HEADER TRANSCRIPTION 19-AUG-16 5LRS
TITLE THE TRANSCRIPTIONAL REGULATOR PRFA FROM LISTERIA MONOCYTOGENES IN
TITLE 2 COMPLEX WITH GLUTATHIONE AND A 30-BP OPERATOR PRFA-BOX MOTIF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LISTERIOLYSIN POSITIVE REGULATORY FACTOR A;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LISTERIOLYSIN POSITIVE REGULATORY PROTEIN,LISTERIOLYSIN
COMPND 5 REGULATORY PROTEIN,PLEITROPHIC REGULATORY FACTOR A,POSITIVE
COMPND 6 REGULATORY FACTOR A,PRFA;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DNA (30-MER);
COMPND 10 CHAIN: C;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: DNA (30-MER);
COMPND 14 CHAIN: D;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LISTERIA MONOCYTOGENES;
SOURCE 3 ORGANISM_TAXID: 1639;
SOURCE 4 GENE: PRFA, M643_11230;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES;
SOURCE 9 ORGANISM_SCIENTIFIC: LISTERIA MONOCYTOGENES;
SOURCE 10 ORGANISM_TAXID: 1639;
SOURCE 11 MOL_ID: 3;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: LISTERIA MONOCYTOGENES;
SOURCE 14 ORGANISM_TAXID: 1639
KEYWDS TRANSCRIPTION REGULATOR, DNA BINDING, ACTIVATION, GLUTATHIONE,
KEYWDS 2 LISTERIA MONOCYTOGENES, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HALL,C.GRUNDSTROM,A.BEGUM,M.LINDBERG,U.H.SAUER,F.ALMQVIST,
AUTHOR 2 J.JOHANSSON,A.E.SAUER-ERIKSSON
REVDAT 5 17-JAN-24 5LRS 1 REMARK
REVDAT 4 13-SEP-17 5LRS 1 REMARK
REVDAT 3 11-JAN-17 5LRS 1 JRNL
REVDAT 2 21-DEC-16 5LRS 1 JRNL
REVDAT 1 07-DEC-16 5LRS 0
JRNL AUTH M.HALL,C.GRUNDSTROM,A.BEGUM,M.J.LINDBERG,U.H.SAUER,
JRNL AUTH 2 F.ALMQVIST,J.JOHANSSON,A.E.SAUER-ERIKSSON
JRNL TITL STRUCTURAL BASIS FOR GLUTATHIONE-MEDIATED ACTIVATION OF THE
JRNL TITL 2 VIRULENCE REGULATORY PROTEIN PRFA IN LISTERIA.
JRNL REF PROC. NATL. ACAD. SCI. V. 113 14733 2016
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 27930316
JRNL DOI 10.1073/PNAS.1614028114
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 19374
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.250
REMARK 3 R VALUE (WORKING SET) : 0.248
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.820
REMARK 3 FREE R VALUE TEST SET COUNT : 933
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 54.6460 - 5.5458 0.99 2838 146 0.2223 0.2335
REMARK 3 2 5.5458 - 4.4025 1.00 2685 130 0.2291 0.2682
REMARK 3 3 4.4025 - 3.8462 1.00 2637 132 0.2380 0.2682
REMARK 3 4 3.8462 - 3.4946 0.99 2591 137 0.2550 0.3239
REMARK 3 5 3.4946 - 3.2441 0.98 2554 140 0.2811 0.3137
REMARK 3 6 3.2441 - 3.0529 0.98 2557 111 0.3042 0.3470
REMARK 3 7 3.0529 - 2.9000 1.00 2579 137 0.3391 0.3538
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.420
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.970
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 5338
REMARK 3 ANGLE : 0.530 7470
REMARK 3 CHIRALITY : 0.039 826
REMARK 3 PLANARITY : 0.002 728
REMARK 3 DIHEDRAL : 17.640 2924
