HEADER TRANSFERASE/TRANSFERASE INHIBITOR 18-NOV-15 5ETR
TITLE S. AUREUS 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE
TITLE 2 COMPLEXED WITH AMPCPP AND INHIBITOR AT 1.32 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-AMINO-4-HYDROXY-6-HYDROXYMETHYLDIHYDROPTERIDINE
COMPND 3 PYROPHOSPHOKINASE;
COMPND 4 CHAIN: B, A;
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 GENE: RK60_02090, RK67_01645, RK72_06915, RK74_04210, RK75_00240,
SOURCE 5 RK80_01970, RK83_05435, RK84_03130, RK95_04415, RK96_04825,
SOURCE 6 RK98_03440, RK99_07885, RL05_10010, RL06_09555, RL08_05305,
SOURCE 7 TM59_02255;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS INHIBITOR, COMPLEX, AMPCPP, PYROPHOSPHOKINASE, TRANSFERASE-
KEYWDS 2 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.L.DENNIS,T.S.PEAT,J.D.SWARBRICK
REVDAT 2 22-JUN-16 5ETR 1 JRNL
REVDAT 1 04-MAY-16 5ETR 0
JRNL AUTH M.L.DENNIS,N.P.PITCHER,M.D.LEE,A.J.DEBONO,Z.C.WANG,
JRNL AUTH 2 J.R.HARJANI,R.RAHMANI,B.CLEARY,T.S.PEAT,J.B.BAELL,
JRNL AUTH 3 J.D.SWARBRICK
JRNL TITL STRUCTURAL BASIS FOR THE SELECTIVE BINDING OF INHIBITORS TO
JRNL TITL 2 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE FROM
JRNL TITL 3 STAPHYLOCOCCUS AUREUS AND ESCHERICHIA COLI.
JRNL REF J.MED.CHEM. V. 59 5248 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 27094768
JRNL DOI 10.1021/ACS.JMEDCHEM.6B00002
REMARK 2
REMARK 2 RESOLUTION. 1.32 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
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) : 1.32
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 73521
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) : 0.125
REMARK 3 R VALUE (WORKING SET) : 0.124
REMARK 3 FREE R VALUE : 0.152
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3888
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) : 1.32
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.35
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5443
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2230
REMARK 3 BIN FREE R VALUE SET COUNT : 270
REMARK 3 BIN FREE R VALUE : 0.2450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2506
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 111
REMARK 3 SOLVENT ATOMS : 328
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07000
REMARK 3 B22 (A**2) : 0.18000
REMARK 3 B33 (A**2) : -0.20000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.042
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.041
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.979
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.974
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2749 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2629 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3766 ; 1.938 ; 2.037
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6071 ; 3.547 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 337 ; 6.149 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 123 ;36.119 ;24.797
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 495 ;11.256 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;10.871 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 435 ; 0.382 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3132 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 576 ; 0.016 ; 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): 1289 ; 1.148 ; 1.148
