HEADER OXIDOREDUCTASE 13-JUN-06 2IVE
TITLE STRUCTURE OF PROTOPORPHYRINOGEN OXIDASE FROM MYXOCOCCUS XANTHUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTOPORPHYRINOGEN OXIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PPO, PPOX;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYXOCOCCUS XANTHUS;
SOURCE 3 ORGANISM_TAXID: 34;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: JM109
KEYWDS OXIDOREDUCTASE, PROTOPORPHYRINOGEN OXIDASE, PORPHYRIN BIOSYNTHESIS,
KEYWDS 2 CHLOROPHYLL BIOSYNTHESIS, FAD, PORPHYRIA, FLAVOPROTEIN, HEME
KEYWDS 3 BIOSYNTHESIS, HAEM BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR H.R.CORRADI,A.V.CORRIGALL,E.BOIX,C.G.MOHAN,E.D.STURROCK,P.N.MEISSNER,
AUTHOR 2 K.R.ACHARYA
REVDAT 5 13-DEC-23 2IVE 1 REMARK
REVDAT 4 24-FEB-09 2IVE 1 VERSN
REVDAT 3 13-DEC-06 2IVE 1 JRNL
REVDAT 2 25-OCT-06 2IVE 1 JRNL
REVDAT 1 17-OCT-06 2IVE 0
JRNL AUTH H.R.CORRADI,A.V.CORRIGALL,E.BOIX,C.G.MOHAN,E.D.STURROCK,
JRNL AUTH 2 P.N.MEISSNER,K.R.ACHARYA
JRNL TITL CRYSTAL STRUCTURE OF PROTOPORPHYRINOGEN OXIDASE FROM
JRNL TITL 2 MYXOCOCCUS XANTHUS AND ITS COMPLEX WITH THE INHIBITOR
JRNL TITL 3 ACIFLUORFEN.
JRNL REF J.BIOL.CHEM. V. 281 38625 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 17046834
JRNL DOI 10.1074/JBC.M606640200
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 74.33
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 40498
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) : 0.248
REMARK 3 R VALUE (WORKING SET) : 0.247
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.100
REMARK 3 FREE R VALUE TEST SET COUNT : 857
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2914
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3290
REMARK 3 BIN FREE R VALUE SET COUNT : 79
REMARK 3 BIN FREE R VALUE : 0.3350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6648
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 217
REMARK 3 SOLVENT ATOMS : 146
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.04000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.496
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.323
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.262
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.894
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.889
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.849
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6920 ; 0.006 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9399 ; 1.122 ; 2.005
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 897 ; 4.828 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 270 ;29.385 ;21.852
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1007 ;17.243 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 74 ;16.514 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1078 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5194 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3062 ; 0.189 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4622 ; 0.295 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 277 ; 0.118 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 50 ; 0.161 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.114 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4543 ; 0.269 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6992 ; 0.484 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2673 ; 0.431 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2407 ; 0.764 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. RESIDUES 87-93 IN BOTH MOLECULES COULD NOT BE
REMARK 3 MODELLED VERY ACCURATELY DUE TO LOTS OF NOISE IN THE MAPS
REMARK 4
REMARK 4 2IVE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1290029093.
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 : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41382
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 74.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.57000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER, MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1SEZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS/HCL PH 7.5, 1.5M AMMONIUM
REMARK 280 SULPHATE, 20% GLYCEROL, 1% PEG 4000, PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z
REMARK 290 4555 Y+1/2,-X+1/2,Z
REMARK 290 5555 -X+1/2,Y+1/2,-Z
REMARK 290 6555 X+1/2,-Y+1/2,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 74.28300
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 74.28300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 74.28300
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 74.28300
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 74.28300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 74.28300
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 74.28300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 74.28300
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B2052 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 PROTOPORPHYRINOGEN OXIDASE IS RESPONSIBLE FOR THE CATALYTIC
REMARK 400 OXIDATION OF PROTOPORPHYRINOGEN IX.
