HEADER TRANSCRIPTION 26-SEP-17 6EKP
TITLE TRYPTOPHAN REPRESSOR TRPR FROM E.COLI VARIANT T44L T81M S88Y WITH
TITLE 2 INDOLE-3-ACETIC ACID AS LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRP OPERON REPRESSOR;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: TRPR, RTRY, B4393, JW4356;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET21
KEYWDS LIGAND BINDING, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.STIEL,S.SHANMUGARATNAM,O.HERUD-SIKIMIC,G.JUERGENS,B.HOCKER
REVDAT 3 17-JAN-24 6EKP 1 REMARK
REVDAT 2 07-APR-21 6EKP 1 JRNL
REVDAT 1 30-JAN-19 6EKP 0
JRNL AUTH O.HERUD-SIKIMIC,A.C.STIEL,M.KOLB,S.SHANMUGARATNAM,
JRNL AUTH 2 K.W.BERENDZEN,C.FELDHAUS,B.HOCKER,G.JUERGENS
JRNL TITL A BIOSENSOR FOR THE DIRECT VISUALIZATION OF AUXIN
JRNL REF NATURE 2021
JRNL REFN ESSN 1476-4687
JRNL DOI 10.1038/S41586-021-03425-2
REMARK 2
REMARK 2 RESOLUTION. 1.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.90
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 39386
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1970
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 41.9215 - 3.5127 0.99 2858 151 0.1625 0.1811
REMARK 3 2 3.5127 - 2.7883 1.00 2767 146 0.1622 0.1688
REMARK 3 3 2.7883 - 2.4359 1.00 2740 144 0.1628 0.1878
REMARK 3 4 2.4359 - 2.2132 1.00 2702 142 0.1541 0.1656
REMARK 3 5 2.2132 - 2.0546 1.00 2693 142 0.1635 0.1690
REMARK 3 6 2.0546 - 1.9334 0.99 2700 142 0.1760 0.2184
REMARK 3 7 1.9334 - 1.8366 1.00 2679 141 0.1929 0.2173
REMARK 3 8 1.8366 - 1.7567 0.99 2655 140 0.1869 0.2033
REMARK 3 9 1.7567 - 1.6890 0.99 2673 141 0.2023 0.2131
REMARK 3 10 1.6890 - 1.6307 0.99 2631 138 0.2140 0.2586
REMARK 3 11 1.6307 - 1.5798 0.98 2618 138 0.2264 0.2692
REMARK 3 12 1.5798 - 1.5346 0.97 2613 137 0.2543 0.2756
REMARK 3 13 1.5346 - 1.4942 0.98 2614 138 0.2648 0.2965
REMARK 3 14 1.4942 - 1.4577 0.93 2473 130 0.3216 0.3292
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.430
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.17
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.20
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 1759
REMARK 3 ANGLE : 0.497 2370
REMARK 3 CHIRALITY : 0.041 258
REMARK 3 PLANARITY : 0.004 306
REMARK 3 DIHEDRAL : 17.447 687
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 31 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6503 -19.7858 -8.2203
REMARK 3 T TENSOR
REMARK 3 T11: 0.2434 T22: 0.2569
REMARK 3 T33: 0.2503 T12: -0.0066
REMARK 3 T13: 0.0263 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 9.8273 L22: 1.7791
REMARK 3 L33: 5.8166 L12: 1.5301
REMARK 3 L13: 6.4115 L23: 1.4325
REMARK 3 S TENSOR
REMARK 3 S11: 0.0284 S12: -0.5747 S13: 0.0375
REMARK 3 S21: -0.0200 S22: -0.1102 S23: 0.3113
REMARK 3 S31: 0.0488 S32: -0.3293 S33: 0.0713
