HEADER TRANSCRIPTION 11-FEB-18 6FPL
TITLE TETR(D) E147A MUTANT IN COMPLEX WITH TETRACYCLINE AND MAGNESIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TETRACYCLINE REPRESSOR PROTEIN CLASS D;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: STOP CODON AT 209, C-TERMINUS REMOVED FOR BETTER
COMPND 7 CRYSTALLIZATION
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: TETR;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PWH1950
KEYWDS TRANSCRIPTION REGULATION, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR W.HINRICHS,G.J.PALM,L.BERNDT,B.GIRBARDT
REVDAT 3 17-JAN-24 6FPL 1 REMARK LINK
REVDAT 2 18-MAR-20 6FPL 1 JRNL
REVDAT 1 13-MAR-19 6FPL 0
JRNL AUTH G.J.PALM,I.BUCHHOLZ,S.WERTEN,B.GIRBARDT,L.BERNDT,M.DELCEA,
JRNL AUTH 2 W.HINRICHS
JRNL TITL THERMODYNAMICS, COOPERATIVITY AND STABILITY OF THE
JRNL TITL 2 TETRACYCLINE REPRESSOR (TETR) UPON TETRACYCLINE BINDING.
JRNL REF BIOCHIM BIOPHYS ACTA V.1868 40404 2020
JRNL REF 2 PROTEINS PROTEOM
JRNL REFN ISSN 1878-1454
JRNL PMID 32114262
JRNL DOI 10.1016/J.BBAPAP.2020.140404
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.WERTEN,J.SCHNEIDER,G.J.PALM,W.HINRICHS
REMARK 1 TITL MODULAR ORGANISATION OF INDUCER RECOGNITION AND ALLOSTERY IN
REMARK 1 TITL 2 THE TETRACYCLINE REPRESSOR.
REMARK 1 REF FEBS J. V. 283 2102 2016
REMARK 1 REFN ISSN 1742-4658
REMARK 1 PMID 27028290
REMARK 1 DOI 10.1111/FEBS.13723
REMARK 2
REMARK 2 RESOLUTION. 1.60 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 25266
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1318
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1862
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE SET COUNT : 97
REMARK 3 BIN FREE R VALUE : 0.3050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1570
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 95
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.65000
REMARK 3 B22 (A**2) : 1.65000
REMARK 3 B33 (A**2) : -3.30000
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): 0.095
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.096
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.083
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.638
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1677 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1625 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2287 ; 1.837 ; 1.992
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3709 ; 0.939 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 206 ; 5.196 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 81 ;37.058 ;23.457
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 289 ;13.727 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;19.120 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 259 ; 0.146 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1941 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 407 ; 0.001 ; 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): 815 ; 1.987 ; 2.386
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 814 ; 1.981 ; 2.386
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1024 ; 2.647 ; 3.569
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1025 ; 2.646 ; 3.569
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 861 ; 2.904 ; 2.674
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 862 ; 2.903 ; 2.674
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1264 ; 4.275 ; 3.903
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2030 ; 5.226 ;19.550
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1998 ; 5.182 ;19.411
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 45
REMARK 3 RESIDUE RANGE : A 46 A 64
REMARK 3 RESIDUE RANGE : A 1212 A 1216
REMARK 3 ORIGIN FOR THE GROUP (A): 18.9450 28.4028 13.5477
REMARK 3 T TENSOR
REMARK 3 T11: 0.0839 T22: 0.1270
REMARK 3 T33: 0.1150 T12: -0.0335
REMARK 3 T13: -0.0336 T23: -0.0223
REMARK 3 L TENSOR
REMARK 3 L11: 2.1642 L22: 0.6879
REMARK 3 L33: 3.7222 L12: -0.6965
REMARK 3 L13: 2.4130 L23: -0.0900
REMARK 3 S TENSOR
REMARK 3 S11: 0.0063 S12: 0.0536 S13: 0.0397
REMARK 3 S21: 0.1149 S22: 0.0562 S23: -0.0818
REMARK 3 S31: 0.1945 S32: 0.1222 S33: -0.0624
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 7
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 65 A 93
REMARK 3 RESIDUE RANGE : A 101 A 106
