HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 20-MAY-14 4QFD
TITLE CO-CRYSTAL STRUCTURE OF COMPOUND 2 (3-(7-HYDROXY-2-OXO-4-PHENYL-2H-
TITLE 2 CHROMEN-6-YL)PROPANOIC ACID) AND FAD BOUND TO HUMAN DAAO AT 2.85A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-AMINO-ACID OXIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DAAO, DAMOX, DAO;
COMPND 5 EC: 1.4.3.3;
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: DAMOX, DAO, DAO DAMOX;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS OXIDASE, OXIDOREDUCTASE, DAAO, D-AMINO ACID OXIDASE, D-SERINE
KEYWDS 2 COMPETITIVE, SCHIZOPHRENIA, NMDA RECEPTOR, OXIDOREDUCTASE-
KEYWDS 3 OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.E.EDWARDS,L.CHUN,T.L.ARAKAKI
REVDAT 10 20-SEP-23 4QFD 1 REMARK LINK
REVDAT 9 15-JUL-15 4QFD 1 JRNL
REVDAT 8 17-JUN-15 4QFD 1 JRNL
REVDAT 7 25-MAR-15 4QFD 1 JRNL
REVDAT 6 18-MAR-15 4QFD 1 JRNL
REVDAT 5 04-MAR-15 4QFD 1 JRNL
REVDAT 4 31-DEC-14 4QFD 1 JRNL
REVDAT 3 26-NOV-14 4QFD 1 JRNL
REVDAT 2 15-OCT-14 4QFD 1 AUTHOR
REVDAT 1 16-JUL-14 4QFD 0
JRNL AUTH R.T.TERRY-LORENZO,L.E.CHUN,S.P.BROWN,M.L.HEFFERNAN,Q.K.FANG,
JRNL AUTH 2 M.A.ORSINI,L.POLLEGIONI,L.W.HARDY,K.L.SPEAR,T.H.LARGE
JRNL TITL NOVEL HUMAN D-AMINO ACID OXIDASE INHIBITORS STABILIZE AN
JRNL TITL 2 ACTIVE-SITE LID-OPEN CONFORMATION.
JRNL REF BIOSCI.REP. V. 34 2014
JRNL REFN ISSN 0144-8463
JRNL PMID 25001371
JRNL DOI 10.1042/BSR20140071
REMARK 2
REMARK 2 RESOLUTION. 2.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 19539
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) : 0.250
REMARK 3 R VALUE (WORKING SET) : 0.248
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1000
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) : 2.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.92
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1347
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.3410
REMARK 3 BIN FREE R VALUE SET COUNT : 71
REMARK 3 BIN FREE R VALUE : 0.3460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4885
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 154
REMARK 3 SOLVENT ATOMS : 14
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 69.55
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 85.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.63000
REMARK 3 B22 (A**2) : 1.63000
REMARK 3 B33 (A**2) : -5.30000
REMARK 3 B12 (A**2) : 1.63000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.436
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.433
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 52.653
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.912
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.873
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5190 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4592 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7123 ; 1.104 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10470 ; 0.751 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 628 ; 5.687 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 224 ;35.746 ;23.616
