HEADER OXIDOREDUCTASE 12-JUL-07 2V60
TITLE STRUCTURE OF HUMAN MAO B IN COMPLEX WITH THE SELECTIVE INHIBITOR 7-(3-
TITLE 2 CHLOROBENZYLOXY)-4-CARBOXALDEHYDE-COUMARIN
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, MONOAMINE OXIDASE;
COMPND 5 EC: 1.4.3.4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS FAD, MEMBRANE, SAFINAMIDE, FLAVOPROTEIN, HUMAN MAO B STRUCTURE,
KEYWDS 2 REVERSIBLE INHIBITOR BINDING, MITOCHONDRION, TRANSMEMBRANE,
KEYWDS 3 OXIDOREDUCTASE, NEUROPROTECTION, PARKINSON'S DISEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.BINDA,J.WANG,L.PISANI,C.CACCIA,A.CAROTTI,P.SALVATI,D.E.EDMONDSON,
AUTHOR 2 A.MATTEVI
REVDAT 5 13-DEC-23 2V60 1 LINK
REVDAT 4 24-FEB-09 2V60 1 VERSN
REVDAT 3 20-NOV-07 2V60 1 JRNL
REVDAT 2 23-OCT-07 2V60 1 FORMUL LINK HETATM CONECT
REVDAT 1 16-OCT-07 2V60 0
JRNL AUTH C.BINDA,J.WANG,L.PISANI,C.CACCIA,A.CAROTTI,P.SALVATI,
JRNL AUTH 2 D.E.EDMONDSON,A.MATTEVI
JRNL TITL STRUCTURES OF HUMAN MONOAMINE OXIDASE B COMPLEXES WITH
JRNL TITL 2 SELECTIVE NONCOVALENT INHIBITORS: SAFINAMIDE AND COUMARIN
JRNL TITL 3 ANALOGS.
JRNL REF J.MED.CHEM. V. 50 5848 2007
JRNL REFN ISSN 0022-2623
JRNL PMID 17915852
JRNL DOI 10.1021/JM070677Y
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 113.23
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 83205
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.600
REMARK 3 FREE R VALUE TEST SET COUNT : 2206
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6056
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2350
REMARK 3 BIN FREE R VALUE SET COUNT : 158
REMARK 3 BIN FREE R VALUE : 0.3050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7911
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 150
REMARK 3 SOLVENT ATOMS : 756
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.25000
REMARK 3 B22 (A**2) : 0.57000
REMARK 3 B33 (A**2) : -0.32000
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): 0.150
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.146
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.096
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.339
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8271 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11245 ; 1.554 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 991 ; 6.154 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 358 ;33.078 ;23.520
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1408 ;14.295 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 58 ;16.302 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1219 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6222 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3908 ; 0.199 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5546 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 648 ; 0.146 ; 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): 30 ; 0.213 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.402 ; 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): 5144 ; 1.007 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8008 ; 1.494 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3776 ; 2.577 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3237 ; 3.877 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 3 A 99 4
REMARK 3 1 B 3 B 99 4
REMARK 3 2 A 110 A 496 4
REMARK 3 2 B 110 B 496 4
REMARK 3 3 A 600 A 600 4
REMARK 3 3 B 600 B 600 4
REMARK 3 4 A 601 A 601 4
REMARK 3 4 B 601 B 601 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 3932 ; 0.20 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 3932 ; 0.97 ; 2.00
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 : 1.40
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.
REMARK 4
REMARK 4 2V60 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUL-07.
REMARK 100 THE DEPOSITION ID IS D_1290033178.
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 : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85456
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1OJA
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 65.34700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 112.20650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 65.34700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 112.20650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 65.34700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 112.20650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 65.34700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 112.20650
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: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.2 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 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 A1038 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B1079 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B1255 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B1257 LIES ON A SPECIAL POSITION.
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 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 ILE A 501 CG1 CG2 CD1
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 1340 O HOH B 1343 2.14
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 A 1037 O HOH A 1037 3655 1.45
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 A 448 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 448 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG B 448 NE - CZ - NH2 ANGL. DEV. = -4.8 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 -70.47 66.34
REMARK 500 SER A 59 -49.62 -144.78
REMARK 500 THR A 64 -6.93 81.62
REMARK 500 ALA A 133 66.58 -156.32
REMARK 500 THR A 201 -79.59 -90.06
REMARK 500 ARG A 233 74.54 -118.95
REMARK 500 HIS A 252 4.22 82.29
REMARK 500 ALA A 346 -121.20 52.48
REMARK 500 GLU A 379 61.26 -116.70
REMARK 500 SER A 394 -52.19 -121.09
REMARK 500 ASP A 419 -102.38 58.66
REMARK 500 ALA A 424 -150.73 -110.70
REMARK 500 LYS B 52 -75.66 63.10
REMARK 500 SER B 59 -49.61 -138.50
