HEADER OXIDOREDUCTASE 30-JUL-09 2WOV
TITLE TRYPANOSOMA BRUCEI TRYPANOTHIONE REDUCTASE WITH BOUND NADP.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPANOTHIONE REDUCTASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 1.8.1.12;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI;
SOURCE 3 ORGANISM_TAXID: 185431;
SOURCE 4 STRAIN: TREU927;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: CODONPLUS RIL;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS TRYPANOSOMIASIS, SLEEPING SICKNESS, FLAVOPROTEIN, TRYPANOTHIONE,
KEYWDS 2 OXIDOREDUCTASE, REDUCTASE, REDOX-ACTIVE CENTER
EXPDTA X-RAY DIFFRACTION
AUTHOR M.S.ALPHEY,A.H.FAIRLAMB
REVDAT 4 20-DEC-23 2WOV 1 REMARK LINK
REVDAT 3 28-JUN-17 2WOV 1 REMARK
REVDAT 2 19-OCT-11 2WOV 1 JRNL REMARK FORMUL VERSN
REVDAT 1 04-AUG-10 2WOV 0
JRNL AUTH S.PATTERSON,M.S.ALPHEY,D.C.JONES,E.J.SHANKS,I.P.STREET,
JRNL AUTH 2 J.A.FREARSON,P.G.WYATT,I.H.GILBERT,A.H.FAIRLAMB
JRNL TITL DIHYDROQUINAZOLINES AS A NOVEL CLASS OF TRYPANOSOMA BRUCEI
JRNL TITL 2 TRYPANOTHIONE REDUCTASE INHIBITORS: DISCOVERY, SYNTHESIS,
JRNL TITL 3 AND CHARACTERIZATION OF THEIR BINDING MODE BY PROTEIN
JRNL TITL 4 CRYSTALLOGRAPHY.
JRNL REF J.MED.CHEM. V. 54 6514 2011
JRNL REFN ISSN 0022-2623
JRNL PMID 21851087
JRNL DOI 10.1021/JM200312V
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0088
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 72538
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3627
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4909
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2300
REMARK 3 BIN FREE R VALUE SET COUNT : 258
REMARK 3 BIN FREE R VALUE : 0.3330
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14831
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 411
REMARK 3 SOLVENT ATOMS : 440
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.45200
REMARK 3 B22 (A**2) : -0.11200
REMARK 3 B33 (A**2) : 1.57500
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.04200
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.730
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.304
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.223
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.955
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.891
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15611 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 21261 ; 1.730 ; 1.996
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1957 ; 6.614 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 610 ;35.940 ;24.492
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2545 ;17.684 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 69 ;17.004 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2413 ; 0.109 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11581 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 7166 ; 0.223 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 10668 ; 0.315 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 811 ; 0.142 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 4 ; 0.131 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 42 ; 0.279 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.255 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 9679 ; 0.738 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15625 ; 1.390 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5932 ; 2.237 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5632 ; 3.581 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 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 : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. SOME RESIDUES AT N- AND C-TERMINI WERE MODELLED AS
REMARK 3 ALANINES OR OMITTED FROM THE MODEL DUE TO THEIR FLEXIBILITY AND
REMARK 3 POOR ELECTRON DENSITY
REMARK 4
REMARK 4 2WOV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1290040539.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JAN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72546
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 19.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2WOI
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15MG/ML PROTEIN IN 25MM HEPES PH 7.5
