HEADER OXIDOREDUCTASE 04-JAN-12 4ADW
TITLE CRYSTAL STRUCTURE OF LEISHMANIA INFANTUM TRYPANOTHIONE REDUCTASE IN
TITLE 2 COMPLEX WITH NADPH AND TRYPANOTHIONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPANOTHIONE REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.8.1.12;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEISHMANIA INFANTUM;
SOURCE 3 ORGANISM_TAXID: 5671;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET28
KEYWDS OXIDOREDUCTASE, INHIBITION MECHANISM
EXPDTA X-RAY DIFFRACTION
AUTHOR P.BAIOCCO,A.ILARI,G.COLOTTI,F.MALATESTA,A.FIORILLO
REVDAT 4 20-DEC-23 4ADW 1 REMARK
REVDAT 3 10-JUL-13 4ADW 1 JRNL
REVDAT 2 26-JUN-13 4ADW 1 JRNL
REVDAT 1 16-JAN-13 4ADW 0
JRNL AUTH P.BAIOCCO,G.POCE,S.ALFONSO,M.COCOZZA,G.C.PORRETTA,G.COLOTTI,
JRNL AUTH 2 M.BIAVA,F.MORACA,M.BOTTA,V.YARDLEY,A.FIORILLO,A.LANTELLA,
JRNL AUTH 3 F.MALATESTA,A.ILARI
JRNL TITL INHIBITION OF LEISHMANIA INFANTUM TRYPANOTHIONE REDUCTASE BY
JRNL TITL 2 AZOLE-BASED COMPOUNDS: A COMPARATIVE ANALYSIS WITH ITS
JRNL TITL 3 PHYSIOLOGICAL SUBSTRATE BY X-RAY CRYSTALLOGRAPHY.
JRNL REF CHEMMEDCHEM V. 8 1175 2013
JRNL REFN ISSN 1860-7179
JRNL PMID 23733388
JRNL DOI 10.1002/CMDC.201300176
REMARK 2
REMARK 2 RESOLUTION. 3.61 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 3.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 21745
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) : 0.252
REMARK 3 R VALUE (WORKING SET) : 0.249
REMARK 3 FREE R VALUE : 0.304
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1193
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) : 3.61
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.70
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1620
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.36
REMARK 3 BIN R VALUE (WORKING SET) : 0.3370
REMARK 3 BIN FREE R VALUE SET COUNT : 89
REMARK 3 BIN FREE R VALUE : 0.3860
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7388
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 298
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 84.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.73000
REMARK 3 B22 (A**2) : 5.73000
REMARK 3 B33 (A**2) : -11.47000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.670
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.570
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 41.015
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.909
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.866
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7848 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10654 ; 1.480 ; 1.996
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 974 ; 5.574 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 314 ;34.940 ;24.331
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1260 ;19.254 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;12.444 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1190 ; 0.118 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5854 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 3
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 488 4
