HEADER DNA BINDING PROTEIN 08-NOV-17 6EXK
TITLE THE TRANSCRIPTIONAL REGULATOR PRFA FROM LISTERIA MONOCYTOGENES IN
TITLE 2 COMPLEX WITH A RING-FUSED 2-PYRIDONE (MK206) - UNFOLDED HTH MOTIF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LISTERIOLYSIN REGULATORY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LISTERIA MONOCYTOGENES EGD-E;
SOURCE 3 ORGANISM_TAXID: 169963;
SOURCE 4 STRAIN: ATCC BAA-679 / EGD-E;
SOURCE 5 GENE: PRFA, LMO0200;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSCRIPTION REGULATOR, DNA BINDING, 2-PYRIDONE, DRUG DESIGN,
KEYWDS 2 LISTERIA MONOCYTOGENES, DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HALL,C.GRUNDSTROM,A.BEGUM,M.KULEN,M.LINDGREN,J.JOHANSSON,
AUTHOR 2 F.ALMQVIST,U.H.SAUER,A.E.SAUER-ERIKSSON
REVDAT 4 17-JAN-24 6EXK 1 LINK
REVDAT 3 21-NOV-18 6EXK 1 LINK
REVDAT 2 23-MAY-18 6EXK 1 JRNL
REVDAT 1 02-MAY-18 6EXK 0
JRNL AUTH M.KULEN,M.LINDGREN,S.HANSEN,A.G.CAIRNS,C.GRUNDSTROM,A.BEGUM,
JRNL AUTH 2 I.VAN DER LINGEN,K.BRANNSTROM,M.HALL,U.H.SAUER,J.JOHANSSON,
JRNL AUTH 3 A.E.SAUER-ERIKSSON,F.ALMQVIST
JRNL TITL STRUCTURE-BASED DESIGN OF INHIBITORS TARGETING PRFA, THE
JRNL TITL 2 MASTER VIRULENCE REGULATOR OF LISTERIA MONOCYTOGENES.
JRNL REF J. MED. CHEM. V. 61 4165 2018
JRNL REFN ISSN 1520-4804
JRNL PMID 29667825
JRNL DOI 10.1021/ACS.JMEDCHEM.8B00289
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.A.GOOD,C.ANDERSSON,S.HANSEN,J.WALL,K.S.KRISHNAN,A.BEGUM,
REMARK 1 AUTH 2 C.GRUNDSTROM,M.S.NIEMIEC,K.VAITKEVICIUS,E.CHORELL,
REMARK 1 AUTH 3 P.WITTUNG-STAFSHEDE,U.H.SAUER,A.E.SAUER-ERIKSSON,F.ALMQVIST,
REMARK 1 AUTH 4 J.JOHANSSON
REMARK 1 TITL ATTENUATING LISTERIA MONOCYTOGENES VIRULENCE BY TARGETING
REMARK 1 TITL 2 THE REGULATORY PROTEIN PRFA.
REMARK 1 REF CELL CHEM BIOL V. 23 404 2016
REMARK 1 REFN ESSN 2451-9456
REMARK 1 PMID 26991105
REMARK 1 DOI 10.1016/J.CHEMBIOL.2016.02.013
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.90
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 29794
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 1469
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 47.9074 - 4.5233 1.00 3015 156 0.1590 0.1832
REMARK 3 2 4.5233 - 3.5906 1.00 2867 161 0.1613 0.2292
REMARK 3 3 3.5906 - 3.1369 1.00 2848 146 0.2127 0.2616
REMARK 3 4 3.1369 - 2.8501 1.00 2809 144 0.2330 0.2799
REMARK 3 5 2.8501 - 2.6458 1.00 2816 145 0.2342 0.3462
REMARK 3 6 2.6458 - 2.4898 1.00 2824 139 0.2552 0.3270
REMARK 3 7 2.4898 - 2.3652 1.00 2783 159 0.2454 0.3105
REMARK 3 8 2.3652 - 2.2622 1.00 2792 136 0.2399 0.3231
REMARK 3 9 2.2622 - 2.1751 1.00 2770 131 0.2536 0.3320
REMARK 3 10 2.1751 - 2.1001 1.00 2801 152 0.2804 0.3520
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.390
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 : 0.015 3954
REMARK 3 ANGLE : 1.302 5350
REMARK 3 CHIRALITY : 0.068 578
REMARK 3 PLANARITY : 0.008 660
REMARK 3 DIHEDRAL : 15.549 2316
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 6EXK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1200007414.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.992
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29801
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 47.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.10
REMARK 200 R MERGE FOR SHELL (I) : 0.97800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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: 5F1R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PRFA WAS CO-CRYSTALLIZED WITH COMPLEX
REMARK 280 (5 MOL EXCESS) USING THE HANGING-DROP VAPOR-DIFFUSION TECHNIQUE.