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1288 ; 1.149 ; 1.146
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1618 ; 1.514 ; 1.729
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1619 ; 1.515 ; 1.730
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1460 ; 1.837 ; 1.438
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1461 ; 1.837 ; 1.438
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2139 ; 2.267 ; 2.042
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3421 ; 2.918 ;10.741
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3248 ; 2.747 ;10.108
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 5378 ;12.948 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 89 ;26.358 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 5563 ; 7.638 ; 5.000
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
REMARK 4
REMARK 4 5ETR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215443.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.1
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) : 1.0329
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77438
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.320
REMARK 200 RESOLUTION RANGE LOW (A) : 45.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.32
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.83200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: 5ETQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN 6.9 MG/ML 1 MM AMPCPP, 1 MM
REMARK 280 INHIBITOR, 0.202 M MGCL2, 0.1 M TRIS CHLORIDE, 19.6%W/V PEG8000,
REMARK 280 50 MM SODIUM THIOCYANATE, PH 7.1, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 281K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 34.05500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 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 350
REMARK 350 BIOMOLECULE: 2
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 B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 LYS B 158
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 LYS A 158
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 TYR B 48 -159.50 -151.45
REMARK 500 ALA B 132 30.28 -145.26
REMARK 500 TYR A 48 -153.29 -151.40
REMARK 500 ALA A 132 30.69 -145.18
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 B 203 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 27 O
REMARK 620 2 TYR B 29 O 104.6
REMARK 620 3 ILE B 32 O 89.3 88.3
REMARK 620 4 HOH B 407 O 146.0 109.2 88.8
REMARK 620 5 HOH B 436 O 100.4 96.0 168.0 79.2
REMARK 620 6 HOH A 353 O 69.4 172.4 96.3 77.1 80.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 205 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 95 OD1
REMARK 620 2 ASP B 97 OD1 92.4
REMARK 620 3 APC B 201 O1B 90.8 94.5
REMARK 620 4 APC B 201 O1A 91.3 174.5 89.5
REMARK 620 5 HOH B 331 O 91.1 87.2 177.4 88.6
REMARK 620 6 HOH B 391 O 177.7 87.2 91.6 89.0 86.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 206 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 95 OD2
REMARK 620 2 ASP B 97 OD2 90.2
REMARK 620 3 APC B 201 O1G 177.0 92.8
REMARK 620 4 APC B 201 O1B 91.6 99.4 88.2
REMARK 620 5 HOH B 343 O 87.0 169.7 90.1 90.6