REMARK 280 AND 50MM NABR EQUILIBRATED AGAINST 24% MPD, 10% PEG3350 AND 40MM
REMARK 280 IMIDAZOLE PH 8.0.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 31.72500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 12890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -107.8 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
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: 13000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -115.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 -2
REMARK 465 ASP A 489
REMARK 465 SER A 490
REMARK 465 ASN A 491
REMARK 465 LEU A 492
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 PRO B 488
REMARK 465 ASP B 489
REMARK 465 SER B 490
REMARK 465 ASN B 491
REMARK 465 LEU B 492
REMARK 465 GLY C -2
REMARK 465 ASP C 489
REMARK 465 SER C 490
REMARK 465 ASN C 491
REMARK 465 LEU C 492
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 ASP D 489
REMARK 465 SER D 490
REMARK 465 ASN D 491
REMARK 465 LEU D 492
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 PRO D 488 CG CD
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ASP A 358 O HOH A 2098 2.06
REMARK 500 O GLU A 387 O VAL A 479 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 290 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 222 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 PRO B 320 C - N - CA ANGL. DEV. = 13.6 DEGREES
REMARK 500 ASP C 121 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 PRO C 213 C - N - CA ANGL. DEV. = 11.3 DEGREES
REMARK 500 LEU D 260 CB - CG - CD2 ANGL. DEV. = 10.4 DEGREES
REMARK 500 PRO D 320 C - N - CA ANGL. DEV. = 11.5 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 12 57.76 -96.50
REMARK 500 TYR A 45 -66.24 67.67
REMARK 500 LEU A 48 118.21 -22.54
REMARK 500 VAL A 55 49.51 -149.91
REMARK 500 ALA A 159 52.94 -147.17
REMARK 500 ASN A 223 -159.41 -122.49
REMARK 500 ARG A 331 -102.98 -92.77
REMARK 500 TYR B 45 -75.38 61.50
REMARK 500 CYS B 52 -68.16 -29.64
REMARK 500 VAL B 55 44.21 -147.38
REMARK 500 LYS B 132 -26.05 -34.56
REMARK 500 ALA B 146 88.52 -63.86
REMARK 500 VAL B 147 121.70 -31.61
REMARK 500 ALA B 159 42.76 -143.44
REMARK 500 SER B 177 -168.10 -118.12
REMARK 500 ASN B 223 -162.63 -116.03
REMARK 500 PRO B 320 -51.54 -18.27
REMARK 500 PHE B 367 50.25 -66.56
REMARK 500 SER B 470 12.45 -145.45
REMARK 500 ALA C 12 52.26 -96.80
REMARK 500 TYR C 45 -63.54 69.41
REMARK 500 ALA C 47 -167.91 -165.06
REMARK 500 VAL C 55 40.03 -154.62
REMARK 500 PRO C 143 0.01 -65.90
REMARK 500 ALA C 159 39.86 -142.04
REMARK 500 PRO C 213 -68.11 -20.94
REMARK 500 ASN C 223 -153.74 -116.82
REMARK 500 ARG C 228 131.88 -35.98
REMARK 500 ARG C 331 -79.34 -82.26
REMARK 500 LYS C 353 70.62 -154.85
REMARK 500 ILE C 403 -35.83 -130.20
REMARK 500 ALA D 12 49.24 -95.56
REMARK 500 TYR D 45 -66.83 59.28
REMARK 500 ALA D 47 -166.09 -172.37
REMARK 500 LEU D 48 108.26 -44.11
REMARK 500 VAL D 55 46.71 -151.06
REMARK 500 LYS D 132 -49.37 -20.17
REMARK 500 ALA D 159 50.82 -146.51
REMARK 500 PRO D 213 130.21 -39.95
REMARK 500 ASN D 223 -160.26 -118.93
REMARK 500 PRO D 320 -52.09 -26.59
REMARK 500 ARG D 331 -78.55 -86.38
REMARK 500 PHE D 367 48.43 -83.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY C 214 GLY C 215 -143.78
REMARK 500 ASN C 352 LYS C 353 -147.40
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 A1489 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 455 O
REMARK 620 2 THR A 457 O 86.7
REMARK 620 3 CYS A 469 O 88.2 101.5
REMARK 620 4 HOH A2110 O 176.0 92.4 95.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B1488 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 455 O
REMARK 620 2 THR B 457 O 81.6
REMARK 620 3 CYS B 469 O 90.1 107.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C1490 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE C 114 O
REMARK 620 2 THR C 117 O 99.9
REMARK 620 3 LEU C 120 O 98.3 88.0
REMARK 620 4 HOH C2032 O 95.0 83.8 165.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C1489 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR C 455 O
REMARK 620 2 THR C 457 O 86.1
REMARK 620 3 HOH C2112 O 85.6 167.2
REMARK 620 N 1 2