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 -6
REMARK 465 ASP A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 MET A 4
REMARK 465 PRO A 5
REMARK 465 ARG A 6
REMARK 465 THR A 7
REMARK 465 THR A 8
REMARK 465 GLY A 9
REMARK 465 ALA A 210
REMARK 465 LEU A 211
REMARK 465 PRO A 212
REMARK 465 ALA A 213
REMARK 465 GLY A 465
REMARK 465 ASN A 466
REMARK 465 THR A 467
REMARK 465 SER A 468
REMARK 465 HIS A 469
REMARK 465 ALA A 470
REMARK 465 PRO A 471
REMARK 465 MET B -6
REMARK 465 ASP B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 HIS B 1
REMARK 465 HIS B 2
REMARK 465 HIS B 3
REMARK 465 MET B 4
REMARK 465 PRO B 5
REMARK 465 ARG B 6
REMARK 465 THR B 7
REMARK 465 THR B 8
REMARK 465 GLY B 9
REMARK 465 ALA B 210
REMARK 465 LEU B 211
REMARK 465 PRO B 212
REMARK 465 ALA B 213
REMARK 465 GLY B 214
REMARK 465 THR B 215
REMARK 465 ALA B 216
REMARK 465 THR B 467
REMARK 465 SER B 468
REMARK 465 HIS B 469
REMARK 465 ALA B 470
REMARK 465 PRO B 471
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 MET A 10 CG SD CE
REMARK 470 GLN A 206 CD OE1 NE2
REMARK 470 ARG A 207 CD NE CZ NH1 NH2
REMARK 470 MET B 10 CG SD CE
REMARK 470 ASP B 258 CG OD1 OD2
REMARK 470 ARG B 432 CD NE CZ NH1 NH2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ASP A 89 CG OD1 OD2
REMARK 480 LYS A 93 CG CD CE NZ
REMARK 480 ARG A 134 NE CZ NH1 NH2
REMARK 480 THR A 215 CB OG1 CG2
REMARK 480 LYS A 218 CD CE NZ
REMARK 480 ARG A 256 NE CZ NH1 NH2
REMARK 480 ARG A 262 NE CZ NH1 NH2
REMARK 480 ARG A 270 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 290 CD CE NZ
REMARK 480 ASP B 89 CG OD1 OD2
REMARK 480 LYS B 93 CG CD CE NZ
REMARK 480 GLN B 203 CG CD OE1 NE2
REMARK 480 GLN B 206 CD OE1 NE2
REMARK 480 ARG B 207 CD NE CZ NH1 NH2
REMARK 480 GLN B 208 CG CD OE1 NE2
REMARK 480 ARG B 262 NE CZ NH1 NH2
REMARK 480 LYS B 290 CE NZ
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 CB ALA A 92 CA GLY A 328 2.18
REMARK 500 CB ALA A 88 O LEU A 223 2.18
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 ARG A 262 CD ARG A 262 NE 0.118
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 PRO A 217 C - N - CA ANGL. DEV. = -12.7 DEGREES
REMARK 500 PRO B 90 C - N - CD ANGL. DEV. = -16.8 DEGREES
REMARK 500 GLN B 206 CG - CD - OE1 ANGL. DEV. = -12.2 DEGREES
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 SER A 30 10.60 -69.04
REMARK 500 ALA A 78 12.03 -69.57
REMARK 500 ALA A 87 129.19 -33.20
REMARK 500 ALA A 88 84.89 -63.51
REMARK 500 ASP A 89 -146.05 -67.48
REMARK 500 PRO A 90 -112.04 -77.83
REMARK 500 ALA A 91 -137.01 43.35
REMARK 500 ARG A 193 -65.99 71.49
REMARK 500 GLN A 208 57.52 -110.88