REMARK 620 6 HOH B 394 O 86.7 86.5 93.3 173.8 83.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 204 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 107 OD1
REMARK 620 2 ASP A 107 OD1 165.5
REMARK 620 3 HOH B 347 O 89.1 86.8
REMARK 620 4 HOH A 351 O 89.7 97.2 168.1
REMARK 620 5 HOH A 355 O 88.0 78.5 95.5 96.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 203 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 27 O
REMARK 620 2 TYR A 29 O 103.8
REMARK 620 3 ILE A 32 O 92.3 86.3
REMARK 620 4 HOH A 353 O 69.6 173.3 95.1
REMARK 620 5 HOH B 407 O 92.1 100.7 170.6 78.7
REMARK 620 6 HOH B 436 O 149.6 106.5 91.7 80.0 80.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 205 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 95 OD1
REMARK 620 2 ASP A 97 OD1 92.4
REMARK 620 3 APC A 201 O1B 90.4 94.2
REMARK 620 4 APC A 201 O2A 89.3 176.6 88.8
REMARK 620 5 HOH A 333 O 90.6 88.1 177.5 88.9
REMARK 620 6 HOH A 377 O 177.1 87.7 92.5 90.5 86.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 204 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 95 OD2
REMARK 620 2 ASP A 97 OD2 91.0
REMARK 620 3 APC A 201 O3G 176.5 92.4
REMARK 620 4 APC A 201 O1B 91.1 99.5 87.2
REMARK 620 5 HOH A 344 O 86.0 171.4 90.8 88.6
REMARK 620 6 HOH A 390 O 87.7 88.2 93.5 172.2 83.7
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 B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5RW B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue APC A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5RW A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 206
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5ETM RELATED DB: PDB
REMARK 900 5ETM CONTAINS THE SAME INHIBITOR COMPLEXED WITH THE E. COLI FORM OF
REMARK 900 HPPK
REMARK 900 RELATED ID: 5ETK RELATED DB: PDB
REMARK 900 RELATED ID: 5ETL RELATED DB: PDB
REMARK 900 RELATED ID: 5ETN RELATED DB: PDB
REMARK 900 RELATED ID: 5ETO RELATED DB: PDB
REMARK 900 RELATED ID: 5ETP RELATED DB: PDB
REMARK 900 RELATED ID: 5ETQ RELATED DB: PDB
REMARK 900 RELATED ID: 5ETS RELATED DB: PDB
REMARK 900 RELATED ID: 5ETT RELATED DB: PDB
REMARK 900 RELATED ID: 5ETV RELATED DB: PDB
DBREF1 5ETR B 1 158 UNP A0A0H1ZSM1_STAAU
DBREF2 5ETR B A0A0H1ZSM1 1 158
DBREF1 5ETR A 1 158 UNP A0A0H1ZSM1_STAAU
DBREF2 5ETR A A0A0H1ZSM1 1 158
SEQADV 5ETR GLY B -2 UNP A0A0H1ZSM EXPRESSION TAG
SEQADV 5ETR SER B -1 UNP A0A0H1ZSM EXPRESSION TAG
SEQADV 5ETR HIS B 0 UNP A0A0H1ZSM EXPRESSION TAG
SEQADV 5ETR GLY A -2 UNP A0A0H1ZSM EXPRESSION TAG
SEQADV 5ETR SER A -1 UNP A0A0H1ZSM EXPRESSION TAG
SEQADV 5ETR HIS A 0 UNP A0A0H1ZSM EXPRESSION TAG
SEQRES 1 B 161 GLY SER HIS MET ILE GLN ALA TYR LEU GLY LEU GLY SER
SEQRES 2 B 161 ASN ILE GLY ASP ARG GLU SER GLN LEU ASN ASP ALA ILE
SEQRES 3 B 161 LYS ILE LEU ASN GLU TYR ASP GLY ILE SER VAL SER ASN
SEQRES 4 B 161 ILE SER PRO ILE TYR GLU THR ALA PRO VAL GLY TYR THR
SEQRES 5 B 161 GLU GLN PRO ASN PHE LEU ASN LEU CYS VAL GLU ILE GLN
SEQRES 6 B 161 THR THR LEU THR VAL LEU GLN LEU LEU GLU CYS CYS LEU
SEQRES 7 B 161 LYS THR GLU GLU CYS LEU HIS ARG ILE ARG LYS GLU ARG
SEQRES 8 B 161 TRP GLY PRO ARG THR LEU ASP VAL ASP ILE LEU LEU TYR
SEQRES 9 B 161 GLY GLU GLU MET ILE ASP LEU PRO LYS LEU SER VAL PRO
SEQRES 10 B 161 HIS PRO ARG MET ASN GLU ARG ALA PHE VAL LEU ILE PRO