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP C 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP D 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD D 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 1488
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1489
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 1489
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 1489
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 1490
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 1490
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 1489
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WOI RELATED DB: PDB
REMARK 900 TRYPANOTHIONE REDUCTASE FROM TRYPANOSOMA BRUCEI
REMARK 900 RELATED ID: 2WOW RELATED DB: PDB
REMARK 900 TRYPANOSOMA BRUCEI TRYPANOTHIONE REDUCTASE WITH NADP AND
REMARK 900 TRYPANOTHIONE BOUND
DBREF 2WOV A 1 492 UNP Q389T8 Q389T8_9TRYP 1 492
DBREF 2WOV B 1 492 UNP Q389T8 Q389T8_9TRYP 1 492
DBREF 2WOV C 1 492 UNP Q389T8 Q389T8_9TRYP 1 492
DBREF 2WOV D 1 492 UNP Q389T8 Q389T8_9TRYP 1 492
SEQADV 2WOV GLY A -2 UNP Q389T8 EXPRESSION TAG
SEQADV 2WOV SER A -1 UNP Q389T8 EXPRESSION TAG
SEQADV 2WOV HIS A 0 UNP Q389T8 EXPRESSION TAG
SEQADV 2WOV GLY B -2 UNP Q389T8 EXPRESSION TAG
SEQADV 2WOV SER B -1 UNP Q389T8 EXPRESSION TAG
SEQADV 2WOV HIS B 0 UNP Q389T8 EXPRESSION TAG
SEQADV 2WOV GLY C -2 UNP Q389T8 EXPRESSION TAG
SEQADV 2WOV SER C -1 UNP Q389T8 EXPRESSION TAG
SEQADV 2WOV HIS C 0 UNP Q389T8 EXPRESSION TAG
SEQADV 2WOV GLY D -2 UNP Q389T8 EXPRESSION TAG
SEQADV 2WOV SER D -1 UNP Q389T8 EXPRESSION TAG
SEQADV 2WOV HIS D 0 UNP Q389T8 EXPRESSION TAG
SEQRES 1 A 495 GLY SER HIS MET SER LYS ALA PHE ASP LEU VAL VAL ILE
SEQRES 2 A 495 GLY ALA GLY SER GLY GLY LEU GLU ALA GLY TRP ASN ALA
SEQRES 3 A 495 ALA THR LEU TYR GLY LYS ARG VAL ALA VAL VAL ASP VAL
SEQRES 4 A 495 GLN THR SER HIS GLY PRO PRO PHE TYR ALA ALA LEU GLY
SEQRES 5 A 495 GLY THR CYS VAL ASN VAL GLY CYS VAL PRO LYS LYS LEU
SEQRES 6 A 495 MET VAL THR GLY ALA GLN TYR MET ASP HIS LEU ARG GLU
SEQRES 7 A 495 SER ALA GLY PHE GLY TRP GLU PHE ASP GLY SER SER VAL
SEQRES 8 A 495 LYS ALA ASN TRP LYS LYS LEU ILE ALA ALA LYS ASN GLU
SEQRES 9 A 495 ALA VAL LEU ASP ILE ASN LYS SER TYR GLU GLY MET PHE
SEQRES 10 A 495 ASN ASP THR GLU GLY LEU ASP PHE PHE LEU GLY TRP GLY
SEQRES 11 A 495 SER LEU GLU SER LYS ASN VAL VAL VAL VAL ARG GLU THR
SEQRES 12 A 495 ALA ASP PRO LYS SER ALA VAL LYS GLU ARG LEU GLN ALA
SEQRES 13 A 495 ASP HIS ILE LEU LEU ALA THR GLY SER TRP PRO GLN MET
SEQRES 14 A 495 PRO ALA ILE PRO GLY ILE GLU HIS CYS ILE SER SER ASN
SEQRES 15 A 495 GLU ALA PHE TYR LEU PRO GLU PRO PRO ARG ARG VAL LEU
SEQRES 16 A 495 THR VAL GLY GLY GLY PHE ILE SER VAL GLU PHE ALA GLY
SEQRES 17 A 495 ILE PHE ASN ALA TYR LYS PRO PRO GLY GLY LYS VAL THR
SEQRES 18 A 495 LEU CYS TYR ARG ASN ASN LEU ILE LEU ARG GLY PHE ASP
SEQRES 19 A 495 GLU THR ILE ARG GLU GLU VAL THR LYS GLN LEU THR ALA
SEQRES 20 A 495 ASN GLY ILE GLU ILE MET THR ASN GLU ASN PRO ALA LYS
SEQRES 21 A 495 VAL SER LEU ASN THR ASP GLY SER LYS HIS VAL THR PHE
SEQRES 22 A 495 GLU SER GLY LYS THR LEU ASP VAL ASP VAL VAL MET MET
SEQRES 23 A 495 ALA ILE GLY ARG ILE PRO ARG THR ASN ASP LEU GLN LEU
SEQRES 24 A 495 GLY ASN VAL GLY VAL LYS LEU THR PRO LYS GLY GLY VAL
SEQRES 25 A 495 GLN VAL ASP GLU PHE SER ARG THR ASN VAL PRO ASN ILE
SEQRES 26 A 495 TYR ALA ILE GLY ASP ILE THR ASP ARG LEU MET LEU THR
SEQRES 27 A 495 PRO VAL ALA ILE ASN GLU GLY ALA ALA LEU VAL ASP THR
SEQRES 28 A 495 VAL PHE GLY ASN LYS PRO ARG LYS THR ASP HIS THR ARG
SEQRES 29 A 495 VAL ALA SER ALA VAL PHE SER ILE PRO PRO ILE GLY THR
SEQRES 30 A 495 CYS GLY LEU ILE GLU GLU VAL ALA ALA LYS GLU PHE GLU
SEQRES 31 A 495 LYS VAL ALA VAL TYR MET SER SER PHE THR PRO LEU MET
SEQRES 32 A 495 HIS ASN ILE SER GLY SER LYS TYR LYS LYS PHE VAL ALA
SEQRES 33 A 495 LYS ILE VAL THR ASN HIS SER ASP GLY THR VAL LEU GLY
SEQRES 34 A 495 VAL HIS LEU LEU GLY ASP GLY ALA PRO GLU ILE ILE GLN
SEQRES 35 A 495 ALA VAL GLY VAL CYS LEU ARG LEU ASN ALA LYS ILE SER
SEQRES 36 A 495 ASP PHE TYR ASN THR ILE GLY VAL HIS PRO THR SER ALA
SEQRES 37 A 495 GLU GLU LEU CYS SER MET ARG THR PRO SER TYR TYR TYR