REMARK 500 THR A 215 70.12 140.12
REMARK 500 ALA A 216 178.82 112.49
REMARK 500 PRO A 217 -164.96 -106.28
REMARK 500 THR A 225 -159.12 -146.44
REMARK 500 GLU A 257 90.51 -178.85
REMARK 500 ASP A 258 74.57 49.87
REMARK 500 GLU A 267 -100.69 -104.86
REMARK 500 LEU A 410 79.30 -106.50
REMARK 500 TYR A 443 -76.84 -100.38
REMARK 500 ASN B 80 71.71 31.88
REMARK 500 ALA B 88 76.67 54.59
REMARK 500 ASP B 89 -114.05 -103.92
REMARK 500 PRO B 90 -167.44 -6.21
REMARK 500 ARG B 193 -59.52 69.58
REMARK 500 ASP B 258 -99.92 -42.54
REMARK 500 HIS B 268 -42.68 67.79
REMARK 500 LEU B 410 72.68 -108.63
REMARK 500 TYR B 443 -78.21 -106.54
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 A 88 ASP A 89 -149.75
REMARK 500 ASP A 89 PRO A 90 -131.60
REMARK 500 ALA A 92 LYS A 93 145.86
REMARK 500 ILE A 345 HIS A 346 57.02
REMARK 500 ASP B 89 PRO B 90 -106.87
REMARK 500 GLY B 269 ARG B 270 76.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A2114
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TWN A4002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B2114
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TWN B4001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TWN B4003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A3003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B3005
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B3006
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B3007
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2IVD RELATED DB: PDB
REMARK 900 STRUCTURE OF PROTOPORPHYRINOGEN OXIDASE FROM MYXOCOCCUS XANTHUS
REMARK 900 WITH ACIFLUORFEN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FIRST MET IN THE PPOX SEQUENCE WAS REPLACED BY THE
REMARK 999 HIS TAG IN THE CONSTRUCT, BUT THIS RESIDUE WAS NOT
REMARK 999 OBSERVED IN THE STRUCTURE
DBREF 2IVE A -6 3 PDB 2IVE 2IVE -6 3
DBREF 2IVE A 4 471 UNP P56601 PPOX_MYXXA 4 471
DBREF 2IVE B -6 3 PDB 2IVE 2IVE -6 3
DBREF 2IVE B 4 471 UNP P56601 PPOX_MYXXA 4 471
SEQRES 1 A 478 MET ASP HIS HIS HIS HIS HIS HIS HIS HIS MET PRO ARG
SEQRES 2 A 478 THR THR GLY MET ASN VAL ALA VAL VAL GLY GLY GLY ILE
SEQRES 3 A 478 SER GLY LEU ALA VAL ALA HIS HIS LEU ARG SER ARG GLY
SEQRES 4 A 478 THR ASP ALA VAL LEU LEU GLU SER SER ALA ARG LEU GLY
SEQRES 5 A 478 GLY ALA VAL GLY THR HIS ALA LEU ALA GLY TYR LEU VAL
SEQRES 6 A 478 GLU GLN GLY PRO ASN SER PHE LEU ASP ARG GLU PRO ALA
SEQRES 7 A 478 THR ARG ALA LEU ALA ALA ALA LEU ASN LEU GLU GLY ARG
SEQRES 8 A 478 ILE ARG ALA ALA ASP PRO ALA ALA LYS ARG ARG TYR VAL
SEQRES 9 A 478 TYR THR ARG GLY ARG LEU ARG SER VAL PRO ALA SER PRO