SEQRES 11 B 161 LEU ASN ASP ILE ALA ALA ASN VAL VAL GLU PRO ARG SER
SEQRES 12 B 161 LYS LEU LYS VAL LYS ASP LEU VAL PHE VAL ASP ASP SER
SEQRES 13 B 161 VAL LYS ARG TYR LYS
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 B 201 31
HET 5RW B 202 20
HET NA B 203 1
HET NA B 204 1
HET MG B 205 1
HET MG B 206 1
HET CL B 207 1
HET APC A 201 31
HET 5RW A 202 20
HET NA A 203 1
HET MG A 204 1
HET MG A 205 1
HET CL A 206 1
HETNAM APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER
HETNAM 5RW 2-AZANYL-8-[(4-FLUOROPHENYL)METHYLSULFANYL]-1,7-
HETNAM 2 5RW DIHYDROPURIN-6-ONE
HETNAM NA SODIUM ION
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETSYN APC ALPHA,BETA-METHYLENEADENOSINE-5'-TRIPHOSPHATE
FORMUL 3 APC 2(C11 H18 N5 O12 P3)
FORMUL 4 5RW 2(C12 H10 F N5 O S)
FORMUL 5 NA 3(NA 1+)
FORMUL 7 MG 4(MG 2+)
FORMUL 9 CL 2(CL 1-)
FORMUL 16 HOH *328(H2 O)
HELIX 1 AA1 ASP B 14 TYR B 29 1 16
HELIX 2 AA2 THR B 66 LEU B 81 1 16
HELIX 3 AA3 ARG B 117 GLU B 120 5 4
HELIX 4 AA4 ARG B 121 ALA B 133 1 13
HELIX 5 AA5 VAL B 144 VAL B 148 1 5
HELIX 6 AA6 ASP A 14 TYR A 29 1 16
HELIX 7 AA7 THR A 66 LEU A 81 1 16
HELIX 8 AA8 ARG A 117 GLU A 120 5 4
HELIX 9 AA9 ARG A 121 ALA A 133 1 13
HELIX 10 AB1 VAL A 144 VAL A 148 1 5
SHEET 1 AA1 4 ILE B 32 ILE B 37 0
SHEET 2 AA1 4 PHE B 54 THR B 63 -1 O GLU B 60 N ASN B 36
SHEET 3 AA1 4 ILE B 2 SER B 10 -1 N ILE B 2 O THR B 63
SHEET 4 AA1 4 ASP B 95 TYR B 101 -1 O ASP B 97 N GLY B 7
SHEET 1 AA2 4 ILE B 32 ILE B 37 0
SHEET 2 AA2 4 PHE B 54 THR B 63 -1 O GLU B 60 N ASN B 36
SHEET 3 AA2 4 TYR B 41 THR B 43 -1 N TYR B 41 O ASN B 56
SHEET 4 AA2 4 VAL B 154 ARG B 156 -1 O LYS B 155 N GLU B 42
SHEET 1 AA3 2 ILE B 106 LEU B 108 0
SHEET 2 AA3 2 LEU B 111 VAL B 113 -1 O VAL B 113 N ILE B 106
SHEET 1 AA4 2 VAL B 136 GLU B 137 0
SHEET 2 AA4 2 LEU B 142 LYS B 143 -1 O LEU B 142 N GLU B 137
SHEET 1 AA5 4 ILE A 32 ILE A 37 0
SHEET 2 AA5 4 PHE A 54 THR A 63 -1 O GLU A 60 N ASN A 36
SHEET 3 AA5 4 ILE A 2 SER A 10 -1 N ILE A 2 O THR A 63
SHEET 4 AA5 4 ASP A 95 TYR A 101 -1 O ASP A 97 N GLY A 7
SHEET 1 AA6 4 ILE A 32 ILE A 37 0
SHEET 2 AA6 4 PHE A 54 THR A 63 -1 O GLU A 60 N ASN A 36
SHEET 3 AA6 4 TYR A 41 THR A 43 -1 N TYR A 41 O ASN A 56
SHEET 4 AA6 4 VAL A 154 ARG A 156 -1 O LYS A 155 N GLU A 42
SHEET 1 AA7 2 ILE A 106 LEU A 108 0
SHEET 2 AA7 2 LEU A 111 VAL A 113 -1 O VAL A 113 N ILE A 106
SHEET 1 AA8 2 VAL A 136 GLU A 137 0
SHEET 2 AA8 2 LEU A 142 LYS A 143 -1 O LEU A 142 N GLU A 137
LINK O ASN B 27 NA NA B 203 1555 1555 2.39
LINK O TYR B 29 NA NA B 203 1555 1555 2.35
LINK O ILE B 32 NA NA B 203 1555 1555 2.24
LINK OD1 ASP B 95 MG MG B 205 1555 1555 2.07
LINK OD2 ASP B 95 MG MG B 206 1555 1555 2.06
LINK OD1 ASP B 97 MG MG B 205 1555 1555 2.07
LINK OD2 ASP B 97 MG MG B 206 1555 1555 2.08
LINK OD1 ASP B 107 NA NA B 204 1555 1555 2.08
LINK O ASN A 27 NA NA A 203 1555 1555 2.38
LINK O TYR A 29 NA NA A 203 1555 1555 2.38
LINK O ILE A 32 NA NA A 203 1555 1555 2.20
LINK OD1 ASP A 95 MG MG A 205 1555 1555 2.06
LINK OD2 ASP A 95 MG MG A 204 1555 1555 2.08
LINK OD1 ASP A 97 MG MG A 205 1555 1555 2.04
LINK OD2 ASP A 97 MG MG A 204 1555 1555 2.09
LINK OD1 ASP A 107 NA NA B 204 1555 1555 2.32
LINK O1G APC B 201 MG MG B 206 1555 1555 2.02
LINK O1B APC B 201 MG MG B 205 1555 1555 2.08