REMARK 500 THR B 64 -9.24 75.31
REMARK 500 ALA B 133 68.56 -158.93
REMARK 500 THR B 201 -75.34 -88.15
REMARK 500 ALA B 346 -125.99 52.26
REMARK 500 GLU B 379 67.64 -118.54
REMARK 500 ASP B 419 -104.09 62.24
REMARK 500 ALA B 424 -155.13 -108.75
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 A1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C17 A1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B1497
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C17 B1498
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GOS RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B
REMARK 900 RELATED ID: 1H8R RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE TYPE B (TRUNCATED)
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: 1OJA RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH ISATIN
REMARK 900 RELATED ID: 1OJB RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH TRANYLCYPROMINE
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: 1OJD RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH LAURYLDIMETHYLAMINE-N-
REMARK 900 OXIDE (LDAO)
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: 1S2Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MAOB IN COMPLEX WITH N-PROPARGYL-1(S)-
REMARK 900 AMINOINDAN
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: 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: 2BK3 RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH FARNESOL
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: 2BYB RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH DEPRENYL
REMARK 900 RELATED ID: 2C64 RELATED DB: PDB
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES
REMARK 900 RELATED ID: 2C65 RELATED DB: PDB
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES
REMARK 900 RELATED ID: 2C66 RELATED DB: PDB
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES
REMARK 900 RELATED ID: 2C67 RELATED DB: PDB
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES
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: 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: 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: 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: 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: 2V5Z RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN MAO B IN COMPLEX WITH THE SELECTIVE INHIBITOR
REMARK 900 SAFINAMIDE
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
DBREF 2V60 A 1 1 PDB 2V60 2V60 1 1
DBREF 2V60 A 2 520 UNP P27338 AOFB_HUMAN 1 519
DBREF 2V60 B 1 1 PDB 2V60 2V60 1 1
DBREF 2V60 B 2 520 UNP P27338 AOFB_HUMAN 1 519
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 ILE 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 ILE 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 FAD A1502 53
HET C17 A1503 22
HET FAD B1497 53
HET C17 B1498 22
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM C17 7-[(3-CHLOROBENZYL)OXY]-2-OXO-2H-CHROMENE-4-
HETNAM 2 C17 CARBALDEHYDE
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 C17 2(C17 H11 CL O4)
FORMUL 7 HOH *756(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 SER A 214 GLY A 226 1 13
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 GLY A 373 1 18
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 GLY B 215 GLY B 226 1 12
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 LEU B 495 1 8
SHEET 1 AA 5 VAL A 229 LEU A 231 0
SHEET 2 AA 5 VAL A 30 GLU A 34 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 3 TYR A 60 VAL A 61 0
SHEET 2 AC 3 ARG A 208 PHE A 210 -1 O ARG A 208 N VAL A 61
SHEET 3 AC 3 THR A 79 LYS A 81 -1 O TYR A 80 N LYS A 209
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 LEU B 231 0
SHEET 2 BA 5 VAL B 30 GLU B 34 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 ASN B 48 0
SHEET 2 BB 2 LYS B 52 ASP B 55 -1 O LYS B 52 N ASN B 48
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 FAD A1502 1555 1555 1.67
LINK SG CYS B 397 C8M FAD B1497 1555 1555 1.68
CISPEP 1 ASN A 275 PRO A 276 0 -4.43
CISPEP 2 CYS A 397 TYR A 398 0 -8.47
CISPEP 3 ASN B 275 PRO B 276 0 -1.12
CISPEP 4 CYS B 397 TYR B 398 0 2.68
SITE 1 AC1 39 VAL A 10 GLY A 11 GLY A 12 GLY A 13
SITE 2 AC1 39 ILE A 14 SER A 15 LEU A 33 GLU A 34
SITE 3 AC1 39 ALA A 35 ARG A 36 GLY A 40 GLY A 41
SITE 4 AC1 39 ARG A 42 THR A 43 GLY A 58 SER A 59
SITE 5 AC1 39 TYR A 60 PRO A 234 VAL A 235 ALA A 263
SITE 6 AC1 39 ILE A 264 TRP A 388 TYR A 393 CYS A 397
SITE 7 AC1 39 TYR A 398 GLY A 425 THR A 426 GLY A 434
SITE 8 AC1 39 TYR A 435 MET A 436 ALA A 439 HOH A1027
SITE 9 AC1 39 HOH A1055 HOH A1206 HOH A1347 HOH A1348
SITE 10 AC1 39 HOH A1349 HOH A1350 HOH A1352
SITE 1 AC2 13 PRO A 102 LEU A 164 LEU A 171 CYS A 172
SITE 2 AC2 13 ILE A 198 ILE A 199 GLN A 206 ILE A 316
SITE 3 AC2 13 TYR A 326 PHE A 343 TYR A 435 HOH A1159
SITE 4 AC2 13 HOH A1351
SITE 1 AC3 41 VAL B 10 GLY B 11 GLY B 13 ILE B 14
SITE 2 AC3 41 SER B 15 LEU B 33 GLU B 34 ALA B 35
SITE 3 AC3 41 ARG B 36 GLY B 40 GLY B 41 ARG B 42
SITE 4 AC3 41 THR B 43 GLY B 58 SER B 59 TYR B 60
SITE 5 AC3 41 ARG B 233 PRO B 234 VAL B 235 ALA B 263
SITE 6 AC3 41 ILE B 264 TRP B 388 TYR B 393 CYS B 397
SITE 7 AC3 41 TYR B 398 GLY B 425 THR B 426 GLY B 434
SITE 8 AC3 41 TYR B 435 MET B 436 ALA B 439 HOH B1036
SITE 9 AC3 41 HOH B1037 HOH B1065 HOH B1207 HOH B1228
SITE 10 AC3 41 HOH B1249 HOH B1401 HOH B1402 HOH B1403
SITE 11 AC3 41 HOH B1404
SITE 1 AC4 15 TYR B 60 PRO B 102 LEU B 164 LEU B 171
SITE 2 AC4 15 CYS B 172 ILE B 198 ILE B 199 GLN B 206
SITE 3 AC4 15 ILE B 316 TYR B 326 PHE B 343 TYR B 398
SITE 4 AC4 15 TYR B 435 HOH B1193 HOH B1401
CRYST1 130.694 224.413 86.811 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 0.007651 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004456 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011519 0.00000
MTRIX1 1 -0.525740 -0.495390 -0.691510 140.00504 1
MTRIX2 1 -0.495940 -0.481970 0.722320 210.02158 1
MTRIX3 1 -0.691120 0.722700 0.007710 -54.68348 1
(ATOM LINES ARE NOT SHOWN.)
END