REMARK 280 CRYSTALS GREW IN 5 DAYS AFTER 2 MICROL OF THE PROTEIN SOLUTION
REMARK 280 (3.2-3.5 MG PER ML PRFA, 200 MM NACL, 20 MM NAP BUFFER, PH 6.5)
REMARK 280 WAS MIXED WITH AN EQUAL VOLUME OF PRECIPITANT SOLUTION
REMARK 280 CONTAINING 20-24% PEG-4000, 17% ISOPROPANOL, 100 MM NA CITRATE
REMARK 280 PH 5.5 AND ALLOWED TO EQUILIBRATE OVER A 1 ML SOLUTION OF THE
REMARK 280 PRECIPITANT IN A LINBRO PLATE (HAMPTON RESEARCH)., VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 46.07600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.16300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.07600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.16300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 SER A 177
REMARK 465 SER A 178
REMARK 465 GLY A 179
REMARK 465 ILE A 180
REMARK 465 ALA A 181
REMARK 465 GLY B -1
REMARK 465 ALA B 0
REMARK 465 SER B 177
REMARK 465 SER B 178
REMARK 465 GLY B 179
REMARK 465 ILE B 180
REMARK 465 ALA B 181
REMARK 465 HIS B 182
REMARK 465 SER B 183
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 24 129.78 -38.87
REMARK 500 LYS A 25 -2.21 85.68
REMARK 500 GLN A 61 137.00 -170.26
REMARK 500 ASN A 109 83.66 -162.70
REMARK 500 LYS B 25 1.82 83.10
REMARK 500 THR B 165 38.91 -91.42
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 A 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 30 O
REMARK 620 2 GLU A 36 OE1 170.0
REMARK 620 3 HOH A 405 O 100.1 83.5
REMARK 620 4 HOH A 418 O 95.1 75.1 119.3
REMARK 620 5 HOH A 423 O 93.4 95.1 101.4 136.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 30 O
REMARK 620 2 GLU B 36 OE1 175.8
REMARK 620 3 HOH B 408 O 102.8 80.6
REMARK 620 4 HOH B 427 O 91.1 90.4 104.9
REMARK 620 5 HOH B 434 O 93.7 82.3 122.0 130.3
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue C2Q A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue C2Q B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA B 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5F1R RELATED DB: PDB
DBREF 6EXK A 1 237 UNP P22262 PRFA_LISMO 1 237
DBREF 6EXK B 1 237 UNP P22262 PRFA_LISMO 1 237
SEQADV 6EXK GLY A -1 UNP P22262 EXPRESSION TAG
SEQADV 6EXK ALA A 0 UNP P22262 EXPRESSION TAG
SEQADV 6EXK GLY B -1 UNP P22262 EXPRESSION TAG
SEQADV 6EXK ALA B 0 UNP P22262 EXPRESSION TAG
SEQRES 1 A 239 GLY ALA MET ASN ALA GLN ALA GLU GLU PHE LYS LYS TYR
SEQRES 2 A 239 LEU GLU THR ASN GLY ILE LYS PRO LYS GLN PHE HIS LYS
SEQRES 3 A 239 LYS GLU LEU ILE PHE ASN GLN TRP ASP PRO GLN GLU TYR
SEQRES 4 A 239 CYS ILE PHE LEU TYR ASP GLY ILE THR LYS LEU THR SER
SEQRES 5 A 239 ILE SER GLU ASN GLY THR ILE MET ASN LEU GLN TYR TYR
SEQRES 6 A 239 LYS GLY ALA PHE VAL ILE MET SER GLY PHE ILE ASP THR
SEQRES 7 A 239 GLU THR SER VAL GLY TYR TYR ASN LEU GLU VAL ILE SER
SEQRES 8 A 239 GLU GLN ALA THR ALA TYR VAL ILE LYS ILE ASN GLU LEU
