQRES 37 A 571 ASN SER LEU VAL SER SER GLY LYS ASP THR ASP PHE GLU
SEQRES 38 A 571 ARG PRO ASN LEU PRO ARG ALA LEU ASN GLU GLY ASN TYR
SEQRES 39 A 571 TYR ALA ILE GLU VAL THR PRO GLY VAL HIS HIS THR MET
SEQRES 40 A 571 GLY GLY VAL MET ILE ASP THR LYS ALA GLU VAL MET ASN
SEQRES 41 A 571 ALA LYS LYS GLN VAL ILE PRO GLY LEU TYR GLY ALA GLY
SEQRES 42 A 571 GLU VAL THR GLY GLY VAL HIS GLY ALA ASN ARG LEU GLY
SEQRES 43 A 571 GLY ASN ALA ILE SER ASP ILE ILE THR PHE GLY ARG LEU
SEQRES 44 A 571 ALA GLY GLU GLU ALA ALA LYS TYR SER LYS LYS ASN
SEQRES 1 B 571 ALA ASP ASN LEU ALA GLU PHE HIS VAL GLN ASN GLN GLU
SEQRES 2 B 571 CYS ASP SER CYS HIS THR PRO ASP GLY GLU LEU SER ASN
SEQRES 3 B 571 ASP SER LEU THR TYR GLU ASN THR GLN CYS VAL SER CYS
SEQRES 4 B 571 HIS GLY THR LEU ALA GLU VAL ALA GLU THR THR LYS HIS
SEQRES 5 B 571 GLU HIS TYR ASN ALA HIS ALA SER HIS PHE PRO GLY GLU
SEQRES 6 B 571 VAL ALA CYS THR SER CYS HIS SER ALA HIS GLU LYS SER
SEQRES 7 B 571 MET VAL TYR CYS ASP SER CYS HIS SER PHE ASP PHE ASN
SEQRES 8 B 571 MET PRO TYR ALA LYS LYS TRP LEU ARG ASP GLU PRO THR
SEQRES 9 B 571 ILE ALA GLU LEU ALA LYS ASP LYS SER GLU ARG GLN ALA
SEQRES 10 B 571 ALA LEU ALA SER ALA PRO HIS ASP THR VAL ASP VAL VAL
SEQRES 11 B 571 VAL VAL GLY SER GLY GLY ALA GLY PHE SER ALA ALA ILE
SEQRES 12 B 571 SER ALA THR ASP SER GLY ALA LYS VAL ILE LEU ILE GLU
SEQRES 13 B 571 LYS GLU PRO VAL ILE GLY GLY ASN ALA LYS LEU ALA ALA
SEQRES 14 B 571 GLY GLY MET ASN ALA ALA TRP THR ASP GLN GLN LYS ALA
SEQRES 15 B 571 LYS LYS ILE THR ASP SER PRO GLU LEU MET PHE GLU ASP
SEQRES 16 B 571 THR MET LYS GLY GLY GLN ASN ILE ASN ASP PRO ALA LEU
SEQRES 17 B 571 VAL LYS VAL LEU SER SER HIS SER LYS ASP SER VAL ASP
SEQRES 18 B 571 TRP MET THR ALA MET GLY ALA ASP LEU THR ASP VAL GLY
SEQRES 19 B 571 MET MET GLY GLY ALA SER VAL ASN ARG ALA HIS ARG PRO
SEQRES 20 B 571 THR GLY GLY ALA GLY VAL GLY ALA HIS VAL VAL GLN VAL
SEQRES 21 B 571 LEU TYR ASP ASN ALA VAL LYS ARG ASN ILE ASP LEU ARG
SEQRES 22 B 571 MET ASN THR ARG GLY ILE GLU VAL LEU LYS ASP ASP LYS
SEQRES 23 B 571 GLY THR VAL LYS GLY ILE LEU VAL LYS GLY MET TYR LYS
SEQRES 24 B 571 GLY TYR TYR TRP VAL LYS ALA ASP ALA VAL ILE LEU ALA
SEQRES 25 B 571 THR GLY GLY PHE ALA LYS ASN ASN GLU ARG VAL ALA LYS
SEQRES 26 B 571 LEU ASP PRO SER LEU LYS GLY PHE ILE SER THR ASN GLN