SEQRES 10 A 478 PRO ALA PHE LEU ALA SER ASP ILE LEU PRO LEU GLY ALA
SEQRES 11 A 478 ARG LEU ARG VAL ALA GLY GLU LEU PHE SER ARG ARG ALA
SEQRES 12 A 478 PRO GLU GLY VAL ASP GLU SER LEU ALA ALA PHE GLY ARG
SEQRES 13 A 478 ARG HIS LEU GLY HIS ARG ALA THR GLN VAL LEU LEU ASP
SEQRES 14 A 478 ALA VAL GLN THR GLY ILE TYR ALA GLY ASP VAL GLU GLN
SEQRES 15 A 478 LEU SER VAL ALA ALA THR PHE PRO MET LEU VAL LYS MET
SEQRES 16 A 478 GLU ARG GLU HIS ARG SER LEU ILE LEU GLY ALA ILE ARG
SEQRES 17 A 478 ALA GLN LYS ALA GLN ARG GLN ALA ALA LEU PRO ALA GLY
SEQRES 18 A 478 THR ALA PRO LYS LEU SER GLY ALA LEU SER THR PHE ASP
SEQRES 19 A 478 GLY GLY LEU GLN VAL LEU ILE ASP ALA LEU ALA ALA SER
SEQRES 20 A 478 LEU GLY ASP ALA ALA HIS VAL GLY ALA ARG VAL GLU GLY
SEQRES 21 A 478 LEU ALA ARG GLU ASP GLY GLY TRP ARG LEU ILE ILE GLU
SEQRES 22 A 478 GLU HIS GLY ARG ARG ALA GLU LEU SER VAL ALA GLN VAL
SEQRES 23 A 478 VAL LEU ALA ALA PRO ALA HIS ALA THR ALA LYS LEU LEU
SEQRES 24 A 478 ARG PRO LEU ASP ASP ALA LEU ALA ALA LEU VAL ALA GLY
SEQRES 25 A 478 ILE ALA TYR ALA PRO ILE ALA VAL VAL HIS LEU GLY PHE
SEQRES 26 A 478 ASP ALA GLY THR LEU PRO ALA PRO ASP GLY PHE GLY PHE
SEQRES 27 A 478 LEU VAL PRO ALA GLU GLU GLN ARG ARG MET LEU GLY ALA
SEQRES 28 A 478 ILE HIS ALA SER THR THR PHE PRO PHE ARG ALA GLU GLY
SEQRES 29 A 478 GLY ARG VAL LEU TYR SER CYS MET VAL GLY GLY ALA ARG
SEQRES 30 A 478 GLN PRO GLY LEU VAL GLU GLN ASP GLU ASP ALA LEU ALA
SEQRES 31 A 478 ALA LEU ALA ARG GLU GLU LEU LYS ALA LEU ALA GLY VAL
SEQRES 32 A 478 THR ALA ARG PRO SER PHE THR ARG VAL PHE ARG TRP PRO
SEQRES 33 A 478 LEU GLY ILE PRO GLN TYR ASN LEU GLY HIS LEU GLU ARG
SEQRES 34 A 478 VAL ALA ALA ILE ASP ALA ALA LEU GLN ARG LEU PRO GLY
SEQRES 35 A 478 LEU HIS LEU ILE GLY ASN ALA TYR LYS GLY VAL GLY LEU
SEQRES 36 A 478 ASN ASP CYS ILE ARG ASN ALA ALA GLN LEU ALA ASP ALA
SEQRES 37 A 478 LEU VAL ALA GLY ASN THR SER HIS ALA PRO
SEQRES 1 B 478 MET ASP HIS HIS HIS HIS HIS HIS HIS HIS MET PRO ARG
SEQRES 2 B 478 THR THR GLY MET ASN VAL ALA VAL VAL GLY GLY GLY ILE
SEQRES 3 B 478 SER GLY LEU ALA VAL ALA HIS HIS LEU ARG SER ARG GLY
SEQRES 4 B 478 THR ASP ALA VAL LEU LEU GLU SER SER ALA ARG LEU GLY
SEQRES 5 B 478 GLY ALA VAL GLY THR HIS ALA LEU ALA GLY TYR LEU VAL
SEQRES 6 B 478 GLU GLN GLY PRO ASN SER PHE LEU ASP ARG GLU PRO ALA
SEQRES 7 B 478 THR ARG ALA LEU ALA ALA ALA LEU ASN LEU GLU GLY ARG
SEQRES 8 B 478 ILE ARG ALA ALA ASP PRO ALA ALA LYS ARG ARG TYR VAL
SEQRES 9 B 478 TYR THR ARG GLY ARG LEU ARG SER VAL PRO ALA SER PRO
SEQRES 10 B 478 PRO ALA PHE LEU ALA SER ASP ILE LEU PRO LEU GLY ALA
SEQRES 11 B 478 ARG LEU ARG VAL ALA GLY GLU LEU PHE SER ARG ARG ALA
