HEADER REPLICATION/DNA 20-JAN-15 4XR0
TITLE ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED WITH
TITLE 2 DNA- G/T MISMATCH.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA REPLICATION TERMINUS SITE-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TER-BINDING PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA (5'-D(*AP*GP*TP*TP*AP*CP*AP*AP*CP*AP*TP*AP*GP*T)-3');
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES;
COMPND 11 OTHER_DETAILS: TERA COMPLIMENTARY STRAND;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: DNA (5'-D(*AP*TP*TP*AP*TP*GP*TP*TP*GP*TP*AP*AP*CP*TP*A)-
COMPND 14 3');
COMPND 15 CHAIN: C;
COMPND 16 ENGINEERED: YES;
COMPND 17 MUTATION: YES;
COMPND 18 OTHER_DETAILS: TERA
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: TUS, TAU, B1610, JW1602;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCM862;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 13 ORGANISM_TAXID: 562;
SOURCE 14 OTHER_DETAILS: TERA;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 18 ORGANISM_TAXID: 562
KEYWDS DNA COMPLEX, REPLICATION, TUS, TER, REPLICATION-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.OAKLEY
REVDAT 5 27-SEP-23 4XR0 1 REMARK
REVDAT 4 01-JAN-20 4XR0 1 JRNL REMARK
REVDAT 3 30-SEP-15 4XR0 1 JRNL
REVDAT 2 16-SEP-15 4XR0 1 JRNL
REVDAT 1 26-AUG-15 4XR0 0
JRNL AUTH M.M.ELSHENAWY,S.JERGIC,Z.Q.XU,M.A.SOBHY,M.TAKAHASHI,
JRNL AUTH 2 A.J.OAKLEY,N.E.DIXON,S.M.HAMDAN
JRNL TITL REPLISOME SPEED DETERMINES THE EFFICIENCY OF THE TUS-TER
JRNL TITL 2 REPLICATION TERMINATION BARRIER.
JRNL REF NATURE V. 525 394 2015
JRNL REFN ESSN 1476-4687
JRNL PMID 26322585
JRNL DOI 10.1038/NATURE14866
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 12822
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) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.296
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 682
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) : 2.79
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 854
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.3750
REMARK 3 BIN FREE R VALUE SET COUNT : 47
REMARK 3 BIN FREE R VALUE : 0.4940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2504
REMARK 3 NUCLEIC ACID ATOMS : 577
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 31
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 66.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.75000
REMARK 3 B22 (A**2) : 2.75000
REMARK 3 B33 (A**2) : -5.50000
REMARK 3 B12 (A**2) : 0.00000
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): 1.943
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.418
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.369
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 41.108
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.924
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.862
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3214 ; 0.016 ; 0.017
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4485 ; 2.160 ; 1.782
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 307 ; 8.520 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 129 ;38.088 ;23.721
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 451 ;23.702 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;17.505 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 476 ; 0.134 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2249 ; 0.011 ; 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): 1231 ; 1.924 ; 2.454
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1537 ; 3.266 ; 3.675
