HEADER OXIDOREDUCTASE 01-SEP-17 5YAK
TITLE THE CRYSTAL STRUCTURE OF HUMAN IYD THR239 MUTANT WITH LIGAND 3-
TITLE 2 FLUOROTYROSINE (F-TYR)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IODOTYROSINE DEIODINASE 1;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: UNP RESIDUES 32-289;
COMPND 5 SYNONYM: IYD-1,IODOTYROSINE DEHALOGENASE 1;
COMPND 6 EC: 1.21.1.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 OTHER_DETAILS: FMN(FLAVIN MONONUCLEOTIDE) YOF(3-MONOFLUOROTYROSINE)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: IYD, C6ORF71, DEHAL1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28-SUMO
KEYWDS HIYD, FMN, MFT, T239A MUTANT, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.HU,S.E.ROKITA,J.SCHLESSMAN
REVDAT 3 26-DEC-18 5YAK 1 JRNL
REVDAT 2 15-AUG-18 5YAK 1 JRNL
REVDAT 1 08-AUG-18 5YAK 0
JRNL AUTH J.HU,Q.SU,J.L.SCHLESSMAN,S.E.ROKITA
JRNL TITL REDOX CONTROL OF IODOTYROSINE DEIODINASE
JRNL REF PROTEIN SCI. V. 28 68 2019
JRNL REFN ESSN 1469-896X
JRNL PMID 30052294
JRNL DOI 10.1002/PRO.3479
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.M.HU,S.E.ROKITA
REMARK 1 TITL THE ROLE OF THR239 ON THE CATALYSIS OF HIYD
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 78650
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4144
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5790
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.2150
REMARK 3 BIN FREE R VALUE SET COUNT : 293
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10536
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 270
REMARK 3 SOLVENT ATOMS : 297
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.01000
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): 0.244
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.199
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11058 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 10958 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15005 ; 1.544 ; 1.998
REMARK 3 BOND ANGLES OTHERS (DEGREES): 25229 ; 3.433 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1292 ; 6.456 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 459 ;34.989 ;23.333
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2006 ;16.129 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 78 ;17.714 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1685 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11900 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2402 ; 0.014 ; 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): 5219 ; 3.925 ; 4.510
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5219 ; 3.925 ; 4.510
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6494 ; 5.228 ; 6.741
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 6495 ; 5.228 ; 6.741
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5839 ; 4.854 ; 5.024
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 5840 ; 4.854 ; 5.023
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 8512 ; 7.129 ; 7.295
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 13142 ; 8.465 ;36.449
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 13063 ; 8.479 ;36.434
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5YAK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1300003521.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-FEB-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4-8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 82734
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 46.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 41.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.00
REMARK 200 R MERGE FOR SHELL (I) : 0.09300
REMARK 200 R SYM FOR SHELL (I) : 0.08400
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: 4TTC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17 M SODIUM ACETATE, 85 MM TRIS-HCL
REMARK 280 (PH 8.5), 22.5 % W/V POLYETHYLENE GLYCOL 4,000 AND 15 %