SEQRES 12 B 478 PRO GLU GLY VAL ASP GLU SER LEU ALA ALA PHE GLY ARG
SEQRES 13 B 478 ARG HIS LEU GLY HIS ARG ALA THR GLN VAL LEU LEU ASP
SEQRES 14 B 478 ALA VAL GLN THR GLY ILE TYR ALA GLY ASP VAL GLU GLN
SEQRES 15 B 478 LEU SER VAL ALA ALA THR PHE PRO MET LEU VAL LYS MET
SEQRES 16 B 478 GLU ARG GLU HIS ARG SER LEU ILE LEU GLY ALA ILE ARG
SEQRES 17 B 478 ALA GLN LYS ALA GLN ARG GLN ALA ALA LEU PRO ALA GLY
SEQRES 18 B 478 THR ALA PRO LYS LEU SER GLY ALA LEU SER THR PHE ASP
SEQRES 19 B 478 GLY GLY LEU GLN VAL LEU ILE ASP ALA LEU ALA ALA SER
SEQRES 20 B 478 LEU GLY ASP ALA ALA HIS VAL GLY ALA ARG VAL GLU GLY
SEQRES 21 B 478 LEU ALA ARG GLU ASP GLY GLY TRP ARG LEU ILE ILE GLU
SEQRES 22 B 478 GLU HIS GLY ARG ARG ALA GLU LEU SER VAL ALA GLN VAL
SEQRES 23 B 478 VAL LEU ALA ALA PRO ALA HIS ALA THR ALA LYS LEU LEU
SEQRES 24 B 478 ARG PRO LEU ASP ASP ALA LEU ALA ALA LEU VAL ALA GLY
SEQRES 25 B 478 ILE ALA TYR ALA PRO ILE ALA VAL VAL HIS LEU GLY PHE
SEQRES 26 B 478 ASP ALA GLY THR LEU PRO ALA PRO ASP GLY PHE GLY PHE
SEQRES 27 B 478 LEU VAL PRO ALA GLU GLU GLN ARG ARG MET LEU GLY ALA
SEQRES 28 B 478 ILE HIS ALA SER THR THR PHE PRO PHE ARG ALA GLU GLY
SEQRES 29 B 478 GLY ARG VAL LEU TYR SER CYS MET VAL GLY GLY ALA ARG
SEQRES 30 B 478 GLN PRO GLY LEU VAL GLU GLN ASP GLU ASP ALA LEU ALA
SEQRES 31 B 478 ALA LEU ALA ARG GLU GLU LEU LYS ALA LEU ALA GLY VAL
SEQRES 32 B 478 THR ALA ARG PRO SER PHE THR ARG VAL PHE ARG TRP PRO
SEQRES 33 B 478 LEU GLY ILE PRO GLN TYR ASN LEU GLY HIS LEU GLU ARG
SEQRES 34 B 478 VAL ALA ALA ILE ASP ALA ALA LEU GLN ARG LEU PRO GLY
SEQRES 35 B 478 LEU HIS LEU ILE GLY ASN ALA TYR LYS GLY VAL GLY LEU
SEQRES 36 B 478 ASN ASP CYS ILE ARG ASN ALA ALA GLN LEU ALA ASP ALA
SEQRES 37 B 478 LEU VAL ALA GLY ASN THR SER HIS ALA PRO
HET FAD A2114 53
HET GOL A3001 6
HET GOL A3002 6
HET GOL A3003 6
HET TWN A4002 25
HET FAD B2114 53
HET GOL B3005 6
HET GOL B3006 6
HET GOL B3007 6
HET TWN B4001 25
HET TWN B4003 25
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM GOL GLYCEROL
HETNAM TWN (3S)-3-[(2S,3S,4R)-3,4-DIMETHYLTETRAHYDROFURAN-2-
HETNAM 2 TWN YL]BUTYL LAURATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 GOL 6(C3 H8 O3)
FORMUL 7 TWN 3(C22 H42 O3)
FORMUL 14 HOH *146(H2 O)
HELIX 1 1 GLY A 18 SER A 30 1 13
HELIX 2 2 GLU A 69 ALA A 78 1 10
HELIX 3 3 LEU A 81 GLY A 83 5 3
HELIX 4 4 SER A 109 SER A 116 1 8
HELIX 5 5 PRO A 120 GLY A 129 1 10
HELIX 6 6 GLU A 130 SER A 133 5 4
HELIX 7 7 SER A 143 LEU A 152 1 10
HELIX 8 8 GLY A 153 TYR A 169 1 17
HELIX 9 9 SER A 177 PHE A 182 1 6
HELIX 10 10 PHE A 182 ARG A 193 1 12
