HEADER TRANSFERASE 02-APR-14 4CWB
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;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HPPK;
COMPND 5 EC: 2.7.6.3;
COMPND 6 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_VECTOR_TYPE: PLASMID;
SOURCE 8 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 2 08-MAY-19 4CWB 1 REMARK
REVDAT 1 28-JAN-15 4CWB 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. 1.56 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) : 1.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.33
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 28270
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) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1505
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) : 1.56
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.60
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2013
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE SET COUNT : 115
REMARK 3 BIN FREE R VALUE : 0.2230
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 : 64
REMARK 3 SOLVENT ATOMS : 141
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.24000
REMARK 3 B22 (A**2) : 0.24000
REMARK 3 B33 (A**2) : -0.77000
REMARK 3 B12 (A**2) : 0.24000
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): 0.067
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.067
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.042
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.162
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1466 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1398 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2012 ; 1.600 ; 2.039
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3239 ; 0.771 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 182 ; 6.468 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 65 ;36.562 ;25.231
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 267 ;11.553 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;12.576 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 222 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1714 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 324 ; 0.002 ; 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 : 1.10
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY. AN ALTERNATE
REMARK 3 CONFORMATION OF THE LOOP 3 RESIDUE LYS86 IS SUGGESTED, THIS WAS
REMARK 3 NOT MODELLED DUE TO POOR DENSITY. THE TERMINAL RESIDUE LYS158 IS
REMARK 3 SUGGESTED TO ADOPT MULTIPLE CONFORMATIONS. ONLY THE PREDOMINANT
REMARK 3 CONFORMATION IS MODELLED DUE TO ELSEWISE POOR DENSITY.
REMARK 4
REMARK 4 4CWB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1290060158.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-14
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) : 0.953700
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 : 29793
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.560
REMARK 200 RESOLUTION RANGE LOW (A) : 42.290
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 11.20
REMARK 200 R MERGE (I) : 0.09000
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) : 1.56
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : 10.30
REMARK 200 R MERGE FOR SHELL (I) : 0.67000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: PDB ENTRY 4AD6
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN 6.9 MG/ML 1 MM AMPCPP, 1 MM
REMARK 280 INHIBITOR, 2 MM MAGNESIUM CHLORIDE, AMMONIUM NITRATE 0.275 M,
REMARK 280 PEG3350 22.2% W/V, SITTING DROP, 281 K, PH 8, VAPOR DIFFUSION,
REMARK 280 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 17.34667
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 34.69333
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 26.02000