SEQRES 27 B 571 PRO GLY ALA VAL GLY ASP GLY LEU ASP VAL ALA GLU ASN
SEQRES 28 B 571 ALA GLY GLY ALA LEU LYS ASP MET GLN TYR ILE GLN ALA
SEQRES 29 B 571 HIS PRO THR LEU SER VAL LYS GLY GLY VAL MET VAL THR
SEQRES 30 B 571 GLU ALA VAL ARG GLY ASN GLY ALA ILE LEU VAL ASN ARG
SEQRES 31 B 571 GLU GLY LYS ARG PHE VAL ASN GLU ILE THR THR ALA ASP
SEQRES 32 B 571 LYS ALA SER ALA ALA ILE LEU ALA GLN THR GLY LYS SER
SEQRES 33 B 571 ALA TYR LEU ILE PHE ASP ASP SER VAL ARG LYS SER LEU
SEQRES 34 B 571 SER LYS ILE ASP LYS TYR ILE GLY LEU GLY VAL ALA PRO
SEQRES 35 B 571 THR ALA ASP SER LEU VAL LYS LEU GLY LYS MET GLU GLY
SEQRES 36 B 571 ILE ASP GLY LYS ALA LEU THR GLU THR VAL ALA ARG TYR
SEQRES 37 B 571 ASN SER LEU VAL SER SER GLY LYS ASP THR ASP PHE GLU
SEQRES 38 B 571 ARG PRO ASN LEU PRO ARG ALA LEU ASN GLU GLY ASN TYR
SEQRES 39 B 571 TYR ALA ILE GLU VAL THR PRO GLY VAL HIS HIS THR MET
SEQRES 40 B 571 GLY GLY VAL MET ILE ASP THR LYS ALA GLU VAL MET ASN
SEQRES 41 B 571 ALA LYS LYS GLN VAL ILE PRO GLY LEU TYR GLY ALA GLY
SEQRES 42 B 571 GLU VAL THR GLY GLY VAL HIS GLY ALA ASN ARG LEU GLY
SEQRES 43 B 571 GLY ASN ALA ILE SER ASP ILE ILE THR PHE GLY ARG LEU
SEQRES 44 B 571 ALA GLY GLU GLU ALA ALA LYS TYR SER LYS LYS ASN
HET NA A1810 1
HET HEM A 801 43
HET HEM A 802 43
HET HEM A 803 43
HET HEM A 804 43
HET FAD A1805 53
HET FUM A1806 8
HET NA B2810 1
HET HEM B 801 43
HET HEM B 802 43
HET HEM B 803 43
HET HEM B 804 43
HET FAD B2805 53
HET FUM B2806 8
HETNAM NA SODIUM ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM FUM FUMARIC ACID
HETSYN HEM HEME
FORMUL 3 NA 2(NA 1+)
FORMUL 4 HEM 8(C34 H32 FE N4 O4)
FORMUL 8 FAD 2(C27 H33 N9 O15 P2)
FORMUL 9 FUM 2(C4 H4 O4)
FORMUL 17 HOH *1676(H2 O)
HELIX 1 1 ASN A 3 GLN A 10 1 8
HELIX 2 2 ASN A 11 GLN A 12 5 2
HELIX 3 3 GLU A 13 CYS A 17 5 5
HELIX 4 4 LEU A 29 GLY A 41 1 13
HELIX 5 5 THR A 42 THR A 49 1 8
HELIX 6 6 ALA A 67 CYS A 71 5 5
HELIX 7 7 TYR A 81 CYS A 85 5 5
HELIX 8 8 ALA A 106 LYS A 110 5 5
HELIX 9 9 ASP A 111 SER A 121 1 11
HELIX 10 10 GLY A 135 SER A 148 1 14
HELIX 11 11 ASN A 164 ALA A 168 5 5
HELIX 12 12 THR A 177 LYS A 183 1 7
HELIX 13 13 SER A 188 GLY A 200 1 13
HELIX 14 14 ASP A 205 MET A 226 1 22
HELIX 15 15 GLY A 252 ARG A 268 1 17
HELIX 16 16 ASN A 319 ASP A 327 1 9
HELIX 17 17 PRO A 328 LYS A 331 5 4