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 688 ;15.539 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;12.668 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 779 ; 0.057 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5893 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1261 ; 0.002 ; 0.020
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): 2539 ; 1.066 ; 3.193
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2538 ; 1.067 ; 3.193
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3158 ; 1.849 ; 4.783
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 336
REMARK 3 RESIDUE RANGE : A 401 A 403
REMARK 3 ORIGIN FOR THE GROUP (A): -0.054 -14.826 16.776
REMARK 3 T TENSOR
REMARK 3 T11: 0.8428 T22: 0.2399
REMARK 3 T33: 0.4553 T12: -0.1924
REMARK 3 T13: -0.0312 T23: 0.0676
REMARK 3 L TENSOR
REMARK 3 L11: 0.8808 L22: 3.8699
REMARK 3 L33: 2.3165 L12: -0.8529
REMARK 3 L13: -1.3048 L23: 1.9448
REMARK 3 S TENSOR
REMARK 3 S11: -0.5402 S12: 0.0041 S13: -0.0283
REMARK 3 S21: -0.2775 S22: 0.3927 S23: 0.4428
REMARK 3 S31: 0.2952 S32: 0.1132 S33: 0.1476
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 336
REMARK 3 RESIDUE RANGE : B 401 B 403
REMARK 3 ORIGIN FOR THE GROUP (A): 32.924 -9.913 13.705
REMARK 3 T TENSOR
REMARK 3 T11: 0.7198 T22: 0.5178
REMARK 3 T33: 0.4732 T12: -0.1475
REMARK 3 T13: 0.2665 T23: -0.2074
REMARK 3 L TENSOR
REMARK 3 L11: 1.7021 L22: 0.8311
REMARK 3 L33: 2.8157 L12: 0.9375
REMARK 3 L13: 0.7297 L23: 1.1555
REMARK 3 S TENSOR
REMARK 3 S11: -0.5610 S12: 0.4060 S13: -0.4413
REMARK 3 S21: -0.1612 S22: 0.4392 S23: -0.2374
REMARK 3 S31: -0.0725 S32: 0.2251 S33: 0.1217
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED HYDROGENS
REMARK 3 HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 4QFD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000085984.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.12709
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19576
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.7600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.72800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.2
REMARK 200 STARTING MODEL: PDB ENTRY 3CUK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: DAAO AT 2 MG/ML IN 50 MM SODIUM
REMARK 280 PHOSPHATE PH 6.6, 10 UM FAD INCUBATED WITH 5-FOLD EXCESS OF SEP-
REMARK 280 0374036 OVERNIGHT AT 277 K, CRYSTALLIZED AGAINST 13.6% PEG3350,
REMARK 280 0.1 M TRIS PH 7.4, 150 MM POTASSIUM CITRATE TRIBASIC AND 20 MM
REMARK 280 GLYCEROL AS CRYO-PROTECTANT, CRYSTAL TRACKING ID 241709B5,