REMARK 280 GLYCEROL., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 100.06733
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 200.13467
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 150.10100
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 250.16833
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 50.03367
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: 11330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F
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
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: 11820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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
REMARK 350 BIOMOLECULE: 3
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: 11820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E
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 GLY A 32
REMARK 465 GLU A 33
REMARK 465 PRO A 34
REMARK 465 ARG A 35
REMARK 465 THR A 36
REMARK 465 ARG A 37
REMARK 465 ALA A 38
REMARK 465 GLU A 39
REMARK 465 ALA A 40
REMARK 465 ARG A 41
REMARK 465 PRO A 42
REMARK 465 TRP A 43
REMARK 465 VAL A 44
REMARK 465 ASP A 45
REMARK 465 GLU A 46
REMARK 465 ASP A 47
REMARK 465 LEU A 48
REMARK 465 LYS A 49
REMARK 465 ASP A 50
REMARK 465 SER A 51
REMARK 465 SER A 52
REMARK 465 ASP A 53
REMARK 465 LEU A 54
REMARK 465 HIS A 55
REMARK 465 GLN A 56
REMARK 465 ALA A 57
REMARK 465 GLU A 58
REMARK 465 GLU A 59
REMARK 465 ASP A 60
REMARK 465 ALA A 61
REMARK 465 ASP A 62
REMARK 465 GLU A 63
REMARK 465 TRP A 64
REMARK 465 GLN A 65
REMARK 465 GLU A 66
REMARK 465 SER A 67
REMARK 465 GLU A 68
REMARK 465 GLU A 69
REMARK 465 ASN A 70
REMARK 465 VAL A 71
REMARK 465 ALA A 203
REMARK 465 ASN A 204
REMARK 465 VAL A 289
REMARK 465 HIS A 290
REMARK 465 HIS A 291
REMARK 465 HIS A 292
REMARK 465 HIS A 293
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 GLY B 32
REMARK 465 GLU B 33
REMARK 465 PRO B 34
REMARK 465 ARG B 35
REMARK 465 THR B 36
REMARK 465 ARG B 37
REMARK 465 ALA B 38
REMARK 465 GLU B 39
REMARK 465 ALA B 40
REMARK 465 ARG B 41
REMARK 465 PRO B 42
REMARK 465 TRP B 43
REMARK 465 VAL B 44
REMARK 465 ASP B 45
REMARK 465 GLU B 46
REMARK 465 ASP B 47
REMARK 465 LEU B 48
REMARK 465 LYS B 49
REMARK 465 ASP B 50
REMARK 465 SER B 51
REMARK 465 SER B 52
REMARK 465 ASP B 53
REMARK 465 LEU B 54
REMARK 465 HIS B 55
REMARK 465 GLN B 56
REMARK 465 ALA B 57
REMARK 465 GLU B 58
REMARK 465 GLU B 59
REMARK 465 ASP B 60
REMARK 465 ALA B 61
REMARK 465 ASP B 62
REMARK 465 GLU B 63
REMARK 465 TRP B 64
REMARK 465 GLN B 65
REMARK 465 GLU B 66
REMARK 465 SER B 67
REMARK 465 GLU B 68
REMARK 465 GLU B 69
REMARK 465 ASN B 70
REMARK 465 ALA B 203
REMARK 465 HIS B 290
REMARK 465 HIS B 291
REMARK 465 HIS B 292
REMARK 465 HIS B 293
REMARK 465 HIS B 294
REMARK 465 HIS B 295
REMARK 465 GLY C 32
REMARK 465 GLU C 33
REMARK 465 PRO C 34
REMARK 465 ARG C 35
REMARK 465 THR C 36
REMARK 465 ARG C 37
REMARK 465 ALA C 38
REMARK 465 GLU C 39
REMARK 465 ALA C 40
REMARK 465 ARG C 41
REMARK 465 PRO C 42
REMARK 465 TRP C 43
REMARK 465 VAL C 44
REMARK 465 ASP C 45
REMARK 465 GLU C 46
REMARK 465 ASP C 47
REMARK 465 LEU C 48
REMARK 465 LYS C 49
REMARK 465 ASP C 50
REMARK 465 SER C 51
REMARK 465 SER C 52
REMARK 465 ASP C 53
REMARK 465 LEU C 54
REMARK 465 HIS C 55
REMARK 465 GLN C 56
REMARK 465 ALA C 57
REMARK 465 GLU C 58
REMARK 465 GLU C 59
REMARK 465 ASP C 60
REMARK 465 ALA C 61
REMARK 465 ASP C 62
REMARK 465 GLU C 63
REMARK 465 TRP C 64
REMARK 465 GLN C 65
REMARK 465 GLU C 66
REMARK 465 SER C 67
REMARK 465 GLU C 68
REMARK 465 GLU C 69
REMARK 465 ASN C 70
REMARK 465 ALA C 203
REMARK 465 ASN C 204
REMARK 465 HIS C 290
REMARK 465 HIS C 291
REMARK 465 HIS C 292
REMARK 465 HIS C 293
REMARK 465 HIS C 294
REMARK 465 HIS C 295
REMARK 465 GLY D 32
REMARK 465 GLU D 33
REMARK 465 PRO D 34
REMARK 465 ARG D 35
REMARK 465 THR D 36
REMARK 465 ARG D 37
REMARK 465 ALA D 38
