HEADER TRANSFERASE/TRANSFERASE INHIBITOR 12-JAN-11 3QBC
TITLE STRUCTURE AND DESIGN OF A NEW PTERIN SITE INHIBITOR OF S. AUREUS HPPK
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-AMINO-4-HYDROXY-6-HYDROXYMETHYLDIHYDROPTERIDINE
COMPND 3 PYROPHOSPHOKINASE;
COMPND 4 CHAIN: A, B;
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: 158878;
SOURCE 4 STRAIN: MU50;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS PROTEIN-INHIBITOR COMPLEX, FERREDOXIN-LIKE FOLD, KINASE, ATP BINDING,
KEYWDS 2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.S.PEAT,S.CHHABRA,J.D.SWARBRICK
REVDAT 4 23-OCT-19 3QBC 1 REMARK SEQADV
REVDAT 3 27-JUN-12 3QBC 1 JRNL
REVDAT 2 01-FEB-12 3QBC 1 JRNL
REVDAT 1 25-JAN-12 3QBC 0
JRNL AUTH S.CHHABRA,O.DOLEZAL,B.M.COLLINS,J.NEWMAN,J.S.SIMPSON,
JRNL AUTH 2 I.G.MACREADIE,R.FERNLEY,T.S.PEAT,J.D.SWARBRICK
JRNL TITL STRUCTURE OF S. AUREUS HPPK AND THE DISCOVERY OF A NEW
JRNL TITL 2 SUBSTRATE SITE INHIBITOR
JRNL REF PLOS ONE V. 7 29444 2012
JRNL REFN ESSN 1932-6203
JRNL PMID 22276115
JRNL DOI 10.1371/JOURNAL.PONE.0029444
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.CHHABRA,J.NEWMAN,T.S.PEAT,R.T.FERNLEY,J.CAINE,J.S.SIMPSON,
REMARK 1 AUTH 2 J.D.SWARBRICK
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF
REMARK 1 TITL 2 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE FROM
REMARK 1 TITL 3 STAPHYLOCOCCUS AUREUS
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 66 575 2010
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 20445263
REMARK 1 DOI 10.1107/S1744309110010857
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 32158
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1684
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2373
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2170
REMARK 3 BIN FREE R VALUE SET COUNT : 130
REMARK 3 BIN FREE R VALUE : 0.2690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2562
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 254
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.38000
REMARK 3 B22 (A**2) : -0.73000
REMARK 3 B33 (A**2) : -0.48000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.50000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.116
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.115
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.074
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.125
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2824 ; 0.024 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3868 ; 2.156 ; 2.006
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 365 ; 6.293 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 123 ;40.448 ;24.634
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 530 ;15.055 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;18.582 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 448 ; 0.152 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2182 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1730 ; 1.330 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2861 ; 2.075 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1094 ; 2.948 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1000 ; 4.229 ; 4.500
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 : 1.40
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 3QBC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000063429.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-SEP-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
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) : 0.955
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33864
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 50.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.44700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.700
