HEADER TRANSFERASE 27-FEB-14 4CRJ
TITLE STAPHYLOCOCCUS AUREUS 7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-
TITLE 2 PYROPHOSPHOKINASE IN COMPLEX WITH AMPCPP AND AN INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-PYROPHOSPHOKINASE (HPPK);
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.7.6.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS TRANSFERASE, FOLATE, STRUCTURE-BASED DRUG DESIGN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.L.DENNIS,J.D.SWARBRICK,T.S.PEAT
REVDAT 3 08-MAY-19 4CRJ 1 REMARK
REVDAT 2 28-DEC-16 4CRJ 1 HETNAM HETATM CONECT
REVDAT 1 28-JAN-15 4CRJ 0
JRNL AUTH M.L.DENNIS,S.CHHABRA,Z.WANG,A.DEBONO,O.DOLEZAL,J.NEWMAN,
JRNL AUTH 2 N.P.PITCHER,R.RAHMANI,B.CLEARY,N.BARLOW,M.HATTARKI,B.GRAHAM,
JRNL AUTH 3 T.S.PEAT,J.B.BAELL,J.D.SWARBRICK
JRNL TITL STRUCTURE-BASED DESIGN AND DEVELOPMENT OF FUNCTIONALIZED
JRNL TITL 2 MERCAPTOGUANINE DERIVATIVES AS INHIBITORS OF THE FOLATE
JRNL TITL 3 BIOSYNTHESIS PATHWAY ENZYME
JRNL TITL 4 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE FROM
JRNL TITL 5 STAPHYLOCOCCUS AUREUS.
JRNL REF J.MED.CHEM. V. 57 9612 2014
JRNL REFN ISSN 0022-2623
JRNL PMID 25357262
JRNL DOI 10.1021/JM501417F
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 13074
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 685
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 929
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.05
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 43
REMARK 3 BIN FREE R VALUE : 0.2380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1273
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 83
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.89000
REMARK 3 B22 (A**2) : 0.89000
REMARK 3 B33 (A**2) : -2.89000
REMARK 3 B12 (A**2) : 0.89000
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): 0.146
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.135
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.087
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.080
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1376 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1315 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1878 ; 1.362 ; 2.043
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3034 ; 0.769 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 162 ; 6.344 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 61 ;34.750 ;24.918
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 244 ;12.906 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;14.001 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 212 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1549 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 289 ; 0.001 ; 0.020
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 : 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 RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4CRJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1290059856.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95370
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13792