SEQRES 38 A 495 VAL LYS GLY GLU LYS MET GLU LYS LEU PRO ASP SER ASN
SEQRES 39 A 495 LEU
SEQRES 1 B 495 GLY SER HIS MET SER LYS ALA PHE ASP LEU VAL VAL ILE
SEQRES 2 B 495 GLY ALA GLY SER GLY GLY LEU GLU ALA GLY TRP ASN ALA
SEQRES 3 B 495 ALA THR LEU TYR GLY LYS ARG VAL ALA VAL VAL ASP VAL
SEQRES 4 B 495 GLN THR SER HIS GLY PRO PRO PHE TYR ALA ALA LEU GLY
SEQRES 5 B 495 GLY THR CYS VAL ASN VAL GLY CYS VAL PRO LYS LYS LEU
SEQRES 6 B 495 MET VAL THR GLY ALA GLN TYR MET ASP HIS LEU ARG GLU
SEQRES 7 B 495 SER ALA GLY PHE GLY TRP GLU PHE ASP GLY SER SER VAL
SEQRES 8 B 495 LYS ALA ASN TRP LYS LYS LEU ILE ALA ALA LYS ASN GLU
SEQRES 9 B 495 ALA VAL LEU ASP ILE ASN LYS SER TYR GLU GLY MET PHE
SEQRES 10 B 495 ASN ASP THR GLU GLY LEU ASP PHE PHE LEU GLY TRP GLY
SEQRES 11 B 495 SER LEU GLU SER LYS ASN VAL VAL VAL VAL ARG GLU THR
SEQRES 12 B 495 ALA ASP PRO LYS SER ALA VAL LYS GLU ARG LEU GLN ALA
SEQRES 13 B 495 ASP HIS ILE LEU LEU ALA THR GLY SER TRP PRO GLN MET
SEQRES 14 B 495 PRO ALA ILE PRO GLY ILE GLU HIS CYS ILE SER SER ASN
SEQRES 15 B 495 GLU ALA PHE TYR LEU PRO GLU PRO PRO ARG ARG VAL LEU
SEQRES 16 B 495 THR VAL GLY GLY GLY PHE ILE SER VAL GLU PHE ALA GLY
SEQRES 17 B 495 ILE PHE ASN ALA TYR LYS PRO PRO GLY GLY LYS VAL THR
SEQRES 18 B 495 LEU CYS TYR ARG ASN ASN LEU ILE LEU ARG GLY PHE ASP
SEQRES 19 B 495 GLU THR ILE ARG GLU GLU VAL THR LYS GLN LEU THR ALA
SEQRES 20 B 495 ASN GLY ILE GLU ILE MET THR ASN GLU ASN PRO ALA LYS
SEQRES 21 B 495 VAL SER LEU ASN THR ASP GLY SER LYS HIS VAL THR PHE
SEQRES 22 B 495 GLU SER GLY LYS THR LEU ASP VAL ASP VAL VAL MET MET
SEQRES 23 B 495 ALA ILE GLY ARG ILE PRO ARG THR ASN ASP LEU GLN LEU
SEQRES 24 B 495 GLY ASN VAL GLY VAL LYS LEU THR PRO LYS GLY GLY VAL
SEQRES 25 B 495 GLN VAL ASP GLU PHE SER ARG THR ASN VAL PRO ASN ILE
SEQRES 26 B 495 TYR ALA ILE GLY ASP ILE THR ASP ARG LEU MET LEU THR
SEQRES 27 B 495 PRO VAL ALA ILE ASN GLU GLY ALA ALA LEU VAL ASP THR
SEQRES 28 B 495 VAL PHE GLY ASN LYS PRO ARG LYS THR ASP HIS THR ARG
SEQRES 29 B 495 VAL ALA SER ALA VAL PHE SER ILE PRO PRO ILE GLY THR
SEQRES 30 B 495 CYS GLY LEU ILE GLU GLU VAL ALA ALA LYS GLU PHE GLU
SEQRES 31 B 495 LYS VAL ALA VAL TYR MET SER SER PHE THR PRO LEU MET
SEQRES 32 B 495 HIS ASN ILE SER GLY SER LYS TYR LYS LYS PHE VAL ALA
SEQRES 33 B 495 LYS ILE VAL THR ASN HIS SER ASP GLY THR VAL LEU GLY
SEQRES 34 B 495 VAL HIS LEU LEU GLY ASP GLY ALA PRO GLU ILE ILE GLN
SEQRES 35 B 495 ALA VAL GLY VAL CYS LEU ARG LEU ASN ALA LYS ILE SER
SEQRES 36 B 495 ASP PHE TYR ASN THR ILE GLY VAL HIS PRO THR SER ALA
SEQRES 37 B 495 GLU GLU LEU CYS SER MET ARG THR PRO SER TYR TYR TYR
SEQRES 38 B 495 VAL LYS GLY GLU LYS MET GLU LYS LEU PRO ASP SER ASN
SEQRES 39 B 495 LEU
SEQRES 1 C 495 GLY SER HIS MET SER LYS ALA PHE ASP LEU VAL VAL ILE
SEQRES 2 C 495 GLY ALA GLY SER GLY GLY LEU GLU ALA GLY TRP ASN ALA
SEQRES 3 C 495 ALA THR LEU TYR GLY LYS ARG VAL ALA VAL VAL ASP VAL
SEQRES 4 C 495 GLN THR SER HIS GLY PRO PRO PHE TYR ALA ALA LEU GLY
SEQRES 5 C 495 GLY THR CYS VAL ASN VAL GLY CYS VAL PRO LYS LYS LEU
SEQRES 6 C 495 MET VAL THR GLY ALA GLN TYR MET ASP HIS LEU ARG GLU
SEQRES 7 C 495 SER ALA GLY PHE GLY TRP GLU PHE ASP GLY SER SER VAL
SEQRES 8 C 495 LYS ALA ASN TRP LYS LYS LEU ILE ALA ALA LYS ASN GLU
SEQRES 9 C 495 ALA VAL LEU ASP ILE ASN LYS SER TYR GLU GLY MET PHE
SEQRES 10 C 495 ASN ASP THR GLU GLY LEU ASP PHE PHE LEU GLY TRP GLY
SEQRES 11 C 495 SER LEU GLU SER LYS ASN VAL VAL VAL VAL ARG GLU THR
SEQRES 12 C 495 ALA ASP PRO LYS SER ALA VAL LYS GLU ARG LEU GLN ALA
SEQRES 13 C 495 ASP HIS ILE LEU LEU ALA THR GLY SER TRP PRO GLN MET
SEQRES 14 C 495 PRO ALA ILE PRO GLY ILE GLU HIS CYS ILE SER SER ASN
SEQRES 15 C 495 GLU ALA PHE TYR LEU PRO GLU PRO PRO ARG ARG VAL LEU
SEQRES 16 C 495 THR VAL GLY GLY GLY PHE ILE SER VAL GLU PHE ALA GLY
SEQRES 17 C 495 ILE PHE ASN ALA TYR LYS PRO PRO GLY GLY LYS VAL THR
SEQRES 18 C 495 LEU CYS TYR ARG ASN ASN LEU ILE LEU ARG GLY PHE ASP
SEQRES 19 C 495 GLU THR ILE ARG GLU GLU VAL THR LYS GLN LEU THR ALA
SEQRES 20 C 495 ASN GLY ILE GLU ILE MET THR ASN GLU ASN PRO ALA LYS
SEQRES 21 C 495 VAL SER LEU ASN THR ASP GLY SER LYS HIS VAL THR PHE
SEQRES 22 C 495 GLU SER GLY LYS THR LEU ASP VAL ASP VAL VAL MET MET