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5LRS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1200001251.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.073
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19427
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 58.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 25.60
REMARK 200 R MERGE (I) : 0.17600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 26.20
REMARK 200 R MERGE FOR SHELL (I) : 1.21800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2BGC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PRIOR TO THE CRYSTALLIZATION SETUP GSH
REMARK 280 AND DTT WERE ADDED TO THE PROTEIN SOLUTION TO FINAL
REMARK 280 CONCENTRATIONS OF 5 MM AND 1 MM, RESPECTIVELY. PROTEIN AND
REMARK 280 DUPLEX DNA WERE INCUBATED TOGETHER AT A RATIO OF 1:1.3 (PRFA
REMARK 280 DIMER:HLY DNA) AT FINAL CONCENTRATIONS OF 50 MICROM AND 70
REMARK 280 MICROM RESPECTIVELY IN 20 MM TRIS-HCL PH 8.0, 150 MM NACL, 1 MM
REMARK 280 DTT FOR 60 MIN AT ROOM TEMPERATURE, BEFORE BEING USED FOR
REMARK 280 CRYSTAL SETUPS. CRYSTALS WERE OBTAINED AFTER 24 H BY MIXING 4
REMARK 280 MICROL PROTEIN-DNA SOLUTION WITH 2 MICROL RESERVOIR SOLUTION
REMARK 280 CONSISTING OF 8% PEG 8000, 100 MM SODIUM ACETATE PH 4.6, 100 MM
REMARK 280 MAGNESIUM ACETATE, 20% GLYCEROL. PRIOR TO VITRIFICATION THE
REMARK 280 SOAKING OF PRFAWT-DNA CRYSTALS WERE SOAKED IN A RESERVOIR
REMARK 280 SOLUTION CONTAINING 30% GLYCEROL AND 100 MM GSH FOR 24 H., VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 132.61200
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.48050
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.48050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 198.91800
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.48050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.48050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 66.30600
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.48050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.48050
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 198.91800
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.48050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.48050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 66.30600
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 132.61200
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -100.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 MET A 1
REMARK 465 MET B 1
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 HH TYR A 63 OE1 GLN A 123 1.55
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 LYS A 25 -7.65 72.49
REMARK 500 ASP A 33 79.58 -118.59
REMARK 500 LEU A 41 101.91 -56.96
REMARK 500 GLN A 61 175.44 178.30
REMARK 500 ASP A 75 -70.85 -86.39
REMARK 500 ASN B 15 39.33 -94.07
REMARK 500 PHE B 40 79.47 -107.38
REMARK 500 LEU B 41 103.90 -58.56
REMARK 500 GLN B 61 157.86 174.93