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 42.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 21.50
REMARK 200 R MERGE (I) : 0.22000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 19.70
REMARK 200 R MERGE FOR SHELL (I) : 1.02000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
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: PDB ENTRY 4AD6
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN 7.5 MG/ML PLUS 1MM AMPCPP PLUS
REMARK 280 1MM INHIBITOR, AMMONIUM SULFATE 0.275 M, PEG4000 22.1% W/V,
REMARK 280 SITTING DROP, 281 K, PH 8, VAPOR DIFFUSION, SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 17.39100
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 34.78200
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 26.08650
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 43.47750
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 8.69550
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 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 -2
REMARK 465 SER A -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 GLU A 50 56.77 -92.05
REMARK 500 ALA A 132 34.93 -144.54
REMARK 500 TYR A 157 -51.34 -121.46
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 MG A1160 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 APC A1159 O1A
REMARK 620 2 APC A1159 O1B 89.1
REMARK 620 3 ASP A 95 OD1 92.4 91.8
REMARK 620 4 ASP A 97 OD1 171.9 98.7 89.6
REMARK 620 5 HOH A2047 O 94.7 86.8 172.8 83.6
REMARK 620 6 HOH A2034 O 86.3 175.3 88.3 86.0 93.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1161 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 APC A1159 O1B
REMARK 620 2 APC A1159 O1G 88.9
REMARK 620 3 ASP A 95 OD2 85.5 174.3
REMARK 620 4 ASP A 97 OD2 102.3 93.9 87.6
REMARK 620 5 HOH A2045 O 87.9 89.0 90.4 169.4
REMARK 620 6 HOH A2046 O 171.1 95.9 89.7 84.9 84.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APC A 1159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1160
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 1162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YH5 A 1163
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 HEXAHISTIDINE-TAG WITH THROMBIN CLEAVAGE SITE AT THE N-
REMARK 999 TERMINUS
DBREF 4CRJ A 1 158 UNP C8MLE4 C8MLE4_STAAU 1 158
SEQADV 4CRJ GLY A -2 UNP C8MLE4 EXPRESSION TAG
SEQADV 4CRJ SER A -1 UNP C8MLE4 EXPRESSION TAG
SEQADV 4CRJ HIS A 0 UNP C8MLE4 EXPRESSION TAG
SEQRES 1 A 161 GLY SER HIS MET ILE GLN ALA TYR LEU GLY LEU GLY SER
SEQRES 2 A 161 ASN ILE GLY ASP ARG GLU SER GLN LEU ASN ASP ALA ILE
SEQRES 3 A 161 LYS ILE LEU ASN GLU TYR ASP GLY ILE SER VAL SER ASN
SEQRES 4 A 161 ILE SER PRO ILE TYR GLU THR ALA PRO VAL GLY TYR THR
SEQRES 5 A 161 GLU GLN PRO ASN PHE LEU ASN LEU CYS VAL GLU ILE GLN
SEQRES 6 A 161 THR THR LEU THR VAL LEU GLN LEU LEU GLU CYS CYS LEU
SEQRES 7 A 161 LYS THR GLU GLU CYS LEU HIS ARG ILE ARG LYS GLU ARG
SEQRES 8 A 161 TRP GLY PRO ARG THR LEU ASP VAL ASP ILE LEU LEU TYR
SEQRES 9 A 161 GLY GLU GLU MET ILE ASP LEU PRO LYS LEU SER VAL PRO
SEQRES 10 A 161 HIS PRO ARG MET ASN GLU ARG ALA PHE VAL LEU ILE PRO
SEQRES 11 A 161 LEU ASN ASP ILE ALA ALA ASN VAL VAL GLU PRO ARG SER