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: 1RAO, 1CBK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 90MM BIS-TRIS(PH 6.5), 10MM SODIUM
REMARK 280 ACETATE(PH 4.6), 175MM SODIUM FORMATE, 1.08M SODIUM MALONATE,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K, PH 7
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 38.28300
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, 3
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 254 O HOH A 266 2.07
REMARK 500 OG1 THR A 93 O HOH A 209 2.11
REMARK 500 O HOH A 189 O HOH A 203 2.16
REMARK 500 O ILE A 32 O HOH A 168 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 OD1 ASN A 20 OE2 GLU B 50 2545 1.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 15 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 LEU B 94 CA - CB - CG ANGL. DEV. = -14.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 85 -62.51 -92.81
REMARK 500 VAL A 124 -60.02 -90.62
REMARK 500 LYS B 86 115.10 147.80
REMARK 500 LYS B 86 114.05 147.85
REMARK 500 ALA B 132 29.41 -141.81
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 B55 A 159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B55 B 163
DBREF 3QBC A 1 158 UNP Q99W87 Q99W87_STAAM 1 158
DBREF 3QBC B 1 158 UNP Q99W87 Q99W87_STAAM 1 158
SEQADV 3QBC GLY A -2 UNP Q99W87 EXPRESSION TAG
SEQADV 3QBC SER A -1 UNP Q99W87 EXPRESSION TAG
SEQADV 3QBC HIS A 0 UNP Q99W87 EXPRESSION TAG
SEQADV 3QBC GLY B -2 UNP Q99W87 EXPRESSION TAG
SEQADV 3QBC SER B -1 UNP Q99W87 EXPRESSION TAG
SEQADV 3QBC HIS B 0 UNP Q99W87 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
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
HET B55 A 159 12
HET B55 B 163 12
HETNAM B55 2-AMINO-8-SULFANYL-1,9-DIHYDRO-6H-PURIN-6-ONE
HETSYN B55 2-AMINO-8-MERCAPTO-1H-PURIN-6(9H)-ONE
FORMUL 3 B55 2(C5 H5 N5 O S)
FORMUL 5 HOH *254(H2 O)
HELIX 1 1 ASP A 14 TYR A 29 1 16
HELIX 2 2 THR A 66 ARG A 83 1 18
HELIX 3 3 LYS A 86 GLY A 90 5 5
HELIX 4 4 ARG A 117 GLU A 120 5 4
HELIX 5 5 ARG A 121 ALA A 133 1 13
HELIX 6 6 VAL A 144 VAL A 148 1 5
HELIX 7 7 ASP B 14 TYR B 29 1 16
HELIX 8 8 THR B 66 HIS B 82 1 17
HELIX 9 9 ARG B 117 GLU B 120 5 4
HELIX 10 10 ARG B 121 ALA B 133 1 13
HELIX 11 11 LYS B 143 VAL B 148 1 6
SHEET 1 A 4 ILE A 32 ILE A 37 0
SHEET 2 A 4 PHE A 54 THR A 63 -1 O GLU A 60 N ASN A 36
SHEET 3 A 4 ILE A 2 SER A 10 -1 N ILE A 2 O THR A 63
SHEET 4 A 4 ASP A 95 TYR A 101 -1 O ASP A 97 N GLY A 7
SHEET 1 B 4 ILE A 32 ILE A 37 0
SHEET 2 B 4 PHE A 54 THR A 63 -1 O GLU A 60 N ASN A 36
SHEET 3 B 4 TYR A 41 THR A 43 -1 N THR A 43 O PHE A 54
SHEET 4 B 4 VAL A 154 ARG A 156 -1 O LYS A 155 N GLU A 42
SHEET 1 C 2 ILE A 106 LEU A 108 0
SHEET 2 C 2 LEU A 111 VAL A 113 -1 O VAL A 113 N ILE A 106
SHEET 1 D 2 VAL A 136 GLU A 137 0
SHEET 2 D 2 LEU A 142 LYS A 143 -1 O LEU A 142 N GLU A 137
SHEET 1 E 4 ILE B 32 ILE B 37 0
SHEET 2 E 4 PHE B 54 THR B 63 -1 O GLU B 60 N ASN B 36
SHEET 3 E 4 ILE B 2 SER B 10 -1 N ALA B 4 O ILE B 61
SHEET 4 E 4 ASP B 95 TYR B 101 -1 O ASP B 97 N GLY B 7
SHEET 1 F 4 ILE B 32 ILE B 37 0
SHEET 2 F 4 PHE B 54 THR B 63 -1 O GLU B 60 N ASN B 36
SHEET 3 F 4 TYR B 41 THR B 43 -1 N TYR B 41 O ASN B 56
SHEET 4 F 4 VAL B 154 ARG B 156 -1 O LYS B 155 N GLU B 42
SHEET 1 G 2 ILE B 106 LEU B 108 0
SHEET 2 G 2 LEU B 111 VAL B 113 -1 O VAL B 113 N ILE B 106
CISPEP 1 VAL A 113 PRO A 114 0 -9.26
CISPEP 2 VAL B 113 PRO B 114 0 -9.22
SITE 1 AC1 9 THR A 43 ALA A 44 VAL A 46 PHE A 54
SITE 2 AC1 9 ASN A 56 PHE A 123 HOH A 268 PRO B 109
SITE 3 AC1 9 LYS B 110
SITE 1 AC2 10 PRO A 109 LYS A 110 THR B 43 ALA B 44
SITE 2 AC2 10 VAL B 46 PHE B 54 ASN B 56 PHE B 123
SITE 3 AC2 10 HOH B 211 HOH B 249
CRYST1 36.790 76.566 51.522 90.00 100.17 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 0.027182 0.000000 0.004877 0.00000
SCALE2 0.000000 0.013061 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019719 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