LINK O1B APC B 201 MG MG B 206 1555 1555 2.15
LINK O1A APC B 201 MG MG B 205 1555 1555 2.08
LINK NA NA B 203 O HOH B 407 1555 1555 2.44
LINK NA NA B 203 O HOH B 436 1555 1555 2.40
LINK NA NA B 204 O HOH B 347 1555 1555 2.04
LINK NA NA B 204 O HOH A 351 1555 1555 2.03
LINK NA NA B 204 O HOH A 355 1555 1555 2.04
LINK MG MG B 205 O HOH B 331 1555 1555 2.08
LINK MG MG B 205 O HOH B 391 1555 1555 2.10
LINK MG MG B 206 O HOH B 343 1555 1555 2.10
LINK MG MG B 206 O HOH B 394 1555 1555 2.13
LINK O3G APC A 201 MG MG A 204 1555 1555 2.02
LINK O1B APC A 201 MG MG A 204 1555 1555 2.16
LINK O1B APC A 201 MG MG A 205 1555 1555 2.12
LINK O2A APC A 201 MG MG A 205 1555 1555 2.10
LINK NA NA A 203 O HOH A 353 1555 1555 2.46
LINK MG MG A 204 O HOH A 344 1555 1555 2.14
LINK MG MG A 204 O HOH A 390 1555 1555 2.11
LINK MG MG A 205 O HOH A 333 1555 1555 2.06
LINK MG MG A 205 O HOH A 377 1555 1555 2.08
LINK NA NA B 203 O HOH A 353 1555 1454 2.46
LINK NA NA A 203 O HOH B 407 1555 1656 2.35
LINK NA NA A 203 O HOH B 436 1555 1656 2.43
CISPEP 1 VAL B 113 PRO B 114 0 -8.06
CISPEP 2 VAL A 113 PRO A 114 0 -9.37
SITE 1 AC1 29 LEU B 71 ARG B 83 ARG B 85 ARG B 92
SITE 2 AC1 29 ASP B 95 ASP B 97 ILE B 98 LYS B 110
SITE 3 AC1 29 LEU B 111 SER B 112 HIS B 115 ARG B 117
SITE 4 AC1 29 ARG B 121 MG B 205 MG B 206 HOH B 318
SITE 5 AC1 29 HOH B 319 HOH B 320 HOH B 324 HOH B 327
SITE 6 AC1 29 HOH B 331 HOH B 343 HOH B 348 HOH B 391
SITE 7 AC1 29 HOH B 392 HOH B 394 HOH B 405 HOH B 431
SITE 8 AC1 29 HOH B 437
SITE 1 AC2 16 ASN B 11 THR B 43 ALA B 44 PRO B 45
SITE 2 AC2 16 VAL B 46 TYR B 48 GLN B 51 PHE B 54
SITE 3 AC2 16 ASN B 56 GLY B 90 PRO B 91 ARG B 92
SITE 4 AC2 16 ARG B 121 PHE B 123 HOH B 343 HOH B 418
SITE 1 AC3 7 NA A 203 HOH A 353 ASN B 27 TYR B 29
SITE 2 AC3 7 ILE B 32 HOH B 407 HOH B 436
SITE 1 AC4 5 ASP A 107 HOH A 351 HOH A 355 ASP B 107
SITE 2 AC4 5 HOH B 347
SITE 1 AC5 6 ASP B 95 ASP B 97 APC B 201 MG B 206
SITE 2 AC5 6 HOH B 331 HOH B 391
SITE 1 AC6 6 ASP B 95 ASP B 97 APC B 201 MG B 205
SITE 2 AC6 6 HOH B 343 HOH B 394
SITE 1 AC7 4 ILE B 84 ARG B 92 THR B 93 HOH B 475
SITE 1 AC8 27 LEU A 71 ARG A 83 ARG A 92 ASP A 95
SITE 2 AC8 27 ASP A 97 ILE A 98 LYS A 110 LEU A 111
SITE 3 AC8 27 SER A 112 HIS A 115 ARG A 117 ARG A 121
SITE 4 AC8 27 MG A 204 MG A 205 HOH A 312 HOH A 316
SITE 5 AC8 27 HOH A 328 HOH A 333 HOH A 335 HOH A 338
SITE 6 AC8 27 HOH A 341 HOH A 344 HOH A 350 HOH A 377
SITE 7 AC8 27 HOH A 379 HOH A 390 HOH A 400
SITE 1 AC9 15 ASN A 11 THR A 43 ALA A 44 PRO A 45
SITE 2 AC9 15 VAL A 46 GLN A 51 PHE A 54 ASN A 56
SITE 3 AC9 15 GLY A 90 PRO A 91 ARG A 92 ARG A 121
SITE 4 AC9 15 PHE A 123 HOH A 344 HOH A 404
SITE 1 AD1 7 ASN A 27 TYR A 29 ILE A 32 HOH A 353
SITE 2 AD1 7 NA B 203 HOH B 407 HOH B 436
SITE 1 AD2 6 ASP A 95 ASP A 97 APC A 201 MG A 205
SITE 2 AD2 6 HOH A 344 HOH A 390
SITE 1 AD3 6 ASP A 95 ASP A 97 APC A 201 MG A 204
SITE 2 AD3 6 HOH A 333 HOH A 377
SITE 1 AD4 4 ILE A 84 PRO A 91 ARG A 92 THR A 93
CRYST1 47.582 68.110 53.227 90.00 106.12 90.00 P 1 21 1 4
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 0.021016 0.000000 0.006073 0.00000
SCALE2 0.000000 0.014682 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019556 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