REMARK 3 RESIDUE RANGE : A 107 A 123
REMARK 3 RESIDUE RANGE : A 94 A 100
REMARK 3 RESIDUE RANGE : A 124 A 155
REMARK 3 RESIDUE RANGE : A 182 A 208
REMARK 3 RESIDUE RANGE : A 1209 A 1211
REMARK 3 ORIGIN FOR THE GROUP (A): 24.9475 32.4410 39.2720
REMARK 3 T TENSOR
REMARK 3 T11: 0.1312 T22: 0.0812
REMARK 3 T33: 0.1225 T12: 0.0989
REMARK 3 T13: -0.0196 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 0.6441 L22: 0.1503
REMARK 3 L33: 1.1570 L12: 0.2718
REMARK 3 L13: 0.0031 L23: 0.1602
REMARK 3 S TENSOR
REMARK 3 S11: 0.0151 S12: 0.0454 S13: 0.0185
REMARK 3 S21: -0.0005 S22: 0.0093 S23: 0.0448
REMARK 3 S31: 0.0351 S32: -0.0450 S33: -0.0244
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 : A 165 A 181
REMARK 3 ORIGIN FOR THE GROUP (A): 50.5302 20.5510 35.6989
REMARK 3 T TENSOR
REMARK 3 T11: 0.3470 T22: 0.1404
REMARK 3 T33: 0.1830 T12: 0.2007
REMARK 3 T13: 0.0719 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 4.9460 L22: 2.8582
REMARK 3 L33: 0.6175 L12: 3.7540
REMARK 3 L13: 1.7323 L23: 1.3126
REMARK 3 S TENSOR
REMARK 3 S11: -0.0268 S12: 0.1648 S13: -0.4925
REMARK 3 S21: -0.0880 S22: 0.1334 S23: -0.3586
REMARK 3 S31: 0.0290 S32: 0.0824 S33: -0.1066
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 6FPL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1200008642.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28147
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.602
REMARK 200 RESOLUTION RANGE LOW (A) : 63.590
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : 17.66
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.9500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 2TRT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PRECIPITANT 0.1M NA-CITRAT, 0.8M
REMARK 280 LI2SO4, 0.5M (NH4)2SO4, 0.1ML PROTEIN (10.19MG/ML, 0.1M MES PH
REMARK 280 6.5) + 0.1ML 2MM TC + 0.001ML 3M MGCL2 1:4 PRECIPITANT/PROTEIN,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -Y+1/2,-X+1/2,-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 34.01000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 34.01000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 89.51500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.01000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 44.75750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.01000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 134.27250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.01000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 134.27250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.01000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 44.75750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 34.01000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 34.01000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 89.51500
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 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 34.01000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 34.01000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 89.51500
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 34.01000
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 134.27250
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 34.01000
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 44.75750
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 34.01000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 44.75750
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 34.01000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 134.27250
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 34.01000
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 34.01000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 89.51500
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: 8850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -161.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 68.02000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 68.02000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 429 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 495 LIES ON A SPECIAL POSITION.
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 THR A 156
REMARK 465 ASP A 157
REMARK 465 ARG A 158
REMARK 465 PRO A 159
REMARK 465 ALA A 160
