HEADER OXIDOREDUCTASE 12-JUL-95 1FEB
TITLE UNLIGANDED CRITHIDIA FASCICULATA TRYPANOTHIONE REDUCTASE AT
TITLE 2 2.0 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPANOTHIONE REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.6.4.8;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: ORTHORHOMBIC CRYSTAL FORM, DIMER IN THE
COMPND 7 ASYMMETRIC UNIT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRITHIDIA FASCICULATA;
SOURCE 3 ORGANISM_TAXID: 5656;
SOURCE 4 GENE: TR1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: T7;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-TR1;
SOURCE 9 EXPRESSION_SYSTEM_GENE: TR1;
SOURCE 10 OTHER_DETAILS: SEE STRICKLAND, ET. AL. (1995) ACTA CRYST.
SOURCE 11 D51, 337-341
KEYWDS REDOX-ACTIVE CENTER, OXIDOREDUCTASE, FLAVOPROTEIN, FAD, NADP
EXPDTA X-RAY DIFFRACTION
AUTHOR C.STRICKLAND,P.KARPLUS
REVDAT 2 24-FEB-09 1FEB 1 VERSN
REVDAT 1 11-JAN-97 1FEB 0
JRNL AUTH C.L.STRICKLAND,P.A.KARPLUS
JRNL TITL CRITHIDIA FASCICULATA TRYPANOTHIONE REDUCTASE AT
JRNL TITL 2 1.70 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.STRICKLAND,R.PUCHALSKI,S.SAVVIDES,P.KARPLUS
REMARK 1 TITL OVEREXPRESSION OF CRITHIDIA FASCICULATA
REMARK 1 TITL 2 TRYPANOTHIONE REDUCTASE AND CRYSTALLIZATION USING
REMARK 1 TITL 3 A NOVEL GEOMETRY
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 51 337 1995
REMARK 1 REFN ISSN 0907-4449
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.BAILEY,A.FAIRLAMB,W.HUNTER
REMARK 1 TITL STRUCTURE OF TRYPANOTHIONE REDUCTASE FROM
REMARK 1 TITL 2 CRITHIDIA FASCICULATA AT 2.6 A RESOLUTION:
REMARK 1 TITL 3 ENZYME-NADP INTERACTIONS OF 2.8 A RESOLUTION
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.B V. 50 139 1994
REMARK 1 REFN ISSN 0108-7681
REMARK 1 REFERENCE 3
REMARK 1 AUTH C.B.LANTWIN,I.SCHLICHTING,W.KABSCH,E.F.PAI,
REMARK 1 AUTH 2 R.L.KRAUTH-SIEGEL
REMARK 1 TITL THE STRUCTURE OF TRYPANOSOMA CRUZI TRYPANOTHIONE
REMARK 1 TITL 2 REDUCTASE IN THE OXIDIZED AND NADPH REDUCED STATE
REMARK 1 REF PROTEINS V. 18 161 1994
REMARK 1 REFN ISSN 0887-3585
REMARK 1 REFERENCE 4
REMARK 1 AUTH S.BAILEY,K.SMITH,A.H.FAIRLAMB,W.N.HUNTER
REMARK 1 TITL SUBSTRATE INTERACTIONS BETWEEN TRYPANOTHIONE
REMARK 1 TITL 2 REDUCTASE AND N1-GLUTATHIONYLSPERMIDINE DISULPHIDE
REMARK 1 TITL 3 AT 0.28-NM RESOLUTION
REMARK 1 REF EUR.J.BIOCHEM. V. 213 67 1993
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 5
REMARK 1 AUTH J.KURIYAN,X.P.KONG,T.S.KRISHNA,R.M.SWEET,
REMARK 1 AUTH 2 N.J.MURGOLO,H.FIELD,A.CERAMI,G.B.HENDERSON
REMARK 1 TITL X-RAY STRUCTURE OF TRYPANOTHIONE REDUCTASE FROM
REMARK 1 TITL 2 CRITHIDIA FASCICULATA AT 2.4-A RESOLUTION
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 88 8764 1991