REMARK 3 1 B 1 B 488 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 3694 ; 0.25 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 3694 ; 0.25 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1489 A 1489 4
REMARK 3 1 B 1489 B 1489 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 53 ; 0.07 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 B (A): 53 ; 0.07 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1490 A 1490 4
REMARK 3 1 B 1490 B 1490 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 A (A): 48 ; 0.37 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 B (A): 48 ; 0.37 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4ADW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1290050847.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 6
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23097
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.37000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
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 2JK6
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5, 2.2 M AMMONIUM
REMARK 280 SULPHATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 96.12200
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 48.06100
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 144.18300
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: 13490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 SER A 489
REMARK 465 ASN A 490
REMARK 465 LEU A 491
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 SER B 489
REMARK 465 ASN B 490
REMARK 465 LEU B 491
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 28 13.98 57.21
REMARK 500 ALA A 47 -164.87 -172.36
REMARK 500 ARG A 85 15.59 -68.91
REMARK 500 GLU A 86 17.21 -141.84
REMARK 500 ASP A 131 -167.45 -162.94
REMARK 500 LYS A 189 -70.01 -78.45
REMARK 500 TYR A 198 -59.40 -26.68
REMARK 500 LEU A 227 70.94 55.05
REMARK 500 GLN A 295 71.80 58.20
REMARK 500 SER A 315 3.62 80.96
REMARK 500 THR A 317 -160.45 -100.25
REMARK 500 ASN A 330 0.82 81.10
REMARK 500 ARG A 331 -179.98 -64.75
REMARK 500 PHE A 367 47.34 -81.68
REMARK 500 LYS A 407 32.15 -82.06
REMARK 500 LYS A 409 33.55 -89.97
REMARK 500 PHE A 454 -71.70 -73.96
REMARK 500 ARG A 472 -70.65 -92.61
REMARK 500 LYS A 486 -164.67 -106.86
REMARK 500 LEU A 487 -37.53 -139.41
REMARK 500 LYS B 28 8.11 57.65
REMARK 500 ALA B 47 -158.80 -148.08
REMARK 500 LEU B 48 103.31 -55.88
REMARK 500 ARG B 85 2.30 -62.80
REMARK 500 ASP B 131 -155.72 -154.89
REMARK 500 PRO B 170 120.27 -38.49
REMARK 500 TYR B 198 -63.31 -29.82
REMARK 500 THR B 232 -8.87 -57.24
REMARK 500 GLN B 292 6.84 -67.54
REMARK 500 LYS B 298 2.37 -64.21
REMARK 500 SER B 315 3.11 81.65
REMARK 500 THR B 317 -155.99 -96.81
REMARK 500 PHE B 367 49.37 -83.68
REMARK 500 SER B 368 -178.59 -69.97
REMARK 500 LYS B 384 -85.29 -89.69
REMARK 500 GLU B 387 -73.38 -53.76
REMARK 500 SER B 394 118.40 -168.63
REMARK 500 LYS B 407 22.79 -74.42
REMARK 500 LYS B 409 44.60 -87.23
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 1489
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 1489
