HEADER OXIDOREDUCTASE 26-MAY-10 2XFO
TITLE TRANYLCYPROMINE-INHIBITED HUMAN MONOAMINE OXIDASE B ILE199ALA MUTANT
TITLE 2 IN COMPLEX WITH 2-(2-BENZOFURANYL)-2-IMIDAZOLINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINE OXIDASE [FLAVIN-CONTAINING] B;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MONOAMINE OXIDASE TYPE B,MAO-B;
COMPND 5 EC: 1.4.3.4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MAOB;
SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS FLAVOPROTEIN, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.BONIVENTO,E.M.MILCZEK,G.R.MCDONALD,C.BINDA,A.HOLT,D.E.EDMONDSON,
AUTHOR 2 A.MATTEVI
REVDAT 6 20-DEC-23 2XFO 1 REMARK LINK
REVDAT 5 25-JUL-18 2XFO 1 COMPND SOURCE DBREF
REVDAT 4 16-MAY-18 2XFO 1 REMARK
REVDAT 3 20-DEC-17 2XFO 1 JRNL
REVDAT 2 24-NOV-10 2XFO 1 JRNL
REVDAT 1 06-OCT-10 2XFO 0
JRNL AUTH D.BONIVENTO,E.M.MILCZEK,G.R.MCDONALD,C.BINDA,A.HOLT,
JRNL AUTH 2 D.E.EDMONDSON,A.MATTEVI
JRNL TITL POTENTIATION OF LIGAND BINDING THROUGH COOPERATIVE EFFECTS
JRNL TITL 2 IN MONOAMINE OXIDASE B.
JRNL REF J. BIOL. CHEM. V. 285 36849 2010
JRNL REFN ESSN 1083-351X
JRNL PMID 20855894
JRNL DOI 10.1074/JBC.M110.169482
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 67613
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.600
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7908
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 154
REMARK 3 SOLVENT ATOMS : 303
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED 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 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2XFO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-MAY-10.
REMARK 100 THE DEPOSITION ID IS D_1290043796.
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
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69410
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.02000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.58100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 1OJB
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 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 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y+1/2,-Z
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 65.27300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 110.93150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 65.27300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 110.93150
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 65.27300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 110.93150
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 65.27300
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 110.93150
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 ENGINEERED RESIDUE IN CHAIN A, ILE 199 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ILE 199 TO ALA