HELIX 11 11 SER A 194 ARG A 207 1 14
HELIX 12 12 LEU A 230 GLY A 242 1 13
HELIX 13 13 PRO A 284 ARG A 293 1 10
HELIX 14 14 ASP A 296 GLY A 305 1 10
HELIX 15 15 PRO A 334 GLN A 338 5 5
HELIX 16 16 ALA A 347 PHE A 351 1 5
HELIX 17 17 PRO A 352 ARG A 354 5 3
HELIX 18 18 GLN A 371 GLN A 377 5 7
HELIX 19 19 ASP A 378 ALA A 394 1 17
HELIX 20 20 GLY A 418 GLN A 431 1 14
HELIX 21 21 GLY A 447 VAL A 463 1 17
HELIX 22 22 GLY B 18 GLY B 32 1 15
HELIX 23 23 GLU B 69 LEU B 79 1 11
HELIX 24 24 LEU B 81 GLY B 83 5 3
HELIX 25 25 SER B 109 SER B 116 1 8
HELIX 26 26 PRO B 120 GLY B 129 1 10
HELIX 27 27 GLU B 130 SER B 133 5 4
HELIX 28 28 SER B 143 LEU B 152 1 10
HELIX 29 29 GLY B 153 ALA B 170 1 18
HELIX 30 30 SER B 177 PHE B 182 1 6
HELIX 31 31 PHE B 182 ARG B 193 1 12
HELIX 32 32 SER B 194 ARG B 207 1 14
HELIX 33 33 LEU B 230 GLY B 242 1 13
HELIX 34 34 PRO B 284 ARG B 293 1 10
HELIX 35 35 ASP B 296 GLY B 305 1 10
HELIX 36 36 PRO B 334 GLN B 338 5 5
HELIX 37 37 ALA B 347 PHE B 351 1 5
HELIX 38 38 PRO B 352 ARG B 354 5 3
HELIX 39 39 GLN B 371 GLN B 377 5 7
HELIX 40 40 ASP B 378 GLY B 395 1 18
HELIX 41 41 GLY B 418 GLN B 431 1 14
HELIX 42 42 GLY B 447 GLY B 465 1 19
SHEET 1 AA 5 ALA A 245 VAL A 247 0
SHEET 2 AA 5 ALA A 35 GLU A 39 1 O LEU A 37 N HIS A 246
SHEET 3 AA 5 VAL A 12 VAL A 15 1 O VAL A 12 N VAL A 36
SHEET 4 AA 5 GLN A 278 LEU A 281 1 O GLN A 278 N ALA A 13
SHEET 5 AA 5 LEU A 436 LEU A 438 1 O HIS A 437 N LEU A 281
SHEET 1 AB 2 THR A 50 LEU A 53 0
SHEET 2 AB 2 TYR A 56 GLU A 59 -1 O TYR A 56 N LEU A 53
SHEET 1 AC 3 PHE A 65 LEU A 66 0
SHEET 2 AC 3 LEU A 223 PHE A 226 -1 O SER A 224 N PHE A 65
SHEET 3 AC 3 ILE A 85 ALA A 87 -1 O ARG A 86 N THR A 225
SHEET 1 AD 7 ARG A 102 SER A 105 0
SHEET 2 AD 7 TYR A 96 THR A 99 -1 O VAL A 97 N ARG A 104
SHEET 3 AD 7 PHE A 331 LEU A 332 1 O LEU A 332 N TYR A 98
SHEET 4 AD 7 GLY A 343 HIS A 346 -1 O ALA A 344 N PHE A 331
SHEET 5 AD 7 VAL A 360 GLY A 367 -1 O SER A 363 N ILE A 345
SHEET 6 AD 7 TYR A 308 PHE A 318 -1 O ALA A 312 N VAL A 366
SHEET 7 AD 7 PHE A 402 PRO A 413 -1 O PHE A 402 N GLY A 317
SHEET 1 AE 3 ARG A 250 ARG A 256 0
SHEET 2 AE 3 TRP A 261 GLU A 266 -1 O ARG A 262 N ALA A 255
SHEET 3 AE 3 ARG A 271 VAL A 276 -1 O ALA A 272 N ILE A 265
SHEET 1 BA 5 ALA B 245 VAL B 247 0
SHEET 2 BA 5 ASP B 34 GLU B 39 1 O LEU B 37 N HIS B 246
SHEET 3 BA 5 ASN B 11 VAL B 15 1 O VAL B 12 N VAL B 36
SHEET 4 BA 5 GLN B 278 LEU B 281 1 O GLN B 278 N ALA B 13
SHEET 5 BA 5 LEU B 436 LEU B 438 1 O HIS B 437 N LEU B 281
SHEET 1 BB 2 THR B 50 LEU B 53 0
SHEET 2 BB 2 TYR B 56 GLU B 59 -1 O TYR B 56 N LEU B 53
SHEET 1 BC 3 PHE B 65 LEU B 66 0