SEQRES 9 A 239 LYS GLU LEU LEU SER LYS ASN LEU THR HIS PHE PHE TYR
SEQRES 10 A 239 VAL PHE GLN THR LEU GLN LYS GLN VAL SER TYR SER LEU
SEQRES 11 A 239 ALA LYS PHE ASN ASP PHE SER ILE ASN GLY LYS LEU GLY
SEQRES 12 A 239 SER ILE CYS GLY GLN LEU LEU ILE LEU THR TYR VAL TYR
SEQRES 13 A 239 GLY LYS GLU THR PRO ASP GLY ILE LYS ILE THR LEU ASP
SEQRES 14 A 239 ASN LEU THR MET GLN GLU LEU GLY TYR SER SER GLY ILE
SEQRES 15 A 239 ALA HIS SER SER ALA VAL SER ARG ILE ILE SER LYS LEU
SEQRES 16 A 239 LYS GLN GLU LYS VAL ILE VAL TYR LYS ASN SER CYS PHE
SEQRES 17 A 239 TYR VAL GLN ASN LEU ASP TYR LEU LYS ARG TYR ALA PRO
SEQRES 18 A 239 LYS LEU ASP GLU TRP PHE TYR LEU ALA CYS PRO ALA THR
SEQRES 19 A 239 TRP GLY LYS LEU ASN
SEQRES 1 B 239 GLY ALA MET ASN ALA GLN ALA GLU GLU PHE LYS LYS TYR
SEQRES 2 B 239 LEU GLU THR ASN GLY ILE LYS PRO LYS GLN PHE HIS LYS
SEQRES 3 B 239 LYS GLU LEU ILE PHE ASN GLN TRP ASP PRO GLN GLU TYR
SEQRES 4 B 239 CYS ILE PHE LEU TYR ASP GLY ILE THR LYS LEU THR SER
SEQRES 5 B 239 ILE SER GLU ASN GLY THR ILE MET ASN LEU GLN TYR TYR
SEQRES 6 B 239 LYS GLY ALA PHE VAL ILE MET SER GLY PHE ILE ASP THR
SEQRES 7 B 239 GLU THR SER VAL GLY TYR TYR ASN LEU GLU VAL ILE SER
SEQRES 8 B 239 GLU GLN ALA THR ALA TYR VAL ILE LYS ILE ASN GLU LEU
SEQRES 9 B 239 LYS GLU LEU LEU SER LYS ASN LEU THR HIS PHE PHE TYR
SEQRES 10 B 239 VAL PHE GLN THR LEU GLN LYS GLN VAL SER TYR SER LEU
SEQRES 11 B 239 ALA LYS PHE ASN ASP PHE SER ILE ASN GLY LYS LEU GLY
SEQRES 12 B 239 SER ILE CYS GLY GLN LEU LEU ILE LEU THR TYR VAL TYR
SEQRES 13 B 239 GLY LYS GLU THR PRO ASP GLY ILE LYS ILE THR LEU ASP
SEQRES 14 B 239 ASN LEU THR MET GLN GLU LEU GLY TYR SER SER GLY ILE
SEQRES 15 B 239 ALA HIS SER SER ALA VAL SER ARG ILE ILE SER LYS LEU
SEQRES 16 B 239 LYS GLN GLU LYS VAL ILE VAL TYR LYS ASN SER CYS PHE
SEQRES 17 B 239 TYR VAL GLN ASN LEU ASP TYR LEU LYS ARG TYR ALA PRO
SEQRES 18 B 239 LYS LEU ASP GLU TRP PHE TYR LEU ALA CYS PRO ALA THR
SEQRES 19 B 239 TRP GLY LYS LEU ASN
HET C2Q A 301 28
HET NA A 302 1
HET IPA A 303 4
HET C2Q B 301 28
HET NA B 302 1
HET IPA B 303 4
HETNAM C2Q [(3~{R})-3-CARBOXY-7-[(4-METHYLNAPHTHALEN-1-YL)METHYL]-
HETNAM 2 C2Q 5-OXIDANYLIDENE-2,3-DIHYDRO-[1,3]THIAZOLO[3,2-
HETNAM 3 C2Q A]PYRIDIN-8-YL]-DIMETHYL-AZANIUM
HETNAM NA SODIUM ION
HETNAM IPA ISOPROPYL ALCOHOL
HETSYN IPA 2-PROPANOL
FORMUL 3 C2Q 2(C22 H23 N2 O3 S 1+)
FORMUL 4 NA 2(NA 1+)
FORMUL 5 IPA 2(C3 H8 O)
FORMUL 9 HOH *82(H2 O)
HELIX 1 AA1 ALA A 3 ASN A 15 1 13
HELIX 2 AA2 ILE A 99 LYS A 108 1 10
HELIX 3 AA3 ASN A 109 TYR A 154 1 46
HELIX 4 AA4 ASP A 167 LEU A 174 1 8
HELIX 5 AA5 SER A 183 LYS A 197 1 15
HELIX 6 AA6 ASN A 210 ALA A 218 1 9
HELIX 7 AA7 ALA A 218 CYS A 229 1 12
HELIX 8 AA8 CYS A 229 LEU A 236 1 8
HELIX 9 AA9 ASN B 2 THR B 14 1 13
HELIX 10 AB1 ILE B 99 LYS B 108 1 10