REMARK 465 GLU D 39
REMARK 465 ALA D 40
REMARK 465 ARG D 41
REMARK 465 PRO D 42
REMARK 465 TRP D 43
REMARK 465 VAL D 44
REMARK 465 ASP D 45
REMARK 465 GLU D 46
REMARK 465 ASP D 47
REMARK 465 LEU D 48
REMARK 465 LYS D 49
REMARK 465 ASP D 50
REMARK 465 SER D 51
REMARK 465 SER D 52
REMARK 465 ASP D 53
REMARK 465 LEU D 54
REMARK 465 HIS D 55
REMARK 465 GLN D 56
REMARK 465 ALA D 57
REMARK 465 GLU D 58
REMARK 465 GLU D 59
REMARK 465 ASP D 60
REMARK 465 ALA D 61
REMARK 465 ASP D 62
REMARK 465 GLU D 63
REMARK 465 TRP D 64
REMARK 465 GLN D 65
REMARK 465 GLU D 66
REMARK 465 SER D 67
REMARK 465 GLU D 68
REMARK 465 GLU D 69
REMARK 465 ASN D 70
REMARK 465 ALA D 202
REMARK 465 ALA D 203
REMARK 465 ASN D 204
REMARK 465 LYS D 206
REMARK 465 HIS D 290
REMARK 465 HIS D 291
REMARK 465 HIS D 292
REMARK 465 HIS D 293
REMARK 465 HIS D 294
REMARK 465 HIS D 295
REMARK 465 GLY E 32
REMARK 465 GLU E 33
REMARK 465 PRO E 34
REMARK 465 ARG E 35
REMARK 465 THR E 36
REMARK 465 ARG E 37
REMARK 465 ALA E 38
REMARK 465 GLU E 39
REMARK 465 ALA E 40
REMARK 465 ARG E 41
REMARK 465 PRO E 42
REMARK 465 TRP E 43
REMARK 465 VAL E 44
REMARK 465 ASP E 45
REMARK 465 GLU E 46
REMARK 465 ASP E 47
REMARK 465 LEU E 48
REMARK 465 LYS E 49
REMARK 465 ASP E 50
REMARK 465 SER E 51
REMARK 465 SER E 52
REMARK 465 ASP E 53
REMARK 465 LEU E 54
REMARK 465 HIS E 55
REMARK 465 GLN E 56
REMARK 465 ALA E 57
REMARK 465 GLU E 58
REMARK 465 GLU E 59
REMARK 465 ASP E 60
REMARK 465 ALA E 61
REMARK 465 ASP E 62
REMARK 465 GLU E 63
REMARK 465 TRP E 64
REMARK 465 GLN E 65
REMARK 465 GLU E 66
REMARK 465 SER E 67
REMARK 465 GLU E 68
REMARK 465 GLU E 69
REMARK 465 ASN E 70
REMARK 465 HIS E 290
REMARK 465 HIS E 291
REMARK 465 HIS E 292
REMARK 465 HIS E 293
REMARK 465 HIS E 294
REMARK 465 HIS E 295
REMARK 465 GLY F 32
REMARK 465 GLU F 33
REMARK 465 PRO F 34
REMARK 465 ARG F 35
REMARK 465 THR F 36
REMARK 465 ARG F 37
REMARK 465 ALA F 38
REMARK 465 GLU F 39
REMARK 465 ALA F 40
REMARK 465 ARG F 41
REMARK 465 PRO F 42
REMARK 465 TRP F 43
REMARK 465 VAL F 44
REMARK 465 ASP F 45
REMARK 465 GLU F 46
REMARK 465 ASP F 47
REMARK 465 LEU F 48
REMARK 465 LYS F 49
REMARK 465 ASP F 50
REMARK 465 SER F 51
REMARK 465 SER F 52
REMARK 465 ASP F 53
REMARK 465 LEU F 54
REMARK 465 HIS F 55
REMARK 465 GLN F 56
REMARK 465 ALA F 57
REMARK 465 GLU F 58
REMARK 465 GLU F 59
REMARK 465 ASP F 60
REMARK 465 ALA F 61
REMARK 465 ASP F 62
REMARK 465 GLU F 63
REMARK 465 TRP F 64
REMARK 465 GLN F 65
REMARK 465 GLU F 66
REMARK 465 SER F 67
REMARK 465 GLU F 68
REMARK 465 GLU F 69
REMARK 465 ASN F 70
REMARK 465 HIS F 290
REMARK 465 HIS F 291
REMARK 465 HIS F 292
REMARK 465 HIS F 293
REMARK 465 HIS F 294
REMARK 465 HIS F 295
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 ALA A 130 34.76 38.44
REMARK 500 PRO A 134 41.94 -87.58
REMARK 500 ASN A 179 -157.46 -142.46
REMARK 500 PRO B 134 49.01 -96.77
REMARK 500 LYS B 163 -51.51 -129.23
REMARK 500 ASN B 179 -159.76 -150.19
REMARK 500 PRO C 134 40.95 -88.37
REMARK 500 LYS C 163 -56.55 -130.58
REMARK 500 ALA D 130 27.73 48.55
REMARK 500 PRO D 134 38.25 -87.16
REMARK 500 LYS D 163 -49.51 -141.29
REMARK 500 PRO E 134 41.23 -84.43
REMARK 500 LYS E 163 -39.64 -142.92
REMARK 500 ASN E 179 -157.53 -144.87
REMARK 500 ASN E 204 4.62 -69.09
REMARK 500 ASN E 242 17.44 59.84
REMARK 500 PRO F 134 41.49 -83.58
REMARK 500 LYS F 163 -50.59 -140.18
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 FMN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue YOF A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue YOF B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue YOF C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue YOF D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue YOF E 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN F 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue YOF F 502
DBREF 5YAK A 32 289 UNP Q6PHW0 IYD1_HUMAN 32 289