REMARK 280 UNIQUE PUCK ID XSS6-4, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 125.31333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 62.65667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 62.65667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 125.31333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 6160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 62.65667
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 6470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 62.65667
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -138.0 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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 62.65667
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 SER A 25
REMARK 465 VAL A 26
REMARK 465 LEU A 27
REMARK 465 GLN A 28
REMARK 465 PRO A 29
REMARK 465 SER A 57
REMARK 465 ASP A 58
REMARK 465 PRO A 59
REMARK 465 ASN A 60
REMARK 465 ASN A 61
REMARK 465 GLY A 299
REMARK 465 PRO A 300
REMARK 465 SER A 301
REMARK 465 ASN A 302
REMARK 465 LYS A 337
REMARK 465 LYS A 338
REMARK 465 LEU A 339
REMARK 465 SER A 340
REMARK 465 ARG A 341
REMARK 465 MET A 342
REMARK 465 PRO A 343
REMARK 465 PRO A 344
REMARK 465 SER A 345
REMARK 465 HIS A 346
REMARK 465 LEU A 347
REMARK 465 SER B 25
REMARK 465 VAL B 26
REMARK 465 LEU B 27
REMARK 465 GLN B 28
REMARK 465 PRO B 29
REMARK 465 SER B 57
REMARK 465 ASP B 58
REMARK 465 PRO B 59
REMARK 465 ASN B 60
REMARK 465 ASN B 61
REMARK 465 PRO B 219
REMARK 465 GLU B 220
REMARK 465 ARG B 221
REMARK 465 GLY B 222
REMARK 465 LEU B 296
REMARK 465 ARG B 297
REMARK 465 THR B 298
REMARK 465 GLY B 299
REMARK 465 PRO B 300
REMARK 465 SER B 301
REMARK 465 ASN B 302
REMARK 465 LYS B 337
REMARK 465 LYS B 338
REMARK 465 LEU B 339
REMARK 465 SER B 340
REMARK 465 ARG B 341
REMARK 465 MET B 342
REMARK 465 PRO B 343
REMARK 465 PRO B 344
REMARK 465 SER B 345
REMARK 465 HIS B 346
REMARK 465 LEU B 347
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 MET A 1 CG SD CE
REMARK 470 ARG A 2 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 22 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 33 CG CD CE NZ
REMARK 470 GLU A 100 CG CD OE1 OE2
REMARK 470 LYS A 108 CG CD CE NZ
REMARK 470 LYS A 116 CG CD CE NZ
REMARK 470 ARG A 120 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 142 CG CD CE NZ
REMARK 470 LYS A 158 CG CD CE NZ
REMARK 470 ARG A 162 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 165 CG CD OE1 OE2
REMARK 470 GLU A 173 CG CD OE1 OE2
REMARK 470 LYS A 204 CG CD CE NZ
REMARK 470 GLU A 220 CG CD OE1 OE2
REMARK 470 ARG A 265 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 271 CG CD CE NZ
REMARK 470 ASN A 272 CG OD1 ND2
REMARK 470 ARG A 274 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 293 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 295 CG CD OE1 NE2
REMARK 470 LEU A 296 CG CD1 CD2
REMARK 470 ARG A 297 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 325 CG CD OE1 OE2
REMARK 470 LYS A 328 CG CD CE NZ
REMARK 470 ARG A 332 CG CD NE CZ NH1 NH2
REMARK 470 MET B 1 CG SD CE