SEQRES 12 A 161 LYS LEU LYS VAL LYS ASP LEU VAL PHE VAL ASP ASP SER
SEQRES 13 A 161 VAL LYS ARG TYR LYS
HET APC A1159 31
HET MG A1160 1
HET MG A1161 1
HET NO3 A1162 4
HET YH5 A1163 23
HETNAM APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER
HETNAM MG MAGNESIUM ION
HETNAM NO3 NITRATE ION
HETNAM YH5 2-AMINO-8-{[2-(4-METHOXYPHENYL)-2-OXOETHYL]SULFANYL}-1,
HETNAM 2 YH5 9-DIHYDRO-6H-PURIN-6-ONE
HETSYN APC ALPHA,BETA-METHYLENEADENOSINE-5'-TRIPHOSPHATE
FORMUL 2 APC C11 H18 N5 O12 P3
FORMUL 3 MG 2(MG 2+)
FORMUL 5 NO3 N O3 1-
FORMUL 6 YH5 C14 H13 N5 O3 S
FORMUL 7 HOH *83(H2 O)
HELIX 1 1 ASP A 14 TYR A 29 1 16
HELIX 2 2 THR A 66 LEU A 81 1 16
HELIX 3 3 ARG A 117 GLU A 120 5 4
HELIX 4 4 ARG A 121 ALA A 133 1 13
HELIX 5 5 VAL A 144 VAL A 148 1 5
SHEET 1 AA 2 ILE A 32 ILE A 37 0
SHEET 2 AA 2 PHE A 54 THR A 63 -1 O GLU A 60 N SER A 35
SHEET 1 AB 5 ASP A 95 TYR A 101 0
SHEET 2 AB 5 ILE A 2 SER A 10 -1 O TYR A 5 N LEU A 99
SHEET 3 AB 5 PHE A 54 THR A 63 -1 O LEU A 55 N SER A 10
SHEET 4 AB 5 ILE A 40 THR A 43 -1 O TYR A 41 N ASN A 56
SHEET 5 AB 5 VAL A 154 LYS A 158 -1 O LYS A 155 N GLU A 42
SHEET 1 AC 4 ASP A 95 TYR A 101 0
SHEET 2 AC 4 ILE A 2 SER A 10 -1 O TYR A 5 N LEU A 99
SHEET 3 AC 4 PHE A 54 THR A 63 -1 O LEU A 55 N SER A 10
SHEET 4 AC 4 ILE A 32 ILE A 37 -1 O SER A 33 N GLN A 62
SHEET 1 AD 2 ILE A 106 LEU A 108 0
SHEET 2 AD 2 LEU A 111 VAL A 113 -1 O LEU A 111 N LEU A 108
SHEET 1 AE 2 VAL A 136 GLU A 137 0
SHEET 2 AE 2 LEU A 142 LYS A 143 -1 O LEU A 142 N GLU A 137
LINK O1A APC A1159 MG MG A1160 1555 1555 2.08
LINK O1B APC A1159 MG MG A1160 1555 1555 2.06
LINK O1B APC A1159 MG MG A1161 1555 1555 2.18
LINK O1G APC A1159 MG MG A1161 1555 1555 2.07
LINK MG MG A1160 OD1 ASP A 95 1555 1555 2.15
LINK MG MG A1160 OD1 ASP A 97 1555 1555 2.11
LINK MG MG A1160 O HOH A2047 1555 1555 2.07
LINK MG MG A1160 O HOH A2034 1555 1555 2.10
LINK MG MG A1161 OD2 ASP A 95 1555 1555 2.17
LINK MG MG A1161 OD2 ASP A 97 1555 1555 2.05
LINK MG MG A1161 O HOH A2045 1555 1555 2.11
LINK MG MG A1161 O HOH A2046 1555 1555 2.15
CISPEP 1 VAL A 113 PRO A 114 0 -4.83
SITE 1 AC1 23 LEU A 71 ARG A 83 ARG A 88 ARG A 92
SITE 2 AC1 23 ASP A 95 ASP A 97 ILE A 98 LYS A 110
SITE 3 AC1 23 LEU A 111 SER A 112 HIS A 115 ARG A 117
SITE 4 AC1 23 ARG A 121 MG A1160 MG A1161 HOH A2033
SITE 5 AC1 23 HOH A2034 HOH A2039 HOH A2040 HOH A2041
SITE 6 AC1 23 HOH A2045 HOH A2047 HOH A2083
SITE 1 AC2 6 ASP A 95 ASP A 97 APC A1159 MG A1161
SITE 2 AC2 6 HOH A2034 HOH A2047
SITE 1 AC3 6 ASP A 95 ASP A 97 APC A1159 MG A1160
SITE 2 AC3 6 HOH A2045 HOH A2046
SITE 1 AC4 6 ILE A 12 ARG A 83 ILE A 84 ARG A 85
SITE 2 AC4 6 ARG A 92 THR A 93
SITE 1 AC5 14 THR A 43 ALA A 44 PRO A 45 VAL A 46
SITE 2 AC5 14 GLY A 47 PHE A 54 ASN A 56 GLU A 104
SITE 3 AC5 14 MET A 105 ILE A 106 ARG A 121 PHE A 123
SITE 4 AC5 14 HOH A2044 HOH A2045
CRYST1 82.480 82.480 52.173 90.00 90.00 120.00 P 61 6
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 0.012124 0.007000 0.000000 0.00000
SCALE2 0.000000 0.014000 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019167 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
