HEADER OXIDOREDUCTASE 12-JUL-07 2V5Z
TITLE STRUCTURE OF HUMAN MAO B IN COMPLEX WITH THE SELECTIVE INHIBITOR
TITLE 2 SAFINAMIDE
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
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: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: YEAST;
SOURCE 8 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 6 07-FEB-24 2V5Z 1 REMARK
REVDAT 5 18-JAN-23 2V5Z 1 COMPND SOURCE JRNL REMARK
REVDAT 5 2 1 DBREF HELIX SHEET SITE
REVDAT 5 3 1 ATOM
REVDAT 4 24-FEB-09 2V5Z 1 VERSN
REVDAT 3 20-NOV-07 2V5Z 1 JRNL
REVDAT 2 30-OCT-07 2V5Z 1 REMARK
REVDAT 1 16-OCT-07 2V5Z 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. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 160119
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) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.600
REMARK 3 FREE R VALUE TEST SET COUNT : 4192
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 11773
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.52
REMARK 3 BIN R VALUE (WORKING SET) : 0.2900
REMARK 3 BIN FREE R VALUE SET COUNT : 314
REMARK 3 BIN FREE R VALUE : 0.2820
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 : 717
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.53000
REMARK 3 B22 (A**2) : -0.24000
REMARK 3 B33 (A**2) : -0.29000
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): 0.090
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.087
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.057
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.598
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8265 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11231 ; 1.059 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 991 ; 5.202 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 358 ;33.253 ;23.520
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1408 ;12.963 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 58 ;15.588 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1221 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6218 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3812 ; 0.193 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5625 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 583 ; 0.096 ; 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): 54 ; 0.295 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.165 ; 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): 5123 ; 0.536 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8008 ; 0.804 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3682 ; 1.366 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3223 ; 2.167 ; 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 : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 3 A 99 1
REMARK 3 1 B 3 B 99 1
REMARK 3 2 A 110 A 496 1
REMARK 3 2 B 110 B 496 1
REMARK 3 3 A 600 A 600 1
REMARK 3 3 B 600 B 600 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 3910 ; 0.04 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 3910 ; 0.08 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 2V5Z 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_1290033167.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUL-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 164454
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
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 (%) : 97.9
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.08000
