HEADER TRANSFERASE 14-SEP-07 2VBQ
TITLE STRUCTURE OF AAC(6')-IY IN COMPLEX WITH BISUBSTRATE ANALOG COA-S-
TITLE 2 MONOMETHYL-ACETYLNEAMINE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINOGLYCOSIDE 6'-N-ACETYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: AMINOGLYCOSIDE ACETYLTRANSFERASE IY;
COMPND 5 EC: 2.3.1.82;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA CHOLERAESUIS;
SOURCE 3 ORGANISM_TAXID: 591;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS AMINOGLYCOSIDE, ACETYLTRANSFERASE, DRUG RESISTANCE, BISUBSTRATE
KEYWDS 2 INHIBITOR, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.W.VETTING,M.L.MAGALHAES,L.FREIBURGER,F.GAO,K.AUCLAIR,J.S.BLANCHARD
REVDAT 6 11-MAR-20 2VBQ 1 REMARK
REVDAT 5 06-MAR-19 2VBQ 1 REMARK
REVDAT 4 05-JUL-17 2VBQ 1 REMARK
REVDAT 3 24-FEB-09 2VBQ 1 VERSN
REVDAT 2 15-JAN-08 2VBQ 1 JRNL
REVDAT 1 08-JAN-08 2VBQ 0
JRNL AUTH M.L.MAGALHAES,M.W.VETTING,F.GAO,L.FREIBURGER,K.AUCLAIR,
JRNL AUTH 2 J.S.BLANCHARD
JRNL TITL KINETIC AND STRUCTURAL ANALYSIS OF BISUBSTRATE INHIBITION OF
JRNL TITL 2 THE SALMONELLA ENTERICA AMINOGLYCOSIDE
JRNL TITL 3 6'-N-ACETYLTRANSFERASE.
JRNL REF BIOCHEMISTRY V. 47 579 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18095712
JRNL DOI 10.1021/BI701957C
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 88.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 20546
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1102
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) : 1365
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2210
REMARK 3 BIN FREE R VALUE SET COUNT : 87
REMARK 3 BIN FREE R VALUE : 0.2670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2310
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 155
REMARK 3 SOLVENT ATOMS : 219
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.04000
REMARK 3 B22 (A**2) : -0.56000
REMARK 3 B33 (A**2) : 0.36000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.19000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.195
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.172
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.106
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.702
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2524 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3428 ; 1.562 ; 2.000
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 289 ; 5.947 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 123 ;34.138 ;23.252
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 397 ;16.498 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;22.006 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 373 ; 0.109 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1896 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1089 ; 0.202 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1670 ; 0.296 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 209 ; 0.150 ; 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): 45 ; 0.203 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.161 ; 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): 1497 ; 0.970 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2308 ; 1.580 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1175 ; 2.326 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1120 ; 3.607 ; 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 : 1.20
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. N-TERMINAL THROMBIN CLEAVABLE 6X-HIS TAG CLEAVED
REMARK 3 PRIOR TO CRYSTALLIZATION (PET28 ORIGIN).
REMARK 4
REMARK 4 2VBQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1290033816.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 190
REMARK 200 PH : 5.75
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : CONFOCAL BLUE
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU-MSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21649
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.9000