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 32 THROUGH 63 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0460 -10.2491 -8.4204
REMARK 3 T TENSOR
REMARK 3 T11: 0.1565 T22: 0.2667
REMARK 3 T33: 0.2220 T12: -0.0012
REMARK 3 T13: 0.0089 T23: 0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 1.4349 L22: 7.4564
REMARK 3 L33: 1.1597 L12: -1.1342
REMARK 3 L13: -0.0004 L23: -1.1743
REMARK 3 S TENSOR
REMARK 3 S11: -0.0377 S12: -0.1373 S13: 0.1605
REMARK 3 S21: 0.0214 S22: -0.0269 S23: -0.5378
REMARK 3 S31: -0.0047 S32: 0.0930 S33: 0.0478
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 64 THROUGH 78 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.5498 7.5532 -16.0981
REMARK 3 T TENSOR
REMARK 3 T11: 0.3859 T22: 0.4186
REMARK 3 T33: 0.5495 T12: -0.0330
REMARK 3 T13: 0.0830 T23: 0.0660
REMARK 3 L TENSOR
REMARK 3 L11: 7.6752 L22: 2.1125
REMARK 3 L33: 5.1549 L12: -1.5641
REMARK 3 L13: -3.5478 L23: 0.9333
REMARK 3 S TENSOR
REMARK 3 S11: -0.1230 S12: 0.0880 S13: 0.6527
REMARK 3 S21: -0.5032 S22: 0.1574 S23: -1.1008
REMARK 3 S31: -0.2103 S32: 0.4789 S33: 0.0229
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 79 THROUGH 91 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7148 2.4420 -15.2670
REMARK 3 T TENSOR
REMARK 3 T11: 0.2699 T22: 0.2768
REMARK 3 T33: 0.2487 T12: 0.0225
REMARK 3 T13: -0.0047 T23: 0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 8.6009 L22: 8.4407
REMARK 3 L33: 3.2093 L12: 3.2885
REMARK 3 L13: -3.8335 L23: -4.6084
REMARK 3 S TENSOR
REMARK 3 S11: 0.1045 S12: 0.2486 S13: 0.2608
REMARK 3 S21: -0.5678 S22: 0.1875 S23: 0.2061
REMARK 3 S31: 0.0027 S32: -0.2335 S33: -0.2805
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 92 THROUGH 105 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4747 1.7624 0.3926
REMARK 3 T TENSOR
REMARK 3 T11: 0.3271 T22: 0.3065
REMARK 3 T33: 0.2873 T12: -0.0119
REMARK 3 T13: 0.0307 T23: -0.0561
REMARK 3 L TENSOR
REMARK 3 L11: 2.0835 L22: 8.2091
REMARK 3 L33: 9.4938 L12: 3.8155
REMARK 3 L13: -1.0279 L23: -3.3534
REMARK 3 S TENSOR
REMARK 3 S11: 0.3857 S12: -0.2851 S13: 0.0875
REMARK 3 S21: 0.8909 S22: -0.2079 S23: -0.4046
REMARK 3 S31: -0.7934 S32: 0.3986 S33: -0.0926
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 31 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.2845 -8.4689 -6.4879
REMARK 3 T TENSOR
REMARK 3 T11: 0.2164 T22: 0.3054
REMARK 3 T33: 0.3169 T12: -0.0099
REMARK 3 T13: 0.0010 T23: -0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 4.0032 L22: 2.0259
REMARK 3 L33: 6.6435 L12: 1.4280
REMARK 3 L13: -5.4824 L23: -1.0502
REMARK 3 S TENSOR
REMARK 3 S11: -0.0751 S12: -0.6765 S13: 0.1474
REMARK 3 S21: -0.0924 S22: 0.0298 S23: -0.4014
REMARK 3 S31: 0.0268 S32: 0.5791 S33: 0.0155
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 32 THROUGH 63 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2323 -17.6818 -9.5468