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 1490
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 1490
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GCG A 1491
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GCG B 1491
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2JK6 RELATED DB: PDB
REMARK 900 STRUCTURE OF TRYPANOTHIONE REDUCTASE FROM LEISHMANIA INFANTUM
REMARK 900 RELATED ID: 2W0H RELATED DB: PDB
REMARK 900 X RAY STRUCTURE OF LEISHMANIA INFANTUM TRYPANOTHIONE REDUCTASE IN
REMARK 900 COMPLEX WITH ANTIMONY AND NADPH
REMARK 900 RELATED ID: 2X50 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TRYPANOTHIONE REDUCTASE FROM LEISHMANIA
REMARK 900 INFANTUM IN COMPLEX WITH NADPH AND SILVER
REMARK 900 RELATED ID: 2YAU RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF THE LEISHMANIA INFANTUM TRYOPANOTHIONE REDUCTASE
REMARK 900 IN COMPLEX WITH AURANOFIN
DBREF 4ADW A 1 491 UNP A4HSF7 A4HSF7_LEIIN 1 491
DBREF 4ADW B 1 491 UNP A4HSF7 A4HSF7_LEIIN 1 491
SEQADV 4ADW MET A -19 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW GLY A -18 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW SER A -17 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW SER A -16 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW HIS A -15 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW HIS A -14 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW HIS A -13 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW HIS A -12 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW HIS A -11 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW HIS A -10 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW SER A -9 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW SER A -8 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW GLY A -7 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW LEU A -6 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW VAL A -5 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW PRO A -4 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW ARG A -3 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW GLY A -2 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW SER A -1 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW HIS A 0 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW MET B -19 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW GLY B -18 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW SER B -17 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW SER B -16 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW HIS B -15 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW HIS B -14 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW HIS B -13 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW HIS B -12 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW HIS B -11 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW HIS B -10 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW SER B -9 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW SER B -8 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW GLY B -7 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW LEU B -6 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW VAL B -5 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW PRO B -4 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW ARG B -3 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW GLY B -2 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW SER B -1 UNP A4HSF7 EXPRESSION TAG