HELIX 11 AB2 ASN B 109 TYR B 154 1 46
HELIX 12 AB3 ASP B 167 LEU B 174 1 8
HELIX 13 AB4 ALA B 185 GLU B 196 1 12
HELIX 14 AB5 ASN B 210 ALA B 218 1 9
HELIX 15 AB6 ALA B 218 CYS B 229 1 12
HELIX 16 AB7 CYS B 229 LYS B 235 1 7
SHEET 1 AA1 4 PRO A 19 HIS A 23 0
SHEET 2 AA1 4 GLN A 91 LYS A 98 -1 O ALA A 94 N LYS A 20
SHEET 3 AA1 4 TYR A 37 ASP A 43 -1 N CYS A 38 O ILE A 97
SHEET 4 AA1 4 PHE A 67 MET A 70 -1 O PHE A 67 N LEU A 41
SHEET 1 AA2 4 LEU A 27 PHE A 29 0
SHEET 2 AA2 4 ASN A 84 VAL A 87 -1 O LEU A 85 N ILE A 28
SHEET 3 AA2 4 ILE A 45 SER A 50 -1 N LYS A 47 O GLU A 86
SHEET 4 AA2 4 MET A 58 LYS A 64 -1 O GLN A 61 N LEU A 48
SHEET 1 AA3 4 GLY A 155 THR A 158 0
SHEET 2 AA3 4 GLY A 161 ILE A 164 -1 O LYS A 163 N LYS A 156
SHEET 3 AA3 4 PHE A 206 VAL A 208 -1 O VAL A 208 N ILE A 162
SHEET 4 AA3 4 ILE A 199 TYR A 201 -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 CYS B 38 O ILE B 97
SHEET 4 AA4 4 PHE B 67 MET B 70 -1 O ILE B 69 N ILE B 39
SHEET 1 AA5 4 LEU B 27 PHE B 29 0
SHEET 2 AA5 4 ASN B 84 VAL B 87 -1 O LEU B 85 N ILE B 28
SHEET 3 AA5 4 ILE B 45 ILE B 51 -1 N THR B 49 O ASN B 84
SHEET 4 AA5 4 ILE B 57 LYS B 64 -1 O GLN B 61 N LEU B 48
SHEET 1 AA6 4 GLY B 155 THR B 158 0
SHEET 2 AA6 4 GLY B 161 ILE B 164 -1 O GLY B 161 N THR B 158
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
LINK O ASN A 30 NA NA A 302 1555 1555 2.42
LINK OE1 GLU A 36 NA NA A 302 1555 1555 2.65
LINK NA NA A 302 O HOH A 405 1555 1555 2.22
LINK NA NA A 302 O HOH A 418 1555 1555 2.52
LINK NA NA A 302 O HOH A 423 1555 1555 2.42
LINK O ASN B 30 NA NA B 302 1555 1555 2.37
LINK OE1 GLU B 36 NA NA B 302 1555 1555 2.60
LINK NA NA B 302 O HOH B 408 1555 1555 2.25
LINK NA NA B 302 O HOH B 427 1555 1555 2.48
LINK NA NA B 302 O HOH B 434 1555 1555 2.34
CISPEP 1 GLY A 65 ALA A 66 0 -5.50
CISPEP 2 GLY B 65 ALA B 66 0 1.68
SITE 1 AC1 13 GLN A 61 TYR A 62 TYR A 63 LYS A 64
SITE 2 AC1 13 PHE A 67 LYS A 122 TYR A 126 GLN A 146
SITE 3 AC1 13 LEU A 150 VAL A 153 TRP A 224 HOH A 431
SITE 4 AC1 13 HOH A 433
SITE 1 AC2 6 ASN A 30 ASP A 33 GLU A 36 HOH A 405
SITE 2 AC2 6 HOH A 418 HOH A 423
SITE 1 AC3 5 TYR A 63 MET A 70 GLN A 123 VAL B 124
SITE 2 AC3 5 LEU B 128
SITE 1 AC4 13 GLN B 61 TYR B 62 TYR B 63 LYS B 64
SITE 2 AC4 13 PHE B 67 LYS B 122 TYR B 126 ILE B 149
SITE 3 AC4 13 LEU B 150 TRP B 224 CYS B 229 HOH B 416
SITE 4 AC4 13 HOH B 432
SITE 1 AC5 5 ASN B 30 GLU B 36 HOH B 408 HOH B 427
SITE 2 AC5 5 HOH B 434
SITE 1 AC6 6 LEU A 128 HOH A 435 TYR B 63 ILE B 69
SITE 2 AC6 6 MET B 70 VAL B 80
CRYST1 92.152 112.326 47.895 90.00 90.00 90.00 P 21 21 2 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 0.010852 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008903 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020879 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