REMARK 3 T TENSOR
REMARK 3 T11: 0.1560 T22: 0.2206
REMARK 3 T33: 0.1546 T12: -0.0102
REMARK 3 T13: 0.0145 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 1.3140 L22: 6.1900
REMARK 3 L33: 1.4041 L12: -0.2794
REMARK 3 L13: -0.0060 L23: 1.6955
REMARK 3 S TENSOR
REMARK 3 S11: 0.0133 S12: -0.1471 S13: -0.0075
REMARK 3 S21: 0.0138 S22: -0.1146 S23: 0.2022
REMARK 3 S31: 0.0717 S32: -0.1048 S33: 0.1402
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 64 THROUGH 91 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4332 -31.7004 -19.0504
REMARK 3 T TENSOR
REMARK 3 T11: 0.2445 T22: 0.2340
REMARK 3 T33: 0.1838 T12: 0.0164
REMARK 3 T13: 0.0371 T23: -0.0301
REMARK 3 L TENSOR
REMARK 3 L11: 5.7424 L22: 4.3951
REMARK 3 L33: 3.9261 L12: 1.1258
REMARK 3 L13: 1.0872 L23: 1.0077
REMARK 3 S TENSOR
REMARK 3 S11: 0.0521 S12: 0.3659 S13: -0.3081
REMARK 3 S21: -0.3071 S22: -0.0451 S23: 0.0631
REMARK 3 S31: 0.1549 S32: -0.2565 S33: 0.0354
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 92 THROUGH 106 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9530 -31.1944 -1.7500
REMARK 3 T TENSOR
REMARK 3 T11: 0.2835 T22: 0.2709
REMARK 3 T33: 0.2159 T12: -0.0247
REMARK 3 T13: -0.0267 T23: 0.0667
REMARK 3 L TENSOR
REMARK 3 L11: 2.2334 L22: 8.7384
REMARK 3 L33: 5.8046 L12: 1.8216
REMARK 3 L13: 1.9994 L23: 0.5710
REMARK 3 S TENSOR
REMARK 3 S11: 0.1327 S12: 0.0154 S13: -0.2262
REMARK 3 S21: 0.5036 S22: 0.0093 S23: 0.3991
REMARK 3 S31: 0.6343 S32: -0.4948 S33: -0.0688
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6EKP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1200006768.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-AUG-14
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 : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000020
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39396
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.460
REMARK 200 RESOLUTION RANGE LOW (A) : 41.904
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 4.292
REMARK 200 R MERGE (I) : 0.03300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.46
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.13
REMARK 200 R MERGE FOR SHELL (I) : 0.82300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: 1TRO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 CALCIUM CHLORIDE 0.1M BIS-TRIS PH
REMARK 280 6.5 30% PEG 550 MME, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 27.51750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 32.32000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.56150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 32.32000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.51750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.56150
