HEADER OXIDOREDUCTASE 12-JUN-06 2IVD
TITLE STRUCTURE OF PROTOPORPHYRINOGEN OXIDASE FROM MYXOCOCCUS
TITLE 2 XANTHUS WITH ACIFLUORFEN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTOPORPHYRINOGEN OXIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PPO, PPOX;
COMPND 5 EC: 1.3.3.4;
COMPND 6 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 PROTOPORPHYRINOGEN OXIDASE, PORPHYRIN BIOSYNTHESIS,
KEYWDS 2 CHLOROPHYLL BIOSYNTHESIS, OXIDOREDUCTASE, HAEM
KEYWDS 3 BIOSYNTHESIS, HEME BIOSYNTHESIS, FAD, PORPHYRIA,
KEYWDS 4 ACIFLUORFEN, FLAVOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.R.CORRADI,A.V.CORRIGALL,E.BOIX,C.G.MOHAN,E.D.STURROCK,
AUTHOR 2 P.N.MEISSNER,K.R.ACHARYA
REVDAT 4 24-FEB-09 2IVD 1 VERSN
REVDAT 3 13-DEC-06 2IVD 1 JRNL
REVDAT 2 25-OCT-06 2IVD 1 JRNL
REVDAT 1 17-OCT-06 2IVD 0
JRNL AUTH H.R.CORRADI,A.V.CORRIGALL,E.BOIX,C.G.MOHAN,
JRNL AUTH 2 E.D.STURROCK,P.N.MEISSNER,K.R.ACHARYA
JRNL TITL CRYSTAL STRUCTURE OF PROTOPORPHYRINOGEN OXIDASE
JRNL TITL 2 FROM MYXOCOCCUS XANTHUS AND ITS COMPLEX WITH THE
JRNL TITL 3 INHIBITOR 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. 2.3 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.3
REMARK 3 NUMBER OF REFLECTIONS : 55419
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) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.283
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1748
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2942
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3650
REMARK 3 BIN FREE R VALUE SET COUNT : 94
REMARK 3 BIN FREE R VALUE : 0.5000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6632
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 209
REMARK 3 SOLVENT ATOMS : 288
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.82
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) : -0.03000
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): 0.292
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.247
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.175
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.202
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.923
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.893
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6912 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9402 ; 1.487 ; 2.006
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 893 ; 6.564 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 273 ;29.041 ;21.722
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1011 ;18.733 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 77 ;20.545 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1072 ; 0.128 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5233 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2968 ; 0.193 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4566 ; 0.296 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 399 ; 0.153 ; 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): 87 ; 0.258 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.193 ; 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): 4531 ; 0.519 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6975 ; 0.918 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2723 ; 1.103 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2427 ; 1.835 ; 4.500
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
REMARK 3 RIDING POSITIONS. RESIDUES 87-93 IN BOTH MOLECULES COULD NOT
REMARK 3 BE MODELLED VERY ACCURATELY DUE TO LOTS OF NOISE IN THE MAPS
REMARK 4
REMARK 4 2IVD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUN-06.
REMARK 100 THE PDBE ID CODE IS EBI-29084.