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) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.46600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
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: 1OJ9
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
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 66.27550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 111.80100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 66.27550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 111.80100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 66.27550
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 111.80100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 66.27550
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 111.80100
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: 4770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.4 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 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: 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 -71.37 66.90
REMARK 500 SER A 59 -45.71 -142.79
REMARK 500 THR A 64 -6.15 80.61
REMARK 500 ALA A 133 66.77 -162.65
REMARK 500 THR A 201 -80.49 -83.34
REMARK 500 ALA A 346 -121.84 51.42
REMARK 500 GLU A 379 62.71 -119.46
REMARK 500 ASP A 419 -103.10 57.67
REMARK 500 ALA A 424 -151.37 -105.53
REMARK 500 LYS B 52 -72.59 65.14
REMARK 500 SER B 59 -43.23 -141.84
REMARK 500 THR B 64 -6.66 81.23
REMARK 500 ALA B 133 67.82 -164.15
REMARK 500 THR B 201 -78.09 -83.82
REMARK 500 ALA B 346 -123.42 52.08
REMARK 500 GLU B 379 62.70 -119.46
REMARK 500 ASP B 419 -102.73 59.45
REMARK 500 ALA B 424 -152.28 -105.24
REMARK 500
REMARK 500 REMARK: NULL
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
DBREF 2V5Z A 1 520 UNP P27338 AOFB_HUMAN 1 520
DBREF 2V5Z B 1 520 UNP P27338 AOFB_HUMAN 1 520
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 A 600 53
HET SAG A 601 22
HET FAD B 600 53
HET SAG B 601 22
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM SAG (S)-(+)-2-[4-(FLUOROBENZYLOXY-BENZYLAMINO)PROPIONAMIDE]
HETSYN SAG SAFINAMIDE
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 SAG 2(C17 H17 F N2 O2)
FORMUL 7 HOH *717(H2 O)
HELIX 1 AA1 GLY A 13 SER A 26 1 14
HELIX 2 AA2 GLN A 65 LEU A 75 1 11
HELIX 3 AA3 ASN A 108 ARG A 127 1 20
HELIX 4 AA4 ALA A 133 ALA A 137 5 5
HELIX 5 AA5 LEU A 139 ASN A 145 1 7
HELIX 6 AA6 THR A 147 CYS A 156 1 10
HELIX 7 AA7 THR A 158 THR A 174 1 17
HELIX 8 AA8 SER A 181 GLN A 191 1 11
HELIX 9 AA9 GLY A 194 SER A 200 1 7
HELIX 10 AB1 SER A 214 GLY A 226 1 13
HELIX 11 AB2 PRO A 265 ILE A 272 5 8
HELIX 12 AB3 PRO A 279 ILE A 286 1 8
HELIX 13 AB4 PRO A 304 LYS A 309 5 6
HELIX 14 AB5 ALA A 346 ALA A 353 1 8
HELIX 15 AB6 THR A 356 GLY A 373 1 18
HELIX 16 AB7 SER A 374 GLU A 379 5 6
HELIX 17 AB8 CYS A 389 GLU A 391 5 3
HELIX 18 AB9 GLY A 405 GLY A 411 1 7
HELIX 19 AC1 ARG A 412 LEU A 414 5 3
HELIX 20 AC2 GLY A 425 ALA A 429 5 5
HELIX 21 AC3 TYR A 435 MET A 454 1 20
HELIX 22 AC4 PRO A 458 ILE A 462 5 5
HELIX 23 AC5 THR A 480 LEU A 486 1 7
HELIX 24 AC6 SER A 488 THR A 500 1 13
HELIX 25 AC7 GLY B 13 SER B 26 1 14
HELIX 26 AC8 GLN B 65 LEU B 75 1 11
HELIX 27 AC9 ASN B 108 ARG B 127 1 20
HELIX 28 AD1 ALA B 133 ALA B 137 5 5
HELIX 29 AD2 LEU B 139 ASN B 145 1 7
HELIX 30 AD3 THR B 147 CYS B 156 1 10
HELIX 31 AD4 THR B 158 THR B 174 1 17
HELIX 32 AD5 SER B 181 GLN B 191 1 11