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 64277
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7397
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 106
REMARK 3 SOLVENT ATOMS : 317
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.017
REMARK 3 BOND ANGLES (DEGREES) : 1.93
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FEB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAR-93
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : XUONG-HAMLIN MULTIWIRE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SDMS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69192
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.11900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 52.95000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 30.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 84.80000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 30.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.95000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 84.80000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 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 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 488
REMARK 465 ASN A 489
REMARK 465 LEU A 490
REMARK 465 LYS B 485
REMARK 465 ILE B 486
REMARK 465 ASP B 487
REMARK 465 SER B 488
REMARK 465 ASN B 489
REMARK 465 LEU B 490
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ALA A 208 CA ALA A 208 CB -0.127
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 397 C - N - CA ANGL. DEV. = -9.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 11 46.85 -100.32
REMARK 500 ALA A 23 -71.99 -71.45
REMARK 500 TYR A 44 -66.59 63.55
REMARK 500 ALA A 46 -167.00 -164.70
REMARK 500 VAL A 54 41.44 -148.75
REMARK 500 ASN A 131 6.03 -55.83
REMARK 500 ASP A 319 -19.33 -44.09
REMARK 500 ARG A 330 -89.90 -102.07
REMARK 500 SER A 432 -8.44 81.47
REMARK 500 ALA A 448 142.05 -38.46
REMARK 500 ARG B 2 118.98 83.96
REMARK 500 ALA B 11 51.60 -93.62
REMARK 500 TYR B 44 -71.65 71.56
REMARK 500 ASP B 130 -177.42 -170.22
REMARK 500 ASN B 131 5.14 -65.83
REMARK 500 ALA B 158 50.69 -145.29
REMARK 500 THR B 264 160.08 -37.97
REMARK 500 ALA B 283 46.20 -155.43
REMARK 500 ARG B 330 -82.50 -103.91
REMARK 500 ASN B 351 29.66 48.54
REMARK 500 PHE B 366 48.58 -78.28
REMARK 500 ASP B 386 -71.23 -30.88
REMARK 500 SER B 432 -7.07 80.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 376 0.08 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 499
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 499
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FEA RELATED DB: PDB
REMARK 900 RELATED ID: 1FEC RELATED DB: PDB
DBREF 1FEB A 1 490 UNP P39040 TYTR_CRIFA 2 491