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 1
REMARK 465 SER A 2
REMARK 465 PHE A 502
REMARK 465 SER A 503
REMARK 465 ALA A 504
REMARK 465 THR A 505
REMARK 465 ALA A 506
REMARK 465 LEU A 507
REMARK 465 GLY A 508
REMARK 465 PHE A 509
REMARK 465 LEU A 510
REMARK 465 ALA A 511
REMARK 465 HIS A 512
REMARK 465 LYS A 513
REMARK 465 ARG A 514
REMARK 465 GLY A 515
REMARK 465 LEU A 516
REMARK 465 LEU A 517
REMARK 465 VAL A 518
REMARK 465 ARG A 519
REMARK 465 VAL A 520
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLY B 497
REMARK 465 LEU B 498
REMARK 465 THR B 499
REMARK 465 THR B 500
REMARK 465 ILE B 501
REMARK 465 PHE B 502
REMARK 465 SER B 503
REMARK 465 ALA B 504
REMARK 465 THR B 505
REMARK 465 ALA B 506
REMARK 465 LEU B 507
REMARK 465 GLY B 508
REMARK 465 PHE B 509
REMARK 465 LEU B 510
REMARK 465 ALA B 511
REMARK 465 HIS B 512
REMARK 465 LYS B 513
REMARK 465 ARG B 514
REMARK 465 GLY B 515
REMARK 465 LEU B 516
REMARK 465 LEU B 517
REMARK 465 VAL B 518
REMARK 465 ARG B 519
REMARK 465 VAL B 520
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 O HOH B 2006 O HOH B 2009 1.36
REMARK 500 O HOH B 2094 O HOH B 2095 1.43
REMARK 500 NH2 ARG B 220 O HOH B 2093 1.81
REMARK 500 N5 FA8 A 1502 CB 3PL A 1503 2.17
REMARK 500 CA GLY B 27 O HOH B 2008 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 2111 O HOH B 2111 2565 1.33
REMARK 500 O HOH A 2048 O HOH A 2049 6565 1.95
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 184 CB TRP A 184 CG -0.108
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 ARG B 87 NE - CZ - NH1 ANGL. DEV. = -3.8 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 LYS A 52 -63.41 70.16
REMARK 500 SER A 59 -54.98 -142.89
REMARK 500 THR A 64 -10.36 83.41
REMARK 500 ALA A 133 61.78 -159.08
REMARK 500 THR A 174 46.25 33.01
REMARK 500 THR A 201 -85.48 -91.73
REMARK 500 ARG A 233 71.95 -116.53
REMARK 500 ASN A 251 34.13 -84.27
REMARK 500 HIS A 252 53.08 32.37
REMARK 500 ALA A 263 43.40 -109.48
REMARK 500 ALA A 346 -120.13 52.48
REMARK 500 GLU A 379 60.91 -114.86
REMARK 500 ASP A 419 -100.66 56.46
REMARK 500 ALA A 424 -154.19 -112.47
REMARK 500 LYS B 52 -70.96 63.34
REMARK 500 SER B 59 -46.31 -139.63
REMARK 500 THR B 64 -12.63 87.91
REMARK 500 ALA B 133 68.33 -166.69
REMARK 500 THR B 201 -76.08 -97.05
REMARK 500 ALA B 346 -124.27 57.88
REMARK 500 GLU B 379 68.74 -115.82
REMARK 500 HIS B 382 163.11 176.21
REMARK 500 ASP B 419 -97.59 64.41
REMARK 500 ALA B 424 -153.10 -114.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 TRANYLCYPROMINE (TRA): CAK ATOM OF TRA IS COVALENTLY
REMARK 600 ATTACHED TO C4A ATOM OF FAD
REMARK 600 FLAVIN-ADENINE DINUCLEOTIDE (REDUCED) (FAD): C4A ATOM OF
REMARK 600 FAD IS COVALENTLY ATTACHED TO CAK ATOM OF TRA
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XCG A 1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XCG B 1499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF RESIDUES 1502 TO