HELIX 33 AD6 GLY B 194 SER B 200 1 7
HELIX 34 AD7 GLY B 215 GLY B 226 1 12
HELIX 35 AD8 PRO B 265 ILE B 272 5 8
HELIX 36 AD9 PRO B 279 ILE B 286 1 8
HELIX 37 AE1 PRO B 304 LYS B 309 5 6
HELIX 38 AE2 ALA B 346 ALA B 353 1 8
HELIX 39 AE3 THR B 356 GLY B 373 1 18
HELIX 40 AE4 SER B 374 GLU B 379 5 6
HELIX 41 AE5 CYS B 389 GLU B 391 5 3
HELIX 42 AE6 GLY B 405 GLY B 411 1 7
HELIX 43 AE7 ARG B 412 LEU B 414 5 3
HELIX 44 AE8 GLY B 425 ALA B 429 5 5
HELIX 45 AE9 TYR B 435 MET B 454 1 20
HELIX 46 AF1 PRO B 458 ILE B 462 5 5
HELIX 47 AF2 THR B 480 LEU B 486 1 7
HELIX 48 AF3 SER B 488 ILE B 496 1 9
SHEET 1 AA1 5 VAL A 229 LEU A 231 0
SHEET 2 AA1 5 VAL A 30 GLU A 34 1 N VAL A 32 O LYS A 230
SHEET 3 AA1 5 VAL A 7 VAL A 10 1 N VAL A 9 O VAL A 31
SHEET 4 AA1 5 TYR A 259 SER A 262 1 O ILE A 261 N VAL A 10
SHEET 5 AA1 5 ILE A 421 PHE A 423 1 O TYR A 422 N SER A 262
SHEET 1 AA2 2 THR A 45 LEU A 46 0
SHEET 2 AA2 2 VAL A 54 ASP A 55 -1 O VAL A 54 N LEU A 46
SHEET 1 AA3 3 TYR A 60 VAL A 61 0
SHEET 2 AA3 3 ARG A 208 PHE A 210 -1 O ARG A 208 N VAL A 61
SHEET 3 AA3 3 THR A 79 LYS A 81 -1 N TYR A 80 O LYS A 209
SHEET 1 AA4 7 LYS A 95 PHE A 99 0
SHEET 2 AA4 7 ARG A 87 VAL A 92 -1 N LEU A 88 O PHE A 99
SHEET 3 AA4 7 TYR A 311 ILE A 317 1 O ILE A 316 N HIS A 91
SHEET 4 AA4 7 TYR A 326 ASP A 329 -1 O THR A 327 N MET A 315
SHEET 5 AA4 7 ALA A 339 LEU A 345 -1 O MET A 341 N LEU A 328
SHEET 6 AA4 7 VAL A 294 TYR A 300 -1 N CYS A 297 O GLY A 342
SHEET 7 AA4 7 HIS A 382 ASN A 387 -1 O GLU A 384 N ILE A 298
SHEET 1 AA5 4 MET A 254 ALA A 257 0
SHEET 2 AA5 4 VAL A 245 THR A 249 -1 N VAL A 247 O TYR A 255
SHEET 3 AA5 4 VAL A 235 ASP A 239 -1 N ASP A 239 O LEU A 246
SHEET 4 AA5 4 HIS A 273 ASN A 275 1 O HIS A 273 N ILE A 236
SHEET 1 AA6 5 VAL B 229 LYS B 230 0
SHEET 2 AA6 5 VAL B 30 LEU B 33 1 N VAL B 32 O LYS B 230
SHEET 3 AA6 5 VAL B 7 VAL B 10 1 N VAL B 9 O VAL B 31
SHEET 4 AA6 5 TYR B 259 SER B 262 1 O ILE B 261 N VAL B 10
SHEET 5 AA6 5 ILE B 421 PHE B 423 1 O TYR B 422 N SER B 262
SHEET 1 AA7 2 THR B 45 ASN B 48 0
SHEET 2 AA7 2 LYS B 52 ASP B 55 -1 O VAL B 54 N LEU B 46
SHEET 1 AA8 3 TYR B 60 VAL B 61 0
SHEET 2 AA8 3 ARG B 208 PHE B 210 -1 O ARG B 208 N VAL B 61
SHEET 3 AA8 3 THR B 79 LYS B 81 -1 N TYR B 80 O LYS B 209
SHEET 1 AA9 7 LYS B 95 PHE B 99 0
SHEET 2 AA9 7 ARG B 87 VAL B 92 -1 N LEU B 88 O PHE B 99
SHEET 3 AA9 7 TYR B 311 ILE B 317 1 O ILE B 316 N HIS B 91
SHEET 4 AA9 7 TYR B 326 ASP B 329 -1 O THR B 327 N MET B 315
SHEET 5 AA9 7 ALA B 339 LEU B 345 -1 O MET B 341 N LEU B 328
SHEET 6 AA9 7 VAL B 294 TYR B 300 -1 N CYS B 297 O GLY B 342
SHEET 7 AA9 7 HIS B 382 ASN B 387 -1 O GLU B 384 N ILE B 298
SHEET 1 AB1 4 MET B 254 ALA B 257 0
SHEET 2 AB1 4 VAL B 245 THR B 249 -1 N VAL B 247 O TYR B 255
SHEET 3 AB1 4 VAL B 235 ASP B 239 -1 N TYR B 237 O GLU B 248
SHEET 4 AB1 4 HIS B 273 ASN B 275 1 O HIS B 273 N ILE B 236
CISPEP 1 ASN A 275 PRO A 276 0 -3.44
CISPEP 2 CYS A 397 TYR A 398 0 0.35
CISPEP 3 ASN B 275 PRO B 276 0 -2.53
CISPEP 4 CYS B 397 TYR B 398 0 1.05
CRYST1 132.551 223.602 86.589 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 0.007544 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004472 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011549 0.00000
MTRIX1 1 -0.527350 -0.495610 -0.690120 140.46417 1
MTRIX2 1 -0.494970 -0.480980 0.723640 209.12799 1
MTRIX3 1 -0.690580 0.723210 0.008340 -54.12844 1
(ATOM LINES ARE NOT SHOWN.)
END