SEQRES 23 C 495 ALA ILE GLY ARG ILE PRO ARG THR ASN ASP LEU GLN LEU
SEQRES 24 C 495 GLY ASN VAL GLY VAL LYS LEU THR PRO LYS GLY GLY VAL
SEQRES 25 C 495 GLN VAL ASP GLU PHE SER ARG THR ASN VAL PRO ASN ILE
SEQRES 26 C 495 TYR ALA ILE GLY ASP ILE THR ASP ARG LEU MET LEU THR
SEQRES 27 C 495 PRO VAL ALA ILE ASN GLU GLY ALA ALA LEU VAL ASP THR
SEQRES 28 C 495 VAL PHE GLY ASN LYS PRO ARG LYS THR ASP HIS THR ARG
SEQRES 29 C 495 VAL ALA SER ALA VAL PHE SER ILE PRO PRO ILE GLY THR
SEQRES 30 C 495 CYS GLY LEU ILE GLU GLU VAL ALA ALA LYS GLU PHE GLU
SEQRES 31 C 495 LYS VAL ALA VAL TYR MET SER SER PHE THR PRO LEU MET
SEQRES 32 C 495 HIS ASN ILE SER GLY SER LYS TYR LYS LYS PHE VAL ALA
SEQRES 33 C 495 LYS ILE VAL THR ASN HIS SER ASP GLY THR VAL LEU GLY
SEQRES 34 C 495 VAL HIS LEU LEU GLY ASP GLY ALA PRO GLU ILE ILE GLN
SEQRES 35 C 495 ALA VAL GLY VAL CYS LEU ARG LEU ASN ALA LYS ILE SER
SEQRES 36 C 495 ASP PHE TYR ASN THR ILE GLY VAL HIS PRO THR SER ALA
SEQRES 37 C 495 GLU GLU LEU CYS SER MET ARG THR PRO SER TYR TYR TYR
SEQRES 38 C 495 VAL LYS GLY GLU LYS MET GLU LYS LEU PRO ASP SER ASN
SEQRES 39 C 495 LEU
SEQRES 1 D 495 GLY SER HIS MET SER LYS ALA PHE ASP LEU VAL VAL ILE
SEQRES 2 D 495 GLY ALA GLY SER GLY GLY LEU GLU ALA GLY TRP ASN ALA
SEQRES 3 D 495 ALA THR LEU TYR GLY LYS ARG VAL ALA VAL VAL ASP VAL
SEQRES 4 D 495 GLN THR SER HIS GLY PRO PRO PHE TYR ALA ALA LEU GLY
SEQRES 5 D 495 GLY THR CYS VAL ASN VAL GLY CYS VAL PRO LYS LYS LEU
SEQRES 6 D 495 MET VAL THR GLY ALA GLN TYR MET ASP HIS LEU ARG GLU
SEQRES 7 D 495 SER ALA GLY PHE GLY TRP GLU PHE ASP GLY SER SER VAL
SEQRES 8 D 495 LYS ALA ASN TRP LYS LYS LEU ILE ALA ALA LYS ASN GLU
SEQRES 9 D 495 ALA VAL LEU ASP ILE ASN LYS SER TYR GLU GLY MET PHE
SEQRES 10 D 495 ASN ASP THR GLU GLY LEU ASP PHE PHE LEU GLY TRP GLY
SEQRES 11 D 495 SER LEU GLU SER LYS ASN VAL VAL VAL VAL ARG GLU THR
SEQRES 12 D 495 ALA ASP PRO LYS SER ALA VAL LYS GLU ARG LEU GLN ALA
SEQRES 13 D 495 ASP HIS ILE LEU LEU ALA THR GLY SER TRP PRO GLN MET
SEQRES 14 D 495 PRO ALA ILE PRO GLY ILE GLU HIS CYS ILE SER SER ASN
SEQRES 15 D 495 GLU ALA PHE TYR LEU PRO GLU PRO PRO ARG ARG VAL LEU
SEQRES 16 D 495 THR VAL GLY GLY GLY PHE ILE SER VAL GLU PHE ALA GLY
SEQRES 17 D 495 ILE PHE ASN ALA TYR LYS PRO PRO GLY GLY LYS VAL THR
SEQRES 18 D 495 LEU CYS TYR ARG ASN ASN LEU ILE LEU ARG GLY PHE ASP
SEQRES 19 D 495 GLU THR ILE ARG GLU GLU VAL THR LYS GLN LEU THR ALA
SEQRES 20 D 495 ASN GLY ILE GLU ILE MET THR ASN GLU ASN PRO ALA LYS
SEQRES 21 D 495 VAL SER LEU ASN THR ASP GLY SER LYS HIS VAL THR PHE
SEQRES 22 D 495 GLU SER GLY LYS THR LEU ASP VAL ASP VAL VAL MET MET
SEQRES 23 D 495 ALA ILE GLY ARG ILE PRO ARG THR ASN ASP LEU GLN LEU
SEQRES 24 D 495 GLY ASN VAL GLY VAL LYS LEU THR PRO LYS GLY GLY VAL
SEQRES 25 D 495 GLN VAL ASP GLU PHE SER ARG THR ASN VAL PRO ASN ILE
SEQRES 26 D 495 TYR ALA ILE GLY ASP ILE THR ASP ARG LEU MET LEU THR
SEQRES 27 D 495 PRO VAL ALA ILE ASN GLU GLY ALA ALA LEU VAL ASP THR
SEQRES 28 D 495 VAL PHE GLY ASN LYS PRO ARG LYS THR ASP HIS THR ARG
SEQRES 29 D 495 VAL ALA SER ALA VAL PHE SER ILE PRO PRO ILE GLY THR
SEQRES 30 D 495 CYS GLY LEU ILE GLU GLU VAL ALA ALA LYS GLU PHE GLU
SEQRES 31 D 495 LYS VAL ALA VAL TYR MET SER SER PHE THR PRO LEU MET
SEQRES 32 D 495 HIS ASN ILE SER GLY SER LYS TYR LYS LYS PHE VAL ALA
SEQRES 33 D 495 LYS ILE VAL THR ASN HIS SER ASP GLY THR VAL LEU GLY
SEQRES 34 D 495 VAL HIS LEU LEU GLY ASP GLY ALA PRO GLU ILE ILE GLN
SEQRES 35 D 495 ALA VAL GLY VAL CYS LEU ARG LEU ASN ALA LYS ILE SER
SEQRES 36 D 495 ASP PHE TYR ASN THR ILE GLY VAL HIS PRO THR SER ALA
SEQRES 37 D 495 GLU GLU LEU CYS SER MET ARG THR PRO SER TYR TYR TYR
SEQRES 38 D 495 VAL LYS GLY GLU LYS MET GLU LYS LEU PRO ASP SER ASN
SEQRES 39 D 495 LEU
HET NDP A 800 48
HET FAD A 998 53
HET NA A1489 1
HET NDP B 800 48
HET FAD B 998 53
HET NA B1488 1
HET NA B1489 1
HET NDP C 800 48
HET FAD C 998 53
HET NA C1489 1
HET NA C1490 1
HET NDP D 800 48
HET FAD D 998 53
HET NA D1489 1
HET NA D1490 1
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM NA SODIUM ION
FORMUL 5 NDP 4(C21 H30 N7 O17 P3)
FORMUL 6 FAD 4(C27 H33 N9 O15 P2)
FORMUL 7 NA 7(NA 1+)
FORMUL 20 HOH *440(H2 O)