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1983 ; 2.009 ; 2.608
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): 5042 ; 6.363 ;22.264
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 : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 309
REMARK 3 RESIDUE RANGE : A 1001 A 1005
REMARK 3 RESIDUE RANGE : B 401 B 401
REMARK 3 ORIGIN FOR THE GROUP (A): -27.5315 -7.1069 -14.9032
REMARK 3 T TENSOR
REMARK 3 T11: 0.0296 T22: 0.1237
REMARK 3 T33: 0.1641 T12: -0.0473
REMARK 3 T13: -0.0579 T23: 0.0548
REMARK 3 L TENSOR
REMARK 3 L11: 0.7375 L22: 0.9764
REMARK 3 L33: 4.0527 L12: -0.1982
REMARK 3 L13: -0.0546 L23: 0.3530
REMARK 3 S TENSOR
REMARK 3 S11: 0.0241 S12: -0.0210 S13: -0.1333
REMARK 3 S21: 0.0005 S22: 0.0024 S23: 0.1261
REMARK 3 S31: 0.1191 S32: -0.3151 S33: -0.0265
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 311 B 325
REMARK 3 ORIGIN FOR THE GROUP (A): -24.5290 -5.1080 -8.0324
REMARK 3 T TENSOR
REMARK 3 T11: 0.1133 T22: 0.2002
REMARK 3 T33: 0.0476 T12: 0.0412
REMARK 3 T13: 0.0106 T23: 0.0453
REMARK 3 L TENSOR
REMARK 3 L11: 8.9880 L22: 4.9514
REMARK 3 L33: 2.4529 L12: -0.5300
REMARK 3 L13: 0.8212 L23: 1.9636
REMARK 3 S TENSOR
REMARK 3 S11: 0.2417 S12: -0.0958 S13: 0.4003
REMARK 3 S21: 0.2386 S22: -0.1794 S23: 0.1059
REMARK 3 S31: 0.1433 S32: -0.2658 S33: -0.0623
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 328 C 342
REMARK 3 ORIGIN FOR THE GROUP (A): -25.8652 -4.3844 -7.1498
REMARK 3 T TENSOR
REMARK 3 T11: 0.0529 T22: 0.1404
REMARK 3 T33: 0.0424 T12: 0.0311
REMARK 3 T13: -0.0310 T23: -0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 1.8783 L22: 6.3113
REMARK 3 L33: 6.2466 L12: 0.0690
REMARK 3 L13: 0.2002 L23: -0.5602
REMARK 3 S TENSOR
REMARK 3 S11: 0.1524 S12: 0.2637 S13: -0.1503
REMARK 3 S21: 0.2753 S22: -0.0053 S23: 0.1185
REMARK 3 S31: -0.1134 S32: -0.5433 S33: -0.1471
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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4XR0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000206146.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2 - 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
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 QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13845
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 75.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 22.10
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 39.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 18.90
REMARK 200 R MERGE FOR SHELL (I) : 0.74000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.600
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: 2I06
REMARK 200
REMARK 200 REMARK: BIPYRAMIDS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8-12% (V/V) PEG 3350, 100 MM NAI, 50
REMARK 280 MM BIS-TRIS, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 124.16750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 32.26150
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 32.26150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 62.08375
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 32.26150
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 32.26150
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 186.25125
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 32.26150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 32.26150
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 62.08375
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 32.26150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 32.26150
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 186.25125