REMARK 800 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF RESIDUES 1497 TO
REMARK 800 1498
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2C67 RELATED DB: PDB
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES
REMARK 900 RELATED ID: 1OJA RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH ISATIN
REMARK 900 RELATED ID: 2V5Z RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN MAO B IN COMPLEX WITH THE SELECTIVE INHIBITOR
REMARK 900 SAFINAMIDE
REMARK 900 RELATED ID: 1S3E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MAOB IN COMPLEX WITH 6-HYDROXY-N-PROPARGYL-1(R)
REMARK 900 -AMINOINDAN
REMARK 900 RELATED ID: 2C73 RELATED DB: PDB
REMARK 900 FUNCTIONAL ROLE OF THE AROMATIC CAGE IN HUMAN MONOAMINE OXIDASE B:
REMARK 900 STRUCTURES AND CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS
REMARK 900 RELATED ID: 1OJB RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH TRANYLCYPROMINE
REMARK 900 RELATED ID: 2V60 RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN MAO B IN COMPLEX WITH THE SELECTIVE INHIBITOR 7-
REMARK 900 (3-CHLOROBENZYLOXY )-4-CARBOXALDEHYDE-COUMARIN
REMARK 900 RELATED ID: 2BYB RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH DEPRENYL
REMARK 900 RELATED ID: 2VRM RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN MAO B IN COMPLEX WITH PHENYETHYLHYDRAZINE
REMARK 900 RELATED ID: 2C65 RELATED DB: PDB
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES
REMARK 900 RELATED ID: 2C64 RELATED DB: PDB
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES
REMARK 900 RELATED ID: 2XCG RELATED DB: PDB
REMARK 900 TRANYLCYPROMINE-INHIBITED HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH
REMARK 900 2-(2- BENZOFURANYL)-2-IMIDAZOLINE
REMARK 900 RELATED ID: 1OJ9 RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH 1,4-DIPHENYL-2-BUTENE
REMARK 900 RELATED ID: 2VZ2 RELATED DB: PDB
REMARK 900 HUMAN MAO B IN COMPLEX WITH MOFEGILINE
REMARK 900 RELATED ID: 1OJD RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH LAURYLDIMETHYLAMINE-N-
REMARK 900 OXIDE (LDAO)
REMARK 900 RELATED ID: 1S3B RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MAOB IN COMPLEX WITH N-METHYL-N-PROPARGYL-1(R)-
REMARK 900 AMINOINDAN
REMARK 900 RELATED ID: 2C66 RELATED DB: PDB
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES
REMARK 900 RELATED ID: 2BK4 RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B: I199F MUTANT IN COMPLEX WITH RASAGILINE
REMARK 900 RELATED ID: 2BK5 RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B: I199F MUTANT IN COMPLEX WITH ISATIN
REMARK 900 RELATED ID: 1H8R RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE TYPE B (TRUNCATED)
REMARK 900 RELATED ID: 2C70 RELATED DB: PDB
REMARK 900 FUNCTIONAL ROLE OF THE AROMATIC CAGE IN HUMAN MONOAMINE OXIDASE B:
REMARK 900 STRUCTURES AND CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS
REMARK 900 RELATED ID: 2BK3 RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH FARNESOL
REMARK 900 RELATED ID: 2C75 RELATED DB: PDB
REMARK 900 FUNCTIONAL ROLE OF THE AROMATIC CAGE IN HUMAN MONOAMINE OXIDASE B:
REMARK 900 STRUCTURES AND CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS
REMARK 900 RELATED ID: 2V61 RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN MAO B IN COMPLEX WITH THE SELECTIVE INHIBITOR 7-
REMARK 900 (3-CHLOROBENZYLOXY )-4-(METHYLAMINO)METHYL-COUMARIN
REMARK 900 RELATED ID: 2C72 RELATED DB: PDB
REMARK 900 FUNCTIONAL ROLE OF THE AROMATIC CAGE IN HUMAN MONOAMINE OXIDASE B:
REMARK 900 STRUCTURES AND CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS
REMARK 900 RELATED ID: 1S2Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MAOB IN COMPLEX WITH N-PROPARGYL-1(S)-
REMARK 900 AMINOINDAN
REMARK 900 RELATED ID: 1GOS RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B
REMARK 900 RELATED ID: 1S2Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MAOB IN COMPLEX WITH N-PROPARGYL-1(R)-
REMARK 900 AMINOINDAN (RASAGILINE)
REMARK 900 RELATED ID: 2C76 RELATED DB: PDB
REMARK 900 FUNCTIONAL ROLE OF THE AROMATIC CAGE IN HUMAN MONOAMINE OXIDASE B:
REMARK 900 STRUCTURES AND CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS
REMARK 900 RELATED ID: 2VRL RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN MAO B IN COMPLEX WITH BENZYLHYDRAZINE
REMARK 900 RELATED ID: 1OJC RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH N-(2-AMINOETHYL)-P-
REMARK 900 CHLOROBENZAMIDE
REMARK 900 RELATED ID: 2XFQ RELATED DB: PDB
REMARK 900 RASAGILINE-INHIBITED HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH 2-(2-
REMARK 900 BENZOFURANYL)-2- IMIDAZOLINE
REMARK 900 RELATED ID: 2XFN RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH 2-(2-BENZOFURANYL)-2-
REMARK 900 IMIDAZOLINE
REMARK 900 RELATED ID: 2XFP RELATED DB: PDB
REMARK 900 ISATIN-INHIBITED HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH 2-(2-
REMARK 900 BENZOFURANYL)-2- IMIDAZOLINE
DBREF 2XFO A 1 520 UNP P27338 AOFB_HUMAN 1 520
DBREF 2XFO B 1 520 UNP P27338 AOFB_HUMAN 1 520
SEQADV 2XFO ALA A 199 UNP P27338 ILE 199 ENGINEERED MUTATION
SEQADV 2XFO ALA B 199 UNP P27338 ILE 199 ENGINEERED MUTATION
SEQRES 1 A 520 MET SER ASN LYS CYS ASP VAL VAL VAL VAL GLY GLY GLY
SEQRES 2 A 520 ILE SER GLY MET ALA ALA ALA LYS LEU LEU HIS ASP SER
SEQRES 3 A 520 GLY LEU ASN VAL VAL VAL LEU GLU ALA ARG ASP ARG VAL
SEQRES 4 A 520 GLY GLY ARG THR TYR THR LEU ARG ASN GLN LYS VAL LYS
SEQRES 5 A 520 TYR VAL ASP LEU GLY GLY SER TYR VAL GLY PRO THR GLN
SEQRES 6 A 520 ASN ARG ILE LEU ARG LEU ALA LYS GLU LEU GLY LEU GLU
SEQRES 7 A 520 THR TYR LYS VAL ASN GLU VAL GLU ARG LEU ILE HIS HIS
SEQRES 8 A 520 VAL LYS GLY LYS SER TYR PRO PHE ARG GLY PRO PHE PRO