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 (%) : 92.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.19000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN (15MG/ML, 10 MM TEA PH 8.0,
REMARK 280 100 MM AMMONIUM SULFATE), PRECIPITANT (20 % PEG6000, 100 MM MES
REMARK 280 PH 5.75) VAPOUR DIFFUSION UNDER OIL, VAPOR DIFFUSION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 42.48200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.29950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 42.48200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.29950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 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 MET A -19
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 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
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 B 2011 O HOH B 2013 2.16
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 O HOH A 2022 O HOH B 2037 3445 2.14
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 VAL B 76 CB - CA - C ANGL. DEV. = -11.9 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 HIS A 25 109.38 -57.81
REMARK 500 PRO A 26 143.71 -39.58
REMARK 500 HIS B 25 128.03 -33.71
REMARK 500 THR B 135 -67.05 -108.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 2-(BIPHENYL-4-SULFONYL)-1,2,3,
REMARK 600 4-TETRAHYDRO-ISOQUINOLINE-3-CARBOXYLIC ACID (BSJ):
REMARK 600 COA-S-MONOMETHYL-ACETYLNEAMINE COENZYMEA COVALENTLY LINKED
REMARK 600 TO N-ACETYLNEAMINE THROUGH A METHYL LINKER NOVEL HETROGEN
REMARK 600 REQUIRES NEW HET CODE
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 NI A1001 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 64 NE2
REMARK 620 2 HIS A 0 NE2 106.0
REMARK 620 3 HIS A 42 NE2 111.8 111.3
REMARK 620 4 ASP A 2 OD1 113.8 114.8 99.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BSJ A1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BSJ B1146
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1S3Z RELATED DB: PDB
REMARK 900 AMINOGLYCOSIDE N-ACETYLTRANSFERASE AAC(6')-IY IN COMPLEXWITH COA
REMARK 900 AND RIBOSTAMYCIN
REMARK 900 RELATED ID: 1S5K RELATED DB: PDB
REMARK 900 AMINOGLYCOSIDE N-ACETYLTRANSFERASE AAC(6')-IY IN COMPLEXWITH COA
REMARK 900 AND N-TERMINAL HIS(6 )-TAG (CRYSTAL FORM 1)
REMARK 900 RELATED ID: 1S60 RELATED DB: PDB
REMARK 900 AMINOGLYCOSIDE N-ACETYLTRANSFERASE AAC(6')-IY IN COMPLEXWITH COA
REMARK 900 AND N-TERMINAL HIS(6 )-TAG (CRYSTAL FORM 2)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 PROTEIN CONTAINS N-TERMINAL TAG
DBREF 2VBQ A -19 0 PDB 2VBQ 2VBQ -19 0
DBREF 2VBQ A 1 145 UNP Q9R381 Q9R381_SALEN 1 145
DBREF 2VBQ B -19 0 PDB 2VBQ 2VBQ -19 0
DBREF 2VBQ B 1 145 UNP Q9R381 Q9R381_SALEN 1 145
SEQRES 1 A 165 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 165 LEU VAL PRO ARG GLY SER HIS MET ASP ILE ARG GLN MET
SEQRES 3 A 165 ASN LYS THR HIS LEU GLU HIS TRP ARG GLY LEU ARG LYS
SEQRES 4 A 165 GLN LEU TRP PRO GLY HIS PRO ASP ASP ALA HIS LEU ALA
SEQRES 5 A 165 ASP GLY GLU GLU ILE LEU GLN ALA ASP HIS LEU ALA SER
SEQRES 6 A 165 PHE ILE ALA MET ALA ASP GLY VAL ALA ILE GLY PHE ALA
SEQRES 7 A 165 ASP ALA SER ILE ARG HIS ASP TYR VAL ASN GLY CYS ASP
SEQRES 8 A 165 SER SER PRO VAL VAL PHE LEU GLU GLY ILE PHE VAL LEU
SEQRES 9 A 165 PRO SER PHE ARG GLN ARG GLY VAL ALA LYS GLN LEU ILE
SEQRES 10 A 165 ALA ALA VAL GLN ARG TRP GLY THR ASN LYS GLY CYS ARG
SEQRES 11 A 165 GLU MET ALA SER ASP THR SER PRO GLU ASN THR ILE SER
SEQRES 12 A 165 GLN LYS VAL HIS GLN ALA LEU GLY PHE GLU GLU THR GLU
SEQRES 13 A 165 ARG VAL ILE PHE TYR ARG LYS ARG CYS
SEQRES 1 B 165 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 165 LEU VAL PRO ARG GLY SER HIS MET ASP ILE ARG GLN MET
SEQRES 3 B 165 ASN LYS THR HIS LEU GLU HIS TRP ARG GLY LEU ARG LYS
SEQRES 4 B 165 GLN LEU TRP PRO GLY HIS PRO ASP ASP ALA HIS LEU ALA
SEQRES 5 B 165 ASP GLY GLU GLU ILE LEU GLN ALA ASP HIS LEU ALA SER
SEQRES 6 B 165 PHE ILE ALA MET ALA ASP GLY VAL ALA ILE GLY PHE ALA