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 GSH A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GSH B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BEO RELATED DB: PDB
REMARK 900 2BEO CONTAINS THE NATIVE PROTEIN
DBREF 5LRS A 1 237 UNP Q4TVQ0 Q4TVQ0_LISMN 1 237
DBREF 5LRS B 1 237 UNP Q4TVQ0 Q4TVQ0_LISMN 1 237
DBREF 5LRS C -15 15 PDB 5LRS 5LRS -15 15
DBREF 5LRS D -15 15 PDB 5LRS 5LRS -15 15
SEQRES 1 A 237 MET ASN ALA GLN ALA GLU GLU PHE LYS LYS TYR LEU GLU
SEQRES 2 A 237 THR ASN GLY ILE LYS PRO LYS GLN PHE HIS LYS LYS GLU
SEQRES 3 A 237 LEU ILE PHE ASN GLN TRP ASP PRO GLN GLU TYR CYS ILE
SEQRES 4 A 237 PHE LEU TYR ASP GLY ILE THR LYS LEU THR SER ILE SER
SEQRES 5 A 237 GLU ASN GLY THR ILE MET ASN LEU GLN TYR TYR LYS GLY
SEQRES 6 A 237 ALA PHE VAL ILE MET SER GLY PHE ILE ASP THR GLU THR
SEQRES 7 A 237 SER VAL GLY TYR TYR ASN LEU GLU VAL ILE SER GLU GLN
SEQRES 8 A 237 ALA THR ALA TYR VAL ILE LYS ILE ASN GLU LEU LYS GLU
SEQRES 9 A 237 LEU LEU SER LYS ASN LEU THR HIS PHE PHE TYR VAL PHE
SEQRES 10 A 237 GLN THR LEU GLN LYS GLN VAL SER TYR SER LEU ALA LYS
SEQRES 11 A 237 PHE ASN ASP PHE SER ILE ASN GLY LYS LEU GLY SER ILE
SEQRES 12 A 237 CYS GLY GLN LEU LEU ILE LEU THR TYR VAL TYR GLY LYS
SEQRES 13 A 237 GLU THR PRO ASP GLY ILE LYS ILE THR LEU ASP ASN LEU
SEQRES 14 A 237 THR MET GLN GLU LEU GLY TYR SER SER GLY ILE ALA HIS
SEQRES 15 A 237 SER SER ALA VAL SER ARG ILE ILE SER LYS LEU LYS GLN
SEQRES 16 A 237 GLU LYS VAL ILE VAL TYR LYS ASN SER CYS PHE TYR VAL
SEQRES 17 A 237 GLN ASN LEU ASP TYR LEU LYS ARG TYR ALA PRO LYS LEU
SEQRES 18 A 237 ASP GLU TRP PHE TYR LEU ALA CYS PRO ALA THR TRP GLY
SEQRES 19 A 237 LYS LEU ASN
SEQRES 1 B 237 MET ASN ALA GLN ALA GLU GLU PHE LYS LYS TYR LEU GLU
SEQRES 2 B 237 THR ASN GLY ILE LYS PRO LYS GLN PHE HIS LYS LYS GLU
SEQRES 3 B 237 LEU ILE PHE ASN GLN TRP ASP PRO GLN GLU TYR CYS ILE
SEQRES 4 B 237 PHE LEU TYR ASP GLY ILE THR LYS LEU THR SER ILE SER
SEQRES 5 B 237 GLU ASN GLY THR ILE MET ASN LEU GLN TYR TYR LYS GLY
SEQRES 6 B 237 ALA PHE VAL ILE MET SER GLY PHE ILE ASP THR GLU THR
SEQRES 7 B 237 SER VAL GLY TYR TYR ASN LEU GLU VAL ILE SER GLU GLN
SEQRES 8 B 237 ALA THR ALA TYR VAL ILE LYS ILE ASN GLU LEU LYS GLU
SEQRES 9 B 237 LEU LEU SER LYS ASN LEU THR HIS PHE PHE TYR VAL PHE
SEQRES 10 B 237 GLN THR LEU GLN LYS GLN VAL SER TYR SER LEU ALA LYS
SEQRES 11 B 237 PHE ASN ASP PHE SER ILE ASN GLY LYS LEU GLY SER ILE
SEQRES 12 B 237 CYS GLY GLN LEU LEU ILE LEU THR TYR VAL TYR GLY LYS
SEQRES 13 B 237 GLU THR PRO ASP GLY ILE LYS ILE THR LEU ASP ASN LEU
SEQRES 14 B 237 THR MET GLN GLU LEU GLY TYR SER SER GLY ILE ALA HIS
SEQRES 15 B 237 SER SER ALA VAL SER ARG ILE ILE SER LYS LEU LYS GLN
SEQRES 16 B 237 GLU LYS VAL ILE VAL TYR LYS ASN SER CYS PHE TYR VAL
SEQRES 17 B 237 GLN ASN LEU ASP TYR LEU LYS ARG TYR ALA PRO LYS LEU
SEQRES 18 B 237 ASP GLU TRP PHE TYR LEU ALA CYS PRO ALA THR TRP GLY
SEQRES 19 B 237 LYS LEU ASN