SEQRES 9 A 520 PRO VAL TRP ASN PRO ILE THR TYR LEU ASP HIS ASN ASN
SEQRES 10 A 520 PHE TRP ARG THR MET ASP ASP MET GLY ARG GLU ILE PRO
SEQRES 11 A 520 SER ASP ALA PRO TRP LYS ALA PRO LEU ALA GLU GLU TRP
SEQRES 12 A 520 ASP ASN MET THR MET LYS GLU LEU LEU ASP LYS LEU CYS
SEQRES 13 A 520 TRP THR GLU SER ALA LYS GLN LEU ALA THR LEU PHE VAL
SEQRES 14 A 520 ASN LEU CYS VAL THR ALA GLU THR HIS GLU VAL SER ALA
SEQRES 15 A 520 LEU TRP PHE LEU TRP TYR VAL LYS GLN CYS GLY GLY THR
SEQRES 16 A 520 THR ARG ILE ALA SER THR THR ASN GLY GLY GLN GLU ARG
SEQRES 17 A 520 LYS PHE VAL GLY GLY SER GLY GLN VAL SER GLU ARG ILE
SEQRES 18 A 520 MET ASP LEU LEU GLY ASP ARG VAL LYS LEU GLU ARG PRO
SEQRES 19 A 520 VAL ILE TYR ILE ASP GLN THR ARG GLU ASN VAL LEU VAL
SEQRES 20 A 520 GLU THR LEU ASN HIS GLU MET TYR GLU ALA LYS TYR VAL
SEQRES 21 A 520 ILE SER ALA ILE PRO PRO THR LEU GLY MET LYS ILE HIS
SEQRES 22 A 520 PHE ASN PRO PRO LEU PRO MET MET ARG ASN GLN MET ILE
SEQRES 23 A 520 THR ARG VAL PRO LEU GLY SER VAL ILE LYS CYS ILE VAL
SEQRES 24 A 520 TYR TYR LYS GLU PRO PHE TRP ARG LYS LYS ASP TYR CYS
SEQRES 25 A 520 GLY THR MET ILE ILE ASP GLY GLU GLU ALA PRO VAL ALA
SEQRES 26 A 520 TYR THR LEU ASP ASP THR LYS PRO GLU GLY ASN TYR ALA
SEQRES 27 A 520 ALA ILE MET GLY PHE ILE LEU ALA HIS LYS ALA ARG LYS
SEQRES 28 A 520 LEU ALA ARG LEU THR LYS GLU GLU ARG LEU LYS LYS LEU
SEQRES 29 A 520 CYS GLU LEU TYR ALA LYS VAL LEU GLY SER LEU GLU ALA
SEQRES 30 A 520 LEU GLU PRO VAL HIS TYR GLU GLU LYS ASN TRP CYS GLU
SEQRES 31 A 520 GLU GLN TYR SER GLY GLY CYS TYR THR THR TYR PHE PRO
SEQRES 32 A 520 PRO GLY ILE LEU THR GLN TYR GLY ARG VAL LEU ARG GLN
SEQRES 33 A 520 PRO VAL ASP ARG ILE TYR PHE ALA GLY THR GLU THR ALA
SEQRES 34 A 520 THR HIS TRP SER GLY TYR MET GLU GLY ALA VAL GLU ALA
SEQRES 35 A 520 GLY GLU ARG ALA ALA ARG GLU ILE LEU HIS ALA MET GLY
SEQRES 36 A 520 LYS ILE PRO GLU ASP GLU ILE TRP GLN SER GLU PRO GLU
SEQRES 37 A 520 SER VAL ASP VAL PRO ALA GLN PRO ILE THR THR THR PHE
SEQRES 38 A 520 LEU GLU ARG HIS LEU PRO SER VAL PRO GLY LEU LEU ARG
SEQRES 39 A 520 LEU ILE GLY LEU THR THR ILE PHE SER ALA THR ALA LEU
SEQRES 40 A 520 GLY PHE LEU ALA HIS LYS ARG GLY LEU LEU VAL ARG VAL
SEQRES 1 B 520 MET SER ASN LYS CYS ASP VAL VAL VAL VAL GLY GLY GLY
SEQRES 2 B 520 ILE SER GLY MET ALA ALA ALA LYS LEU LEU HIS ASP SER
SEQRES 3 B 520 GLY LEU ASN VAL VAL VAL LEU GLU ALA ARG ASP ARG VAL
SEQRES 4 B 520 GLY GLY ARG THR TYR THR LEU ARG ASN GLN LYS VAL LYS
SEQRES 5 B 520 TYR VAL ASP LEU GLY GLY SER TYR VAL GLY PRO THR GLN
SEQRES 6 B 520 ASN ARG ILE LEU ARG LEU ALA LYS GLU LEU GLY LEU GLU
SEQRES 7 B 520 THR TYR LYS VAL ASN GLU VAL GLU ARG LEU ILE HIS HIS
SEQRES 8 B 520 VAL LYS GLY LYS SER TYR PRO PHE ARG GLY PRO PHE PRO
SEQRES 9 B 520 PRO VAL TRP ASN PRO ILE THR TYR LEU ASP HIS ASN ASN