SEQADV 4ADW HIS B 0 UNP A4HSF7 EXPRESSION TAG
SEQRES 1 A 511 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 511 LEU VAL PRO ARG GLY SER HIS MET SER ARG ALA TYR ASP
SEQRES 3 A 511 LEU VAL VAL LEU GLY ALA GLY SER GLY GLY LEU GLU ALA
SEQRES 4 A 511 GLY TRP ASN ALA ALA VAL THR HIS LYS LYS LYS VAL ALA
SEQRES 5 A 511 VAL VAL ASP VAL GLN ALA THR HIS GLY PRO PRO LEU PHE
SEQRES 6 A 511 ALA ALA LEU GLY GLY THR CYS VAL ASN VAL GLY CYS VAL
SEQRES 7 A 511 PRO LYS LYS LEU MET VAL THR GLY ALA GLN TYR MET ASP
SEQRES 8 A 511 LEU ILE ARG GLU SER GLY GLY PHE GLY TRP GLU MET ASP
SEQRES 9 A 511 ARG GLU SER LEU CYS PRO ASN TRP LYS THR LEU ILE ALA
SEQRES 10 A 511 ALA LYS ASN LYS VAL VAL ASN SER ILE ASN GLU SER TYR
SEQRES 11 A 511 LYS SER MET PHE ALA ASP THR GLU GLY LEU SER PHE HIS
SEQRES 12 A 511 MET GLY PHE GLY ALA LEU GLN ASP ALA HIS THR VAL VAL
SEQRES 13 A 511 VAL ARG LYS SER GLU ASP PRO HIS SER ASP VAL LEU GLU
SEQRES 14 A 511 THR LEU ASP THR GLU TYR ILE LEU ILE ALA THR GLY SER
SEQRES 15 A 511 TRP PRO THR ARG LEU GLY VAL PRO GLY ASP GLU PHE CYS
SEQRES 16 A 511 ILE THR SER ASN GLU ALA PHE TYR LEU GLU ASP ALA PRO
SEQRES 17 A 511 LYS ARG MET LEU CYS VAL GLY GLY GLY TYR ILE ALA VAL
SEQRES 18 A 511 GLU PHE ALA GLY ILE PHE ASN GLY TYR LYS PRO CYS GLY
SEQRES 19 A 511 GLY TYR VAL ASP LEU CYS TYR ARG GLY ASP LEU ILE LEU
SEQRES 20 A 511 ARG GLY PHE ASP THR GLU VAL ARG LYS SER LEU THR LYS
SEQRES 21 A 511 GLN LEU GLY ALA ASN GLY ILE ARG VAL ARG THR ASN LEU
SEQRES 22 A 511 ASN PRO THR LYS ILE THR LYS ASN GLU ASP GLY SER ASN
SEQRES 23 A 511 HIS VAL HIS PHE ASN ASP GLY THR GLU GLU ASP TYR ASP
SEQRES 24 A 511 GLN VAL MET LEU ALA ILE GLY ARG VAL PRO ARG SER GLN
SEQRES 25 A 511 ALA LEU GLN LEU ASP LYS ALA GLY VAL ARG THR GLY LYS
SEQRES 26 A 511 ASN GLY ALA VAL GLN VAL ASP ALA TYR SER LYS THR SER
SEQRES 27 A 511 VAL ASP ASN ILE TYR ALA ILE GLY ASP VAL THR ASN ARG
SEQRES 28 A 511 VAL MET LEU THR PRO VAL ALA ILE ASN GLU GLY ALA ALA
SEQRES 29 A 511 PHE VAL GLU THR VAL PHE GLY GLY LYS PRO ARG ALA THR
SEQRES 30 A 511 ASP HIS THR LYS VAL ALA CYS ALA VAL PHE SER ILE PRO
SEQRES 31 A 511 PRO ILE GLY THR CYS GLY MET THR GLU GLU GLU ALA ALA
SEQRES 32 A 511 LYS ASN TYR GLU THR VAL ALA VAL TYR ALA SER SER PHE
SEQRES 33 A 511 THR PRO LEU MET HIS ASN ILE SER GLY SER LYS HIS LYS
SEQRES 34 A 511 GLU PHE MET ILE ARG ILE ILE THR ASN GLU SER ASN GLY
SEQRES 35 A 511 GLU VAL LEU GLY VAL HIS MET LEU GLY ASP SER ALA PRO
SEQRES 36 A 511 GLU ILE ILE GLN SER VAL GLY ILE CYS MET LYS MET GLY
SEQRES 37 A 511 ALA LYS ILE SER ASP PHE HIS SER THR ILE GLY VAL HIS
SEQRES 38 A 511 PRO THR SER ALA GLU GLU LEU CYS SER MET ARG THR PRO
SEQRES 39 A 511 ALA TYR PHE TYR GLU SER GLY LYS ARG VAL GLU LYS LEU
SEQRES 40 A 511 SER SER ASN LEU