REMARK 470 ARG B 2 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 22 CG CD NE CZ NH1 NH2
REMARK 470 HIS B 24 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 33 CG CD CE NZ
REMARK 470 LEU B 42 CG CD1 CD2
REMARK 470 LEU B 56 CG CD1 CD2
REMARK 470 GLN B 63 CG CD OE1 NE2
REMARK 470 GLN B 69 CG CD OE1 NE2
REMARK 470 ASN B 83 CG OD1 ND2
REMARK 470 GLU B 100 CG CD OE1 OE2
REMARK 470 LYS B 108 CG CD CE NZ
REMARK 470 LYS B 116 CG CD CE NZ
REMARK 470 LYS B 142 CG CD CE NZ
REMARK 470 GLU B 154 CG CD OE1 OE2
REMARK 470 LYS B 158 CG CD CE NZ
REMARK 470 GLU B 168 CG CD OE1 OE2
REMARK 470 VAL B 170 CG1 CG2
REMARK 470 ARG B 172 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 173 CG CD OE1 OE2
REMARK 470 GLN B 196 CG CD OE1 NE2
REMARK 470 LYS B 204 CG CD CE NZ
REMARK 470 ASP B 218 CG OD1 OD2
REMARK 470 GLN B 254 CG CD OE1 NE2
REMARK 470 LYS B 271 CG CD CE NZ
REMARK 470 ARG B 274 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 286 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 288 CG CD OE1 NE2
REMARK 470 ARG B 290 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 293 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 295 CG CD OE1 NE2
REMARK 470 LYS B 328 CG CD CE NZ
REMARK 470 ILE B 333 CG1 CG2 CD1
REMARK 470 GLU B 335 CG CD OE1 OE2
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 PRO A 41 35.13 -89.48
REMARK 500 GLN A 53 114.97 176.72
REMARK 500 HIS A 99 -78.92 -101.72
REMARK 500 ASP A 192 93.46 -161.07
REMARK 500 ASN A 225 70.03 -118.21
REMARK 500 ASN A 272 43.82 -99.71
REMARK 500 ASN A 308 79.34 -150.51
REMARK 500 PRO B 41 35.36 -90.97
REMARK 500 GLN B 53 113.66 177.04
REMARK 500 HIS B 99 -78.91 -101.64
REMARK 500 ASP B 192 93.16 -160.76
REMARK 500 ASN B 225 71.04 -118.42
REMARK 500 ASN B 272 44.04 -100.05
REMARK 500 ASN B 308 79.31 -150.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 122 O
REMARK 620 2 PHE A 125 O 71.5
REMARK 620 3 TYR A 128 O 97.4 68.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU B 122 O
REMARK 620 2 PHE B 125 O 69.3
REMARK 620 3 TYR B 128 O 91.0 67.4
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 31R A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 31R B 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QFC RELATED DB: PDB
REMARK 900 DAAO BOUND TO SEP0376049
DBREF 4QFD A 1 347 UNP P14920 OXDA_HUMAN 1 347
DBREF 4QFD B 1 347 UNP P14920 OXDA_HUMAN 1 347
SEQRES 1 A 347 MET ARG VAL VAL VAL ILE GLY ALA GLY VAL ILE GLY LEU
SEQRES 2 A 347 SER THR ALA LEU CYS ILE HIS GLU ARG TYR HIS SER VAL
SEQRES 3 A 347 LEU GLN PRO LEU ASP ILE LYS VAL TYR ALA ASP ARG PHE
SEQRES 4 A 347 THR PRO LEU THR THR THR ASP VAL ALA ALA GLY LEU TRP
SEQRES 5 A 347 GLN PRO TYR LEU SER ASP PRO ASN ASN PRO GLN GLU ALA
SEQRES 6 A 347 ASP TRP SER GLN GLN THR PHE ASP TYR LEU LEU SER HIS
SEQRES 7 A 347 VAL HIS SER PRO ASN ALA GLU ASN LEU GLY LEU PHE LEU
SEQRES 8 A 347 ILE SER GLY TYR ASN LEU PHE HIS GLU ALA ILE PRO ASP