HELIX 1 1 TRP A 21 TYR A 27 1 7
HELIX 2 2 CYS A 57 THR A 65 1 9
HELIX 3 3 ALA A 67 ALA A 77 1 11
HELIX 4 4 ASN A 91 GLU A 111 1 21
HELIX 5 5 SER A 177 PHE A 182 1 6
HELIX 6 6 PHE A 198 ALA A 204 1 7
HELIX 7 7 ILE A 206 LYS A 211 1 6
HELIX 8 8 ASP A 231 ASN A 245 1 15
HELIX 9 9 LEU A 334 GLU A 341 1 8
HELIX 10 10 ALA A 343 PHE A 350 1 8
HELIX 11 11 ILE A 378 PHE A 386 1 9
HELIX 12 12 LEU A 399 SER A 404 1 6
HELIX 13 13 ALA A 434 GLN A 439 1 6
HELIX 14 14 LYS A 450 THR A 457 1 8
HELIX 15 15 SER A 464 SER A 470 5 7
HELIX 16 16 TRP B 21 LEU B 26 1 6
HELIX 17 17 CYS B 57 THR B 65 1 9
HELIX 18 18 GLN B 68 SER B 76 1 9
HELIX 19 19 ASN B 91 GLU B 111 1 21
HELIX 20 20 MET B 113 THR B 117 5 5
HELIX 21 21 SER B 177 PHE B 182 1 6
HELIX 22 22 PHE B 198 ALA B 204 1 7
HELIX 23 23 ILE B 206 LYS B 211 1 6
HELIX 24 24 ASP B 231 ASN B 245 1 15
HELIX 25 25 LEU B 334 GLU B 341 1 8
HELIX 26 26 ALA B 343 PHE B 350 1 8
HELIX 27 27 ILE B 378 PHE B 386 1 9
HELIX 28 28 LEU B 399 SER B 404 1 6
HELIX 29 29 VAL B 443 ASN B 448 5 6
HELIX 30 30 LYS B 450 THR B 457 1 8
HELIX 31 31 SER B 464 SER B 470 5 7
HELIX 32 32 TRP C 21 LEU C 26 1 6
HELIX 33 33 CYS C 57 THR C 65 1 9
HELIX 34 34 ALA C 67 SER C 76 1 10
HELIX 35 35 ASN C 91 GLU C 111 1 21
HELIX 36 36 SER C 177 PHE C 182 1 6
HELIX 37 37 PHE C 198 ALA C 204 1 7
HELIX 38 38 ILE C 206 LYS C 211 1 6
HELIX 39 39 ASP C 231 ASN C 245 1 15
HELIX 40 40 LEU C 334 GLU C 341 1 8
HELIX 41 41 ALA C 343 PHE C 350 1 8
HELIX 42 42 ILE C 378 PHE C 386 1 9
HELIX 43 43 PRO C 398 ILE C 403 5 6
HELIX 44 44 ALA C 434 GLN C 439 1 6
HELIX 45 45 LYS C 450 THR C 457 1 8
HELIX 46 46 SER C 464 SER C 470 5 7
HELIX 47 47 TRP D 21 LEU D 26 1 6
HELIX 48 48 CYS D 57 THR D 65 1 9
HELIX 49 49 GLN D 68 SER D 76 1 9
HELIX 50 50 ASN D 91 GLU D 111 1 21
HELIX 51 51 SER D 177 PHE D 182 1 6
HELIX 52 52 PHE D 198 ALA D 204 1 7
HELIX 53 53 ILE D 206 LYS D 211 1 6
HELIX 54 54 ASP D 231 ASN D 245 1 15
HELIX 55 55 LEU D 334 GLU D 341 1 8
HELIX 56 56 ALA D 343 PHE D 350 1 8
HELIX 57 57 ILE D 378 PHE D 386 1 9
HELIX 58 58 PRO D 398 SER D 404 1 7
HELIX 59 59 VAL D 443 ASN D 448 5 6
HELIX 60 60 LYS D 450 THR D 457 1 8
HELIX 61 61 SER D 464 SER D 470 5 7
SHEET 1 AA 6 ASP A 121 PHE A 123 0
SHEET 2 AA 6 VAL A 31 VAL A 34 1 O VAL A 31 N ASP A 121
SHEET 3 AA 6 LYS A 3 ILE A 10 1 O LEU A 7 N ALA A 32
SHEET 4 AA 6 VAL A 147 LEU A 158 1 O ARG A 150 N LYS A 3
SHEET 5 AA 6 VAL A 134 ARG A 138 -1 O VAL A 135 N LEU A 151
SHEET 6 AA 6 LEU A 129 SER A 131 -1 N GLU A 130 O VAL A 134
SHEET 1 AB 4 ASP A 121 PHE A 123 0
SHEET 2 AB 4 VAL A 31 VAL A 34 1 O VAL A 31 N ASP A 121
SHEET 3 AB 4 LYS A 3 ILE A 10 1 O LEU A 7 N ALA A 32
SHEET 4 AB 4 VAL A 147 LEU A 158 1 O ARG A 150 N LYS A 3
SHEET 1 AC 4 GLU A 248 THR A 251 0
SHEET 2 AC 4 VAL A 217 TYR A 221 1 O VAL A 217 N GLU A 248
SHEET 3 AC 4 VAL A 191 VAL A 194 1 O VAL A 191 N THR A 218
SHEET 4 AC 4 VAL A 280 MET A 283 1 O VAL A 280 N LEU A 192
SHEET 1 AD 3 PRO A 255 LEU A 260 0
SHEET 2 AD 3 LYS A 266 PHE A 270 -1 O HIS A 267 N SER A 259
SHEET 3 AD 3 THR A 275 VAL A 278 -1 O LEU A 276 N VAL A 268
SHEET 1 AE 5 HIS A 428 LEU A 430 0
SHEET 2 AE 5 PHE A 411 ASN A 418 -1 O VAL A 412 N LEU A 430
SHEET 3 AE 5 VAL A 389 PHE A 396 -1 O ALA A 390 N THR A 417
SHEET 4 AE 5 TYR A 476 TYR A 478 -1 O TYR A 476 N VAL A 391
SHEET 5 AE 5 LYS A 483 MET A 484 -1 O MET A 484 N TYR A 477
SHEET 1 BA 6 ASP B 121 PHE B 123 0
SHEET 2 BA 6 VAL B 31 VAL B 34 1 O VAL B 31 N ASP B 121
SHEET 3 BA 6 LYS B 3 ILE B 10 1 O LEU B 7 N ALA B 32
SHEET 4 BA 6 GLU B 149 LEU B 158 1 O ARG B 150 N LYS B 3
SHEET 5 BA 6 VAL B 134 VAL B 137 -1 O VAL B 135 N LEU B 151
SHEET 6 BA 6 LEU B 129 SER B 131 -1 N GLU B 130 O VAL B 134
SHEET 1 BB 4 ASP B 121 PHE B 123 0
SHEET 2 BB 4 VAL B 31 VAL B 34 1 O VAL B 31 N ASP B 121
SHEET 3 BB 4 LYS B 3 ILE B 10 1 O LEU B 7 N ALA B 32
SHEET 4 BB 4 GLU B 149 LEU B 158 1 O ARG B 150 N LYS B 3
SHEET 1 BC 4 GLU B 248 THR B 251 0
SHEET 2 BC 4 VAL B 217 TYR B 221 1 O VAL B 217 N GLU B 248
SHEET 3 BC 4 VAL B 191 VAL B 194 1 O VAL B 191 N THR B 218
SHEET 4 BC 4 VAL B 280 MET B 283 1 O VAL B 280 N LEU B 192
SHEET 1 BD 3 PRO B 255 LEU B 260 0
SHEET 2 BD 3 LYS B 266 PHE B 270 -1 O HIS B 267 N SER B 259