HELIX 18 18 GLY A 343 ALA A 352 1 10
HELIX 19 19 GLU A 378 ASN A 383 1 6
HELIX 20 20 THR A 401 ALA A 411 1 11
HELIX 21 21 GLN A 412 SER A 416 5 5
HELIX 22 22 ASP A 423 LEU A 429 1 7
HELIX 23 23 SER A 430 GLY A 439 1 10
HELIX 24 24 SER A 446 GLY A 455 1 10
HELIX 25 25 ASP A 457 GLY A 475 1 19
HELIX 26 26 GLY A 547 SER A 568 1 22
HELIX 27 27 ASN B 3 GLN B 10 1 8
HELIX 28 28 GLU B 13 CYS B 17 5 5
HELIX 29 29 LEU B 29 GLY B 41 1 13
HELIX 30 30 THR B 42 GLU B 48 1 7
HELIX 31 31 ALA B 67 CYS B 71 5 5
HELIX 32 32 TYR B 81 CYS B 85 5 5
HELIX 33 33 ILE B 105 LYS B 110 5 6
HELIX 34 34 ASP B 111 SER B 121 1 11
HELIX 35 35 GLY B 135 SER B 148 1 14
HELIX 36 36 ASN B 164 ALA B 168 5 5
HELIX 37 37 THR B 177 LYS B 183 1 7
HELIX 38 38 SER B 188 GLY B 200 1 13
HELIX 39 39 ASP B 205 MET B 226 1 22
HELIX 40 40 GLY B 252 ARG B 268 1 17
HELIX 41 41 ASN B 319 ASP B 327 1 9
HELIX 42 42 PRO B 328 LYS B 331 5 4
HELIX 43 43 GLY B 343 ALA B 352 1 10
HELIX 44 44 THR B 377 ASN B 383 1 7
HELIX 45 45 THR B 401 ALA B 411 1 11
HELIX 46 46 GLN B 412 SER B 416 5 5
HELIX 47 47 ASP B 423 LEU B 429 1 7
HELIX 48 48 SER B 430 GLY B 439 1 10
HELIX 49 49 SER B 446 GLY B 455 1 10
HELIX 50 50 ASP B 457 GLY B 475 1 19
HELIX 51 51 GLY B 547 SER B 568 1 22
SHEET 1 A 2 SER A 78 MET A 79 0
SHEET 2 A 2 ALA A 95 LYS A 96 1 O LYS A 96 N SER A 78
SHEET 1 B 4 ASP A 125 THR A 126 0
SHEET 2 B 4 GLY A 300 LYS A 305 1 O LYS A 305 N ASP A 125
SHEET 3 B 4 VAL A 289 GLY A 296 -1 N VAL A 294 O TYR A 302
SHEET 4 B 4 THR A 276 LYS A 283 -1 N ARG A 277 O LYS A 295
SHEET 1 C 6 ASP A 271 ARG A 273 0
SHEET 2 C 6 VAL A 152 ILE A 155 1 N LEU A 154 O ASP A 271
SHEET 3 C 6 VAL A 129 VAL A 132 1 N VAL A 131 O ILE A 153
SHEET 4 C 6 ALA A 308 LEU A 311 1 O ILE A 310 N VAL A 132
SHEET 5 C 6 VAL A 525 GLY A 531 1 O TYR A 530 N LEU A 311
SHEET 6 C 6 GLU A 517 MET A 519 -1 N VAL A 518 O LEU A 529
SHEET 1 D 3 MET A 172 ASN A 173 0
SHEET 2 D 3 ALA A 244 ARG A 246 -1 O HIS A 245 N MET A 172
SHEET 3 D 3 ASP A 232 GLY A 234 -1 N ASP A 232 O ARG A 246
SHEET 1 E 3 LEU A 356 LYS A 357 0
SHEET 2 E 3 GLY A 509 MET A 511 -1 O GLY A 509 N LYS A 357
SHEET 3 E 3 THR A 536 GLY A 537 1 O GLY A 537 N VAL A 510
SHEET 1 F 4 ILE A 362 SER A 369 0
SHEET 2 F 4 TYR A 494 THR A 506 -1 O HIS A 504 N GLN A 363
SHEET 3 F 4 ALA A 417 ASP A 422 -1 N ALA A 417 O VAL A 499