SEQRES 9 A 347 PRO SER TRP LYS ASP THR VAL LEU GLY PHE ARG LYS LEU
SEQRES 10 A 347 THR PRO ARG GLU LEU ASP MET PHE PRO ASP TYR GLY TYR
SEQRES 11 A 347 GLY TRP PHE HIS THR SER LEU ILE LEU GLU GLY LYS ASN
SEQRES 12 A 347 TYR LEU GLN TRP LEU THR GLU ARG LEU THR GLU ARG GLY
SEQRES 13 A 347 VAL LYS PHE PHE GLN ARG LYS VAL GLU SER PHE GLU GLU
SEQRES 14 A 347 VAL ALA ARG GLU GLY ALA ASP VAL ILE VAL ASN CYS THR
SEQRES 15 A 347 GLY VAL TRP ALA GLY ALA LEU GLN ARG ASP PRO LEU LEU
SEQRES 16 A 347 GLN PRO GLY ARG GLY GLN ILE MET LYS VAL ASP ALA PRO
SEQRES 17 A 347 TRP MET LYS HIS PHE ILE LEU THR HIS ASP PRO GLU ARG
SEQRES 18 A 347 GLY ILE TYR ASN SER PRO TYR ILE ILE PRO GLY THR GLN
SEQRES 19 A 347 THR VAL THR LEU GLY GLY ILE PHE GLN LEU GLY ASN TRP
SEQRES 20 A 347 SER GLU LEU ASN ASN ILE GLN ASP HIS ASN THR ILE TRP
SEQRES 21 A 347 GLU GLY CYS CYS ARG LEU GLU PRO THR LEU LYS ASN ALA
SEQRES 22 A 347 ARG ILE ILE GLY GLU ARG THR GLY PHE ARG PRO VAL ARG
SEQRES 23 A 347 PRO GLN ILE ARG LEU GLU ARG GLU GLN LEU ARG THR GLY
SEQRES 24 A 347 PRO SER ASN THR GLU VAL ILE HIS ASN TYR GLY HIS GLY
SEQRES 25 A 347 GLY TYR GLY LEU THR ILE HIS TRP GLY CYS ALA LEU GLU
SEQRES 26 A 347 ALA ALA LYS LEU PHE GLY ARG ILE LEU GLU GLU LYS LYS
SEQRES 27 A 347 LEU SER ARG MET PRO PRO SER HIS LEU
SEQRES 1 B 347 MET ARG VAL VAL VAL ILE GLY ALA GLY VAL ILE GLY LEU
SEQRES 2 B 347 SER THR ALA LEU CYS ILE HIS GLU ARG TYR HIS SER VAL
SEQRES 3 B 347 LEU GLN PRO LEU ASP ILE LYS VAL TYR ALA ASP ARG PHE
SEQRES 4 B 347 THR PRO LEU THR THR THR ASP VAL ALA ALA GLY LEU TRP
SEQRES 5 B 347 GLN PRO TYR LEU SER ASP PRO ASN ASN PRO GLN GLU ALA
SEQRES 6 B 347 ASP TRP SER GLN GLN THR PHE ASP TYR LEU LEU SER HIS
SEQRES 7 B 347 VAL HIS SER PRO ASN ALA GLU ASN LEU GLY LEU PHE LEU
SEQRES 8 B 347 ILE SER GLY TYR ASN LEU PHE HIS GLU ALA ILE PRO ASP
SEQRES 9 B 347 PRO SER TRP LYS ASP THR VAL LEU GLY PHE ARG LYS LEU
SEQRES 10 B 347 THR PRO ARG GLU LEU ASP MET PHE PRO ASP TYR GLY TYR
SEQRES 11 B 347 GLY TRP PHE HIS THR SER LEU ILE LEU GLU GLY LYS ASN
SEQRES 12 B 347 TYR LEU GLN TRP LEU THR GLU ARG LEU THR GLU ARG GLY
SEQRES 13 B 347 VAL LYS PHE PHE GLN ARG LYS VAL GLU SER PHE GLU GLU
SEQRES 14 B 347 VAL ALA ARG GLU GLY ALA ASP VAL ILE VAL ASN CYS THR
SEQRES 15 B 347 GLY VAL TRP ALA GLY ALA LEU GLN ARG ASP PRO LEU LEU
SEQRES 16 B 347 GLN PRO GLY ARG GLY GLN ILE MET LYS VAL ASP ALA PRO
SEQRES 17 B 347 TRP MET LYS HIS PHE ILE LEU THR HIS ASP PRO GLU ARG
SEQRES 18 B 347 GLY ILE TYR ASN SER PRO TYR ILE ILE PRO GLY THR GLN
SEQRES 19 B 347 THR VAL THR LEU GLY GLY ILE PHE GLN LEU GLY ASN TRP
SEQRES 20 B 347 SER GLU LEU ASN ASN ILE GLN ASP HIS ASN THR ILE TRP
SEQRES 21 B 347 GLU GLY CYS CYS ARG LEU GLU PRO THR LEU LYS ASN ALA
SEQRES 22 B 347 ARG ILE ILE GLY GLU ARG THR GLY PHE ARG PRO VAL ARG
SEQRES 23 B 347 PRO GLN ILE ARG LEU GLU ARG GLU GLN LEU ARG THR GLY