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: 6090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 1
REMARK 465 ALA A 2
REMARK 465 GLN A 3
REMARK 465 LYS A 106
REMARK 465 SER A 107
REMARK 465 ASP A 108
REMARK 465 LEU A 109
REMARK 465 GLU A 110
REMARK 465 HIS A 111
REMARK 465 HIS A 112
REMARK 465 HIS A 113
REMARK 465 HIS A 114
REMARK 465 HIS A 115
REMARK 465 HIS A 116
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 SER B 107
REMARK 465 ASP B 108
REMARK 465 LEU B 109
REMARK 465 GLU B 110
REMARK 465 HIS B 111
REMARK 465 HIS B 112
REMARK 465 HIS B 113
REMARK 465 HIS B 114
REMARK 465 HIS B 115
REMARK 465 HIS B 116
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 P3G A 202
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IAC A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue P3G A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IAC B 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6EJW RELATED DB: PDB
REMARK 900 RELATED ID: 6EJZ RELATED DB: PDB
REMARK 900 TRYPTOPHAN REPRESSOR TRPR FROM E.COLI VARIANT S88Y WITH INDOLE-3-
REMARK 900 ACETIC ACID AS LIGAND
REMARK 900 RELATED ID: 6ENI RELATED DB: PDB
REMARK 900 TRYPTOPHAN REPRESSOR TRPR FROM E.COLI VARIANT T44L S88Y WITH INDOLE-
REMARK 900 3-ACETIC ACID AS LIGAND
REMARK 900 RELATED ID: 6ENN RELATED DB: PDB
REMARK 900 TRYPTOPHAN REPRESSOR TRPR FROM E.COLI VARIANT T44L T81M N87G S88Y
REMARK 900 WITH INDOLE-3-ACETIC ACID AS LIGAND
REMARK 900 RELATED ID: 6ELB RELATED DB: PDB
REMARK 900 TRYPTOPHAN REPRESSOR TRPR FROM E.COLI VARIANT M42F T44L T81M N87G
REMARK 900 S88Y WITH INDOLE-3-ACETIC ACID AS LIGAND
REMARK 900 RELATED ID: 6ELF RELATED DB: PDB
REMARK 900 TRYPTOPHAN REPRESSOR TRPR FROM E.COLI VARIANT M42F T44L T81I S88Y
REMARK 900 WITH INDOLE-3-ACETIC ACID AS LIGAND
REMARK 900 RELATED ID: 6ELG RELATED DB: PDB
REMARK 900 TRYPTOPHAN REPRESSOR TRPR FROM E.COLI VARIANT M42F T44L T81I S88Y
REMARK 900 WITH INDOLE-3-ACETONITRILE
DBREF 6EKP A 1 108 UNP P0A881 TRPR_ECOLI 1 108
DBREF 6EKP B 1 108 UNP P0A881 TRPR_ECOLI 1 108
SEQADV 6EKP LEU A 44 UNP P0A881 THR 44 ENGINEERED MUTATION
SEQADV 6EKP MET A 81 UNP P0A881 THR 81 ENGINEERED MUTATION
SEQADV 6EKP TYR A 88 UNP P0A881 SER 88 ENGINEERED MUTATION
SEQADV 6EKP LEU A 109 UNP P0A881 EXPRESSION TAG
SEQADV 6EKP GLU A 110 UNP P0A881 EXPRESSION TAG
SEQADV 6EKP HIS A 111 UNP P0A881 EXPRESSION TAG
SEQADV 6EKP HIS A 112 UNP P0A881 EXPRESSION TAG
SEQADV 6EKP HIS A 113 UNP P0A881 EXPRESSION TAG
SEQADV 6EKP HIS A 114 UNP P0A881 EXPRESSION TAG
SEQADV 6EKP HIS A 115 UNP P0A881 EXPRESSION TAG
SEQADV 6EKP HIS A 116 UNP P0A881 EXPRESSION TAG
SEQADV 6EKP LEU B 44 UNP P0A881 THR 44 ENGINEERED MUTATION
SEQADV 6EKP MET B 81 UNP P0A881 THR 81 ENGINEERED MUTATION
SEQADV 6EKP TYR B 88 UNP P0A881 SER 88 ENGINEERED MUTATION
SEQADV 6EKP LEU B 109 UNP P0A881 EXPRESSION TAG