SHEET 3 BD 3 THR B 275 VAL B 278 -1 O LEU B 276 N VAL B 268
SHEET 1 BE 5 HIS B 428 LEU B 430 0
SHEET 2 BE 5 PHE B 411 ASN B 418 -1 O VAL B 412 N LEU B 430
SHEET 3 BE 5 LYS B 388 PHE B 396 -1 O ALA B 390 N THR B 417
SHEET 4 BE 5 TYR B 476 VAL B 479 -1 O TYR B 476 N VAL B 391
SHEET 5 BE 5 LYS B 483 MET B 484 -1 O MET B 484 N TYR B 477
SHEET 1 CA 6 ASP C 121 PHE C 123 0
SHEET 2 CA 6 VAL C 31 VAL C 34 1 O VAL C 31 N ASP C 121
SHEET 3 CA 6 LYS C 3 ILE C 10 1 O LEU C 7 N ALA C 32
SHEET 4 CA 6 VAL C 147 LEU C 158 1 O ARG C 150 N LYS C 3
SHEET 5 CA 6 VAL C 134 ARG C 138 -1 O VAL C 135 N LEU C 151
SHEET 6 CA 6 LEU C 129 SER C 131 -1 N GLU C 130 O VAL C 134
SHEET 1 CB 4 ASP C 121 PHE C 123 0
SHEET 2 CB 4 VAL C 31 VAL C 34 1 O VAL C 31 N ASP C 121
SHEET 3 CB 4 LYS C 3 ILE C 10 1 O LEU C 7 N ALA C 32
SHEET 4 CB 4 VAL C 147 LEU C 158 1 O ARG C 150 N LYS C 3
SHEET 1 CC 4 GLU C 248 MET C 250 0
SHEET 2 CC 4 VAL C 217 CYS C 220 1 O VAL C 217 N GLU C 248
SHEET 3 CC 4 VAL C 191 VAL C 194 1 O VAL C 191 N THR C 218
SHEET 4 CC 4 VAL C 280 MET C 283 1 O VAL C 280 N LEU C 192
SHEET 1 CD 3 PRO C 255 LEU C 260 0
SHEET 2 CD 3 LYS C 266 PHE C 270 -1 O HIS C 267 N SER C 259
SHEET 3 CD 3 THR C 275 VAL C 278 -1 O LEU C 276 N VAL C 268
SHEET 1 CE 5 HIS C 428 LEU C 430 0
SHEET 2 CE 5 PHE C 411 ASN C 418 -1 O VAL C 412 N LEU C 430
SHEET 3 CE 5 LYS C 388 PHE C 396 -1 O ALA C 390 N THR C 417
SHEET 4 CE 5 TYR C 476 VAL C 479 -1 O TYR C 476 N VAL C 391
SHEET 5 CE 5 LYS C 483 MET C 484 -1 O MET C 484 N TYR C 477
SHEET 1 DA 9 ASP D 121 PHE D 123 0
SHEET 2 DA 9 VAL D 31 VAL D 34 1 O VAL D 31 N ASP D 121
SHEET 3 DA 9 LYS D 3 ILE D 10 1 O LEU D 7 N ALA D 32
SHEET 4 DA 9 VAL D 147 LEU D 158 1 O ARG D 150 N LYS D 3
SHEET 5 DA 9 LEU D 129 SER D 131 0
SHEET 6 DA 9 VAL D 134 ARG D 138 -1 O VAL D 134 N GLU D 130
SHEET 7 DA 9 VAL D 147 LEU D 158 -1 N LYS D 148 O VAL D 137
SHEET 8 DA 9 ILE D 322 ALA D 324 1 O TYR D 323 N LEU D 158
SHEET 9 DA 9 VAL D 147 LEU D 158 1 O ILE D 156 N TYR D 323
SHEET 1 DB 4 GLU D 248 MET D 250 0
SHEET 2 DB 4 VAL D 217 CYS D 220 1 O VAL D 217 N GLU D 248
SHEET 3 DB 4 VAL D 191 VAL D 194 1 O VAL D 191 N THR D 218
SHEET 4 DB 4 VAL D 280 MET D 283 1 O VAL D 280 N LEU D 192
SHEET 1 DC 3 PRO D 255 LEU D 260 0
SHEET 2 DC 3 LYS D 266 PHE D 270 -1 O HIS D 267 N SER D 259
SHEET 3 DC 3 THR D 275 VAL D 278 -1 O LEU D 276 N VAL D 268
SHEET 1 DD 5 HIS D 428 LEU D 430 0
SHEET 2 DD 5 PHE D 411 ASN D 418 -1 O VAL D 412 N LEU D 430
SHEET 3 DD 5 LYS D 388 PHE D 396 -1 O ALA D 390 N THR D 417
SHEET 4 DD 5 TYR D 476 VAL D 479 -1 O TYR D 476 N VAL D 391
SHEET 5 DD 5 LYS D 483 MET D 484 -1 O MET D 484 N TYR D 477
SSBOND 1 CYS B 52 CYS B 57 1555 1555 2.93
SSBOND 2 CYS D 52 CYS D 57 1555 1555 2.98
LINK O TYR A 455 NA NA A1489 1555 1555 2.48
LINK O THR A 457 NA NA A1489 1555 1555 2.48
LINK O CYS A 469 NA NA A1489 1555 1555 2.58
LINK NA NA A1489 O HOH A2110 1555 1555 2.42
LINK O PHE B 114 NA NA B1489 1555 1555 2.39
LINK O TYR B 455 NA NA B1488 1555 1555 2.45
LINK O THR B 457 NA NA B1488 1555 1555 2.51
LINK O CYS B 469 NA NA B1488 1555 1555 2.43
LINK O PHE C 114 NA NA C1490 1555 1555 2.18
LINK O THR C 117 NA NA C1490 1555 1555 2.37
LINK O LEU C 120 NA NA C1490 1555 1555 2.57
LINK O TYR C 455 NA NA C1489 1555 1555 2.44
LINK O THR C 457 NA NA C1489 1555 1555 2.49
LINK NA NA C1489 O HOH C2112 1555 1555 2.51
LINK NA NA C1490 O HOH C2032 1555 1555 2.57
LINK O THR D 117 NA NA D1490 1555 1555 2.30
LINK O CYS D 469 NA NA D1489 1555 1555 2.44
CISPEP 1 PRO A 42 PRO A 43 0 2.36
CISPEP 2 ILE A 369 PRO A 370 0 7.94
CISPEP 3 HIS A 461 PRO A 462 0 -9.27
CISPEP 4 PRO B 42 PRO B 43 0 10.96
CISPEP 5 ILE B 369 PRO B 370 0 -1.84
CISPEP 6 HIS B 461 PRO B 462 0 -8.56
CISPEP 7 PRO C 42 PRO C 43 0 2.61
CISPEP 8 ILE C 369 PRO C 370 0 2.83
CISPEP 9 HIS C 461 PRO C 462 0 -7.97
CISPEP 10 PRO D 42 PRO D 43 0 5.17
CISPEP 11 ILE D 369 PRO D 370 0 6.97
CISPEP 12 HIS D 461 PRO D 462 0 2.79
SITE 1 AC1 27 LYS A 60 GLY A 196 GLY A 197 PHE A 198
SITE 2 AC1 27 ILE A 199 GLU A 202 TYR A 221 ARG A 222
SITE 3 AC1 27 ASN A 223 ARG A 228 ASN A 254 ALA A 284
SITE 4 AC1 27 ILE A 285 GLY A 286 MET A 333 LEU A 334
SITE 5 AC1 27 ALA A 365 PHE A 367 FAD A 998 HOH A2071