SEQRES 1 C 30 DT DT DG DA DG DG DC DA DT DT DA DA DC
SEQRES 2 C 30 DA DT DT DT DG DT DT DA DA DC DG DA DC
SEQRES 3 C 30 DG DA DT DA
SEQRES 1 D 30 DT DA DT DC DG DT DC DG DT DT DA DA DC
SEQRES 2 D 30 DA DA DA DT DG DT DT DA DA DT DG DC DC
SEQRES 3 D 30 DT DC DA DA
HET GSH A 301 35
HET GSH B 301 35
HETNAM GSH GLUTATHIONE
FORMUL 5 GSH 2(C10 H17 N3 O6 S)
FORMUL 7 HOH *15(H2 O)
HELIX 1 AA1 ASN A 2 ASN A 15 1 14
HELIX 2 AA2 LYS A 98 ASN A 109 1 12
HELIX 3 AA3 ASN A 109 ASN A 137 1 29
HELIX 4 AA4 ASN A 137 TYR A 154 1 18
HELIX 5 AA5 THR A 170 SER A 178 1 9
HELIX 6 AA6 HIS A 182 GLU A 196 1 15
HELIX 7 AA7 ASN A 210 ALA A 218 1 9
HELIX 8 AA8 ALA A 218 ALA A 228 1 11
HELIX 9 AA9 CYS A 229 LYS A 235 1 7
HELIX 10 AB1 ALA B 3 ASN B 15 1 13
HELIX 11 AB2 ILE B 99 ASN B 109 1 11
HELIX 12 AB3 ASN B 109 ASN B 137 1 29
HELIX 13 AB4 ASN B 137 TYR B 154 1 18
HELIX 14 AB5 THR B 170 SER B 178 1 9
HELIX 15 AB6 HIS B 182 GLU B 196 1 15
HELIX 16 AB7 ASN B 210 ALA B 218 1 9
HELIX 17 AB8 ALA B 218 CYS B 229 1 12
HELIX 18 AB9 CYS B 229 LYS B 235 1 7
SHEET 1 AA1 4 LYS A 20 HIS A 23 0
SHEET 2 AA1 4 GLN A 91 TYR A 95 -1 O ALA A 94 N LYS A 20
SHEET 3 AA1 4 CYS A 38 ASP A 43 -1 N ASP A 43 O THR A 93
SHEET 4 AA1 4 ILE A 69 MET A 70 -1 O ILE A 69 N ILE A 39
SHEET 1 AA2 3 ILE A 57 LYS A 64 0
SHEET 2 AA2 3 ILE A 45 ILE A 51 -1 N LEU A 48 O LEU A 60
SHEET 3 AA2 3 ASN A 84 VAL A 87 -1 O ASN A 84 N THR A 49
SHEET 1 AA3 4 GLY A 155 THR A 158 0
SHEET 2 AA3 4 GLY A 161 ILE A 164 -1 O GLY A 161 N THR A 158
SHEET 3 AA3 4 CYS A 205 VAL A 208 -1 O PHE A 206 N ILE A 164
SHEET 4 AA3 4 ILE A 199 LYS A 202 -1 N VAL A 200 O TYR A 207
SHEET 1 AA4 4 LYS B 20 HIS B 23 0
SHEET 2 AA4 4 GLN B 91 LYS B 98 -1 O ALA B 92 N PHE B 22
SHEET 3 AA4 4 TYR B 37 ASP B 43 -1 N ASP B 43 O THR B 93
SHEET 4 AA4 4 ILE B 69 MET B 70 -1 O ILE B 69 N ILE B 39
SHEET 1 AA5 3 ILE B 57 LYS B 64 0
SHEET 2 AA5 3 ILE B 45 ILE B 51 -1 N LEU B 48 O GLN B 61
SHEET 3 AA5 3 ASN B 84 VAL B 87 -1 O ASN B 84 N THR B 49
SHEET 1 AA6 4 GLY B 155 GLU B 157 0
SHEET 2 AA6 4 ILE B 162 ILE B 164 -1 O LYS B 163 N LYS B 156
SHEET 3 AA6 4 CYS B 205 VAL B 208 -1 O VAL B 208 N ILE B 162
SHEET 4 AA6 4 ILE B 199 LYS B 202 -1 N VAL B 200 O TYR B 207
CISPEP 1 GLY A 65 ALA A 66 0 0.20
CISPEP 2 GLY B 65 ALA B 66 0 0.73
SITE 1 AC1 16 GLN A 61 TYR A 62 TYR A 63 LYS A 64
SITE 2 AC1 16 GLY A 65 ALA A 66 PHE A 67 LYS A 122
SITE 3 AC1 16 GLN A 123 TYR A 126 ILE A 149 TYR A 154
SITE 4 AC1 16 TRP A 224 CYS A 229 HOH A 402 HOH A 405
SITE 1 AC2 11 GLN B 61 TYR B 62 TYR B 63 LYS B 64
SITE 2 AC2 11 ALA B 66 PHE B 67 TYR B 126 ILE B 149
SITE 3 AC2 11 CYS B 229 HOH B 402 HOH B 403
CRYST1 78.961 78.961 265.224 90.00 90.00 90.00 P 43 21 2 16
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 0.012664 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012664 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003770 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