SEQRES 10 B 520 PHE TRP ARG THR MET ASP ASP MET GLY ARG GLU ILE PRO
SEQRES 11 B 520 SER ASP ALA PRO TRP LYS ALA PRO LEU ALA GLU GLU TRP
SEQRES 12 B 520 ASP ASN MET THR MET LYS GLU LEU LEU ASP LYS LEU CYS
SEQRES 13 B 520 TRP THR GLU SER ALA LYS GLN LEU ALA THR LEU PHE VAL
SEQRES 14 B 520 ASN LEU CYS VAL THR ALA GLU THR HIS GLU VAL SER ALA
SEQRES 15 B 520 LEU TRP PHE LEU TRP TYR VAL LYS GLN CYS GLY GLY THR
SEQRES 16 B 520 THR ARG ILE ALA SER THR THR ASN GLY GLY GLN GLU ARG
SEQRES 17 B 520 LYS PHE VAL GLY GLY SER GLY GLN VAL SER GLU ARG ILE
SEQRES 18 B 520 MET ASP LEU LEU GLY ASP ARG VAL LYS LEU GLU ARG PRO
SEQRES 19 B 520 VAL ILE TYR ILE ASP GLN THR ARG GLU ASN VAL LEU VAL
SEQRES 20 B 520 GLU THR LEU ASN HIS GLU MET TYR GLU ALA LYS TYR VAL
SEQRES 21 B 520 ILE SER ALA ILE PRO PRO THR LEU GLY MET LYS ILE HIS
SEQRES 22 B 520 PHE ASN PRO PRO LEU PRO MET MET ARG ASN GLN MET ILE
SEQRES 23 B 520 THR ARG VAL PRO LEU GLY SER VAL ILE LYS CYS ILE VAL
SEQRES 24 B 520 TYR TYR LYS GLU PRO PHE TRP ARG LYS LYS ASP TYR CYS
SEQRES 25 B 520 GLY THR MET ILE ILE ASP GLY GLU GLU ALA PRO VAL ALA
SEQRES 26 B 520 TYR THR LEU ASP ASP THR LYS PRO GLU GLY ASN TYR ALA
SEQRES 27 B 520 ALA ILE MET GLY PHE ILE LEU ALA HIS LYS ALA ARG LYS
SEQRES 28 B 520 LEU ALA ARG LEU THR LYS GLU GLU ARG LEU LYS LYS LEU
SEQRES 29 B 520 CYS GLU LEU TYR ALA LYS VAL LEU GLY SER LEU GLU ALA
SEQRES 30 B 520 LEU GLU PRO VAL HIS TYR GLU GLU LYS ASN TRP CYS GLU
SEQRES 31 B 520 GLU GLN TYR SER GLY GLY CYS TYR THR THR TYR PHE PRO
SEQRES 32 B 520 PRO GLY ILE LEU THR GLN TYR GLY ARG VAL LEU ARG GLN
SEQRES 33 B 520 PRO VAL ASP ARG ILE TYR PHE ALA GLY THR GLU THR ALA
SEQRES 34 B 520 THR HIS TRP SER GLY TYR MET GLU GLY ALA VAL GLU ALA
SEQRES 35 B 520 GLY GLU ARG ALA ALA ARG GLU ILE LEU HIS ALA MET GLY
SEQRES 36 B 520 LYS ILE PRO GLU ASP GLU ILE TRP GLN SER GLU PRO GLU
SEQRES 37 B 520 SER VAL ASP VAL PRO ALA GLN PRO ILE THR THR THR PHE
SEQRES 38 B 520 LEU GLU ARG HIS LEU PRO SER VAL PRO GLY LEU LEU ARG
SEQRES 39 B 520 LEU ILE GLY LEU THR THR ILE PHE SER ALA THR ALA LEU
SEQRES 40 B 520 GLY PHE LEU ALA HIS LYS ARG GLY LEU LEU VAL ARG VAL
HET FA8 A1502 53
HET 3PL A1503 10
HET XCG A1504 14
HET FAD B1497 53
HET 3PL B1498 10
HET XCG B1499 14
HETNAM FA8 [[(2R,3S,4S)-5-[(4AS)-7,8-DIMETHYL-2,4-DIOXO-4A,5-
HETNAM 2 FA8 DIHYDROBENZO[G]PTERIDIN-10-YL]-2,3,4-TRIHYDROXY-
HETNAM 3 FA8 PENTOXY]-HYDROXY-PHOSPHORYL] [(2R,3S,4R,5R)-5-(6-
HETNAM 4 FA8 AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL
HETNAM 5 FA8 HYDROGEN PHOSPHATE
HETNAM 3PL 3-PHENYLPROPANAL
HETNAM XCG 2-(2-BENZOFURANYL)-2-IMIDAZOLINE
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 3 FA8 C27 H35 N9 O15 P2
FORMUL 4 3PL 2(C9 H10 O)
FORMUL 5 XCG 2(C11 H8 N2 O)
FORMUL 6 FAD C27 H33 N9 O15 P2
FORMUL 9 HOH *303(H2 O)
HELIX 1 1 GLY A 13 SER A 26 1 14
HELIX 2 2 GLN A 65 LEU A 75 1 11
HELIX 3 3 ASN A 108 ARG A 127 1 20