DBREF 1FEB B 1 490 UNP P39040 TYTR_CRIFA 2 491
SEQADV 1FEB GLU A 296 UNP P39040 ASP 297 CONFLICT
SEQADV 1FEB GLU A 478 UNP P39040 GLN 479 CONFLICT
SEQADV 1FEB GLU B 296 UNP P39040 ASP 297 CONFLICT
SEQADV 1FEB GLU B 478 UNP P39040 GLN 479 CONFLICT
SEQRES 1 A 490 SER ARG ALA TYR ASP LEU VAL VAL ILE GLY ALA GLY SER
SEQRES 2 A 490 GLY GLY LEU GLU ALA GLY TRP ASN ALA ALA SER LEU HIS
SEQRES 3 A 490 LYS LYS ARG VAL ALA VAL ILE ASP LEU GLN LYS HIS HIS
SEQRES 4 A 490 GLY PRO PRO HIS TYR ALA ALA LEU GLY GLY THR CYS VAL
SEQRES 5 A 490 ASN VAL GLY CYS VAL PRO LYS LYS LEU MET VAL THR GLY
SEQRES 6 A 490 ALA ASN TYR MET ASP THR ILE ARG GLU SER ALA GLY PHE
SEQRES 7 A 490 GLY TRP GLU LEU ASP ARG GLU SER VAL ARG PRO ASN TRP
SEQRES 8 A 490 LYS ALA LEU ILE ALA ALA LYS ASN LYS ALA VAL SER GLY
SEQRES 9 A 490 ILE ASN ASP SER TYR GLU GLY MET PHE ALA ASP THR GLU
SEQRES 10 A 490 GLY LEU THR PHE HIS GLN GLY PHE GLY ALA LEU GLN ASP
SEQRES 11 A 490 ASN HIS THR VAL LEU VAL ARG GLU SER ALA ASP PRO ASN
SEQRES 12 A 490 SER ALA VAL LEU GLU THR LEU ASP THR GLU TYR ILE LEU
SEQRES 13 A 490 LEU ALA THR GLY SER TRP PRO GLN HIS LEU GLY ILE GLU
SEQRES 14 A 490 GLY ASP ASP LEU CYS ILE THR SER ASN GLU ALA PHE TYR
SEQRES 15 A 490 LEU ASP GLU ALA PRO LYS ARG ALA LEU CYS VAL GLY GLY
SEQRES 16 A 490 GLY TYR ILE SER ILE GLU PHE ALA GLY ILE PHE ASN ALA
SEQRES 17 A 490 TYR LYS ALA ARG GLY GLY GLN VAL ASP LEU ALA TYR ARG
SEQRES 18 A 490 GLY ASP MET ILE LEU ARG GLY PHE ASP SER GLU LEU ARG
SEQRES 19 A 490 LYS GLN LEU THR GLU GLN LEU ARG ALA ASN GLY ILE ASN
SEQRES 20 A 490 VAL ARG THR HIS GLU ASN PRO ALA LYS VAL THR LYS ASN
SEQRES 21 A 490 ALA ASP GLY THR ARG HIS VAL VAL PHE GLU SER GLY ALA
SEQRES 22 A 490 GLU ALA ASP TYR ASP VAL VAL MET LEU ALA ILE GLY ARG
SEQRES 23 A 490 VAL PRO ARG SER GLN THR LEU GLN LEU GLU LYS ALA GLY
SEQRES 24 A 490 VAL GLU VAL ALA LYS ASN GLY ALA ILE LYS VAL ASP ALA
SEQRES 25 A 490 TYR SER LYS THR ASN VAL ASP ASN ILE TYR ALA ILE GLY
SEQRES 26 A 490 ASP VAL THR ASP ARG VAL MET LEU THR PRO VAL ALA ILE
SEQRES 27 A 490 ASN GLU GLY ALA ALA PHE VAL ASP THR VAL PHE ALA ASN
SEQRES 28 A 490 LYS PRO ARG ALA THR ASP HIS THR LYS VAL ALA CYS ALA
SEQRES 29 A 490 VAL PHE SER ILE PRO PRO MET GLY VAL CYS GLY TYR VAL
SEQRES 30 A 490 GLU GLU ASP ALA ALA LYS LYS TYR ASP GLN VAL ALA VAL
SEQRES 31 A 490 TYR GLU SER SER PHE THR PRO LEU MET HIS ASN ILE SER
SEQRES 32 A 490 GLY SER THR TYR LYS LYS PHE MET VAL ARG ILE VAL THR
SEQRES 33 A 490 ASN HIS ALA ASP GLY GLU VAL LEU GLY VAL HIS MET LEU
SEQRES 34 A 490 GLY ASP SER SER PRO GLU ILE ILE GLN SER VAL ALA ILE
SEQRES 35 A 490 CYS LEU LYS MET GLY ALA LYS ILE SER ASP PHE TYR ASN
SEQRES 36 A 490 THR ILE GLY VAL HIS PRO THR SER ALA GLU GLU LEU CYS