DBREF 5YAK B 32 289 UNP Q6PHW0 IYD1_HUMAN 32 289
DBREF 5YAK C 32 289 UNP Q6PHW0 IYD1_HUMAN 32 289
DBREF 5YAK D 32 289 UNP Q6PHW0 IYD1_HUMAN 32 289
DBREF 5YAK E 32 289 UNP Q6PHW0 IYD1_HUMAN 32 289
DBREF 5YAK F 32 289 UNP Q6PHW0 IYD1_HUMAN 32 289
SEQADV 5YAK ALA A 239 UNP Q6PHW0 THR 239 ENGINEERED MUTATION
SEQADV 5YAK HIS A 290 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS A 291 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS A 292 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS A 293 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS A 294 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS A 295 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK ALA B 239 UNP Q6PHW0 THR 239 ENGINEERED MUTATION
SEQADV 5YAK HIS B 290 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS B 291 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS B 292 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS B 293 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS B 294 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS B 295 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK ALA C 239 UNP Q6PHW0 THR 239 ENGINEERED MUTATION
SEQADV 5YAK HIS C 290 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS C 291 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS C 292 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS C 293 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS C 294 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS C 295 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK ALA D 239 UNP Q6PHW0 THR 239 ENGINEERED MUTATION
SEQADV 5YAK HIS D 290 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS D 291 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS D 292 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS D 293 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS D 294 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS D 295 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK ALA E 239 UNP Q6PHW0 THR 239 ENGINEERED MUTATION
SEQADV 5YAK HIS E 290 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS E 291 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS E 292 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS E 293 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS E 294 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS E 295 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK ALA F 239 UNP Q6PHW0 THR 239 ENGINEERED MUTATION
SEQADV 5YAK HIS F 290 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS F 291 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS F 292 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS F 293 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS F 294 UNP Q6PHW0 EXPRESSION TAG
SEQADV 5YAK HIS F 295 UNP Q6PHW0 EXPRESSION TAG
SEQRES 1 A 264 GLY GLU PRO ARG THR ARG ALA GLU ALA ARG PRO TRP VAL
SEQRES 2 A 264 ASP GLU ASP LEU LYS ASP SER SER ASP LEU HIS GLN ALA
SEQRES 3 A 264 GLU GLU ASP ALA ASP GLU TRP GLN GLU SER GLU GLU ASN
SEQRES 4 A 264 VAL GLU HIS ILE PRO PHE SER HIS ASN HIS TYR PRO GLU
SEQRES 5 A 264 LYS GLU MET VAL LYS ARG SER GLN GLU PHE TYR GLU LEU
SEQRES 6 A 264 LEU ASN LYS ARG ARG SER VAL ARG PHE ILE SER ASN GLU
SEQRES 7 A 264 GLN VAL PRO MET GLU VAL ILE ASP ASN VAL ILE ARG THR
SEQRES 8 A 264 ALA GLY THR ALA PRO SER GLY ALA HIS THR GLU PRO TRP
SEQRES 9 A 264 THR PHE VAL VAL VAL LYS ASP PRO ASP VAL LYS HIS LYS
SEQRES 10 A 264 ILE ARG LYS ILE ILE GLU GLU GLU GLU GLU ILE ASN TYR
SEQRES 11 A 264 MET LYS ARG MET GLY HIS ARG TRP VAL THR ASP LEU LYS
SEQRES 12 A 264 LYS LEU ARG THR ASN TRP ILE LYS GLU TYR LEU ASP THR
SEQRES 13 A 264 ALA PRO ILE LEU ILE LEU ILE PHE LYS GLN VAL HIS GLY
SEQRES 14 A 264 PHE ALA ALA ASN GLY LYS LYS LYS VAL HIS TYR TYR ASN
SEQRES 15 A 264 GLU ILE SER VAL SER ILE ALA CYS GLY ILE LEU LEU ALA
SEQRES 16 A 264 ALA LEU GLN ASN ALA GLY LEU VAL THR VAL THR THR ALA