SEQRES 24 B 347 PRO SER ASN THR GLU VAL ILE HIS ASN TYR GLY HIS GLY
SEQRES 25 B 347 GLY TYR GLY LEU THR ILE HIS TRP GLY CYS ALA LEU GLU
SEQRES 26 B 347 ALA ALA LYS LEU PHE GLY ARG ILE LEU GLU GLU LYS LYS
SEQRES 27 B 347 LEU SER ARG MET PRO PRO SER HIS LEU
HET NA A 401 1
HET FAD A 402 53
HET 31R A 403 23
HET NA B 401 1
HET FAD B 402 53
HET 31R B 403 23
HETNAM NA SODIUM ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM 31R 3-(7-HYDROXY-2-OXO-4-PHENYL-2H-CHROMEN-6-YL)PROPANOIC
HETNAM 2 31R ACID
FORMUL 3 NA 2(NA 1+)
FORMUL 4 FAD 2(C27 H33 N9 O15 P2)
FORMUL 5 31R 2(C18 H14 O5)
FORMUL 9 HOH *14(H2 O)
HELIX 1 1 GLY A 9 TYR A 23 1 15
HELIX 2 2 THR A 43 ALA A 48 1 6
HELIX 3 3 GLN A 63 VAL A 79 1 17
HELIX 4 4 ASN A 83 GLY A 88 1 6
HELIX 5 5 PRO A 105 THR A 110 5 6
HELIX 6 6 THR A 118 ASP A 123 1 6
HELIX 7 7 GLU A 140 ARG A 155 1 16
HELIX 8 8 SER A 166 ALA A 175 1 10
HELIX 9 9 THR A 182 VAL A 184 5 3
HELIX 10 10 TRP A 185 GLN A 190 1 6
HELIX 11 11 ASP A 218 GLY A 222 5 5
HELIX 12 12 ASN A 252 GLU A 267 1 16
HELIX 13 13 PRO A 268 ALA A 273 5 6
HELIX 14 14 TYR A 314 GLU A 335 1 22
HELIX 15 15 GLY B 9 TYR B 23 1 15
HELIX 16 16 THR B 43 ALA B 48 1 6
HELIX 17 17 GLN B 63 VAL B 79 1 17
HELIX 18 18 ASN B 83 GLY B 88 1 6
HELIX 19 19 PRO B 105 THR B 110 5 6
HELIX 20 20 THR B 118 ASP B 123 1 6
HELIX 21 21 GLU B 140 ARG B 155 1 16
HELIX 22 22 SER B 166 ALA B 175 1 10
HELIX 23 23 THR B 182 VAL B 184 5 3
HELIX 24 24 TRP B 185 GLN B 190 1 6
HELIX 25 25 ASN B 252 GLU B 267 1 16
HELIX 26 26 PRO B 268 ALA B 273 5 6
HELIX 27 27 TYR B 314 GLU B 335 1 22
SHEET 1 A 6 LYS A 158 GLN A 161 0
SHEET 2 A 6 ASP A 31 ALA A 36 1 N VAL A 34 O PHE A 160
SHEET 3 A 6 ARG A 2 ILE A 6 1 N VAL A 5 O TYR A 35
SHEET 4 A 6 VAL A 177 ASN A 180 1 O VAL A 179 N ILE A 6
SHEET 5 A 6 GLU A 304 TYR A 309 1 O GLU A 304 N ILE A 178
SHEET 6 A 6 ARG A 290 GLN A 295 -1 N ARG A 290 O TYR A 309
SHEET 1 B 8 LEU A 112 LYS A 116 0
SHEET 2 B 8 TYR A 130 LEU A 139 -1 O THR A 135 N LEU A 112
SHEET 3 B 8 LEU A 89 PHE A 98 -1 N ILE A 92 O SER A 136
SHEET 4 B 8 PHE A 213 THR A 216 1 O LEU A 215 N LEU A 97
SHEET 5 B 8 TYR A 228 PRO A 231 -1 O ILE A 229 N ILE A 214
SHEET 6 B 8 VAL A 236 GLY A 239 -1 O THR A 237 N ILE A 230
SHEET 7 B 8 GLN A 196 ASP A 206 -1 N VAL A 205 O VAL A 236
SHEET 8 B 8 GLN A 243 LEU A 244 -1 O GLN A 243 N ARG A 199
SHEET 1 C 8 LEU A 112 LYS A 116 0
SHEET 2 C 8 TYR A 130 LEU A 139 -1 O THR A 135 N LEU A 112
SHEET 3 C 8 LEU A 89 PHE A 98 -1 N ILE A 92 O SER A 136
SHEET 4 C 8 PHE A 213 THR A 216 1 O LEU A 215 N LEU A 97
SHEET 5 C 8 TYR A 228 PRO A 231 -1 O ILE A 229 N ILE A 214
SHEET 6 C 8 VAL A 236 GLY A 239 -1 O THR A 237 N ILE A 230
SHEET 7 C 8 GLN A 196 ASP A 206 -1 N VAL A 205 O VAL A 236
SHEET 8 C 8 ARG A 274 VAL A 285 -1 O GLY A 281 N GLY A 200
SHEET 1 D 6 LYS B 158 GLN B 161 0
SHEET 2 D 6 ASP B 31 ALA B 36 1 N VAL B 34 O PHE B 160
SHEET 3 D 6 ARG B 2 ILE B 6 1 N VAL B 5 O TYR B 35
SHEET 4 D 6 VAL B 177 ASN B 180 1 O VAL B 179 N ILE B 6
