HEADER HYDROLASE 08-SEP-15 5ANS
TITLE POTENT AND SELECTIVE INHIBITORS OF MTH1 PROBE ITS ROLE IN
TITLE 2 CANCER CELL SURVIVAL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 7,8-DIHYDRO-8-OXOGUANINE TRIPHOSPHATASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 42-197;
COMPND 5 SYNONYM: 2-HYDROXY-DATP DIPHOSPHATASE, 8-OXO-DGTPASE, NUCLEOSIDE
COMPND 6 DIPHOSPHATE-LINKED MOIETY X MOTIF 1, NUDIX MOTIF 1;
COMPND 7 EC: 3.6.1.55;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: GOLD
KEYWDS MTH1, ONCOLOGY, HYDROLASE, NUCLEOTIDE HYDROLYSIS, INHIBITION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.G.KETTLE,H.ALWAN,M.BISTA,J.BREED,H.KACK,K.ECKERSLEY,K.M.FOOTE,
AUTHOR 2 S.FILLERY,L.GOODWIN,D.JONES,A.LAU,J.W.M.NISSINK,J.READ,J.SCOTT,
AUTHOR 3 B.TAYLOR,G.WALKER,L.WISSLER
REVDAT 2 06-APR-16 5ANS 1 JRNL
REVDAT 1 02-MAR-16 5ANS 0
JRNL AUTH J.G.KETTLE,H.ALWAN,M.BISTA,J.BREED,N.L.DAVIES,K.ECKERSLEY,
JRNL AUTH 2 S.FILLERY,K.M.FOOTE,L.GOODWIN,D.R.JONES,H.KACK,A.LAU,
JRNL AUTH 3 J.W.NISSINK,J.READ,J.S.SCOTT,B.TAYLOR,G.WALKER,L.WISSLER,
JRNL AUTH 4 M.WYLOT
JRNL TITL POTENT AND SELECTIVE INHIBITORS OF MTH1 PROBE ITS ROLE IN
JRNL TITL 2 CANCER CELL SURVIVAL.
JRNL REF J.MED.CHEM. V. 59 2346 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 26878898
JRNL DOI 10.1021/ACS.JMEDCHEM.5B01760
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 152.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.00
REMARK 3 NUMBER OF REFLECTIONS : 20400
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) : 0.20698
REMARK 3 R VALUE (WORKING SET) : 0.20521
REMARK 3 FREE R VALUE : 0.24194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 1097
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) : 1.600
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.642
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1461
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.203
REMARK 3 BIN FREE R VALUE SET COUNT : 75
REMARK 3 BIN FREE R VALUE : 0.238
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1262
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 128
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.785
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.27
REMARK 3 B22 (A**2) : 0.27
REMARK 3 B33 (A**2) : -0.54
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.104
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.104
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.062
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.701
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1321 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1791 ; 1.058 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 158 ; 6.282 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 225 ;13.334 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 183 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1031 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 547 ; 0.186 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 881 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 109 ; 0.106 ; 0.200
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): 53 ; 0.158 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 22 ; 0.192 ; 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): 802 ; 0.650 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1243 ; 1.051 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 618 ; 1.461 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 546 ; 2.323 ; 4.500
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
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 5ANS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-SEP-15.
REMARK 100 THE PDBE ID CODE IS EBI-64943.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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) : 0.9756
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21613
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.60
REMARK 200 RESOLUTION RANGE LOW (A) : 33.70
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.9
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 7.0
REMARK 200 R MERGE FOR SHELL (I) : 0.30
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.60
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: NULL
REMARK 200
REMARK 200 REMARK: IN IN-HOUSE APO STRUCTURE DETERMINED BY MAD PHASING
REMARK 200 WAS USED AS SEARCH MODEL.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
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 75.86500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 22.66350
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 22.66350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 37.93250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 22.66350
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 22.66350
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 113.79750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 22.66350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 22.66350
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 37.93250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 22.66350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 22.66350
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 113.79750
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 75.86500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2022 LIES ON A SPECIAL POSITION.