SEQADV 6EKP GLU B 110 UNP P0A881 EXPRESSION TAG
SEQADV 6EKP HIS B 111 UNP P0A881 EXPRESSION TAG
SEQADV 6EKP HIS B 112 UNP P0A881 EXPRESSION TAG
SEQADV 6EKP HIS B 113 UNP P0A881 EXPRESSION TAG
SEQADV 6EKP HIS B 114 UNP P0A881 EXPRESSION TAG
SEQADV 6EKP HIS B 115 UNP P0A881 EXPRESSION TAG
SEQADV 6EKP HIS B 116 UNP P0A881 EXPRESSION TAG
SEQRES 1 A 116 MET ALA GLN GLN SER PRO TYR SER ALA ALA MET ALA GLU
SEQRES 2 A 116 GLN ARG HIS GLN GLU TRP LEU ARG PHE VAL ASP LEU LEU
SEQRES 3 A 116 LYS ASN ALA TYR GLN ASN ASP LEU HIS LEU PRO LEU LEU
SEQRES 4 A 116 ASN LEU MET LEU LEU PRO ASP GLU ARG GLU ALA LEU GLY
SEQRES 5 A 116 THR ARG VAL ARG ILE VAL GLU GLU LEU LEU ARG GLY GLU
SEQRES 6 A 116 MET SER GLN ARG GLU LEU LYS ASN GLU LEU GLY ALA GLY
SEQRES 7 A 116 ILE ALA MET ILE THR ARG GLY SER ASN TYR LEU LYS ALA
SEQRES 8 A 116 ALA PRO VAL GLU LEU ARG GLN TRP LEU GLU GLU VAL LEU
SEQRES 9 A 116 LEU LYS SER ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 116 MET ALA GLN GLN SER PRO TYR SER ALA ALA MET ALA GLU
SEQRES 2 B 116 GLN ARG HIS GLN GLU TRP LEU ARG PHE VAL ASP LEU LEU
SEQRES 3 B 116 LYS ASN ALA TYR GLN ASN ASP LEU HIS LEU PRO LEU LEU
SEQRES 4 B 116 ASN LEU MET LEU LEU PRO ASP GLU ARG GLU ALA LEU GLY
SEQRES 5 B 116 THR ARG VAL ARG ILE VAL GLU GLU LEU LEU ARG GLY GLU
SEQRES 6 B 116 MET SER GLN ARG GLU LEU LYS ASN GLU LEU GLY ALA GLY
SEQRES 7 B 116 ILE ALA MET ILE THR ARG GLY SER ASN TYR LEU LYS ALA
SEQRES 8 B 116 ALA PRO VAL GLU LEU ARG GLN TRP LEU GLU GLU VAL LEU
SEQRES 9 B 116 LEU LYS SER ASP LEU GLU HIS HIS HIS HIS HIS HIS
HET IAC A 201 21
HET P3G A 202 15
HET IAC B 201 21
HETNAM IAC 1H-INDOL-3-YLACETIC ACID
HETNAM P3G 3,6,9,12,15-PENTAOXAHEPTADECANE
HETSYN IAC INDOLE ACETIC ACID
FORMUL 3 IAC 2(C10 H9 N O2)
FORMUL 4 P3G C12 H26 O5
FORMUL 6 HOH *250(H2 O)
HELIX 1 AA1 SER A 5 ASN A 32 1 28
HELIX 2 AA2 LEU A 34 LEU A 43 1 10
HELIX 3 AA3 LEU A 44 GLY A 64 1 21
HELIX 4 AA4 SER A 67 GLY A 76 1 10
HELIX 5 AA5 GLY A 78 ALA A 92 1 15
HELIX 6 AA6 PRO A 93 LEU A 105 1 13
HELIX 7 AA7 SER B 5 ASN B 32 1 28
HELIX 8 AA8 LEU B 34 LEU B 43 1 10
HELIX 9 AA9 LEU B 44 GLY B 64 1 21
HELIX 10 AB1 SER B 67 GLY B 76 1 10
HELIX 11 AB2 GLY B 78 ALA B 92 1 15
HELIX 12 AB3 PRO B 93 LEU B 105 1 13
SITE 1 AC1 6 ARG A 54 ARG A 84 TYR A 88 HOH A 326
SITE 2 AC1 6 LEU B 41 MET B 42
SITE 1 AC2 9 ASP A 46 GLU A 47 ALA A 50 ARG A 54
SITE 2 AC2 9 HOH A 387 ASP B 46 GLU B 47 ALA B 50
SITE 3 AC2 9 ARG B 54
SITE 1 AC3 6 LEU A 41 MET A 42 ARG B 54 ARG B 84
SITE 2 AC3 6 TYR B 88 HOH B 329
CRYST1 55.035 63.123 64.640 90.00 90.00 90.00 P 21 21 21 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 0.018170 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015842 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015470 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