SEQRES 37 A 490 SER MET ARG THR PRO ALA TYR PHE TYR GLU LYS GLY LYS
SEQRES 38 A 490 ARG VAL GLU LYS ILE ASP SER ASN LEU
SEQRES 1 B 490 SER ARG ALA TYR ASP LEU VAL VAL ILE GLY ALA GLY SER
SEQRES 2 B 490 GLY GLY LEU GLU ALA GLY TRP ASN ALA ALA SER LEU HIS
SEQRES 3 B 490 LYS LYS ARG VAL ALA VAL ILE ASP LEU GLN LYS HIS HIS
SEQRES 4 B 490 GLY PRO PRO HIS TYR ALA ALA LEU GLY GLY THR CYS VAL
SEQRES 5 B 490 ASN VAL GLY CYS VAL PRO LYS LYS LEU MET VAL THR GLY
SEQRES 6 B 490 ALA ASN TYR MET ASP THR ILE ARG GLU SER ALA GLY PHE
SEQRES 7 B 490 GLY TRP GLU LEU ASP ARG GLU SER VAL ARG PRO ASN TRP
SEQRES 8 B 490 LYS ALA LEU ILE ALA ALA LYS ASN LYS ALA VAL SER GLY
SEQRES 9 B 490 ILE ASN ASP SER TYR GLU GLY MET PHE ALA ASP THR GLU
SEQRES 10 B 490 GLY LEU THR PHE HIS GLN GLY PHE GLY ALA LEU GLN ASP
SEQRES 11 B 490 ASN HIS THR VAL LEU VAL ARG GLU SER ALA ASP PRO ASN
SEQRES 12 B 490 SER ALA VAL LEU GLU THR LEU ASP THR GLU TYR ILE LEU
SEQRES 13 B 490 LEU ALA THR GLY SER TRP PRO GLN HIS LEU GLY ILE GLU
SEQRES 14 B 490 GLY ASP ASP LEU CYS ILE THR SER ASN GLU ALA PHE TYR
SEQRES 15 B 490 LEU ASP GLU ALA PRO LYS ARG ALA LEU CYS VAL GLY GLY
SEQRES 16 B 490 GLY TYR ILE SER ILE GLU PHE ALA GLY ILE PHE ASN ALA
SEQRES 17 B 490 TYR LYS ALA ARG GLY GLY GLN VAL ASP LEU ALA TYR ARG
SEQRES 18 B 490 GLY ASP MET ILE LEU ARG GLY PHE ASP SER GLU LEU ARG
SEQRES 19 B 490 LYS GLN LEU THR GLU GLN LEU ARG ALA ASN GLY ILE ASN
SEQRES 20 B 490 VAL ARG THR HIS GLU ASN PRO ALA LYS VAL THR LYS ASN
SEQRES 21 B 490 ALA ASP GLY THR ARG HIS VAL VAL PHE GLU SER GLY ALA
SEQRES 22 B 490 GLU ALA ASP TYR ASP VAL VAL MET LEU ALA ILE GLY ARG
SEQRES 23 B 490 VAL PRO ARG SER GLN THR LEU GLN LEU GLU LYS ALA GLY
SEQRES 24 B 490 VAL GLU VAL ALA LYS ASN GLY ALA ILE LYS VAL ASP ALA
SEQRES 25 B 490 TYR SER LYS THR ASN VAL ASP ASN ILE TYR ALA ILE GLY
SEQRES 26 B 490 ASP VAL THR ASP ARG VAL MET LEU THR PRO VAL ALA ILE
SEQRES 27 B 490 ASN GLU GLY ALA ALA PHE VAL ASP THR VAL PHE ALA ASN
SEQRES 28 B 490 LYS PRO ARG ALA THR ASP HIS THR LYS VAL ALA CYS ALA
SEQRES 29 B 490 VAL PHE SER ILE PRO PRO MET GLY VAL CYS GLY TYR VAL
SEQRES 30 B 490 GLU GLU ASP ALA ALA LYS LYS TYR ASP GLN VAL ALA VAL
SEQRES 31 B 490 TYR GLU SER SER PHE THR PRO LEU MET HIS ASN ILE SER
SEQRES 32 B 490 GLY SER THR TYR LYS LYS PHE MET VAL ARG ILE VAL THR
SEQRES 33 B 490 ASN HIS ALA ASP GLY GLU VAL LEU GLY VAL HIS MET LEU
SEQRES 34 B 490 GLY ASP SER SER PRO GLU ILE ILE GLN SER VAL ALA ILE
SEQRES 35 B 490 CYS LEU LYS MET GLY ALA LYS ILE SER ASP PHE TYR ASN
SEQRES 36 B 490 THR ILE GLY VAL HIS PRO THR SER ALA GLU GLU LEU CYS
SEQRES 37 B 490 SER MET ARG THR PRO ALA TYR PHE TYR GLU LYS GLY LYS
SEQRES 38 B 490 ARG VAL GLU LYS ILE ASP SER ASN LEU
HET FAD A 499 53
HET FAD B 499 53