SHEET 2 BC 3 LEU B 223 PHE B 226 -1 O SER B 224 N PHE B 65
SHEET 3 BC 3 ILE B 85 ARG B 86 -1 O ARG B 86 N THR B 225
SHEET 1 BD 7 ARG B 102 VAL B 106 0
SHEET 2 BD 7 ARG B 95 THR B 99 -1 O ARG B 95 N VAL B 106
SHEET 3 BD 7 GLY B 330 LEU B 332 1 O GLY B 330 N TYR B 96
SHEET 4 BD 7 GLY B 343 HIS B 346 -1 O ALA B 344 N PHE B 331
SHEET 5 BD 7 VAL B 360 GLY B 367 -1 O SER B 363 N ILE B 345
SHEET 6 BD 7 TYR B 308 PHE B 318 -1 O ALA B 312 N VAL B 366
SHEET 7 BD 7 PHE B 402 PRO B 413 -1 O PHE B 402 N GLY B 317
SHEET 1 BE 3 ALA B 249 ARG B 256 0
SHEET 2 BE 3 TRP B 261 GLU B 267 -1 O ARG B 262 N ALA B 255
SHEET 3 BE 3 ARG B 271 VAL B 276 -1 O ALA B 272 N ILE B 265
SITE 1 AC1 27 VAL A 15 GLY A 16 GLY A 18 ILE A 19
SITE 2 AC1 27 SER A 20 LEU A 38 GLU A 39 SER A 40
SITE 3 AC1 27 SER A 41 GLY A 46 ALA A 47 GLY A 61
SITE 4 AC1 27 PRO A 62 ASN A 63 SER A 64 ALA A 249
SITE 5 AC1 27 VAL A 251 ALA A 282 ALA A 287 GLY A 440
SITE 6 AC1 27 ASN A 441 VAL A 446 GLY A 447 LEU A 448
SITE 7 AC1 27 HOH A2003 HOH A2072 TWN A4002
SITE 1 AC2 14 THR A 166 GLY A 167 ILE A 168 ALA A 170
SITE 2 AC2 14 ILE A 311 PHE A 329 GLY A 330 PHE A 331
SITE 3 AC2 14 LEU A 332 GLY A 343 ALA A 344 ILE A 345
SITE 4 AC2 14 MET A 365 FAD A2114
SITE 1 AC3 27 VAL B 15 GLY B 16 GLY B 18 ILE B 19
SITE 2 AC3 27 SER B 20 LEU B 38 GLU B 39 SER B 40
SITE 3 AC3 27 GLY B 46 ALA B 47 GLY B 61 PRO B 62
SITE 4 AC3 27 ASN B 63 SER B 64 VAL B 251 ALA B 282
SITE 5 AC3 27 ALA B 283 PRO B 284 ALA B 287 GLY B 440
SITE 6 AC3 27 ASN B 441 GLY B 447 LEU B 448 HOH B2068
SITE 7 AC3 27 HOH B2069 HOH B2070 TWN B4003
SITE 1 AC4 4 LEU B 125 ARG B 126 GLY B 129 ARG B 134
SITE 1 AC5 11 THR B 166 GLY B 167 ILE B 168 PHE B 329
SITE 2 AC5 11 GLY B 330 PHE B 331 LEU B 332 ALA B 344
SITE 3 AC5 11 ILE B 345 MET B 365 FAD B2114
SITE 1 AC6 6 PRO A 120 LEU A 121 GLY A 122 ALA A 123
SITE 2 AC6 6 ARG A 201 HOH A2073
SITE 1 AC7 8 GLY A 122 ALA A 123 ARG A 193 LEU A 197
SITE 2 AC7 8 ARG A 201 HOH A2026 HOH A2043 HOH A2074
SITE 1 AC8 2 ARG A 126 GLY A 129
SITE 1 AC9 4 PRO B 120 GLY B 122 ARG B 201 HOH B2071
SITE 1 BC1 2 LEU A 125 LEU B 125
SITE 1 BC2 7 GLY B 122 ALA B 123 ARG B 193 LEU B 197
SITE 2 BC2 7 ARG B 201 HOH B2032 HOH B2072
CRYST1 148.566 148.566 132.745 90.00 90.00 90.00 P 4 21 2 16
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 0.006731 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006731 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007533 0.00000
MTRIX1 1 -0.684360 0.729080 0.010240 24.68063 1
MTRIX2 1 0.729150 0.684320 0.006900 -53.83945 1
MTRIX3 1 -0.001970 0.012190 -0.999920 111.49263 1
(ATOM LINES ARE NOT SHOWN.)
END