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 124.16750
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 DT B 310
REMARK 465 DT C 327
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 3 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 4 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 198 CG CD NE CZ NH1 NH2
REMARK 470 DT B 311 P OP1 OP2
REMARK 470 DT B 325 C5' C4' O4' C3' O3' C2' C1'
REMARK 470 DT B 325 N1 C2 O2 N3 C4 O4 C5
REMARK 470 DT B 325 C7 C6
REMARK 470 DA C 328 P OP1 OP2
REMARK 470 DA C 342 C5' C4' O4' C3' O3' C2' C1'
REMARK 470 DA C 342 N9 C8 N7 C5 C6 N6 N1
REMARK 470 DA C 342 C2 N3 C4
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 OH TYR A 280 O HOH A 1107 2.03
REMARK 500 OG SER A 88 OP1 DA B 323 2.06
REMARK 500 O ASP A 247 N LYS A 249 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 DC B 320 O3' DA B 321 P -0.092
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 PRO A 42 C - N - CA ANGL. DEV. = -15.0 DEGREES
REMARK 500 VAL A 307 CB - CA - C ANGL. DEV. = -12.5 DEGREES
REMARK 500 DC B 317 C1' - O4' - C4' ANGL. DEV. = -7.1 DEGREES
REMARK 500 DA B 318 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DA B 323 O5' - P - OP1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 DA C 338 O4' - C1' - N9 ANGL. DEV. = 2.2 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 3 -98.17 -123.47
REMARK 500 ASP A 5 -45.85 74.42
REMARK 500 GLU A 29 10.08 -60.10
REMARK 500 ASN A 51 142.38 -32.80
REMARK 500 PRO A 52 174.37 -56.03
REMARK 500 ILE A 79 21.88 -77.34
REMARK 500 ASN A 85 -16.20 -46.86
REMARK 500 VAL A 130 -61.24 -133.06
REMARK 500 ASN A 174 75.76 -115.79
REMARK 500 ARG A 183 -28.25 -38.04
REMARK 500 LEU A 194 -83.77 -66.89
REMARK 500 LYS A 195 104.06 -59.54
REMARK 500 SER A 196 -104.14 169.46
REMARK 500 PRO A 197 -88.35 -84.92
REMARK 500 ARG A 198 -170.91 88.40
REMARK 500 SER A 199 78.47 54.17
REMARK 500 ALA A 201 -82.30 -12.23
REMARK 500 ARG A 205 -53.03 16.25
REMARK 500 LYS A 227 99.84 -67.82
REMARK 500 LYS A 229 148.19 179.17
REMARK 500 LYS A 235 152.49 -49.55
REMARK 500 GLN A 248 68.02 -51.31
REMARK 500 GLN A 292 140.11 -37.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR A 204 ARG A 205 146.36
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 IOD A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ECR RELATED DB: PDB
REMARK 900 ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED
REMARK 900 WITH DNA
REMARK 900 RELATED ID: 2EWJ RELATED DB: PDB
REMARK 900 ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED
REMARK 900 WITH DNA
REMARK 900 RELATED ID: 2I05 RELATED DB: PDB
REMARK 900 ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED
REMARK 900 WITH DNA
REMARK 900 RELATED ID: 2I06 RELATED DB: PDB
REMARK 900 ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED
REMARK 900 WITH DNA- LOCKED FORM
REMARK 900 RELATED ID: 4XR1 RELATED DB: PDB
REMARK 900 RELATED ID: 4XR2 RELATED DB: PDB
REMARK 900 RELATED ID: 4XR3 RELATED DB: PDB
DBREF 4XR0 A 1 309 UNP P16525 TUS_ECOLI 1 309
DBREF 4XR0 B 310 325 PDB 4XR0 4XR0 310 325
DBREF 4XR0 C 327 342 PDB 4XR0 4XR0 327 342
SEQADV 4XR0 MET A -6 UNP P16525 INITIATING METHIONINE
SEQADV 4XR0 HIS A -5 UNP P16525 EXPRESSION TAG
SEQADV 4XR0 HIS A -4 UNP P16525 EXPRESSION TAG
SEQADV 4XR0 HIS A -3 UNP P16525 EXPRESSION TAG
SEQADV 4XR0 HIS A -2 UNP P16525 EXPRESSION TAG
SEQADV 4XR0 HIS A -1 UNP P16525 EXPRESSION TAG
SEQADV 4XR0 HIS A 0 UNP P16525 EXPRESSION TAG
SEQRES 1 A 316 MET HIS HIS HIS HIS HIS HIS MET ALA ARG TYR ASP LEU
SEQRES 2 A 316 VAL ASP ARG LEU ASN THR THR PHE ARG GLN MET GLU GLN