HELIX 4 4 ALA A 133 ALA A 137 5 5
HELIX 5 5 LEU A 139 ASN A 145 1 7
HELIX 6 6 THR A 147 CYS A 156 1 10
HELIX 7 7 THR A 158 THR A 174 1 17
HELIX 8 8 SER A 181 CYS A 192 1 12
HELIX 9 9 GLY A 194 SER A 200 1 7
HELIX 10 10 GLY A 215 GLY A 226 1 12
HELIX 11 11 PRO A 265 ILE A 272 5 8
HELIX 12 12 PRO A 279 ILE A 286 1 8
HELIX 13 13 PRO A 304 LYS A 309 5 6
HELIX 14 14 ALA A 346 ALA A 353 1 8
HELIX 15 15 THR A 356 LEU A 372 1 17
HELIX 16 16 SER A 374 GLU A 379 5 6
HELIX 17 17 CYS A 389 GLU A 391 5 3
HELIX 18 18 GLY A 405 GLY A 411 1 7
HELIX 19 19 ARG A 412 LEU A 414 5 3
HELIX 20 20 GLY A 425 ALA A 429 5 5
HELIX 21 21 TYR A 435 MET A 454 1 20
HELIX 22 22 PRO A 458 ILE A 462 5 5
HELIX 23 23 THR A 480 LEU A 486 1 7
HELIX 24 24 SER A 488 THR A 500 1 13
HELIX 25 25 GLY B 13 SER B 26 1 14
HELIX 26 26 GLN B 65 LEU B 75 1 11
HELIX 27 27 ASN B 108 ARG B 127 1 20
HELIX 28 28 ALA B 133 ALA B 137 5 5
HELIX 29 29 LEU B 139 ASN B 145 1 7
HELIX 30 30 THR B 147 CYS B 156 1 10
HELIX 31 31 THR B 158 THR B 174 1 17
HELIX 32 32 SER B 181 GLN B 191 1 11
HELIX 33 33 GLY B 194 SER B 200 1 7
HELIX 34 34 SER B 214 GLY B 226 1 13
HELIX 35 35 PRO B 265 ILE B 272 5 8
HELIX 36 36 PRO B 279 ILE B 286 1 8
HELIX 37 37 PRO B 304 LYS B 309 5 6
HELIX 38 38 ALA B 346 ALA B 353 1 8
HELIX 39 39 THR B 356 GLY B 373 1 18
HELIX 40 40 SER B 374 GLU B 379 5 6
HELIX 41 41 CYS B 389 GLU B 391 5 3
HELIX 42 42 GLY B 405 GLY B 411 1 7
HELIX 43 43 ARG B 412 LEU B 414 5 3
HELIX 44 44 GLY B 425 ALA B 429 5 5
HELIX 45 45 TYR B 435 MET B 454 1 20
HELIX 46 46 PRO B 458 ILE B 462 5 5
HELIX 47 47 THR B 480 LEU B 486 1 7
HELIX 48 48 SER B 488 ARG B 494 1 7
SHEET 1 AA 5 VAL A 229 LYS A 230 0
SHEET 2 AA 5 VAL A 30 LEU A 33 1 O VAL A 32 N LYS A 230
SHEET 3 AA 5 VAL A 7 VAL A 10 1 O VAL A 7 N VAL A 31
SHEET 4 AA 5 TYR A 259 SER A 262 1 O TYR A 259 N VAL A 8
SHEET 5 AA 5 ILE A 421 PHE A 423 1 O TYR A 422 N SER A 262
SHEET 1 AB 2 THR A 45 LEU A 46 0
SHEET 2 AB 2 VAL A 54 ASP A 55 -1 O VAL A 54 N LEU A 46
SHEET 1 AC 2 THR A 79 LYS A 81 0
SHEET 2 AC 2 ARG A 208 PHE A 210 -1 O LYS A 209 N TYR A 80
SHEET 1 AD 7 LYS A 95 PHE A 99 0
SHEET 2 AD 7 ARG A 87 VAL A 92 -1 O LEU A 88 N PHE A 99
SHEET 3 AD 7 TYR A 311 ILE A 317 1 N CYS A 312 O ARG A 87
SHEET 4 AD 7 TYR A 326 ASP A 329 -1 O THR A 327 N MET A 315
SHEET 5 AD 7 ALA A 339 LEU A 345 -1 O MET A 341 N LEU A 328
SHEET 6 AD 7 VAL A 294 TYR A 300 -1 O ILE A 295 N ILE A 344
SHEET 7 AD 7 HIS A 382 ASN A 387 -1 O HIS A 382 N TYR A 300
SHEET 1 AE 4 MET A 254 ALA A 257 0
SHEET 2 AE 4 VAL A 245 THR A 249 -1 O VAL A 245 N ALA A 257
SHEET 3 AE 4 VAL A 235 ASP A 239 -1 N ILE A 236 O GLU A 248
SHEET 4 AE 4 HIS A 273 ASN A 275 1 O HIS A 273 N ILE A 238
SHEET 1 BA 5 VAL B 229 LYS B 230 0
SHEET 2 BA 5 VAL B 30 LEU B 33 1 O VAL B 32 N LYS B 230
SHEET 3 BA 5 VAL B 7 VAL B 10 1 O VAL B 7 N VAL B 31
SHEET 4 BA 5 TYR B 259 SER B 262 1 O TYR B 259 N VAL B 8