SITE 6 AC1 27 HOH A2080 HOH A2114 HOH A2115 HOH A2116
SITE 7 AC1 27 HOH A2117 HOH A2118 HOH A2119
SITE 1 AC2 37 ILE A 10 GLY A 11 GLY A 13 SER A 14
SITE 2 AC2 37 GLY A 15 VAL A 34 ASP A 35 ALA A 46
SITE 3 AC2 37 ALA A 47 GLY A 50 THR A 51 CYS A 52
SITE 4 AC2 37 VAL A 55 GLY A 56 CYS A 57 LYS A 60
SITE 5 AC2 37 GLY A 125 TRP A 126 GLY A 127 ALA A 159
SITE 6 AC2 37 THR A 160 GLY A 161 ARG A 287 ARG A 290
SITE 7 AC2 37 GLY A 326 ASP A 327 MET A 333 LEU A 334
SITE 8 AC2 37 THR A 335 PRO A 336 ALA A 338 NDP A 800
SITE 9 AC2 37 HOH A2039 HOH A2040 HOH A2120 HOH A2121
SITE 10 AC2 37 HIS B 461
SITE 1 AC3 21 LYS B 60 GLY B 196 GLY B 197 PHE B 198
SITE 2 AC3 21 ILE B 199 GLU B 202 TYR B 221 ARG B 222
SITE 3 AC3 21 ASN B 223 ARG B 228 ASN B 254 ALA B 284
SITE 4 AC3 21 ILE B 285 GLY B 286 MET B 333 LEU B 334
SITE 5 AC3 21 ALA B 365 PHE B 367 FAD B 998 HOH B2094
SITE 6 AC3 21 HOH B2096
SITE 1 AC4 39 HIS A 461 PRO A 462 GLY B 11 GLY B 13
SITE 2 AC4 39 SER B 14 GLY B 15 VAL B 34 ASP B 35
SITE 3 AC4 39 VAL B 36 ALA B 46 ALA B 47 GLY B 50
SITE 4 AC4 39 THR B 51 CYS B 52 VAL B 55 GLY B 56
SITE 5 AC4 39 CYS B 57 LYS B 60 GLY B 125 TRP B 126
SITE 6 AC4 39 GLY B 127 ALA B 159 THR B 160 GLY B 161
SITE 7 AC4 39 ILE B 199 ARG B 287 ARG B 290 GLY B 326
SITE 8 AC4 39 ASP B 327 MET B 333 LEU B 334 THR B 335
SITE 9 AC4 39 PRO B 336 PHE B 367 NDP B 800 HOH B2064
SITE 10 AC4 39 HOH B2097 HOH B2098 HOH B2099
SITE 1 AC5 24 LYS C 60 GLY C 196 GLY C 197 PHE C 198
SITE 2 AC5 24 ILE C 199 GLU C 202 TYR C 221 ARG C 222
SITE 3 AC5 24 ASN C 223 ARG C 228 ASN C 254 ALA C 284
SITE 4 AC5 24 ILE C 285 GLY C 286 MET C 333 LEU C 334
SITE 5 AC5 24 ALA C 365 PHE C 367 FAD C 998 HOH C2098
SITE 6 AC5 24 HOH C2122 HOH C2123 HOH C2124 HOH C2125
SITE 1 AC6 38 ILE C 10 GLY C 11 GLY C 13 SER C 14
SITE 2 AC6 38 GLY C 15 VAL C 34 ASP C 35 ALA C 46
SITE 3 AC6 38 ALA C 47 GLY C 50 THR C 51 CYS C 52
SITE 4 AC6 38 GLY C 56 CYS C 57 LYS C 60 GLY C 125
SITE 5 AC6 38 TRP C 126 GLY C 127 ALA C 159 THR C 160
SITE 6 AC6 38 GLY C 161 ILE C 199 ARG C 287 ARG C 290
SITE 7 AC6 38 GLY C 326 ASP C 327 MET C 333 LEU C 334
SITE 8 AC6 38 THR C 335 PRO C 336 ALA C 338 NDP C 800
SITE 9 AC6 38 HOH C2041 HOH C2126 HOH C2127 HOH C2128
SITE 10 AC6 38 HIS D 461 PRO D 462
SITE 1 AC7 26 LYS D 60 GLY D 196 GLY D 197 PHE D 198
SITE 2 AC7 26 ILE D 199 GLU D 202 TYR D 221 ARG D 222
SITE 3 AC7 26 ARG D 228 ASN D 254 ALA D 284 ILE D 285
SITE 4 AC7 26 GLY D 286 MET D 333 LEU D 334 ALA D 365
SITE 5 AC7 26 FAD D 998 HOH D2016 HOH D2044 HOH D2082
SITE 6 AC7 26 HOH D2083 HOH D2084 HOH D2085 HOH D2086
SITE 7 AC7 26 HOH D2088 HOH D2089
SITE 1 AC8 35 HIS C 461 ILE D 10 GLY D 11 GLY D 13
SITE 2 AC8 35 SER D 14 GLY D 15 VAL D 34 ASP D 35
SITE 3 AC8 35 VAL D 36 ALA D 46 ALA D 47 GLY D 50
SITE 4 AC8 35 THR D 51 CYS D 52 GLY D 56 CYS D 57
SITE 5 AC8 35 LYS D 60 TRP D 126 GLY D 127 ALA D 159
SITE 6 AC8 35 THR D 160 GLY D 161 ILE D 199 ARG D 287
SITE 7 AC8 35 ARG D 290 GLY D 326 ASP D 327 MET D 333
SITE 8 AC8 35 LEU D 334 THR D 335 PRO D 336 NDP D 800
SITE 9 AC8 35 HOH D2090 HOH D2091 HOH D2092
SITE 1 AC9 3 TYR B 455 THR B 457 CYS B 469
SITE 1 BC1 4 TYR A 455 THR A 457 CYS A 469 HOH A2110
SITE 1 BC2 4 TYR C 455 THR C 457 CYS C 469 HOH C2112
SITE 1 BC3 3 TYR D 455 THR D 457 CYS D 469
SITE 1 BC4 4 PHE D 114 THR D 117 LEU D 120 ASP D 121
SITE 1 BC5 5 PHE C 114 THR C 117 LEU C 120 ASP C 121
SITE 2 BC5 5 HOH C2032
SITE 1 BC6 4 PHE B 114 THR B 117 LEU B 120 ASP B 121
CRYST1 100.870 63.450 169.350 90.00 97.85 90.00 P 1 21 1 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 0.009914 0.000000 0.001367 0.00000
SCALE2 0.000000 0.015760 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005961 0.00000
MTRIX1 1 0.010120 0.955920 0.293450 -8.69791 1
MTRIX2 1 0.955300 -0.095960 0.279640 -34.03827 1
MTRIX3 1 0.295480 0.277500 -0.914160 140.27289 1
MTRIX1 2 0.986540 0.160750 0.029950 1.69103 1
MTRIX2 2 -0.162450 0.984390 0.067710 -39.44091 1
MTRIX3 2 -0.018600 -0.071660 0.997260 -81.19545 1
MTRIX1 3 -0.118680 0.925610 0.359380 -70.88835 1
MTRIX2 3 0.953130 0.004750 0.302520 -50.45418 1
MTRIX3 3 0.278310 0.378440 -0.882800 204.08994 1
(ATOM LINES ARE NOT SHOWN.)
END
