HEADER TRANSCRIPTION 29-JUN-16 5LEK
TITLE THE TRANSCRIPTIONAL REGULATOR PRFA-G145S MUTANT FROM LISTERIA
TITLE 2 MONOCYTOGENES IN COMPLEX WITH A 30-BP OPERATOR PRFA-BOX MOTIF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LISTERIOLYSIN REGULATORY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA (30-MER);
COMPND 7 CHAIN: C;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: DNA (30-MER);
COMPND 11 CHAIN: D;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LISTERIA MONOCYTOGENES SEROVAR 1/2A (STRAIN
SOURCE 3 ATCC BAA-679 / EGD-E);
SOURCE 4 ORGANISM_TAXID: 169963;
SOURCE 5 GENE: PRFA, LMO0200;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: LISTERIA MONOCYTOGENES;
SOURCE 11 ORGANISM_TAXID: 1639;
SOURCE 12 MOL_ID: 3;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 ORGANISM_SCIENTIFIC: LISTERIA MONOCYTOGENES;
SOURCE 15 ORGANISM_TAXID: 1639
KEYWDS TRANSCRIPTION REGULATOR, DNA BINDING, ACTIVATION, LISTERIA
KEYWDS 2 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 10-JAN-24 5LEK 1 REMARK
REVDAT 4 13-SEP-17 5LEK 1 REMARK
REVDAT 3 11-JAN-17 5LEK 1 JRNL
REVDAT 2 21-DEC-16 5LEK 1 JRNL
REVDAT 1 07-DEC-16 5LEK 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. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 21616
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 1088
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 47.3038 - 5.5937 0.99 2781 137 0.1895 0.2295
REMARK 3 2 5.5937 - 4.4410 1.00 2646 123 0.2067 0.2207
REMARK 3 3 4.4410 - 3.8799 1.00 2574 147 0.2207 0.2288
REMARK 3 4 3.8799 - 3.5253 0.99 2544 133 0.2426 0.3145
REMARK 3 5 3.5253 - 3.2727 0.99 2498 137 0.2544 0.2804
REMARK 3 6 3.2727 - 3.0798 0.98 2507 127 0.2959 0.3245
REMARK 3 7 3.0798 - 2.9256 0.99 2479 143 0.3407 0.3856
REMARK 3 8 2.9256 - 2.7982 0.99 2499 141 0.3687 0.4455
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) : 0.500
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.240
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 : 0.004 5312
REMARK 3 ANGLE : 0.761 7438
REMARK 3 CHIRALITY : 0.050 825
REMARK 3 PLANARITY : 0.004 721
REMARK 3 DIHEDRAL : 17.032 2928
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 5LEK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1200000624.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JAN-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 : 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) : 0.8729
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 : 21616
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 47.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 1.28100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
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 (%): 56.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AND DUPLEX DNA WERE INCUBATED
REMARK 280 TOGETHER AT A RATIO OF 1:1.3 (PRFA DIMER:HLY DNA) AT FINAL
REMARK 280 CONCENTRATIONS OF 50 MICROM AND 70 MICROM RESPECTIVELY IN 20 MM
REMARK 280 TRIS-HCL PH 8.0, 150 MM NACL, 1 MM DTT FOR 60 MIN AT ROOM
REMARK 280 TEMPERATURE, BEFORE BEING USED FOR CRYSTAL SETUPS. CRYSTALS WERE
REMARK 280 OBTAINED AFTER 24 H BY MIXING 4 MICROL PROTEIN-DNA SOLUTION WITH
REMARK 280 2 MICROL RESERVOIR SOLUTION CONSISTING OF 8% PEG 8000, 100 MM
REMARK 280 SODIUM ACETATE PH 4.6, 100 MM MAGNESIUM ACETATE, 20% GLYCEROL.
REMARK 280 PRIOR TO VITRIFICATION THE SOAKING OF PRFAG145S-DNA CRYSTALS
REMARK 280 WERE SOAKED IN A RESERVOIR SOLUTION CONTAINING 30% GLYCEROL FOR
REMARK 280 24 H, PH 5.5, VAPOR DIFFUSION, HANGING 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 132.98900
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.54050
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.54050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 199.48350
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.54050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.54050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 66.49450
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.54050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.54050
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 199.48350
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.54050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.54050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 66.49450
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 132.98900
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: 9980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 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: 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 -4.25 73.66
REMARK 500 PHE A 40 75.99 -116.98
REMARK 500 LEU A 41 109.98 -55.65
REMARK 500 SER A 52 -179.06 -65.10
REMARK 500 GLU A 77 19.67 59.98
REMARK 500 LYS B 25 -3.67 74.55
REMARK 500 ASP B 33 69.82 -110.54
REMARK 500 PHE B 40 75.85 -116.71
REMARK 500 LEU B 41 109.76 -55.98
REMARK 500 SER B 52 -178.49 -66.70
REMARK 500 ASP B 160 35.12 -98.55
REMARK 500 LEU B 169 64.73 -100.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BEO RELATED DB: PDB
REMARK 900 2BEO CONTAINS THE NATIVE PROTEIN
DBREF 5LEK A 1 237 UNP P22262 PRFA_LISMO 1 237
DBREF 5LEK B 1 237 UNP P22262 PRFA_LISMO 1 237
DBREF 5LEK C -15 15 PDB 5LEK 5LEK -15 15
DBREF 5LEK D -15 15 PDB 5LEK 5LEK -15 15
SEQADV 5LEK SER A 145 UNP P22262 GLY 145 CONFLICT
SEQADV 5LEK SER B 145 UNP P22262 GLY 145 CONFLICT
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 SER 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 SER 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
FORMUL 5 HOH *3(H2 O)
HELIX 1 AA1 ASN A 2 GLU A 13 1 12
HELIX 2 AA2 ILE A 99 ASN A 109 1 11
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 GLY A 179 1 10
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 CYS A 229 1 12
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 GLY B 179 1 10
HELIX 15 AB6 HIS B 182 GLU B 196 1 15
HELIX 16 AB7 TYR B 201 CYS B 205 5 5
HELIX 17 AB8 ASN B 210 ALA B 218 1 9
HELIX 18 AB9 ALA B 218 CYS B 229 1 12
HELIX 19 AC1 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 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 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 GLN A 61
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 GLU A 157 0
SHEET 2 AA3 4 ILE A 162 ILE A 164 -1 O LYS A 163 N LYS A 156
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 94 N LYS B 20
SHEET 3 AA4 4 TYR B 37 ASP B 43 -1 N ASP B 43 O THR B 93
SHEET 4 AA4 4 PHE B 67 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 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 TYR B 207 VAL B 208 -1 O VAL B 208 N ILE B 162
SHEET 4 AA6 4 ILE B 199 VAL B 200 -1 N VAL B 200 O TYR B 207
CISPEP 1 GLY A 65 ALA A 66 0 0.91
CISPEP 2 GLY B 65 ALA B 66 0 5.67
CRYST1 79.081 79.081 265.978 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 0.012645 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012645 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003760 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