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 5 HOH *317(H2 O)
HELIX 1 1 SER A 13 HIS A 26 1 14
HELIX 2 2 GLY A 49 VAL A 54 1 6
HELIX 3 3 CYS A 56 PHE A 78 1 23
HELIX 4 4 ARG A 84 SER A 86 5 3
HELIX 5 5 TRP A 91 ALA A 114 1 24
HELIX 6 6 ASP A 171 LEU A 173 5 3
HELIX 7 7 SER A 177 TYR A 182 1 6
HELIX 8 8 TYR A 197 TYR A 209 1 13
HELIX 9 9 SER A 231 ALA A 243 1 13
HELIX 10 10 LEU A 295 ALA A 298 1 4
HELIX 11 11 GLY A 325 THR A 328 5 4
HELIX 12 12 THR A 334 PHE A 349 1 16
HELIX 13 13 GLU A 378 LYS A 384 1 7
HELIX 14 14 LEU A 398 ILE A 402 5 5
HELIX 15 15 SER A 433 LYS A 445 1 13
HELIX 16 16 ILE A 450 TYR A 454 1 5
HELIX 17 17 ALA A 464 CYS A 468 5 5
HELIX 18 18 SER B 13 LEU B 25 1 13
HELIX 19 19 GLY B 49 VAL B 54 1 6
HELIX 20 20 CYS B 56 ALA B 76 1 21
HELIX 21 21 ARG B 84 SER B 86 5 3
HELIX 22 22 TRP B 91 ALA B 114 1 24
HELIX 23 23 ASP B 171 LEU B 173 5 3
HELIX 24 24 SER B 177 TYR B 182 1 6
HELIX 25 25 TYR B 197 TYR B 209 1 13
HELIX 26 26 SER B 231 ASN B 244 1 14
HELIX 27 27 LEU B 295 ALA B 298 5 4
HELIX 28 28 ASP B 326 THR B 328 5 3
HELIX 29 29 THR B 334 PHE B 349 1 16
HELIX 30 30 GLU B 378 ALA B 382 1 5
HELIX 31 31 LEU B 398 SER B 403 1 6
HELIX 32 32 SER B 433 MET B 446 1 14
HELIX 33 33 ILE B 450 PHE B 453 1 4
HELIX 34 34 ALA B 464 CYS B 468 5 5
SHEET 1 A 5 ILE A 321 ALA A 323 0
SHEET 2 A 5 TYR A 154 LEU A 157 1 N ILE A 155 O TYR A 322
SHEET 3 A 5 LEU A 6 ILE A 9 1 N VAL A 7 O TYR A 154
SHEET 4 A 5 VAL A 30 ASP A 34 1 N ALA A 31 O LEU A 6
SHEET 5 A 5 LEU A 119 GLN A 123 1 N THR A 120 O VAL A 30
SHEET 1 B 2 SER A 161 PRO A 163 0
SHEET 2 B 2 ARG A 286 PRO A 288 -1 N VAL A 287 O TRP A 162
SHEET 1 C 4 VAL A 279 LEU A 282 0
SHEET 2 C 4 ARG A 189 VAL A 193 1 N LEU A 191 O VAL A 279
SHEET 3 C 4 GLN A 215 TYR A 220 1 N GLN A 215 O ALA A 190
SHEET 4 C 4 ASN A 247 THR A 250 1 N ASN A 247 O LEU A 218
SHEET 1 D 3 GLU A 274 TYR A 277 0
SHEET 2 D 3 ARG A 265 PHE A 269 -1 N VAL A 267 O ALA A 275
SHEET 3 D 3 PRO A 254 LYS A 259 -1 N THR A 258 O HIS A 266
SHEET 1 E 7 CYS A 363 VAL A 365 0
SHEET 2 E 7 MET A 371 GLY A 375 -1 N VAL A 373 O CYS A 363
SHEET 3 E 7 GLU A 422 LEU A 429 -1 N MET A 428 O GLY A 372
SHEET 4 E 7 LYS A 409 ASN A 417 -1 N ASN A 417 O GLU A 422
SHEET 5 E 7 GLN A 387 THR A 396 -1 N PHE A 395 O PHE A 410
SHEET 6 E 7 TYR A 475 GLU A 478 -1 N TYR A 477 O VAL A 388
SHEET 7 E 7 LYS A 481 VAL A 483 -1 N VAL A 483 O PHE A 476
SHEET 1 F 5 ILE B 321 ALA B 323 0
SHEET 2 F 5 TYR B 154 LEU B 157 1 N ILE B 155 O TYR B 322
SHEET 3 F 5 LEU B 6 ILE B 9 1 N VAL B 7 O TYR B 154
SHEET 4 F 5 VAL B 30 ASP B 34 1 N ALA B 31 O LEU B 6
SHEET 5 F 5 LEU B 119 GLN B 123 1 N THR B 120 O VAL B 30
SHEET 1 G 2 SER B 161 PRO B 163 0
SHEET 2 G 2 ARG B 286 PRO B 288 -1 N VAL B 287 O TRP B 162