SEQRES 17 A 264 PRO LEU ASN CYS GLY PRO ARG LEU ARG VAL LEU LEU GLY
SEQRES 18 A 264 ARG PRO ALA HIS GLU LYS LEU LEU MET LEU LEU PRO VAL
SEQRES 19 A 264 GLY TYR PRO SER LYS GLU ALA THR VAL PRO ASP LEU LYS
SEQRES 20 A 264 ARG LYS PRO LEU ASP GLN ILE MET VAL THR VAL HIS HIS
SEQRES 21 A 264 HIS HIS HIS HIS
SEQRES 1 B 264 GLY GLU PRO ARG THR ARG ALA GLU ALA ARG PRO TRP VAL
SEQRES 2 B 264 ASP GLU ASP LEU LYS ASP SER SER ASP LEU HIS GLN ALA
SEQRES 3 B 264 GLU GLU ASP ALA ASP GLU TRP GLN GLU SER GLU GLU ASN
SEQRES 4 B 264 VAL GLU HIS ILE PRO PHE SER HIS ASN HIS TYR PRO GLU
SEQRES 5 B 264 LYS GLU MET VAL LYS ARG SER GLN GLU PHE TYR GLU LEU
SEQRES 6 B 264 LEU ASN LYS ARG ARG SER VAL ARG PHE ILE SER ASN GLU
SEQRES 7 B 264 GLN VAL PRO MET GLU VAL ILE ASP ASN VAL ILE ARG THR
SEQRES 8 B 264 ALA GLY THR ALA PRO SER GLY ALA HIS THR GLU PRO TRP
SEQRES 9 B 264 THR PHE VAL VAL VAL LYS ASP PRO ASP VAL LYS HIS LYS
SEQRES 10 B 264 ILE ARG LYS ILE ILE GLU GLU GLU GLU GLU ILE ASN TYR
SEQRES 11 B 264 MET LYS ARG MET GLY HIS ARG TRP VAL THR ASP LEU LYS
SEQRES 12 B 264 LYS LEU ARG THR ASN TRP ILE LYS GLU TYR LEU ASP THR
SEQRES 13 B 264 ALA PRO ILE LEU ILE LEU ILE PHE LYS GLN VAL HIS GLY
SEQRES 14 B 264 PHE ALA ALA ASN GLY LYS LYS LYS VAL HIS TYR TYR ASN
SEQRES 15 B 264 GLU ILE SER VAL SER ILE ALA CYS GLY ILE LEU LEU ALA
SEQRES 16 B 264 ALA LEU GLN ASN ALA GLY LEU VAL THR VAL THR THR ALA
SEQRES 17 B 264 PRO LEU ASN CYS GLY PRO ARG LEU ARG VAL LEU LEU GLY
SEQRES 18 B 264 ARG PRO ALA HIS GLU LYS LEU LEU MET LEU LEU PRO VAL
SEQRES 19 B 264 GLY TYR PRO SER LYS GLU ALA THR VAL PRO ASP LEU LYS
SEQRES 20 B 264 ARG LYS PRO LEU ASP GLN ILE MET VAL THR VAL HIS HIS
SEQRES 21 B 264 HIS HIS HIS HIS
SEQRES 1 C 264 GLY GLU PRO ARG THR ARG ALA GLU ALA ARG PRO TRP VAL
SEQRES 2 C 264 ASP GLU ASP LEU LYS ASP SER SER ASP LEU HIS GLN ALA
SEQRES 3 C 264 GLU GLU ASP ALA ASP GLU TRP GLN GLU SER GLU GLU ASN
SEQRES 4 C 264 VAL GLU HIS ILE PRO PHE SER HIS ASN HIS TYR PRO GLU
SEQRES 5 C 264 LYS GLU MET VAL LYS ARG SER GLN GLU PHE TYR GLU LEU
SEQRES 6 C 264 LEU ASN LYS ARG ARG SER VAL ARG PHE ILE SER ASN GLU
SEQRES 7 C 264 GLN VAL PRO MET GLU VAL ILE ASP ASN VAL ILE ARG THR
SEQRES 8 C 264 ALA GLY THR ALA PRO SER GLY ALA HIS THR GLU PRO TRP
SEQRES 9 C 264 THR PHE VAL VAL VAL LYS ASP PRO ASP VAL LYS HIS LYS
SEQRES 10 C 264 ILE ARG LYS ILE ILE GLU GLU GLU GLU GLU ILE ASN TYR
SEQRES 11 C 264 MET LYS ARG MET GLY HIS ARG TRP VAL THR ASP LEU LYS
SEQRES 12 C 264 LYS LEU ARG THR ASN TRP ILE LYS GLU TYR LEU ASP THR
SEQRES 13 C 264 ALA PRO ILE LEU ILE LEU ILE PHE LYS GLN VAL HIS GLY
SEQRES 14 C 264 PHE ALA ALA ASN GLY LYS LYS LYS VAL HIS TYR TYR ASN
SEQRES 15 C 264 GLU ILE SER VAL SER ILE ALA CYS GLY ILE LEU LEU ALA
SEQRES 16 C 264 ALA LEU GLN ASN ALA GLY LEU VAL THR VAL THR THR ALA
SEQRES 17 C 264 PRO LEU ASN CYS GLY PRO ARG LEU ARG VAL LEU LEU GLY
SEQRES 18 C 264 ARG PRO ALA HIS GLU LYS LEU LEU MET LEU LEU PRO VAL
SEQRES 19 C 264 GLY TYR PRO SER LYS GLU ALA THR VAL PRO ASP LEU LYS
SEQRES 20 C 264 ARG LYS PRO LEU ASP GLN ILE MET VAL THR VAL HIS HIS
SEQRES 21 C 264 HIS HIS HIS HIS
SEQRES 1 D 264 GLY GLU PRO ARG THR ARG ALA GLU ALA ARG PRO TRP VAL
SEQRES 2 D 264 ASP GLU ASP LEU LYS ASP SER SER ASP LEU HIS GLN ALA
SEQRES 3 D 264 GLU GLU ASP ALA ASP GLU TRP GLN GLU SER GLU GLU ASN
SEQRES 4 D 264 VAL GLU HIS ILE PRO PHE SER HIS ASN HIS TYR PRO GLU
SEQRES 5 D 264 LYS GLU MET VAL LYS ARG SER GLN GLU PHE TYR GLU LEU
SEQRES 6 D 264 LEU ASN LYS ARG ARG SER VAL ARG PHE ILE SER ASN GLU
SEQRES 7 D 264 GLN VAL PRO MET GLU VAL ILE ASP ASN VAL ILE ARG THR
SEQRES 8 D 264 ALA GLY THR ALA PRO SER GLY ALA HIS THR GLU PRO TRP
SEQRES 9 D 264 THR PHE VAL VAL VAL LYS ASP PRO ASP VAL LYS HIS LYS
SEQRES 10 D 264 ILE ARG LYS ILE ILE GLU GLU GLU GLU GLU ILE ASN TYR
SEQRES 11 D 264 MET LYS ARG MET GLY HIS ARG TRP VAL THR ASP LEU LYS
SEQRES 12 D 264 LYS LEU ARG THR ASN TRP ILE LYS GLU TYR LEU ASP THR
SEQRES 13 D 264 ALA PRO ILE LEU ILE LEU ILE PHE LYS GLN VAL HIS GLY