SEQRES 1 B 511 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 511 LEU VAL PRO ARG GLY SER HIS MET SER ARG ALA TYR ASP
SEQRES 3 B 511 LEU VAL VAL LEU GLY ALA GLY SER GLY GLY LEU GLU ALA
SEQRES 4 B 511 GLY TRP ASN ALA ALA VAL THR HIS LYS LYS LYS VAL ALA
SEQRES 5 B 511 VAL VAL ASP VAL GLN ALA THR HIS GLY PRO PRO LEU PHE
SEQRES 6 B 511 ALA ALA LEU GLY GLY THR CYS VAL ASN VAL GLY CYS VAL
SEQRES 7 B 511 PRO LYS LYS LEU MET VAL THR GLY ALA GLN TYR MET ASP
SEQRES 8 B 511 LEU ILE ARG GLU SER GLY GLY PHE GLY TRP GLU MET ASP
SEQRES 9 B 511 ARG GLU SER LEU CYS PRO ASN TRP LYS THR LEU ILE ALA
SEQRES 10 B 511 ALA LYS ASN LYS VAL VAL ASN SER ILE ASN GLU SER TYR
SEQRES 11 B 511 LYS SER MET PHE ALA ASP THR GLU GLY LEU SER PHE HIS
SEQRES 12 B 511 MET GLY PHE GLY ALA LEU GLN ASP ALA HIS THR VAL VAL
SEQRES 13 B 511 VAL ARG LYS SER GLU ASP PRO HIS SER ASP VAL LEU GLU
SEQRES 14 B 511 THR LEU ASP THR GLU TYR ILE LEU ILE ALA THR GLY SER
SEQRES 15 B 511 TRP PRO THR ARG LEU GLY VAL PRO GLY ASP GLU PHE CYS
SEQRES 16 B 511 ILE THR SER ASN GLU ALA PHE TYR LEU GLU ASP ALA PRO
SEQRES 17 B 511 LYS ARG MET LEU CYS VAL GLY GLY GLY TYR ILE ALA VAL
SEQRES 18 B 511 GLU PHE ALA GLY ILE PHE ASN GLY TYR LYS PRO CYS GLY
SEQRES 19 B 511 GLY TYR VAL ASP LEU CYS TYR ARG GLY ASP LEU ILE LEU
SEQRES 20 B 511 ARG GLY PHE ASP THR GLU VAL ARG LYS SER LEU THR LYS
SEQRES 21 B 511 GLN LEU GLY ALA ASN GLY ILE ARG VAL ARG THR ASN LEU
SEQRES 22 B 511 ASN PRO THR LYS ILE THR LYS ASN GLU ASP GLY SER ASN
SEQRES 23 B 511 HIS VAL HIS PHE ASN ASP GLY THR GLU GLU ASP TYR ASP
SEQRES 24 B 511 GLN VAL MET LEU ALA ILE GLY ARG VAL PRO ARG SER GLN
SEQRES 25 B 511 ALA LEU GLN LEU ASP LYS ALA GLY VAL ARG THR GLY LYS
SEQRES 26 B 511 ASN GLY ALA VAL GLN VAL ASP ALA TYR SER LYS THR SER
SEQRES 27 B 511 VAL ASP ASN ILE TYR ALA ILE GLY ASP VAL THR ASN ARG
SEQRES 28 B 511 VAL MET LEU THR PRO VAL ALA ILE ASN GLU GLY ALA ALA
SEQRES 29 B 511 PHE VAL GLU THR VAL PHE GLY GLY LYS PRO ARG ALA THR
SEQRES 30 B 511 ASP HIS THR LYS VAL ALA CYS ALA VAL PHE SER ILE PRO
SEQRES 31 B 511 PRO ILE GLY THR CYS GLY MET THR GLU GLU GLU ALA ALA
SEQRES 32 B 511 LYS ASN TYR GLU THR VAL ALA VAL TYR ALA SER SER PHE
SEQRES 33 B 511 THR PRO LEU MET HIS ASN ILE SER GLY SER LYS HIS LYS
SEQRES 34 B 511 GLU PHE MET ILE ARG ILE ILE THR ASN GLU SER ASN GLY
SEQRES 35 B 511 GLU VAL LEU GLY VAL HIS MET LEU GLY ASP SER ALA PRO
SEQRES 36 B 511 GLU ILE ILE GLN SER VAL GLY ILE CYS MET LYS MET GLY
SEQRES 37 B 511 ALA LYS ILE SER ASP PHE HIS SER THR ILE GLY VAL HIS
SEQRES 38 B 511 PRO THR SER ALA GLU GLU LEU CYS SER MET ARG THR PRO
SEQRES 39 B 511 ALA TYR PHE TYR GLU SER GLY LYS ARG VAL GLU LYS LEU
SEQRES 40 B 511 SER SER ASN LEU
HET FAD A1489 53
HET NDP A1490 48
HET GCG A1491 48
HET FAD B1489 53
HET NDP B1490 48
HET GCG B1491 48
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
HETNAM GCG BIS(GAMMA-GLUTAMYL-CYSTEINYL-GLYCINYL)SPERMIDINE
HETSYN GCG TRYPANOTHIONE
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 NDP 2(C21 H30 N7 O17 P3)
FORMUL 5 GCG 2(C27 H49 N9 O10 S2)
HELIX 1 1 GLY A 13 THR A 26 1 14
HELIX 2 2 GLY A 50 VAL A 55 1 6
