HEADER TRANSCRIPTION REGULATION 02-MAR-95 2TCT
TITLE THE COMPLEX FORMED BETWEEN TET REPRESSOR AND TETRACYCLINE-MG2+ REVEALS
TITLE 2 MECHANISM OF ANTIBIOTIC RESISTANCE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TETRACYCLINE REPRESSOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TET REPRESSOR, CLASS D;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: K12 DELTA H1 DELTA TRP;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PWH904 (K. TOVAR, PH.D. THESIS, UNIV.
SOURCE 8 ERLANGEN-NUERNBERG, 1989);
SOURCE 9 OTHER_DETAILS: REMAULT E.,STANSSENS P.,FIERS W. PLASMID VECTORS FOR
SOURCE 10 HIGH-EFFICIENCY EXPRESSION CONTROLLED BY THE PL PROMOTER OF
SOURCE 11 COLIPHAGE LAMBDA. GENE 15, 81-93 (1981).
KEYWDS TRANSCRIPTION REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR W.HINRICHS,C.KISKER,W.SAENGER
REVDAT 5 21-FEB-24 2TCT 1 REMARK LINK
REVDAT 4 29-NOV-17 2TCT 1 HELIX
REVDAT 3 13-JUL-11 2TCT 1 VERSN
REVDAT 2 24-FEB-09 2TCT 1 VERSN
REVDAT 1 03-APR-96 2TCT 0
SPRSDE 03-APR-96 2TCT 1TCT
JRNL AUTH C.KISKER,W.HINRICHS,K.TOVAR,W.HILLEN,W.SAENGER
JRNL TITL THE COMPLEX FORMED BETWEEN TET REPRESSOR AND
JRNL TITL 2 TETRACYCLINE-MG2+ REVEALS MECHANISM OF ANTIBIOTIC
JRNL TITL 3 RESISTANCE.
JRNL REF J.MOL.BIOL. V. 247 260 1995
JRNL REFN ISSN 0022-2836
JRNL PMID 7707374
JRNL DOI 10.1006/JMBI.1994.0138
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.HINRICHS,C.KISKER,M.DUEVEL,A.MUELLER,K.TOVAR,W.HILLEN,
REMARK 1 AUTH 2 W.SAENGER
REMARK 1 TITL STRUCTURE OF THE TET REPRESSOR-TETRACYCLINE COMPLEX AND
REMARK 1 TITL 2 REGULATION OF ANTIBIOTIC RESISTANCE
REMARK 1 REF SCIENCE V. 264 418 1994
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 12229
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1573
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 135
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.017
REMARK 3 BOND ANGLES (DEGREES) : 2.900
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2TCT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178665.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14105
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 34.39000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 34.39000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 90.72500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.39000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 45.36250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.39000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 136.08750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.39000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 136.08750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.39000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 45.36250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 34.39000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 34.39000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 90.72500
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 34.39000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 34.39000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 90.72500
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 34.39000
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 136.08750
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 34.39000
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 45.36250
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 34.39000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 45.36250
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 34.39000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 136.08750
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 34.39000
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 34.39000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 90.72500
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 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 68.78000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 68.78000
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 347 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 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 HIS A 63 NE2 HIS A 63 CD2 -0.069
REMARK 500 HIS A 64 NE2 HIS A 64 CD2 -0.072
REMARK 500 HIS A 139 NE2 HIS A 139 CD2 -0.084
REMARK 500 HIS A 151 NE2 HIS A 151 CD2 -0.068
REMARK 500 HIS A 188 NE2 HIS A 188 CD2 -0.075
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 3 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 3 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 TRP A 43 CD1 - CG - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 TRP A 43 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 49 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 TRP A 75 CD1 - CG - CD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 TRP A 75 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 88 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 LEU A 90 CB - CG - CD1 ANGL. DEV. = -10.3 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 94 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 104 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 171 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 171 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 195 NE - CZ - NH1 ANGL. DEV. = 3.5 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 LEU A 101 124.75 -39.07
REMARK 500 LEU A 204 -114.17 53.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 223 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 100 NE2
REMARK 620 2 CTC A 222 O11 168.5
REMARK 620 3 CTC A 222 O12 95.4 82.0
REMARK 620 4 HOH A 224 O 82.1 99.9 176.0
REMARK 620 5 HOH A 225 O 94.4 96.7 89.1 94.1
REMARK 620 6 HOH A 226 O 87.1 81.9 93.8 83.0 176.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 223
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CTC A 222
DBREF 2TCT A 2 208 UNP P0ACT4 TETR4_ECOLI 1 207
SEQRES 1 A 207 ALA 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 GLU 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 MG A 223 1
HET CTC A 222 33
HETNAM MG MAGNESIUM ION
HETNAM CTC 7-CHLOROTETRACYCLINE
FORMUL 2 MG MG 2+
FORMUL 3 CTC C22 H23 CL N2 O8
FORMUL 4 HOH *135(H2 O)
HELIX 1 A1 ARG A 6 THR A 20 1 15
HELIX 2 A2 THR A 27 LEU A 34 1 8
HELIX 3 A3 GLN A 38 HIS A 44 1 7
HELIX 4 A4 LYS A 48 HIS A 63 1 16
HELIX 5 A5 TRP A 75 LEU A 91 1 17
HELIX 6 A6 GLY A 96 HIS A 100 1 5
HELIX 7 G7 GLU A 107 GLN A 109 5 3
HELIX 8 A7 TYR A 110 GLU A 122 1 13
HELIX 9 A8 LEU A 127 ALA A 153 1 27
HELIX 10 A9 PRO A 168 MET A 177 1 10
HELIX 11 A10 GLU A 183 ALA A 203 1 21
LINK NE2 HIS A 100 MG MG A 223 1555 1555 2.19
LINK O11 CTC A 222 MG MG A 223 1555 1555 2.04
LINK O12 CTC A 222 MG MG A 223 1555 1555 1.73
LINK MG MG A 223 O HOH A 224 1555 1555 2.09
LINK MG MG A 223 O HOH A 225 1555 1555 1.89
LINK MG MG A 223 O HOH A 226 1555 1555 1.93
SITE 1 AC1 5 HIS A 100 CTC A 222 HOH A 224 HOH A 225
SITE 2 AC1 5 HOH A 226
SITE 1 AC2 19 HIS A 64 SER A 67 ASN A 82 PHE A 86
SITE 2 AC2 19 HIS A 100 THR A 103 ARG A 104 VAL A 113
SITE 3 AC2 19 GLN A 116 ILE A 134 SER A 138 LEU A 170
SITE 4 AC2 19 ALA A 173 LEU A 174 MG A 223 HOH A 225
SITE 5 AC2 19 HOH A 226 HOH A 228 HOH A 340
CRYST1 68.780 68.780 181.450 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 0.014539 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014539 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005511 0.00000
(ATOM LINES ARE NOT SHOWN.)
END