SEQRES 14 D 264 PHE ALA ALA ASN GLY LYS LYS LYS VAL HIS TYR TYR ASN
SEQRES 15 D 264 GLU ILE SER VAL SER ILE ALA CYS GLY ILE LEU LEU ALA
SEQRES 16 D 264 ALA LEU GLN ASN ALA GLY LEU VAL THR VAL THR THR ALA
SEQRES 17 D 264 PRO LEU ASN CYS GLY PRO ARG LEU ARG VAL LEU LEU GLY
SEQRES 18 D 264 ARG PRO ALA HIS GLU LYS LEU LEU MET LEU LEU PRO VAL
SEQRES 19 D 264 GLY TYR PRO SER LYS GLU ALA THR VAL PRO ASP LEU LYS
SEQRES 20 D 264 ARG LYS PRO LEU ASP GLN ILE MET VAL THR VAL HIS HIS
SEQRES 21 D 264 HIS HIS HIS HIS
SEQRES 1 E 264 GLY GLU PRO ARG THR ARG ALA GLU ALA ARG PRO TRP VAL
SEQRES 2 E 264 ASP GLU ASP LEU LYS ASP SER SER ASP LEU HIS GLN ALA
SEQRES 3 E 264 GLU GLU ASP ALA ASP GLU TRP GLN GLU SER GLU GLU ASN
SEQRES 4 E 264 VAL GLU HIS ILE PRO PHE SER HIS ASN HIS TYR PRO GLU
SEQRES 5 E 264 LYS GLU MET VAL LYS ARG SER GLN GLU PHE TYR GLU LEU
SEQRES 6 E 264 LEU ASN LYS ARG ARG SER VAL ARG PHE ILE SER ASN GLU
SEQRES 7 E 264 GLN VAL PRO MET GLU VAL ILE ASP ASN VAL ILE ARG THR
SEQRES 8 E 264 ALA GLY THR ALA PRO SER GLY ALA HIS THR GLU PRO TRP
SEQRES 9 E 264 THR PHE VAL VAL VAL LYS ASP PRO ASP VAL LYS HIS LYS
SEQRES 10 E 264 ILE ARG LYS ILE ILE GLU GLU GLU GLU GLU ILE ASN TYR
SEQRES 11 E 264 MET LYS ARG MET GLY HIS ARG TRP VAL THR ASP LEU LYS
SEQRES 12 E 264 LYS LEU ARG THR ASN TRP ILE LYS GLU TYR LEU ASP THR
SEQRES 13 E 264 ALA PRO ILE LEU ILE LEU ILE PHE LYS GLN VAL HIS GLY
SEQRES 14 E 264 PHE ALA ALA ASN GLY LYS LYS LYS VAL HIS TYR TYR ASN
SEQRES 15 E 264 GLU ILE SER VAL SER ILE ALA CYS GLY ILE LEU LEU ALA
SEQRES 16 E 264 ALA LEU GLN ASN ALA GLY LEU VAL THR VAL THR THR ALA
SEQRES 17 E 264 PRO LEU ASN CYS GLY PRO ARG LEU ARG VAL LEU LEU GLY
SEQRES 18 E 264 ARG PRO ALA HIS GLU LYS LEU LEU MET LEU LEU PRO VAL
SEQRES 19 E 264 GLY TYR PRO SER LYS GLU ALA THR VAL PRO ASP LEU LYS
SEQRES 20 E 264 ARG LYS PRO LEU ASP GLN ILE MET VAL THR VAL HIS HIS
SEQRES 21 E 264 HIS HIS HIS HIS
SEQRES 1 F 264 GLY GLU PRO ARG THR ARG ALA GLU ALA ARG PRO TRP VAL
SEQRES 2 F 264 ASP GLU ASP LEU LYS ASP SER SER ASP LEU HIS GLN ALA
SEQRES 3 F 264 GLU GLU ASP ALA ASP GLU TRP GLN GLU SER GLU GLU ASN
SEQRES 4 F 264 VAL GLU HIS ILE PRO PHE SER HIS ASN HIS TYR PRO GLU
SEQRES 5 F 264 LYS GLU MET VAL LYS ARG SER GLN GLU PHE TYR GLU LEU
SEQRES 6 F 264 LEU ASN LYS ARG ARG SER VAL ARG PHE ILE SER ASN GLU
SEQRES 7 F 264 GLN VAL PRO MET GLU VAL ILE ASP ASN VAL ILE ARG THR
SEQRES 8 F 264 ALA GLY THR ALA PRO SER GLY ALA HIS THR GLU PRO TRP
SEQRES 9 F 264 THR PHE VAL VAL VAL LYS ASP PRO ASP VAL LYS HIS LYS
SEQRES 10 F 264 ILE ARG LYS ILE ILE GLU GLU GLU GLU GLU ILE ASN TYR
SEQRES 11 F 264 MET LYS ARG MET GLY HIS ARG TRP VAL THR ASP LEU LYS
SEQRES 12 F 264 LYS LEU ARG THR ASN TRP ILE LYS GLU TYR LEU ASP THR
SEQRES 13 F 264 ALA PRO ILE LEU ILE LEU ILE PHE LYS GLN VAL HIS GLY
SEQRES 14 F 264 PHE ALA ALA ASN GLY LYS LYS LYS VAL HIS TYR TYR ASN
SEQRES 15 F 264 GLU ILE SER VAL SER ILE ALA CYS GLY ILE LEU LEU ALA
SEQRES 16 F 264 ALA LEU GLN ASN ALA GLY LEU VAL THR VAL THR THR ALA
SEQRES 17 F 264 PRO LEU ASN CYS GLY PRO ARG LEU ARG VAL LEU LEU GLY
SEQRES 18 F 264 ARG PRO ALA HIS GLU LYS LEU LEU MET LEU LEU PRO VAL
SEQRES 19 F 264 GLY TYR PRO SER LYS GLU ALA THR VAL PRO ASP LEU LYS
SEQRES 20 F 264 ARG LYS PRO LEU ASP GLN ILE MET VAL THR VAL HIS HIS
SEQRES 21 F 264 HIS HIS HIS HIS
HET FMN A 501 31
HET YOF A 502 14
HET FMN B 501 31
HET YOF B 502 14
HET FMN C 501 31
HET YOF C 502 14
HET FMN D 501 31
HET YOF D 502 14
HET FMN E 501 31
HET YOF E 502 14
HET FMN F 501 31
HET YOF F 502 14
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETNAM YOF 3-FLUOROTYROSINE
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 7 FMN 6(C17 H21 N4 O9 P)
FORMUL 8 YOF 6(C9 H10 F N O3)
FORMUL 19 HOH *297(H2 O)
HELIX 1 AA1 PRO A 82 LYS A 99 1 18
HELIX 2 AA2 PRO A 112 GLY A 124 1 13
HELIX 3 AA3 SER A 128 THR A 132 5 5
HELIX 4 AA4 ASP A 142 LYS A 163 1 22