SHEET 1 H 4 VAL B 279 LEU B 282 0
SHEET 2 H 4 ARG B 189 VAL B 193 1 N LEU B 191 O VAL B 279
SHEET 3 H 4 GLN B 215 TYR B 220 1 N GLN B 215 O ALA B 190
SHEET 4 H 4 ILE B 246 THR B 250 1 N ASN B 247 O VAL B 216
SHEET 1 I 3 GLU B 274 TYR B 277 0
SHEET 2 I 3 ARG B 265 PHE B 269 -1 N VAL B 267 O ALA B 275
SHEET 3 I 3 PRO B 254 LYS B 259 -1 N THR B 258 O HIS B 266
SHEET 1 J 7 CYS B 363 VAL B 365 0
SHEET 2 J 7 MET B 371 GLY B 375 -1 N VAL B 373 O CYS B 363
SHEET 3 J 7 GLU B 422 LEU B 429 -1 N MET B 428 O GLY B 372
SHEET 4 J 7 LYS B 409 ASN B 417 -1 N ASN B 417 O GLU B 422
SHEET 5 J 7 GLN B 387 THR B 396 -1 N PHE B 395 O PHE B 410
SHEET 6 J 7 TYR B 475 GLU B 478 -1 N TYR B 477 O VAL B 388
SHEET 7 J 7 LYS B 481 VAL B 483 -1 N VAL B 483 O PHE B 476
SHEET 1 K 3 PHE A 125 ASP A 130 0
SHEET 2 K 3 THR A 133 ARG A 137 -1 N ARG A 137 O PHE A 125
SHEET 3 K 3 VAL A 146 ASP A 151 -1 N LEU A 150 O VAL A 134
SHEET 1 L 3 PHE B 125 ASP B 130 0
SHEET 2 L 3 THR B 133 ARG B 137 -1 N ARG B 137 O PHE B 125
SHEET 3 L 3 VAL B 146 ASP B 151 -1 N LEU B 150 O VAL B 134
SSBOND 1 CYS A 51 CYS A 56 1555 1555 2.03
SSBOND 2 CYS B 51 CYS B 56 1555 1555 2.05
CISPEP 1 PRO A 41 PRO A 42 0 -10.25
CISPEP 2 ILE A 368 PRO A 369 0 -10.59
CISPEP 3 HIS A 460 PRO A 461 0 -14.43
CISPEP 4 PRO B 41 PRO B 42 0 7.01
CISPEP 5 ILE B 368 PRO B 369 0 7.57
CISPEP 6 HIS B 460 PRO B 461 0 -3.43
SITE 1 AC1 38 GLY A 10 GLY A 12 SER A 13 GLY A 14
SITE 2 AC1 38 ILE A 33 ASP A 34 LEU A 35 ALA A 45
SITE 3 AC1 38 ALA A 46 GLY A 49 THR A 50 CYS A 51
SITE 4 AC1 38 GLY A 55 CYS A 56 LYS A 59 GLY A 124
SITE 5 AC1 38 PHE A 125 GLY A 126 ALA A 158 THR A 159
SITE 6 AC1 38 GLY A 160 TYR A 197 ARG A 286 ARG A 289
SITE 7 AC1 38 GLY A 325 ASP A 326 MET A 332 LEU A 333
SITE 8 AC1 38 THR A 334 PRO A 335 HOH A 518 HOH A 520
SITE 9 AC1 38 HOH A 525 HOH A 528 HOH A 586 HOH A 601
SITE 10 AC1 38 HOH A 618 HIS B 460
SITE 1 AC2 38 HIS A 460 ILE B 9 GLY B 10 GLY B 12
SITE 2 AC2 38 SER B 13 GLY B 14 ILE B 33 ASP B 34
SITE 3 AC2 38 ALA B 45 ALA B 46 GLY B 49 THR B 50
SITE 4 AC2 38 CYS B 51 VAL B 54 GLY B 55 CYS B 56
SITE 5 AC2 38 LYS B 59 GLY B 124 PHE B 125 GLY B 126
SITE 6 AC2 38 ALA B 158 THR B 159 GLY B 160 TYR B 197
SITE 7 AC2 38 ILE B 198 ARG B 286 ARG B 289 GLY B 325
SITE 8 AC2 38 ASP B 326 MET B 332 LEU B 333 THR B 334
SITE 9 AC2 38 PRO B 335 HOH B 500 HOH B 502 HOH B 510
SITE 10 AC2 38 HOH B 516 HOH B 526
CRYST1 105.900 169.600 60.000 90.00 90.00 90.00 P 21 21 21 8
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 0.009443 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005896 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016667 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