SHEET 4 F 4 ILE A 386 VAL A 388 -1 N VAL A 388 O TYR A 418
SHEET 1 G 3 ILE A 362 SER A 369 0
SHEET 2 G 3 TYR A 494 THR A 506 -1 O HIS A 504 N GLN A 363
SHEET 3 G 3 THR A 443 ALA A 444 -1 N ALA A 444 O TYR A 494
SHEET 1 H 2 SER B 78 MET B 79 0
SHEET 2 H 2 ALA B 95 LYS B 96 1 O LYS B 96 N SER B 78
SHEET 1 I 4 ASP B 125 THR B 126 0
SHEET 2 I 4 GLY B 300 LYS B 305 1 O LYS B 305 N ASP B 125
SHEET 3 I 4 VAL B 289 GLY B 296 -1 N VAL B 294 O TYR B 302
SHEET 4 I 4 THR B 276 LYS B 283 -1 N LEU B 282 O LYS B 290
SHEET 1 J 6 ASP B 271 ARG B 273 0
SHEET 2 J 6 VAL B 152 ILE B 155 1 N LEU B 154 O ASP B 271
SHEET 3 J 6 VAL B 129 VAL B 132 1 N VAL B 131 O ILE B 153
SHEET 4 J 6 ALA B 308 LEU B 311 1 O ILE B 310 N VAL B 132
SHEET 5 J 6 VAL B 525 GLY B 531 1 O TYR B 530 N LEU B 311
SHEET 6 J 6 GLU B 517 MET B 519 -1 N VAL B 518 O LEU B 529
SHEET 1 K 3 MET B 172 ASN B 173 0
SHEET 2 K 3 ALA B 244 ARG B 246 -1 O HIS B 245 N MET B 172
SHEET 3 K 3 ASP B 232 GLY B 234 -1 N GLY B 234 O ALA B 244
SHEET 1 L 3 LEU B 356 LYS B 357 0
SHEET 2 L 3 GLY B 509 MET B 511 -1 O GLY B 509 N LYS B 357
SHEET 3 L 3 THR B 536 GLY B 537 1 O GLY B 537 N VAL B 510
SHEET 1 M 4 ILE B 362 SER B 369 0
SHEET 2 M 4 TYR B 494 THR B 506 -1 O HIS B 505 N GLN B 363
SHEET 3 M 4 ALA B 417 ASP B 422 -1 N ALA B 417 O VAL B 499
SHEET 4 M 4 ILE B 386 VAL B 388 -1 N VAL B 388 O TYR B 418
SHEET 1 N 3 ILE B 362 SER B 369 0
SHEET 2 N 3 TYR B 494 THR B 506 -1 O HIS B 505 N GLN B 363
SHEET 3 N 3 THR B 443 ALA B 444 -1 N ALA B 444 O TYR B 494
LINK NE2 HIS A 8 FE HEM A 802 1555 1555 2.16
LINK NE2 HIS A 18 FE HEM A 801 1555 1555 2.03
LINK NE2 HIS A 40 FE HEM A 802 1555 1555 2.02
LINK NE2 HIS A 58 FE HEM A 803 1555 1555 2.09
LINK NE2 HIS A 61 FE HEM A 804 1555 1555 2.02
LINK NE2 HIS A 72 FE HEM A 803 1555 1555 2.06
LINK NE2 HIS A 75 FE HEM A 801 1555 1555 2.10
LINK NE2 HIS A 86 FE HEM A 804 1555 1555 2.06
LINK O THR A 506 NA NA A1810 1555 1555 2.49
LINK O GLY A 508 NA NA A1810 1555 1555 2.43
LINK O GLU A 534 NA NA A1810 1555 1555 2.43
LINK O THR A 536 NA NA A1810 1555 1555 2.43
LINK NA NA A1810 O HOH A1811 1555 1555 2.42
LINK NE2 HIS B 8 FE HEM B 802 1555 1555 2.02
LINK NE2 HIS B 18 FE HEM B 801 1555 1555 1.96
LINK NE2 HIS B 40 FE HEM B 802 1555 1555 2.02
LINK NE2 HIS B 58 FE HEM B 803 1555 1555 2.16
LINK NE2 HIS B 61 FE HEM B 804 1555 1555 2.12