HELIX 5 AA5 GLY A 166 LYS A 174 1 9
HELIX 6 AA6 LYS A 175 ARG A 177 5 3
HELIX 7 AA7 GLU A 183 ALA A 188 1 6
HELIX 8 AA8 TYR A 212 ALA A 231 1 20
HELIX 9 AA9 CYS A 243 LEU A 251 1 9
HELIX 10 AB1 PRO A 281 GLN A 284 5 4
HELIX 11 AB2 PRO B 82 LYS B 99 1 18
HELIX 12 AB3 PRO B 112 GLY B 124 1 13
HELIX 13 AB4 SER B 128 THR B 132 5 5
HELIX 14 AB5 ASP B 142 LYS B 163 1 22
HELIX 15 AB6 GLY B 166 LEU B 173 1 8
HELIX 16 AB7 LYS B 174 ARG B 177 5 4
HELIX 17 AB8 GLU B 183 ALA B 188 1 6
HELIX 18 AB9 TYR B 212 ALA B 231 1 20
HELIX 19 AC1 CYS B 243 LEU B 251 1 9
HELIX 20 AC2 PRO B 281 GLN B 284 5 4
HELIX 21 AC3 PRO C 82 LYS C 99 1 18
HELIX 22 AC4 PRO C 112 GLY C 124 1 13
HELIX 23 AC5 SER C 128 THR C 132 5 5
HELIX 24 AC6 ASP C 142 LYS C 163 1 22
HELIX 25 AC7 GLY C 166 LEU C 173 1 8
HELIX 26 AC8 LYS C 174 ARG C 177 5 4
HELIX 27 AC9 GLU C 183 ALA C 188 1 6
HELIX 28 AD1 TYR C 212 GLY C 232 1 21
HELIX 29 AD2 CYS C 243 GLY C 252 1 10
HELIX 30 AD3 PRO C 281 ILE C 285 1 5
HELIX 31 AD4 PRO D 82 LYS D 99 1 18
HELIX 32 AD5 PRO D 112 GLY D 124 1 13
HELIX 33 AD6 ASP D 142 LYS D 163 1 22
HELIX 34 AD7 GLY D 166 LEU D 173 1 8
HELIX 35 AD8 LYS D 174 ARG D 177 5 4
HELIX 36 AD9 GLU D 183 ALA D 188 1 6
HELIX 37 AE1 TYR D 212 ALA D 231 1 20
HELIX 38 AE2 CYS D 243 GLY D 252 1 10
HELIX 39 AE3 PRO D 281 GLN D 284 5 4
HELIX 40 AE4 PRO E 82 LYS E 99 1 18
HELIX 41 AE5 PRO E 112 GLY E 124 1 13
HELIX 42 AE6 SER E 128 THR E 132 5 5
HELIX 43 AE7 ASP E 142 LYS E 163 1 22
HELIX 44 AE8 GLY E 166 LEU E 173 1 8
HELIX 45 AE9 LYS E 174 ARG E 177 5 4
HELIX 46 AF1 GLU E 183 ALA E 188 1 6
HELIX 47 AF2 TYR E 212 GLY E 232 1 21
HELIX 48 AF3 CYS E 243 LEU E 251 1 9
HELIX 49 AF4 PRO E 281 ILE E 285 1 5
HELIX 50 AF5 PRO F 82 LYS F 99 1 18
HELIX 51 AF6 PRO F 112 GLY F 124 1 13
HELIX 52 AF7 SER F 128 THR F 132 5 5
HELIX 53 AF8 ASP F 142 LYS F 163 1 22
HELIX 54 AF9 GLY F 166 LEU F 173 1 8
HELIX 55 AG1 LYS F 174 ARG F 177 5 4
HELIX 56 AG2 GLU F 183 ALA F 188 1 6
HELIX 57 AG3 TYR F 212 ASN F 230 1 19
HELIX 58 AG4 CYS F 243 LEU F 251 1 9
HELIX 59 AG5 PRO F 281 GLN F 284 5 4
SHEET 1 AA1 2 HIS A 73 PRO A 75 0
SHEET 2 AA1 2 THR F 273 PRO F 275 -1 O VAL F 274 N ILE A 74
SHEET 1 AA2 5 VAL A 234 THR A 235 0
SHEET 2 AA2 5 GLU A 257 GLY A 266 -1 O GLY A 266 N VAL A 234
SHEET 3 AA2 5 ILE A 190 GLN A 197 -1 N ILE A 194 O MET A 261
SHEET 4 AA2 5 TRP A 135 VAL A 140 -1 N VAL A 138 O LEU A 193
SHEET 5 AA2 5 MET F 286 VAL F 289 1 O VAL F 287 N VAL A 139
SHEET 1 AA3 2 GLY A 200 PHE A 201 0
SHEET 2 AA3 2 LYS A 207 LYS A 208 -1 O LYS A 208 N GLY A 200
SHEET 1 AA4 2 THR A 273 PRO A 275 0
SHEET 2 AA4 2 HIS F 73 PRO F 75 -1 O ILE F 74 N VAL A 274
SHEET 1 AA5 4 MET A 286 VAL A 287 0
SHEET 2 AA5 4 TRP F 135 VAL F 140 1 O VAL F 139 N VAL A 287
SHEET 3 AA5 4 ILE F 190 GLN F 197 -1 O LEU F 193 N VAL F 138
SHEET 4 AA5 4 GLU F 257 VAL F 265 -1 O VAL F 265 N ILE F 190
SHEET 1 AA6 2 HIS B 73 PRO B 75 0
SHEET 2 AA6 2 THR C 273 PRO C 275 -1 O VAL C 274 N ILE B 74
SHEET 1 AA7 5 VAL B 234 THR B 235 0
SHEET 2 AA7 5 GLU B 257 GLY B 266 -1 O GLY B 266 N VAL B 234
SHEET 3 AA7 5 ILE B 190 GLN B 197 -1 N ILE B 190 O VAL B 265
SHEET 4 AA7 5 TRP B 135 VAL B 140 -1 N VAL B 140 O LEU B 191
SHEET 5 AA7 5 MET C 286 VAL C 289 1 O VAL C 289 N VAL B 139
SHEET 1 AA8 2 HIS B 199 PHE B 201 0
SHEET 2 AA8 2 LYS B 207 VAL B 209 -1 O LYS B 208 N GLY B 200
SHEET 1 AA9 2 THR B 273 PRO B 275 0
SHEET 2 AA9 2 HIS C 73 PRO C 75 -1 O ILE C 74 N VAL B 274
SHEET 1 AB1 4 MET B 286 VAL B 289 0
SHEET 2 AB1 4 TRP C 135 VAL C 140 1 O VAL C 139 N VAL B 287
SHEET 3 AB1 4 ILE C 190 GLN C 197 -1 O LEU C 193 N VAL C 138
SHEET 4 AB1 4 GLU C 257 VAL C 265 -1 O VAL C 265 N ILE C 190
SHEET 1 AB2 2 SER C 77 ASN C 79 0
SHEET 2 AB2 2 SER E 77 ASN E 79 -1 O HIS E 78 N HIS C 78
SHEET 1 AB3 2 HIS C 199 PHE C 201 0
SHEET 2 AB3 2 LYS C 207 VAL C 209 -1 O LYS C 208 N GLY C 200
SHEET 1 AB4 2 HIS D 73 PRO D 75 0
SHEET 2 AB4 2 THR E 273 PRO E 275 -1 O VAL E 274 N ILE D 74