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 : PX14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.488
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55419
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 49.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 75.2
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 46.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.53000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
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 (%): 66.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS/HCL PH 7.5, 1.5M
REMARK 280 AMMONIUM SULPHATE, 20% GLYCEROL, 1% PEG 4000
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 74.45900
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 74.45900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 74.45900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 74.45900
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 74.45900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 74.45900
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 74.45900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 74.45900
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 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 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 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 400
REMARK 400 COMPOUND
REMARK 400 CATALYZES THE 6-ELECTRON OXIDATION OF PROTOPORPHYRINOGEN
REMARK 400 IX TO FORM PROTOPORPHYRIN 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 ASP A 258
REMARK 465 GLY A 259
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 PRO B 217
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 ASP A 89 CG OD1 OD2
REMARK 470 LYS A 93 CD CE NZ
REMARK 470 LYS A 218 CD CE NZ
REMARK 470 MET B 10 CG SD CE
REMARK 470 ARG B 432 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;
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 480 I=INSERTION CODE):
REMARK 480 M RES CSSEQI ATOMS
REMARK 480 ARG A 134 NE CZ NH2
REMARK 480 MET A 184 SD CE
REMARK 480 GLN A 206 CD OE1 NE2
REMARK 480 ARG A 256 CD NE CZ NH1 NH2
REMARK 480 ARG A 262 CD NE CZ 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 CD OE1 NE2
REMARK 480 GLN B 206 CD OE1 NE2
REMARK 480 GLN B 208 CG CD OE1 NE2
REMARK 480 LYS B 218 CD CE NZ
REMARK 480 ARG B 262 CD NE CZ NH1 NH2
REMARK 480 LYS B 290 CD CE NZ
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 ARG A 149 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 PRO B 90 C - N - CA ANGL. DEV. = 9.3 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 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 ASP A 89 165.46 48.27
REMARK 500 PRO A 90 -86.04 -55.43
REMARK 500 ALA A 91 -129.13 -76.74
REMARK 500 ARG A 193 -65.90 62.98
REMARK 500 ARG A 207 4.89 -69.60
REMARK 500 THR A 225 -159.93 -148.68
REMARK 500 TRP A 261 124.24 165.08
REMARK 500 TYR A 443 -66.69 -107.17
REMARK 500 PRO B 90 -111.79 3.36
REMARK 500 ALA B 92 103.69 -58.85
REMARK 500 ARG B 193 -62.31 72.89
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 ILE A 345 HIS A 346 56.20
REMARK 500 PRO A 409 LEU A 410 121.44
REMARK 500 LEU A 410 GLY A 411 -149.81
REMARK 500 ALA B 87 ALA B 88 -138.18