SHEET 5 BA 5 ILE B 421 PHE B 423 1 O TYR B 422 N SER B 262
SHEET 1 BB 2 THR B 45 LEU B 46 0
SHEET 2 BB 2 VAL B 54 ASP B 55 -1 O VAL B 54 N LEU B 46
SHEET 1 BC 3 TYR B 60 VAL B 61 0
SHEET 2 BC 3 ARG B 208 PHE B 210 -1 O ARG B 208 N VAL B 61
SHEET 3 BC 3 THR B 79 LYS B 81 -1 O TYR B 80 N LYS B 209
SHEET 1 BD 7 LYS B 95 PHE B 99 0
SHEET 2 BD 7 ARG B 87 VAL B 92 -1 O LEU B 88 N PHE B 99
SHEET 3 BD 7 TYR B 311 ILE B 317 1 N CYS B 312 O ARG B 87
SHEET 4 BD 7 TYR B 326 ASP B 329 -1 O THR B 327 N MET B 315
SHEET 5 BD 7 ALA B 339 LEU B 345 -1 O MET B 341 N LEU B 328
SHEET 6 BD 7 VAL B 294 TYR B 300 -1 O ILE B 295 N ILE B 344
SHEET 7 BD 7 HIS B 382 ASN B 387 -1 O HIS B 382 N TYR B 300
SHEET 1 BE 4 MET B 254 ALA B 257 0
SHEET 2 BE 4 VAL B 245 THR B 249 -1 O VAL B 245 N ALA B 257
SHEET 3 BE 4 VAL B 235 ASP B 239 -1 N ILE B 236 O GLU B 248
SHEET 4 BE 4 HIS B 273 ASN B 275 1 O HIS B 273 N ILE B 238
LINK SG CYS A 397 C8M FA8 A1502 1555 1555 1.65
LINK C4X FA8 A1502 CB 3PL A1503 1555 1555 1.75
LINK SG CYS B 397 C8M FAD B1497 1555 1555 1.66
LINK C4X FAD B1497 CB 3PL B1498 1555 1555 1.75
CISPEP 1 ASN A 275 PRO A 276 0 -2.58
CISPEP 2 CYS A 397 TYR A 398 0 -3.52
CISPEP 3 ASN B 275 PRO B 276 0 2.34
CISPEP 4 CYS B 397 TYR B 398 0 6.46
SITE 1 AC1 7 PRO A 102 LEU A 164 PHE A 168 ALA A 199
SITE 2 AC1 7 THR A 201 ILE A 316 TYR A 326
SITE 1 AC2 9 PRO B 102 LEU B 164 LEU B 167 PHE B 168
SITE 2 AC2 9 ALA B 199 THR B 201 ILE B 316 TYR B 326
SITE 3 AC2 9 HOH B2039
SITE 1 AC3 40 VAL A 10 GLY A 11 GLY A 13 ILE A 14
SITE 2 AC3 40 SER A 15 LEU A 33 GLU A 34 ALA A 35
SITE 3 AC3 40 ARG A 36 GLY A 41 ARG A 42 THR A 43
SITE 4 AC3 40 GLY A 57 GLY A 58 SER A 59 TYR A 60
SITE 5 AC3 40 CYS A 172 TYR A 188 ARG A 233 PRO A 234
SITE 6 AC3 40 VAL A 235 ALA A 263 ILE A 264 TRP A 388
SITE 7 AC3 40 TYR A 393 CYS A 397 TYR A 398 GLY A 425
SITE 8 AC3 40 THR A 426 GLY A 434 TYR A 435 MET A 436
SITE 9 AC3 40 ALA A 439 HOH A2003 HOH A2004 HOH A2072
SITE 10 AC3 40 HOH A2105 HOH A2127 HOH A2128 HOH A2130
SITE 1 AC4 41 VAL B 10 GLY B 11 GLY B 13 ILE B 14
SITE 2 AC4 41 SER B 15 LEU B 33 GLU B 34 ALA B 35
SITE 3 AC4 41 ARG B 36 GLY B 40 GLY B 41 ARG B 42
SITE 4 AC4 41 THR B 43 GLY B 58 SER B 59 TYR B 60
SITE 5 AC4 41 CYS B 172 TYR B 188 GLN B 206 ARG B 233
SITE 6 AC4 41 PRO B 234 VAL B 235 ALA B 263 ILE B 264
SITE 7 AC4 41 TRP B 388 TYR B 393 CYS B 397 TYR B 398
SITE 8 AC4 41 GLY B 425 THR B 426 GLY B 434 TYR B 435
SITE 9 AC4 41 MET B 436 HOH B2003 HOH B2028 HOH B2107
SITE 10 AC4 41 HOH B2141 HOH B2170 HOH B2171 HOH B2172
SITE 11 AC4 41 HOH B2173
CRYST1 130.546 221.863 86.033 90.00 90.00 90.00 C 2 2 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 0.007660 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004507 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011623 0.00000
(ATOM LINES ARE NOT SHOWN.)
END