LINK NE2 HIS B 72 FE HEM B 803 1555 1555 2.07
LINK NE2 HIS B 75 FE HEM B 801 1555 1555 2.05
LINK NE2 HIS B 86 FE HEM B 804 1555 1555 1.95
LINK O THR B 506 NA NA B2810 1555 1555 2.43
LINK O GLY B 508 NA NA B2810 1555 1555 2.44
LINK O GLU B 534 NA NA B2810 1555 1555 2.41
LINK O THR B 536 NA NA B2810 1555 1555 2.45
LINK NA NA B2810 O HOH B3033 1555 1555 2.48
CISPEP 1 ALA A 175 TRP A 176 0 21.84
SITE 1 AC1 6 THR A 506 MET A 507 GLY A 508 GLU A 534
SITE 2 AC1 6 THR A 536 HOH A1811
SITE 1 AC2 6 THR B 506 MET B 507 GLY B 508 GLU B 534
SITE 2 AC2 6 THR B 536 HOH B3033
SITE 1 AC3 16 HIS A 8 VAL A 9 CYS A 14 CYS A 17
SITE 2 AC3 16 HIS A 18 LEU A 24 THR A 69 SER A 73
SITE 3 AC3 16 ALA A 74 HIS A 75 TYR A 298 HEM A 802
SITE 4 AC3 16 HOH A2056 HOH A2151 HOH A2172 HOH A2221
SITE 1 AC4 18 LEU A 4 PHE A 7 HIS A 8 GLN A 12
SITE 2 AC4 18 SER A 16 CYS A 17 CYS A 36 CYS A 39
SITE 3 AC4 18 HIS A 40 HIS A 72 TYR A 94 HEM A 801
SITE 4 AC4 18 HEM A 803 HOH A1877 HOH A1909 HOH A2075
SITE 5 AC4 18 HOH A2226 HOH A2540
SITE 1 AC5 24 HIS A 40 GLY A 41 LEU A 43 VAL A 46
SITE 2 AC5 24 THR A 49 THR A 50 HIS A 52 ALA A 57
SITE 3 AC5 24 HIS A 58 VAL A 66 ALA A 67 CYS A 68
SITE 4 AC5 24 CYS A 71 HIS A 72 VAL A 80 CYS A 82
SITE 5 AC5 24 PHE A 90 ASN A 91 MET A 92 HEM A 802
SITE 6 AC5 24 HEM A 804 HOH A1815 HOH A2164 HOH A2321
SITE 1 AC6 27 HIS A 54 TYR A 55 ASN A 56 SER A 60
SITE 2 AC6 27 HIS A 61 PHE A 62 CYS A 82 SER A 84
SITE 3 AC6 27 CYS A 85 HIS A 86 PHE A 88 LEU A 167
SITE 4 AC6 27 GLN A 338 VAL A 374 LYS A 431 LYS A 434
SITE 5 AC6 27 TYR A 435 HEM A 803 HOH A1887 HOH A1973
SITE 6 AC6 27 HOH A1976 HOH A2080 HOH A2091 HOH A2123
SITE 7 AC6 27 HOH A2225 HOH A2245 HOH A2312
SITE 1 AC7 18 HIS B 8 VAL B 9 CYS B 14 CYS B 17
SITE 2 AC7 18 HIS B 18 LEU B 24 SER B 73 ALA B 74
SITE 3 AC7 18 HIS B 75 TYR B 298 HEM B 802 HOH B1278
SITE 4 AC7 18 HOH B1394 HOH B1552 HOH B1638 HOH B1771
SITE 5 AC7 18 HOH B3041 HOH B3284
SITE 1 AC8 21 LEU B 4 PHE B 7 HIS B 8 GLN B 12
SITE 2 AC8 21 SER B 16 CYS B 17 GLN B 35 CYS B 36
SITE 3 AC8 21 CYS B 39 HIS B 40 HIS B 72 PRO B 93
SITE 4 AC8 21 TYR B 94 HEM B 801 HEM B 803 HOH B1469
SITE 5 AC8 21 HOH B1556 HOH B2128 HOH B2192 HOH B3090
SITE 6 AC8 21 HOH B3181
SITE 1 AC9 19 HIS B 40 LEU B 43 VAL B 46 HIS B 52
SITE 2 AC9 19 ALA B 57 HIS B 58 VAL B 66 ALA B 67