HELIX 3 3 GLY A 56 GLY A 77 1 22
HELIX 4 4 ASN A 91 THR A 117 1 27
HELIX 5 5 GLY A 171 CYS A 175 5 5
HELIX 6 6 SER A 178 PHE A 182 1 5
HELIX 7 7 GLY A 197 LYS A 211 1 15
HELIX 8 8 ASP A 231 GLY A 246 1 16
HELIX 9 9 LEU A 296 GLY A 300 5 5
HELIX 10 10 GLY A 304 ALA A 308 5 5
HELIX 11 11 LEU A 334 PHE A 350 1 17
HELIX 12 12 THR A 378 TYR A 386 1 9
HELIX 13 13 PRO A 398 ILE A 403 5 6
HELIX 14 14 SER A 433 MET A 447 1 15
HELIX 15 15 LYS A 450 SER A 456 1 7
HELIX 16 16 SER A 464 CYS A 469 5 6
HELIX 17 17 GLY B 13 THR B 26 1 14
HELIX 18 18 GLY B 56 GLY B 77 1 22
HELIX 19 19 ASN B 91 THR B 117 1 27
HELIX 20 20 GLY B 171 CYS B 175 5 5
HELIX 21 21 SER B 178 PHE B 182 1 5
HELIX 22 22 GLY B 197 LYS B 211 1 15
HELIX 23 23 ASP B 231 ALA B 244 1 14
HELIX 24 24 GLY B 304 ALA B 308 5 5
HELIX 25 25 GLY B 326 ASN B 330 5 5
HELIX 26 26 LEU B 334 PHE B 350 1 17
HELIX 27 27 THR B 378 TYR B 386 1 9
HELIX 28 28 PRO B 398 ILE B 403 5 6
HELIX 29 29 SER B 433 MET B 447 1 15
HELIX 30 30 LYS B 450 SER B 456 1 7
HELIX 31 31 SER B 464 MET B 471 5 8
SHEET 1 AA 5 LEU A 120 MET A 124 0
SHEET 2 AA 5 VAL A 31 ASP A 35 1 O VAL A 31 N SER A 121
SHEET 3 AA 5 TYR A 5 LEU A 10 1 O LEU A 7 N ALA A 32
SHEET 4 AA 5 VAL A 147 ILE A 158 1 O ASP A 152 N TYR A 5
SHEET 5 AA 5 ILE A 322 ALA A 324 -1 O TYR A 323 N ILE A 158
SHEET 1 AB 6 LEU A 120 MET A 124 0
SHEET 2 AB 6 VAL A 31 ASP A 35 1 O VAL A 31 N SER A 121
SHEET 3 AB 6 TYR A 5 LEU A 10 1 O LEU A 7 N ALA A 32
SHEET 4 AB 6 VAL A 147 ILE A 158 1 O ASP A 152 N TYR A 5
SHEET 5 AB 6 THR A 134 ARG A 138 -1 O VAL A 135 N LEU A 151
SHEET 6 AB 6 PHE A 126 LEU A 129 -1 O PHE A 126 N ARG A 138
SHEET 1 AC 2 ILE A 322 ALA A 324 0
SHEET 2 AC 2 VAL A 147 ILE A 158 -1 O ILE A 156 N TYR A 323
SHEET 1 AD 2 TRP A 81 GLU A 82 0
SHEET 2 AD 2 CYS B 89 PRO B 90 -1 O CYS B 89 N GLU A 82
SHEET 1 AE 2 CYS A 89 PRO A 90 0
SHEET 2 AE 2 TRP B 81 GLU B 82 -1 O GLU B 82 N CYS A 89
SHEET 1 AF 2 SER A 162 PRO A 164 0
SHEET 2 AF 2 ARG A 287 PRO A 289 -1 O VAL A 288 N TRP A 163
SHEET 1 AG 5 ILE A 176 THR A 177 0
SHEET 2 AG 5 GLN A 280 LEU A 283 1 O VAL A 281 N ILE A 176
SHEET 3 AG 5 ARG A 190 VAL A 194 1 O LEU A 192 N MET A 282
SHEET 4 AG 5 TYR A 216 CYS A 220 1 O TYR A 216 N MET A 191
SHEET 5 AG 5 ILE A 247 ARG A 250 1 O ARG A 248 N LEU A 219
SHEET 1 AH 3 LYS A 257 LYS A 260 0
SHEET 2 AH 3 ASN A 266 HIS A 269 -1 O HIS A 267 N THR A 259
SHEET 3 AH 3 GLU A 275 TYR A 278 -1 O GLU A 276 N VAL A 268
SHEET 1 AI 7 ALA A 363 VAL A 366 0
SHEET 2 AI 7 ILE A 372 GLY A 376 -1 O ILE A 372 N VAL A 366
SHEET 3 AI 7 VAL A 424 LEU A 430 -1 O VAL A 427 N CYS A 375
SHEET 4 AI 7 PHE A 411 ASN A 418 -1 O MET A 412 N LEU A 430
SHEET 5 AI 7 THR A 388 PHE A 396 -1 O ALA A 390 N THR A 417
SHEET 6 AI 7 TYR A 476 GLU A 479 -1 O TYR A 476 N VAL A 391
SHEET 7 AI 7 ARG A 483 VAL A 484 -1 O VAL A 484 N PHE A 477
SHEET 1 BA 5 LEU B 120 MET B 124 0
SHEET 2 BA 5 VAL B 31 ASP B 35 1 O VAL B 31 N SER B 121
SHEET 3 BA 5 TYR B 5 LEU B 10 1 O LEU B 7 N ALA B 32
SHEET 4 BA 5 VAL B 147 ILE B 158 1 O ASP B 152 N TYR B 5
SHEET 5 BA 5 ILE B 322 ALA B 324 -1 O TYR B 323 N ILE B 158
SHEET 1 BB 6 LEU B 120 MET B 124 0