SEQRES 3 A 316 GLU LEU ALA ILE PHE ALA ALA HIS LEU GLU GLN HIS LYS
SEQRES 4 A 316 LEU LEU VAL ALA ARG VAL PHE SER LEU PRO GLU VAL LYS
SEQRES 5 A 316 LYS GLU ASP GLU HIS ASN PRO LEU ASN ARG ILE GLU VAL
SEQRES 6 A 316 LYS GLN HIS LEU GLY ASN ASP ALA GLN SER LEU ALA LEU
SEQRES 7 A 316 ARG HIS PHE ARG HIS LEU PHE ILE GLN GLN GLN SER GLU
SEQRES 8 A 316 ASN ARG SER SER LYS ALA ALA VAL ARG LEU PRO GLY VAL
SEQRES 9 A 316 LEU CYS TYR GLN VAL ASP ASN LEU SER GLN ALA ALA LEU
SEQRES 10 A 316 VAL SER HIS ILE GLN HIS ILE ASN LYS LEU LYS THR THR
SEQRES 11 A 316 PHE GLU HIS ILE VAL THR VAL GLU SER GLU LEU PRO THR
SEQRES 12 A 316 ALA ALA ARG PHE GLU TRP VAL HIS ARG HIS LEU PRO GLY
SEQRES 13 A 316 LEU ILE THR LEU ASN ALA TYR ARG THR LEU THR VAL LEU
SEQRES 14 A 316 HIS ASP PRO ALA THR LEU ARG PHE GLY TRP ALA ASN LYS
SEQRES 15 A 316 HIS ILE ILE LYS ASN LEU HIS ARG ASP GLU VAL LEU ALA
SEQRES 16 A 316 GLN LEU GLU LYS SER LEU LYS SER PRO ARG SER VAL ALA
SEQRES 17 A 316 PRO TRP THR ARG GLU GLU TRP GLN ARG LYS LEU GLU ARG
SEQRES 18 A 316 GLU TYR GLN ASP ILE ALA ALA LEU PRO GLN ASN ALA LYS
SEQRES 19 A 316 LEU LYS ILE LYS ARG PRO VAL LYS VAL GLN PRO ILE ALA
SEQRES 20 A 316 ARG VAL TRP TYR LYS GLY ASP GLN LYS GLN VAL GLN HIS
SEQRES 21 A 316 ALA CYS PRO THR PRO LEU ILE ALA LEU ILE ASN ARG ASP
SEQRES 22 A 316 ASN GLY ALA GLY VAL PRO ASP VAL GLY GLU LEU LEU ASN
SEQRES 23 A 316 TYR ASP ALA ASP ASN VAL GLN HIS ARG TYR LYS PRO GLN
SEQRES 24 A 316 ALA GLN PRO LEU ARG LEU ILE ILE PRO ARG LEU HIS LEU
SEQRES 25 A 316 TYR VAL ALA ASP
SEQRES 1 B 16 DT DT DA DG DT DT DA DC DA DA DC DA DT
SEQRES 2 B 16 DA DG DT
SEQRES 1 C 16 DT DA DT DT DA DT DG DT DT DG DT DA DA
SEQRES 2 C 16 DC DT DA
HET IOD A1001 1
HET IOD A1002 1
HET IOD A1003 1
HET IOD A1004 1
HET IOD A1005 1
HET MPD B 401 8
HETNAM IOD IODIDE ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 4 IOD 5(I 1-)
FORMUL 9 MPD C6 H14 O2
FORMUL 10 HOH *31(H2 O)
HELIX 1 AA1 LEU A 6 GLU A 29 1 24
HELIX 2 AA2 GLY A 63 ARG A 75 1 13
HELIX 3 AA3 ASP A 103 VAL A 130 1 28
HELIX 4 AA4 PRO A 135 LEU A 147 1 13
HELIX 5 AA5 ILE A 151 ARG A 157 1 7
HELIX 6 AA6 ARG A 183 LYS A 195 1 13
HELIX 7 AA7 THR A 204 ALA A 221 1 18
HELIX 8 AA8 ASP A 266 GLY A 268 5 3
HELIX 9 AA9 ASP A 283 VAL A 285 5 3
HELIX 10 AB1 PRO A 301 LEU A 303 5 3
SHEET 1 AA1 5 LYS A 59 LEU A 62 0
SHEET 2 AA1 5 LEU A 33 SER A 40 -1 N VAL A 38 O HIS A 61
SHEET 3 AA1 5 GLY A 96 VAL A 102 -1 O VAL A 97 N ARG A 37
SHEET 4 AA1 5 LEU A 259 ASN A 264 1 O ILE A 263 N TYR A 100
SHEET 5 AA1 5 VAL A 161 HIS A 163 1 N LEU A 162 O LEU A 262
SHEET 1 AA2 2 ARG A 55 ILE A 56 0
SHEET 2 AA2 2 TYR A 280 ASP A 281 -1 O TYR A 280 N ILE A 56
SHEET 1 AA3 4 VAL A 251 ALA A 254 0
SHEET 2 AA3 4 GLN A 237 TRP A 243 -1 N ALA A 240 O HIS A 253
SHEET 3 AA3 4 THR A 167 ALA A 173 -1 N ALA A 173 O GLN A 237
SHEET 4 AA3 4 ASP A 273 VAL A 274 1 O ASP A 273 N LEU A 168
SHEET 1 AA4 4 HIS A 176 HIS A 182 0
SHEET 2 AA4 4 LYS A 227 PRO A 233 -1 O ARG A 232 N ILE A 177
SHEET 3 AA4 4 LEU A 305 VAL A 307 -1 O TYR A 306 N LYS A 229
SHEET 4 AA4 4 ARG A 297 ILE A 300 -1 N ILE A 299 O LEU A 305
SITE 1 AC1 1 ASP A 103
SITE 1 AC2 2 GLN A 30 ARG A 297
SITE 1 AC3 1 ARG A 232
SITE 1 AC4 1 ALA A 36
SITE 1 AC5 1 GLN A 224
SITE 1 AC6 5 GLU A 125 DA B 319 DC B 320 DT C 335
SITE 2 AC6 5 DG C 336
CRYST1 64.523 64.523 248.335 90.00 90.00 90.00 P 41 21 2 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 0.015498 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015498 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004027 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