REMARK 500 ASP B 89 PRO B 90 -65.10
REMARK 500 PRO B 90 ALA B 91 115.51
REMARK 500 ALA B 91 ALA B 92 146.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACJ A1465
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A1466
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACJ B1468
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B1469
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TWN B1472
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1468
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1470
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1471
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2IVE RELATED DB: PDB
REMARK 900 STRUCTURE OF PROTOPORPHYRINOGEN OXIDASE FROM
REMARK 900 MYXOCOCCUS XANTHUS
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 2IVD A -6 3 PDB 2IVD 2IVD -6 3
DBREF 2IVD A 4 471 UNP P56601 PPOX_MYXXA 4 471
DBREF 2IVD B -6 3 PDB 2IVD 2IVD -6 3
DBREF 2IVD 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 ACJ A1465 24
HET FAD A1466 53
HET ACJ B1468 24
HET FAD B1469 53
HET TWN B1472 25
HET GOL A1467 6
HET GOL A1468 6
HET GOL B1467 6
HET GOL B1470 6
HET GOL B1471 6
HETNAM ACJ 5-[2-CHLORO-4-(TRIFLUOROMETHYL)PHENOXY]-2-
HETNAM 2 ACJ NITROBENZOIC ACID
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM TWN (3S)-3-[(2S,3S,4R)-3,4-
HETNAM 2 TWN DIMETHYLTETRAHYDROFURAN-2-YL]BUTYL LAURATE
HETNAM GOL GLYCEROL
FORMUL 3 ACJ 2(C14 H7 CL F3 N O5)
FORMUL 4 FAD 2(C27 H33 N9 O15 P2)
FORMUL 7 TWN C22 H42 O3
FORMUL 8 GOL 5(C3 H8 O3)
FORMUL 13 HOH *288(H2 O1)
HELIX 1 1 GLY A 18 SER A 30 1 13
HELIX 2 2 GLU A 69 LEU A 79 1 11
HELIX 3 3 LEU A 81 GLY A 83 5 3
HELIX 4 4 SER A 109 ALA A 115 1 7
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 LEU A 160 1 8
HELIX 9 9 LEU A 160 ALA A 170 1 11
HELIX 10 10 SER A 177 PHE A 182 1 6
HELIX 11 11 PHE A 182 ARG A 193 1 12
HELIX 12 12 SER A 194 ARG A 207 1 14
HELIX 13 13 LEU A 230 GLY A 242 1 13
HELIX 14 14 PRO A 284 ARG A 293 1 10
HELIX 15 15 ASP A 296 GLY A 305 1 10
HELIX 16 16 PRO A 334 GLN A 338 5 5
HELIX 17 17 ALA A 347 PHE A 351 1 5
HELIX 18 18 PRO A 352 ARG A 354 5 3
HELIX 19 19 GLN A 371 GLN A 377 5 7
HELIX 20 20 ASP A 378 GLY A 395 1 18
HELIX 21 21 GLY A 418 ARG A 432 1 15
HELIX 22 22 GLY A 447 VAL A 463 1 17
HELIX 23 23 GLY B 18 ARG B 31 1 14
HELIX 24 24 GLU B 69 LEU B 79 1 11
HELIX 25 25 LEU B 81 GLY B 83 5 3
HELIX 26 26 SER B 109 SER B 116 1 8
HELIX 27 27 PRO B 120 GLY B 129 1 10
HELIX 28 28 GLU B 130 SER B 133 5 4
HELIX 29 29 SER B 143 GLY B 153 1 11
HELIX 30 30 GLY B 153 ALA B 170 1 18
HELIX 31 31 SER B 177 PHE B 182 1 6
HELIX 32 32 PHE B 182 ARG B 193 1 12
HELIX 33 33 SER B 194 GLN B 208 1 15
HELIX 34 34 LEU B 230 GLY B 242 1 13
HELIX 35 35 PRO B 284 ARG B 293 1 10
HELIX 36 36 ASP B 296 GLY B 305 1 10
HELIX 37 37 PRO B 334 GLN B 338 5 5
HELIX 38 38 ALA B 347 PHE B 351 1 5
HELIX 39 39 PRO B 352 ARG B 354 5 3
HELIX 40 40 GLN B 371 GLN B 377 5 7
HELIX 41 41 ASP B 378 GLY B 395 1 18
HELIX 42 42 GLY B 418 ARG B 432 1 15
HELIX 43 43 GLY B 447 GLY B 465 1 19
SHEET 1 AA 5 ALA A 245 HIS A 246 0
SHEET 2 AA 5 ALA A 35 LEU A 38 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 ARG A 86 -1 O ARG A 86 N THR A 225
SHEET 1 AD 7 ARG A 102 SER A 105 0