REMARK 465 ALA A 161
REMARK 465 PRO A 162
REMARK 465 ASP A 163
REMARK 465 GLU A 164
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 107 CB CG CD OE1 OE2
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 409 O HOH A 484 2.11
REMARK 500 OE1 GLU A 58 O HOH A 401 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 OE1 GLN A 32 OE1 GLN A 32 15555 2.06
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 LEU A 41 CB - CG - CD2 ANGL. DEV. = 14.2 DEGREES
REMARK 500 ARG A 171 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG A 171 NE - CZ - NH2 ANGL. DEV. = 7.7 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 TYR A 66 63.76 -102.28
REMARK 500 LEU A 204 -123.11 51.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 495 DISTANCE = 6.00 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TAC A 301 O11
REMARK 620 2 TAC A 301 O12 86.4
REMARK 620 3 HOH A 421 O 93.2 178.6
REMARK 620 4 HOH A 439 O 93.7 91.3 87.4
REMARK 620 5 HOH A 457 O 86.9 94.0 87.3 174.7
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TAC A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 308
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2TRT RELATED DB: PDB
REMARK 900 TETR(D) TETRACYCLINE COMPLEX
REMARK 900 RELATED ID: 2TCT RELATED DB: PDB
REMARK 900 TETR(D) 7-CHLORTETRACYCLINE COMPLEX
DBREF 6FPL A 2 208 UNP P0ACT4 TETR4_ECOLX 2 208
SEQADV 6FPL SER A 2 UNP P0ACT4 ALA 2 ENGINEERED MUTATION
SEQADV 6FPL ALA A 147 UNP P0ACT4 GLU 147 ENGINEERED MUTATION
SEQRES 1 A 207 SER ARG LEU ASN ARG GLU SER VAL ILE ASP ALA ALA LEU
SEQRES 2 A 207 GLU LEU LEU ASN GLU THR GLY ILE ASP GLY LEU THR THR
SEQRES 3 A 207 ARG LYS LEU ALA GLN LYS LEU GLY ILE GLU GLN PRO THR
SEQRES 4 A 207 LEU TYR TRP HIS VAL LYS ASN LYS ARG ALA LEU LEU ASP
SEQRES 5 A 207 ALA LEU ALA VAL GLU ILE LEU ALA ARG HIS HIS ASP TYR
SEQRES 6 A 207 SER LEU PRO ALA ALA GLY GLU SER TRP GLN SER PHE LEU
SEQRES 7 A 207 ARG ASN ASN ALA MET SER PHE ARG ARG ALA LEU LEU ARG
SEQRES 8 A 207 TYR ARG ASP GLY ALA LYS VAL HIS LEU GLY THR ARG PRO
SEQRES 9 A 207 ASP GLU LYS GLN TYR ASP THR VAL GLU THR GLN LEU ARG
SEQRES 10 A 207 PHE MET THR GLU ASN GLY PHE SER LEU ARG ASP GLY LEU
SEQRES 11 A 207 TYR ALA ILE SER ALA VAL SER HIS PHE THR LEU GLY ALA
SEQRES 12 A 207 VAL LEU ALA GLN GLN GLU HIS THR ALA ALA LEU THR ASP
SEQRES 13 A 207 ARG PRO ALA ALA PRO ASP GLU ASN LEU PRO PRO LEU LEU
SEQRES 14 A 207 ARG GLU ALA LEU GLN ILE MET ASP SER ASP ASP GLY GLU
SEQRES 15 A 207 GLN ALA PHE LEU HIS GLY LEU GLU SER LEU ILE ARG GLY
SEQRES 16 A 207 PHE GLU VAL GLN LEU THR ALA LEU LEU GLN ILE VAL
HET TAC A 301 32
HET MG A 302 1
HET CL A 303 1
HET CL A 304 1
HET CL A 305 1
HET CL A 306 1
HET CL A 307 1
HET CL A 308 1
HETNAM TAC TETRACYCLINE
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
FORMUL 2 TAC C22 H24 N2 O8
FORMUL 3 MG MG 2+
FORMUL 4 CL 6(CL 1-)
FORMUL 10 HOH *95(H2 O)
HELIX 1 AA1 ASN A 5 GLY A 21 1 17
HELIX 2 AA2 THR A 26 GLY A 35 1 10
HELIX 3 AA3 GLU A 37 VAL A 45 1 9
HELIX 4 AA4 ASN A 47 HIS A 64 1 18
HELIX 5 AA5 SER A 74 ARG A 92 1 19
HELIX 6 AA6 ASP A 95 LEU A 101 1 7
HELIX 7 AA7 ASP A 106 LYS A 108 5 3
HELIX 8 AA8 GLN A 109 ASN A 123 1 15
HELIX 9 AA9 SER A 126 LEU A 155 1 30
HELIX 10 AB1 PRO A 167 ASP A 180 1 14
HELIX 11 AB2 GLY A 182 LEU A 204 1 23
LINK O11 TAC A 301 MG MG A 302 1555 1555 2.00
LINK O12 TAC A 301 MG MG A 302 1555 1555 1.90
LINK MG MG A 302 O HOH A 421 1555 1555 2.13
LINK MG MG A 302 O HOH A 439 1555 1555 2.03
LINK MG MG A 302 O HOH A 457 1555 1555 2.19
SITE 1 AC1 17 HIS A 64 SER A 67 ASN A 82 PHE A 86
SITE 2 AC1 17 HIS A 100 ARG A 104 PRO A 105 VAL A 113
SITE 3 AC1 17 GLN A 116 ILE A 134 SER A 138 MET A 177
SITE 4 AC1 17 MG A 302 HOH A 421 HOH A 439 HOH A 445
SITE 5 AC1 17 HOH A 457
SITE 1 AC2 5 HIS A 100 TAC A 301 HOH A 421 HOH A 439
SITE 2 AC2 5 HOH A 457
SITE 1 AC3 2 GLY A 102 HOH A 421
SITE 1 AC4 5 ARG A 3 LEU A 4 GLN A 76 ARG A 80
SITE 2 AC4 5 HOH A 446
SITE 1 AC5 3 ASN A 5 ARG A 6 GLU A 7
SITE 1 AC6 2 THR A 26 THR A 27
SITE 1 AC7 4 SER A 2 ARG A 3 SER A 74 SER A 77
SITE 1 AC8 1 THR A 26
CRYST1 68.020 68.020 179.030 90.00 90.00 90.00 I 41 2 2 16
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 0.014702 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014702 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005586 0.00000
(ATOM LINES ARE NOT SHOWN.)
END