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 -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 MET A 1
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 VAL A 156 O
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2089 O HOH A 2089 7555 1.94
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 RX8 A1157
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5ANM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF IGE FC IN COMPLEX WITH A
REMARK 900 NEUTRALIZING ANTIBODY
REMARK 900 RELATED ID: 5ANT RELATED DB: PDB
REMARK 900 POTENT AND SELECTIVE INHIBITORS OF MTH1 PROBE ITS ROLE
REMARK 900 IN CANCER CELL SURVIVAL
DBREF 5ANS A 1 156 UNP P36639 8ODP_HUMAN 42 197
SEQADV 5ANS GLY A -18 UNP P36639 EXPRESSION TAG
SEQADV 5ANS SER A -17 UNP P36639 EXPRESSION TAG
SEQADV 5ANS SER A -16 UNP P36639 EXPRESSION TAG
SEQADV 5ANS HIS A -15 UNP P36639 EXPRESSION TAG
SEQADV 5ANS HIS A -14 UNP P36639 EXPRESSION TAG
SEQADV 5ANS HIS A -13 UNP P36639 EXPRESSION TAG
SEQADV 5ANS HIS A -12 UNP P36639 EXPRESSION TAG
SEQADV 5ANS HIS A -11 UNP P36639 EXPRESSION TAG
SEQADV 5ANS HIS A -10 UNP P36639 EXPRESSION TAG
SEQADV 5ANS SER A -9 UNP P36639 EXPRESSION TAG
SEQADV 5ANS SER A -8 UNP P36639 EXPRESSION TAG
SEQADV 5ANS GLY A -7 UNP P36639 EXPRESSION TAG
SEQADV 5ANS LEU A -6 UNP P36639 EXPRESSION TAG
SEQADV 5ANS VAL A -5 UNP P36639 EXPRESSION TAG
SEQADV 5ANS PRO A -4 UNP P36639 EXPRESSION TAG
SEQADV 5ANS ARG A -3 UNP P36639 EXPRESSION TAG
SEQADV 5ANS GLY A -2 UNP P36639 EXPRESSION TAG
SEQADV 5ANS SER A -1 UNP P36639 EXPRESSION TAG
SEQADV 5ANS HIS A 0 UNP P36639 EXPRESSION TAG
SEQRES 1 A 175 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 A 175 VAL PRO ARG GLY SER HIS MET GLY ALA SER ARG LEU TYR
SEQRES 3 A 175 THR LEU VAL LEU VAL LEU GLN PRO GLN ARG VAL LEU LEU
SEQRES 4 A 175 GLY MET LYS LYS ARG GLY PHE GLY ALA GLY ARG TRP ASN
SEQRES 5 A 175 GLY PHE GLY GLY LYS VAL GLN GLU GLY GLU THR ILE GLU
SEQRES 6 A 175 ASP GLY ALA ARG ARG GLU LEU GLN GLU GLU SER GLY LEU
SEQRES 7 A 175 THR VAL ASP ALA LEU HIS LYS VAL GLY GLN ILE VAL PHE
SEQRES 8 A 175 GLU PHE VAL GLY GLU PRO GLU LEU MET ASP VAL HIS VAL
SEQRES 9 A 175 PHE CYS THR ASP SER ILE GLN GLY THR PRO VAL GLU SER
SEQRES 10 A 175 ASP GLU MET ARG PRO CYS TRP PHE GLN LEU ASP GLN ILE
SEQRES 11 A 175 PRO PHE LYS ASP MET TRP PRO ASP ASP SER TYR TRP PHE
SEQRES 12 A 175 PRO LEU LEU LEU GLN LYS LYS LYS PHE HIS GLY TYR PHE
SEQRES 13 A 175 LYS PHE GLN GLY GLN ASP THR ILE LEU ASP TYR THR LEU
SEQRES 14 A 175 ARG GLU VAL ASP THR VAL
HET RX8 A1157 23
HETNAM RX8 1-[4-AMINO-2-(ETHOXYMETHYL)-1H-IMIDAZO[4,5-C]
HETNAM 2 RX8 QUINOLIN-1-YL]-2-METHYLPROPAN-2-OL
HETSYN RX8 R848, RESIQUIMOD
FORMUL 2 RX8 C17 H22 N4 O2
FORMUL 3 HOH *128(H2 O)
HELIX 1 1 THR A 44 GLY A 58 1 15
HELIX 2 2 PRO A 112 ASP A 115 5 4
HELIX 3 3 ASP A 119 GLN A 129 1 11
SHEET 1 AA 2 TRP A 32 ASN A 33 0
SHEET 2 AA 2 ARG A 17 LYS A 23 1 O GLY A 21 N ASN A 33
SHEET 1 AB 2 MET A 101 GLN A 107 0
SHEET 2 AB 2 ARG A 17 LYS A 23 -1 O VAL A 18 N PHE A 106
SHEET 1 AC 7 THR A 144 VAL A 153 0
SHEET 2 AC 7 LYS A 132 GLN A 140 -1 O LYS A 132 N VAL A 153
SHEET 3 AC 7 HIS A 65 PHE A 74 1 O VAL A 67 N PHE A 133
SHEET 4 AC 7 LEU A 80 THR A 88 -1 O MET A 81 N PHE A 72
SHEET 5 AC 7 SER A 4 LEU A 13 1 O ARG A 5 N ASP A 82
SHEET 6 AC 7 ARG A 17 LYS A 23 -1 O LEU A 19 N VAL A 12
SHEET 7 AC 7 TRP A 32 ASN A 33 1 O ASN A 33 N GLY A 21
SHEET 1 AD 7 THR A 144 VAL A 153 0
SHEET 2 AD 7 LYS A 132 GLN A 140 -1 O LYS A 132 N VAL A 153
SHEET 3 AD 7 HIS A 65 PHE A 74 1 O VAL A 67 N PHE A 133
SHEET 4 AD 7 LEU A 80 THR A 88 -1 O MET A 81 N PHE A 72
SHEET 5 AD 7 SER A 4 LEU A 13 1 O ARG A 5 N ASP A 82
SHEET 6 AD 7 ARG A 17 LYS A 23 -1 O LEU A 19 N VAL A 12
SHEET 7 AD 7 MET A 101 GLN A 107 -1 O ARG A 102 N MET A 22
SITE 1 AC1 12 THR A 8 LEU A 9 LYS A 23 ASN A 33
SITE 2 AC1 12 GLY A 34 GLY A 36 GLY A 37 PHE A 72
SITE 3 AC1 12 TRP A 117 ASP A 119 ASP A 120 HOH A2101
CRYST1 45.327 45.327 151.730 90.00 90.00 90.00 P 41 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 0.022062 0.000000 0.000000 0.00000
SCALE2 0.000000 0.022062 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006591 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