SHEET 2 BB 6 VAL B 31 ASP B 35 1 O VAL B 31 N SER B 121
SHEET 3 BB 6 TYR B 5 LEU B 10 1 O LEU B 7 N ALA B 32
SHEET 4 BB 6 VAL B 147 ILE B 158 1 O ASP B 152 N TYR B 5
SHEET 5 BB 6 THR B 134 ARG B 138 -1 O VAL B 135 N LEU B 151
SHEET 6 BB 6 PHE B 126 LEU B 129 -1 O PHE B 126 N ARG B 138
SHEET 1 BC 2 ILE B 322 ALA B 324 0
SHEET 2 BC 2 VAL B 147 ILE B 158 -1 O ILE B 156 N TYR B 323
SHEET 1 BD 2 SER B 162 PRO B 164 0
SHEET 2 BD 2 ARG B 287 PRO B 289 -1 O VAL B 288 N TRP B 163
SHEET 1 BE 5 ILE B 176 THR B 177 0
SHEET 2 BE 5 GLN B 280 LEU B 283 1 O VAL B 281 N ILE B 176
SHEET 3 BE 5 ARG B 190 VAL B 194 1 O LEU B 192 N MET B 282
SHEET 4 BE 5 TYR B 216 CYS B 220 1 O TYR B 216 N MET B 191
SHEET 5 BE 5 ILE B 247 ARG B 250 1 O ARG B 248 N LEU B 219
SHEET 1 BF 3 LYS B 257 LYS B 260 0
SHEET 2 BF 3 ASN B 266 HIS B 269 -1 O HIS B 267 N THR B 259
SHEET 3 BF 3 GLU B 275 TYR B 278 -1 O GLU B 276 N VAL B 268
SHEET 1 BG 7 ALA B 363 VAL B 366 0
SHEET 2 BG 7 ILE B 372 GLY B 376 -1 O ILE B 372 N VAL B 366
SHEET 3 BG 7 VAL B 424 LEU B 430 -1 O VAL B 427 N CYS B 375
SHEET 4 BG 7 PHE B 411 ASN B 418 -1 O MET B 412 N LEU B 430
SHEET 5 BG 7 THR B 388 PHE B 396 -1 O ALA B 390 N THR B 417
SHEET 6 BG 7 TYR B 476 GLU B 479 -1 O TYR B 476 N VAL B 391
SHEET 7 BG 7 ARG B 483 VAL B 484 -1 O VAL B 484 N PHE B 477
SITE 1 AC1 32 GLY A 11 GLY A 13 SER A 14 GLY A 15
SITE 2 AC1 32 VAL A 34 ASP A 35 VAL A 36 ALA A 46
SITE 3 AC1 32 ALA A 47 GLY A 50 THR A 51 CYS A 52
SITE 4 AC1 32 VAL A 55 GLY A 56 CYS A 57 LYS A 60
SITE 5 AC1 32 GLY A 127 ALA A 159 THR A 160 GLY A 161
SITE 6 AC1 32 ARG A 287 ARG A 290 GLY A 326 ASP A 327
SITE 7 AC1 32 MET A 333 LEU A 334 THR A 335 PRO A 336
SITE 8 AC1 32 ALA A 338 NDP A1490 HIS B 461 PRO B 462
SITE 1 AC2 33 HIS A 461 PRO A 462 GLY B 11 GLY B 13
SITE 2 AC2 33 SER B 14 GLY B 15 VAL B 34 ASP B 35
SITE 3 AC2 33 VAL B 36 ALA B 46 ALA B 47 GLY B 50
SITE 4 AC2 33 THR B 51 CYS B 52 VAL B 55 GLY B 56
SITE 5 AC2 33 CYS B 57 LYS B 60 GLY B 127 ALA B 159
SITE 6 AC2 33 THR B 160 GLY B 161 ILE B 199 ARG B 287
SITE 7 AC2 33 ARG B 290 GLY B 326 ASP B 327 MET B 333
SITE 8 AC2 33 LEU B 334 THR B 335 PRO B 336 ALA B 338
SITE 9 AC2 33 NDP B1490
SITE 1 AC3 16 GLY A 196 GLY A 197 TYR A 198 ILE A 199
SITE 2 AC3 16 GLU A 202 TYR A 221 ARG A 222 ARG A 228
SITE 3 AC3 16 ASN A 254 ALA A 284 ILE A 285 GLY A 286
SITE 4 AC3 16 MET A 333 LEU A 334 ALA A 365 FAD A1489
SITE 1 AC4 16 GLY B 196 GLY B 197 TYR B 198 ILE B 199
SITE 2 AC4 16 GLU B 202 TYR B 221 ARG B 222 ARG B 228
SITE 3 AC4 16 ASN B 254 ALA B 284 ILE B 285 GLY B 286
SITE 4 AC4 16 MET B 333 LEU B 334 ALA B 365 FAD B1489
SITE 1 AC5 7 ARG A 3 PHE A 396 LEU A 399 HIS A 461
SITE 2 AC5 7 THR A 463 GLU A 466 CYS B 52
SITE 1 AC6 9 CYS A 52 VAL A 53 ARG B 3 PHE B 396
SITE 2 AC6 9 LEU B 399 HIS B 461 THR B 463 GLU B 466
SITE 3 AC6 9 GLU B 467
CRYST1 103.940 103.940 192.244 90.00 90.00 90.00 P 41 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 0.009621 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009621 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005202 0.00000
(ATOM LINES ARE NOT SHOWN.)
END