SEQRES 7 B 165 ASP ALA SER ILE ARG HIS ASP TYR VAL ASN GLY CYS ASP
SEQRES 8 B 165 SER SER PRO VAL VAL PHE LEU GLU GLY ILE PHE VAL LEU
SEQRES 9 B 165 PRO SER PHE ARG GLN ARG GLY VAL ALA LYS GLN LEU ILE
SEQRES 10 B 165 ALA ALA VAL GLN ARG TRP GLY THR ASN LYS GLY CYS ARG
SEQRES 11 B 165 GLU MET ALA SER ASP THR SER PRO GLU ASN THR ILE SER
SEQRES 12 B 165 GLN LYS VAL HIS GLN ALA LEU GLY PHE GLU GLU THR GLU
SEQRES 13 B 165 ARG VAL ILE PHE TYR ARG LYS ARG CYS
HET BSJ A1000 74
HET NI A1001 1
HET GOL A1002 6
HET BSJ B1146 74
HETNAM BSJ (3R,9Z)-17-[(2R,3S,4R,5R,6R)-5-AMINO-6-{[(1R,2R,3S,4R,
HETNAM 2 BSJ 6S)-4,6-DIAMINO-2,3-DIHYDROXYCYCLOHEXYL]OXY}-3,4-
HETNAM 3 BSJ DIHYDROXYTETRAHYDRO-2H-PYRAN-2-YL]-3-HYDROXY-2,2-
HETNAM 4 BSJ DIMETHYL-4,8,15-TRIOXO-12-THIA-5,9,16-TRIAZAHEPTADEC-
HETNAM 5 BSJ 9-EN-1-YL [(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-4-
HETNAM 6 BSJ HYDROXY-3-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]METHYL
HETNAM 7 BSJ DIHYDROGEN DIPHOSPHATE
HETNAM NI NICKEL (II) ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 BSJ 2(C36 H62 N11 O23 P3 S)
FORMUL 4 NI NI 2+
FORMUL 5 GOL C3 H8 O3
FORMUL 7 HOH *219(H2 O)
HELIX 1 1 ASN A 7 THR A 9 5 3
HELIX 2 2 HIS A 10 TRP A 22 1 13
HELIX 3 3 PRO A 26 ALA A 40 1 15
HELIX 4 4 PRO A 85 ARG A 88 5 4
HELIX 5 5 GLY A 91 LYS A 107 1 17
HELIX 6 6 ASN A 120 LEU A 130 1 11
HELIX 7 7 ASN B 7 THR B 9 5 3
HELIX 8 8 HIS B 10 TRP B 22 1 13
HELIX 9 9 PRO B 26 ALA B 40 1 15
HELIX 10 10 PRO B 85 ARG B 88 5 4
HELIX 11 11 GLY B 91 LYS B 107 1 17
HELIX 12 12 ASN B 120 LEU B 130 1 11
SHEET 1 AA12 ASP A 2 GLN A 5 0
SHEET 2 AA12 LEU A 43 ALA A 50 -1 O ILE A 47 N ARG A 4
SHEET 3 AA12 VAL A 53 ARG A 63 -1 O VAL A 53 N ALA A 50
SHEET 4 AA12 VAL A 75 VAL A 83 -1 O VAL A 75 N ARG A 63
SHEET 5 AA12 GLU A 111 THR A 116 1 O GLU A 111 N VAL A 76
SHEET 6 AA12 GLU B 133 ARG B 144 -1 O ILE B 139 N THR A 116
SHEET 7 AA12 GLU A 133 ARG A 144 -1 O GLU A 133 N ARG B 142
SHEET 8 AA12 GLU B 111 THR B 116 -1 O MET B 112 N LYS A 143
SHEET 9 AA12 VAL B 75 VAL B 83 1 O VAL B 76 N ALA B 113
SHEET 10 AA12 VAL B 53 ARG B 63 -1 O PHE B 57 N PHE B 82
SHEET 11 AA12 LEU B 43 ALA B 50 -1 O ALA B 44 N ALA B 60
SHEET 12 AA12 ILE B 3 GLN B 5 -1 O ARG B 4 N ILE B 47
LINK NI NI A1001 NE2 HIS A 64 1555 4545 1.98
LINK NI NI A1001 NE2 HIS A 0 1555 1555 1.94
LINK NI NI A1001 NE2 HIS A 42 1555 4545 2.03
LINK NI NI A1001 OD1 ASP A 2 1555 1555 2.03
CISPEP 1 SER A 73 PRO A 74 0 2.85
CISPEP 2 SER B 73 PRO B 74 0 5.30
SITE 1 AC1 38 LEU A 21 TRP A 22 HIS A 25 GLU A 79
SITE 2 AC1 38 GLY A 80 ILE A 81 PHE A 82 VAL A 83
SITE 3 AC1 38 ARG A 88 GLN A 89 ARG A 90 GLY A 91
SITE 4 AC1 38 VAL A 92 ALA A 93 LYS A 94 ASP A 115
SITE 5 AC1 38 THR A 116 ASN A 120 ILE A 122 SER A 123
SITE 6 AC1 38 VAL A 126 ALA A 129 LEU A 130 HOH A2057
SITE 7 AC1 38 HOH A2094 HOH A2095 HOH A2096 HOH A2098
SITE 8 AC1 38 HOH A2099 HOH A2100 HOH A2101 HOH A2102
SITE 9 AC1 38 HOH A2104 TYR B 66 ASN B 68 ARG B 110
SITE 10 AC1 38 GLU B 136 VAL B 138
SITE 1 AC2 4 HIS A 0 ASP A 2 HIS A 42 HIS A 64
SITE 1 AC3 41 TYR A 66 ASN A 68 GLU A 136 VAL A 138
SITE 2 AC3 41 TRP B 22 HIS B 25 GLU B 79 GLY B 80
SITE 3 AC3 41 ILE B 81 PHE B 82 VAL B 83 ARG B 88
SITE 4 AC3 41 GLN B 89 ARG B 90 GLY B 91 VAL B 92
SITE 5 AC3 41 ALA B 93 LYS B 94 ASP B 115 THR B 116
SITE 6 AC3 41 ASN B 120 ILE B 122 SER B 123 VAL B 126
SITE 7 AC3 41 HIS B 127 ALA B 129 LEU B 130 HOH B2032
SITE 8 AC3 41 HOH B2049 HOH B2097 HOH B2098 HOH B2100
SITE 9 AC3 41 HOH B2103 HOH B2104 HOH B2105 HOH B2106
SITE 10 AC3 41 HOH B2107 HOH B2108 HOH B2109 HOH B2110
SITE 11 AC3 41 HOH B2111
SITE 1 AC4 7 GLU A 36 HIS A 42 LEU A 43 SER A 61
SITE 2 AC4 7 HOH A2108 HIS B 64 ASP B 65
CRYST1 84.964 44.599 88.387 90.00 93.92 90.00 C 1 2 1 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 0.011770 0.000000 0.000806 0.00000
SCALE2 0.000000 0.022422 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011340 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