SITE 3 AC9 19 CYS B 68 CYS B 71 HIS B 72 PHE B 90
SITE 4 AC9 19 ASN B 91 MET B 92 HEM B 802 HEM B 804
SITE 5 AC9 19 HOH B1021 HOH B1202 HOH B1942
SITE 1 BC1 24 HIS B 54 ASN B 56 SER B 60 HIS B 61
SITE 2 BC1 24 PHE B 62 CYS B 82 SER B 84 CYS B 85
SITE 3 BC1 24 HIS B 86 PHE B 88 LEU B 167 GLN B 338
SITE 4 BC1 24 VAL B 374 LYS B 431 LYS B 434 TYR B 435
SITE 5 BC1 24 HEM B 803 HOH B1006 HOH B1454 HOH B1568
SITE 6 BC1 24 HOH B1594 HOH B1681 HOH B1731 HOH B1884
SITE 1 BC2 45 VAL A 132 GLY A 133 SER A 134 GLY A 135
SITE 2 BC2 45 GLY A 136 ALA A 137 GLU A 156 LYS A 157
SITE 3 BC2 45 GLU A 158 GLY A 162 GLY A 163 ASN A 164
SITE 4 BC2 45 ALA A 165 LEU A 167 ALA A 168 ALA A 169
SITE 5 BC2 45 GLY A 170 GLY A 171 THR A 276 ARG A 277
SITE 6 BC2 45 GLY A 278 ALA A 312 THR A 313 GLY A 314
SITE 7 BC2 45 THR A 336 ASN A 337 GLN A 338 ASP A 344
SITE 8 BC2 45 MET A 375 HIS A 504 HIS A 505 GLY A 533
SITE 9 BC2 45 GLU A 534 ARG A 544 GLY A 547 ASN A 548
SITE 10 BC2 45 ALA A 549 ILE A 550 ILE A 553 FUM A1806
SITE 11 BC2 45 HOH A1819 HOH A1869 HOH A1889 HOH A1905
SITE 12 BC2 45 HOH A1911
SITE 1 BC3 45 VAL B 132 GLY B 133 GLY B 135 GLY B 136
SITE 2 BC3 45 ALA B 137 GLU B 156 LYS B 157 GLU B 158
SITE 3 BC3 45 GLY B 162 GLY B 163 ASN B 164 ALA B 165
SITE 4 BC3 45 LEU B 167 ALA B 168 ALA B 169 GLY B 170
SITE 5 BC3 45 GLY B 171 THR B 276 ARG B 277 GLY B 278
SITE 6 BC3 45 ALA B 312 THR B 313 GLY B 314 THR B 336
SITE 7 BC3 45 ASN B 337 GLN B 338 ASP B 344 MET B 375
SITE 8 BC3 45 HIS B 504 HIS B 505 GLY B 533 GLU B 534
SITE 9 BC3 45 ARG B 544 GLY B 547 ASN B 548 ALA B 549
SITE 10 BC3 45 ILE B 550 ILE B 553 HOH B1009 HOH B1042
SITE 11 BC3 45 HOH B1057 HOH B1150 HOH B1208 FUM B2806
SITE 12 BC3 45 HOH B3035
SITE 1 BC4 11 GLY A 170 MET A 236 HIS A 365 MET A 375
SITE 2 BC4 11 THR A 377 GLU A 378 HIS A 504 ARG A 544
SITE 3 BC4 11 GLY A 546 GLY A 547 FAD A1805
SITE 1 BC5 12 GLY B 170 MET B 236 HIS B 365 MET B 375
SITE 2 BC5 12 THR B 377 GLU B 378 HIS B 504 ARG B 544
SITE 3 BC5 12 GLY B 546 GLY B 547 HOH B1375 FAD B2805
CRYST1 75.966 85.930 88.320 90.00 104.74 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 0.013164 0.000000 0.003463 0.00000
SCALE2 0.000000 0.011637 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011708 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