SHEET 5 D 6 GLU B 304 TYR B 309 1 O GLU B 304 N ILE B 178
SHEET 6 D 6 ARG B 290 GLU B 294 -1 N ARG B 290 O TYR B 309
SHEET 1 E 8 LEU B 112 LYS B 116 0
SHEET 2 E 8 TYR B 130 LEU B 139 -1 O THR B 135 N LEU B 112
SHEET 3 E 8 LEU B 89 PHE B 98 -1 N ILE B 92 O SER B 136
SHEET 4 E 8 PHE B 213 THR B 216 1 O LEU B 215 N LEU B 97
SHEET 5 E 8 TYR B 228 PRO B 231 -1 O ILE B 229 N ILE B 214
SHEET 6 E 8 VAL B 236 GLY B 239 -1 O THR B 237 N ILE B 230
SHEET 7 E 8 GLN B 196 ASP B 206 -1 N VAL B 205 O VAL B 236
SHEET 8 E 8 GLN B 243 LEU B 244 -1 O GLN B 243 N ARG B 199
SHEET 1 F 8 LEU B 112 LYS B 116 0
SHEET 2 F 8 TYR B 130 LEU B 139 -1 O THR B 135 N LEU B 112
SHEET 3 F 8 LEU B 89 PHE B 98 -1 N ILE B 92 O SER B 136
SHEET 4 F 8 PHE B 213 THR B 216 1 O LEU B 215 N LEU B 97
SHEET 5 F 8 TYR B 228 PRO B 231 -1 O ILE B 229 N ILE B 214
SHEET 6 F 8 VAL B 236 GLY B 239 -1 O THR B 237 N ILE B 230
SHEET 7 F 8 GLN B 196 ASP B 206 -1 N VAL B 205 O VAL B 236
SHEET 8 F 8 ARG B 274 VAL B 285 -1 O GLY B 281 N GLY B 200
LINK O LEU A 122 NA NA A 401 1555 1555 2.54
LINK O PHE A 125 NA NA A 401 1555 1555 2.95
LINK O TYR A 128 NA NA A 401 1555 1555 2.61
LINK O LEU B 122 NA NA B 401 1555 1555 2.70
LINK O PHE B 125 NA NA B 401 1555 1555 2.95
LINK O TYR B 128 NA NA B 401 1555 1555 2.70
CISPEP 1 THR A 40 PRO A 41 0 -9.11
CISPEP 2 THR B 40 PRO B 41 0 -8.58
SITE 1 AC1 4 LEU A 122 PHE A 125 PRO A 126 TYR A 128
SITE 1 AC2 33 GLY A 7 ALA A 8 GLY A 9 VAL A 10
SITE 2 AC2 33 ILE A 11 ALA A 36 ASP A 37 ARG A 38
SITE 3 AC2 33 THR A 44 THR A 45 VAL A 47 ALA A 48
SITE 4 AC2 33 ALA A 49 GLY A 50 LEU A 51 ARG A 162
SITE 5 AC2 33 VAL A 164 CYS A 181 THR A 182 GLY A 183
SITE 6 AC2 33 TRP A 185 GLY A 281 ARG A 283 GLY A 312
SITE 7 AC2 33 GLY A 313 TYR A 314 GLY A 315 LEU A 316
SITE 8 AC2 33 THR A 317 31R A 403 HOH A 503 HOH A 504
SITE 9 AC2 33 HOH A 505
SITE 1 AC3 13 GLN A 53 PRO A 54 TYR A 55 LEU A 56
SITE 2 AC3 13 THR A 216 HIS A 217 TYR A 224 SER A 226
SITE 3 AC3 13 TYR A 228 ARG A 283 GLY A 313 FAD A 402
SITE 4 AC3 13 HOH A 508
SITE 1 AC4 4 LEU B 122 PHE B 125 PRO B 126 TYR B 128
SITE 1 AC5 29 GLY B 7 ALA B 8 GLY B 9 VAL B 10
SITE 2 AC5 29 ILE B 11 ALA B 36 ASP B 37 ARG B 38
SITE 3 AC5 29 THR B 44 THR B 45 ALA B 48 ALA B 49
SITE 4 AC5 29 GLY B 50 LEU B 51 ARG B 162 VAL B 164
SITE 5 AC5 29 THR B 182 GLY B 183 TRP B 185 ILE B 202
SITE 6 AC5 29 GLY B 281 ARG B 283 GLY B 312 GLY B 313
SITE 7 AC5 29 TYR B 314 GLY B 315 LEU B 316 THR B 317
SITE 8 AC5 29 31R B 403
SITE 1 AC6 9 GLN B 53 PRO B 54 TYR B 55 TYR B 224
SITE 2 AC6 9 SER B 226 TYR B 228 ARG B 283 GLY B 313
SITE 3 AC6 9 FAD B 402
CRYST1 86.490 86.490 187.970 90.00 90.00 120.00 P 32 2 1 12
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 0.011562 0.006675 0.000000 0.00000
SCALE2 0.000000 0.013351 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005320 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