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 43.36667
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 8.67333
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 ALA A 132 33.21 -142.91
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 A1159 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 APC A1161 O1B
REMARK 620 2 APC A1161 O3G 92.0
REMARK 620 3 ASP A 95 OD2 90.2 174.0
REMARK 620 4 ASP A 97 OD2 114.8 93.6 90.5
REMARK 620 5 HOH A2083 O 103.7 86.0 88.1 141.5
REMARK 620 6 HOH A2084 O 164.0 95.9 80.6 78.6 63.2
REMARK 620 N 1 2 3 4 5
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 HOH A2065 O
REMARK 620 2 ASP A 95 OD1 90.5
REMARK 620 3 ASP A 97 OD1 85.6 91.7
REMARK 620 4 APC A1161 O1B 175.8 89.2 98.6
REMARK 620 5 HOH A2085 O 94.1 173.4 83.9 86.6
REMARK 620 6 APC A1161 O1A 87.9 92.4 172.3 87.9 92.5
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 MG 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 APC 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 X6L A 1163
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 HEXAHISTIDINE-TAG WITH THROMBIN CLEAVAGE AT THE N-TERMINUS
DBREF 4CWB A 1 158 UNP C8MLE4 C8MLE4_STAAU 1 158
SEQADV 4CWB GLY A -2 UNP C8MLE4 EXPRESSION TAG
SEQADV 4CWB SER A -1 UNP C8MLE4 EXPRESSION TAG
SEQADV 4CWB 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 MG A1159 1
HET MG A1160 1
HET APC A1161 31
HET NO3 A1162 4
HET X6L A1163 27
HETNAM MG MAGNESIUM ION
HETNAM APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER
HETNAM NO3 NITRATE ION
HETNAM X6L 2-AMINO-8-[2-OXO-2-(4-PHENYLPHENYL)ETHYL]SULFANYL-1,9-
HETNAM 2 X6L DIHYDROPURIN-6-ONE
HETSYN APC ALPHA,BETA-METHYLENEADENOSINE-5'-TRIPHOSPHATE
FORMUL 2 MG 2(MG 2+)
FORMUL 4 APC C11 H18 N5 O12 P3
FORMUL 5 NO3 N O3 1-
FORMUL 6 X6L C19 H15 N5 O2 S
FORMUL 7 HOH *141(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 LYS A 145 LEU A 147 5 3
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 TYR A 41 THR A 43 -1 O TYR A 41 N ASN A 56
SHEET 5 AB 5 VAL A 154 ARG A 156 -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 MG MG A1159 O1B APC A1161 1555 1555 2.02
LINK MG MG A1159 O3G APC A1161 1555 1555 2.01
LINK MG MG A1159 OD2 ASP A 95 1555 1555 2.09
LINK MG MG A1159 OD2 ASP A 97 1555 1555 1.98
LINK MG MG A1159 O HOH A2083 1555 1555 2.02
LINK MG MG A1159 O HOH A2084 1555 1555 2.69
LINK MG MG A1160 O HOH A2065 1555 1555 2.05
LINK MG MG A1160 OD1 ASP A 95 1555 1555 2.01
LINK MG MG A1160 OD1 ASP A 97 1555 1555 2.11
LINK MG MG A1160 O1B APC A1161 1555 1555 2.12
LINK MG MG A1160 O HOH A2085 1555 1555 2.12
LINK MG MG A1160 O1A APC A1161 1555 1555 2.06
CISPEP 1 VAL A 113 PRO A 114 0 -3.46
SITE 1 AC1 6 ASP A 95 ASP A 97 MG A1160 APC A1161
SITE 2 AC1 6 HOH A2083 HOH A2084
SITE 1 AC2 6 ASP A 95 ASP A 97 MG A1159 APC A1161
SITE 2 AC2 6 HOH A2065 HOH A2085
SITE 1 AC3 25 LEU A 71 ARG A 83 ARG A 88 ARG A 92
SITE 2 AC3 25 ASP A 95 ASP A 97 ILE A 98 LYS A 110
SITE 3 AC3 25 LEU A 111 SER A 112 HIS A 115 ARG A 117
SITE 4 AC3 25 ARG A 121 MG A1159 MG A1160 X6L A1163
SITE 5 AC3 25 HOH A2063 HOH A2065 HOH A2071 HOH A2076
SITE 6 AC3 25 HOH A2079 HOH A2080 HOH A2083 HOH A2085
SITE 7 AC3 25 HOH A2141
SITE 1 AC4 7 ILE A 12 ARG A 83 ILE A 84 ARG A 85
SITE 2 AC4 7 ARG A 92 THR A 93 HOH A2069
SITE 1 AC5 18 THR A 43 ALA A 44 PRO A 45 VAL A 46
SITE 2 AC5 18 PHE A 54 ASN A 56 VAL A 67 ARG A 88
SITE 3 AC5 18 ARG A 92 TYR A 101 GLU A 104 MET A 105
SITE 4 AC5 18 ILE A 106 ARG A 121 PHE A 123 APC A1161
SITE 5 AC5 18 HOH A2082 HOH A2083
CRYST1 83.817 83.817 52.040 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 0.011931 0.006888 0.000000 0.00000
SCALE2 0.000000 0.013776 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019216 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