SHEET 2 AD 7 ARG A 95 THR A 99 -1 O VAL A 97 N ARG A 104
SHEET 3 AD 7 GLY A 330 LEU A 332 1 O GLY A 330 N TYR A 96
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 ILE A 311 PHE A 318 -1 O ALA A 312 N VAL A 366
SHEET 7 AD 7 PHE A 402 TRP A 408 -1 O PHE A 402 N GLY A 317
SHEET 1 AE 3 ALA A 249 ALA A 255 0
SHEET 2 AE 3 ARG A 262 GLU A 267 -1 O ARG A 262 N ALA A 255
SHEET 3 AE 3 ARG A 270 SER A 275 -1 O ARG A 270 N GLU A 267
SHEET 1 BA 5 ALA B 245 HIS B 246 0
SHEET 2 BA 5 ASP B 34 LEU B 38 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 ALA B 87 -1 O ARG B 86 N THR B 225
SHEET 1 BD 7 LEU B 103 SER B 105 0
SHEET 2 BD 7 TYR B 96 TYR B 98 -1 O VAL B 97 N ARG B 104
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 ALA B 307 PHE B 318 -1 O ALA B 312 N VAL B 366
SHEET 7 BD 7 PHE B 402 GLN B 414 -1 O PHE B 402 N GLY B 317
SHEET 1 BE 3 ARG B 250 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 270 VAL B 276 -1 O ARG B 270 N GLU B 267
SITE 1 AC1 15 ARG A 95 THR A 166 GLY A 167 ILE A 168
SITE 2 AC1 15 TYR A 169 ALA A 170 ILE A 311 PHE A 329
SITE 3 AC1 15 GLY A 330 PHE A 331 LEU A 332 MET A 365
SITE 4 AC1 15 ILE A 412 FAD A1466 HOH A2068
SITE 1 AC2 34 GLY A 16 GLY A 18 ILE A 19 SER A 20
SITE 2 AC2 34 LEU A 38 GLU A 39 SER A 40 SER A 41
SITE 3 AC2 34 GLY A 46 ALA A 47 GLY A 61 PRO A 62
SITE 4 AC2 34 ASN A 63 SER A 64 ALA A 249 ARG A 250
SITE 5 AC2 34 VAL A 251 ALA A 282 ALA A 283 ALA A 287
SITE 6 AC2 34 ILE A 412 GLY A 440 ASN A 441 VAL A 446
SITE 7 AC2 34 GLY A 447 LEU A 448 ACJ A1465 HOH A2008
SITE 8 AC2 34 HOH A2016 HOH A2141 HOH A2142 HOH A2143
SITE 9 AC2 34 HOH A2144 HOH A2145
SITE 1 AC3 17 ARG B 95 THR B 166 GLY B 167 ILE B 168
SITE 2 AC3 17 TYR B 169 ALA B 170 ILE B 311 PHE B 329
SITE 3 AC3 17 GLY B 330 PHE B 331 LEU B 332 ALA B 344
SITE 4 AC3 17 ILE B 345 MET B 365 ILE B 412 FAD B1469
SITE 5 AC3 17 HOH B2132
SITE 1 AC4 31 VAL B 15 GLY B 16 GLY B 18 ILE B 19
SITE 2 AC4 31 SER B 20 LEU B 38 GLU B 39 SER B 40
SITE 3 AC4 31 GLY B 46 ALA B 47 GLY B 61 PRO B 62
SITE 4 AC4 31 ASN B 63 SER B 64 VAL B 251 ALA B 283
SITE 5 AC4 31 PRO B 284 ALA B 287 VAL B 313 GLY B 440
SITE 6 AC4 31 ASN B 441 VAL B 446 GLY B 447 LEU B 448
SITE 7 AC4 31 ACJ B1468 HOH B2001 HOH B2129 HOH B2133
SITE 8 AC4 31 HOH B2134 HOH B2136 HOH B2137
SITE 1 AC5 7 LEU B 125 ARG B 126 GLY B 129 ARG B 134
SITE 2 AC5 7 GOL B1467 HOH B2131 HOH B2142
SITE 1 AC6 6 PRO A 120 LEU A 121 GLY A 122 ALA A 123
SITE 2 AC6 6 ARG A 201 HOH A2146
SITE 1 AC7 8 GLY A 122 ALA A 123 ARG A 155 HIS A 192
SITE 2 AC7 8 ARG A 193 LEU A 197 ARG A 201 HOH A2063
SITE 1 AC8 5 ARG B 126 ARG B 193 TWN B1472 HOH B2045
SITE 2 AC8 5 HOH B2131
SITE 1 AC9 6 PRO B 120 LEU B 121 GLY B 122 ALA B 123
SITE 2 AC9 6 ARG B 201 HOH B2138
SITE 1 BC1 8 GLY B 122 ALA B 123 ARG B 193 LEU B 197
SITE 2 BC1 8 ARG B 201 HOH B2072 HOH B2140 HOH B2141
CRYST1 148.918 148.918 131.924 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 0.006715 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006715 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007580 0.00000
MTRIX1 1 -0.674420 0.738270 0.011160 124.69347 1
MTRIX2 1 0.738230 0.674500 -0.008180 -54.60908 1
MTRIX3 1 -0.013570 0.002720 -0.999900 112.24957 1
(ATOM LINES ARE NOT SHOWN.)
END