SHEET 1 AB5 4 GLU D 257 VAL D 265 0
SHEET 2 AB5 4 ILE D 190 GLN D 197 -1 N ILE D 190 O VAL D 265
SHEET 3 AB5 4 TRP D 135 VAL D 140 -1 N THR D 136 O PHE D 195
SHEET 4 AB5 4 MET E 286 VAL E 289 1 O VAL E 289 N VAL D 139
SHEET 1 AB6 2 THR D 273 PRO D 275 0
SHEET 2 AB6 2 HIS E 73 PRO E 75 -1 O ILE E 74 N VAL D 274
SHEET 1 AB7 5 MET D 286 VAL D 289 0
SHEET 2 AB7 5 TRP E 135 VAL E 140 1 O VAL E 139 N VAL D 287
SHEET 3 AB7 5 ILE E 190 GLN E 197 -1 O LEU E 193 N VAL E 138
SHEET 4 AB7 5 GLU E 257 GLY E 266 -1 O MET E 261 N ILE E 194
SHEET 5 AB7 5 VAL E 234 THR E 235 -1 N VAL E 234 O GLY E 266
SHEET 1 AB8 2 HIS E 199 PHE E 201 0
SHEET 2 AB8 2 LYS E 207 VAL E 209 -1 O LYS E 208 N GLY E 200
SHEET 1 AB9 2 HIS F 199 PHE F 201 0
SHEET 2 AB9 2 LYS F 207 VAL F 209 -1 O LYS F 208 N GLY F 200
SITE 1 AC1 22 ARG A 100 ARG A 101 SER A 102 ARG A 104
SITE 2 AC1 22 LEU A 176 THR A 178 THR A 237 THR A 238
SITE 3 AC1 22 ALA A 239 ARG A 279 YOF A 502 HOH A 602
SITE 4 AC1 22 HOH A 605 HOH A 619 HOH A 620 HOH A 624
SITE 5 AC1 22 PRO F 127 SER F 128 GLY F 129 HIS F 131
SITE 6 AC1 22 TYR F 212 SER F 216
SITE 1 AC2 14 GLU A 157 TYR A 161 TRP A 169 LEU A 173
SITE 2 AC2 14 THR A 178 ASN A 179 LYS A 182 ALA A 239
SITE 3 AC2 14 FMN A 501 HOH A 626 GLY F 129 ALA F 130
SITE 4 AC2 14 TYR F 212 HOH F 627
SITE 1 AC3 23 ARG B 100 ARG B 101 SER B 102 ARG B 104
SITE 2 AC3 23 LEU B 176 THR B 178 VAL B 236 THR B 237
SITE 3 AC3 23 THR B 238 ALA B 239 ARG B 279 YOF B 502
SITE 4 AC3 23 HOH B 603 HOH B 609 HOH B 615 HOH B 624
SITE 5 AC3 23 PRO C 127 SER C 128 GLY C 129 HIS C 131
SITE 6 AC3 23 TYR C 212 SER C 216 HOH C 608
SITE 1 AC4 12 GLU B 157 TYR B 161 LEU B 173 LEU B 176
SITE 2 AC4 12 LYS B 182 ALA B 239 FMN B 501 HOH B 612
SITE 3 AC4 12 GLY C 129 ALA C 130 TYR C 212 HOH C 619
SITE 1 AC5 24 PRO B 127 SER B 128 GLY B 129 HIS B 131
SITE 2 AC5 24 TYR B 212 ILE B 215 SER B 216 HOH B 631
SITE 3 AC5 24 ARG C 100 ARG C 101 SER C 102 ARG C 104
SITE 4 AC5 24 LEU C 176 THR C 178 VAL C 236 THR C 237
SITE 5 AC5 24 ALA C 239 LEU C 277 ARG C 279 YOF C 502
SITE 6 AC5 24 HOH C 603 HOH C 610 HOH C 629 HOH C 634
SITE 1 AC6 11 GLY B 129 ALA B 130 HOH B 630 GLU C 157
SITE 2 AC6 11 TYR C 161 LEU C 173 THR C 178 LYS C 182
SITE 3 AC6 11 ALA C 239 FMN C 501 HOH C 640
SITE 1 AC7 23 ARG D 100 ARG D 101 SER D 102 ARG D 104
SITE 2 AC7 23 LEU D 176 THR D 178 THR D 237 THR D 238
SITE 3 AC7 23 ALA D 239 ARG D 279 YOF D 502 HOH D 603
SITE 4 AC7 23 HOH D 606 HOH D 621 HOH D 624 PRO E 127
SITE 5 AC7 23 SER E 128 GLY E 129 HIS E 131 TYR E 212
SITE 6 AC7 23 ILE E 215 SER E 216 HOH E 628
SITE 1 AC8 11 GLU D 157 TYR D 161 LEU D 173 LYS D 182
SITE 2 AC8 11 ALA D 239 FMN D 501 HOH D 618 GLY E 129
SITE 3 AC8 11 ALA E 130 TYR E 212 HOH E 602
SITE 1 AC9 22 PRO D 127 SER D 128 GLY D 129 HIS D 131
SITE 2 AC9 22 TYR D 212 SER D 216 HOH D 619 ARG E 100
SITE 3 AC9 22 ARG E 101 SER E 102 ARG E 104 LEU E 176
SITE 4 AC9 22 VAL E 236 THR E 237 THR E 238 ALA E 239
SITE 5 AC9 22 ARG E 279 YOF E 502 HOH E 609 HOH E 611
SITE 6 AC9 22 HOH E 621 HOH E 626
SITE 1 AD1 10 GLY D 129 ALA D 130 HOH D 631 GLU E 157
SITE 2 AD1 10 TYR E 161 LEU E 173 LYS E 182 ALA E 239
SITE 3 AD1 10 FMN E 501 HOH E 622
SITE 1 AD2 23 PRO A 127 SER A 128 GLY A 129 HIS A 131
SITE 2 AD2 23 TYR A 212 ILE A 215 SER A 216 ARG F 100
SITE 3 AD2 23 ARG F 101 SER F 102 ARG F 104 LEU F 176
SITE 4 AD2 23 THR F 178 VAL F 236 THR F 237 THR F 238
SITE 5 AD2 23 ALA F 239 ARG F 279 YOF F 502 HOH F 609
SITE 6 AD2 23 HOH F 610 HOH F 621 HOH F 636
SITE 1 AD3 11 GLY A 129 ALA A 130 HOH A 628 GLU F 157
SITE 2 AD3 11 TYR F 161 LEU F 173 ASN F 179 LYS F 182
SITE 3 AD3 11 ALA F 239 FMN F 501 HOH F 605
CRYST1 105.079 105.079 300.202 90.00 90.00 120.00 P 61 36
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 0.009517 0.005494 0.000000 0.00000
SCALE2 0.000000 0.010989 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003331 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
