HEADER TRANSCRIPTION 19-JUL-11 3SZT
TITLE QUORUM SENSING CONTROL REPRESSOR, QSCR, BOUND TO N-3-OXO-DODECANOYL-L-
TITLE 2 HOMOSERINE LACTONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: QUORUM-SENSING CONTROL REPRESSOR;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: QCSR;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 STRAIN: PA01;
SOURCE 5 GENE: PA1898, QSCR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: T7;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3A-QSCR
KEYWDS QUORUM SENSING ACYL-HOMOSERINE LACTONE, HELIX-TURN-HELIX,
KEYWDS 2 TRANSCRIPTION FACTOR, 3-OXO-C12 HSL, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.E.A.CHURCHILL,M.J.LINTZ
REVDAT 5 03-APR-24 3SZT 1 REMARK
REVDAT 4 28-FEB-24 3SZT 1 REMARK
REVDAT 3 08-NOV-17 3SZT 1 REMARK
REVDAT 2 05-OCT-11 3SZT 1 JRNL
REVDAT 1 28-SEP-11 3SZT 0
JRNL AUTH M.J.LINTZ,K.OINUMA,C.L.WYSOCZYNSKI,E.P.GREENBERG,
JRNL AUTH 2 M.E.CHURCHILL
JRNL TITL CRYSTAL STRUCTURE OF QSCR, A PSEUDOMONAS AERUGINOSA QUORUM
JRNL TITL 2 SENSING SIGNAL RECEPTOR.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 108 15763 2011
JRNL REFN ISSN 0027-8424
JRNL PMID 21911405
JRNL DOI 10.1073/PNAS.1112398108
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 17116
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) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 953
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) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.61
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1238
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.3350
REMARK 3 BIN FREE R VALUE SET COUNT : 70
REMARK 3 BIN FREE R VALUE : 0.3970
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3608
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 20
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 61.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 78.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.39000
REMARK 3 B22 (A**2) : -0.39000
REMARK 3 B33 (A**2) : 0.58000
REMARK 3 B12 (A**2) : -0.19000
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): 0.724
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.321
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.234
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.666
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3766 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5103 ; 1.295 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 456 ; 4.140 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 159 ;26.967 ;22.327
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 609 ;13.946 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;15.115 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 558 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2837 ; 0.005 ; 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): 2274 ; 1.573 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3646 ; 2.416 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1492 ; 1.117 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1456 ; 1.621 ; 3.000
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 : 18
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 5 A 17
REMARK 3 ORIGIN FOR THE GROUP (A): 22.3501 4.2213 -9.0622
REMARK 3 T TENSOR
REMARK 3 T11: 1.2663 T22: 1.4013
REMARK 3 T33: 1.3971 T12: -0.3234
REMARK 3 T13: 0.0213 T23: 0.1255
REMARK 3 L TENSOR
REMARK 3 L11: 10.8037 L22: 2.9044
REMARK 3 L33: 5.5888 L12: 5.5823
REMARK 3 L13: 7.7676 L23: 4.0182
REMARK 3 S TENSOR
REMARK 3 S11: -1.3510 S12: 0.6492 S13: 1.0815
REMARK 3 S21: -0.6991 S22: 0.4589 S23: 0.7099
REMARK 3 S31: -0.9758 S32: 0.4252 S33: 0.8922
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 : A 18 A 32
REMARK 3 ORIGIN FOR THE GROUP (A): 27.9533 13.2969 -9.9764
REMARK 3 T TENSOR
REMARK 3 T11: 0.5447 T22: 0.4892
REMARK 3 T33: 0.4562 T12: -0.0019
REMARK 3 T13: -0.4015 T23: -0.1138
REMARK 3 L TENSOR
REMARK 3 L11: 3.9408 L22: 14.8471
REMARK 3 L33: 6.5273 L12: 3.3252
REMARK 3 L13: -3.4313 L23: 3.4367
REMARK 3 S TENSOR
REMARK 3 S11: -0.4535 S12: 0.1776 S13: -0.0465
REMARK 3 S21: -1.0791 S22: 0.1684 S23: 0.9393
REMARK 3 S31: 0.2567 S32: 0.0446 S33: 0.2851
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 33 A 64
REMARK 3 ORIGIN FOR THE GROUP (A): 41.4589 14.1037 -4.3289
REMARK 3 T TENSOR
REMARK 3 T11: 0.3170 T22: 0.1559
REMARK 3 T33: 0.0907 T12: 0.0187
REMARK 3 T13: -0.0102 T23: -0.0361
REMARK 3 L TENSOR
REMARK 3 L11: 3.3935 L22: 5.3975
REMARK 3 L33: 2.9191 L12: -0.3598
REMARK 3 L13: -0.3963 L23: -1.4171
REMARK 3 S TENSOR
REMARK 3 S11: 0.1984 S12: 0.3859 S13: -0.4632
REMARK 3 S21: -0.8881 S22: -0.2131 S23: -0.2660
REMARK 3 S31: 0.6476 S32: 0.1780 S33: 0.0147
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 65 A 134
REMARK 3 ORIGIN FOR THE GROUP (A): 39.4259 20.0958 2.8287
REMARK 3 T TENSOR
REMARK 3 T11: 0.0876 T22: 0.0521
REMARK 3 T33: 0.0266 T12: 0.0211
REMARK 3 T13: -0.0258 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 3.6826 L22: 7.0963
REMARK 3 L33: 3.4384 L12: 0.5334
REMARK 3 L13: 0.4510 L23: -0.8127
REMARK 3 S TENSOR
REMARK 3 S11: 0.0230 S12: -0.0129 S13: -0.2447
REMARK 3 S21: 0.1042 S22: 0.0486 S23: -0.0936
REMARK 3 S31: 0.3299 S32: 0.1047 S33: -0.0716
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 135 A 160
REMARK 3 ORIGIN FOR THE GROUP (A): 24.8157 14.2452 2.0585
REMARK 3 T TENSOR
REMARK 3 T11: 0.3904 T22: 0.3629
REMARK 3 T33: 0.4477 T12: -0.0993
REMARK 3 T13: -0.0863 T23: 0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 5.2536 L22: 13.4410
REMARK 3 L33: 4.9903 L12: -4.2270
REMARK 3 L13: -1.1510 L23: 3.6463
REMARK 3 S TENSOR
REMARK 3 S11: -0.0469 S12: 0.1681 S13: -0.6015
REMARK 3 S21: 0.5559 S22: -0.2365 S23: 1.5635
REMARK 3 S31: 0.6982 S32: -0.9837 S33: 0.2835
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 161 A 176
REMARK 3 ORIGIN FOR THE GROUP (A): 41.9472 -5.1725 -4.3460
REMARK 3 T TENSOR
REMARK 3 T11: 0.9862 T22: 0.6804
REMARK 3 T33: 0.9573 T12: 0.0783
REMARK 3 T13: -0.0723 T23: -0.0735
REMARK 3 L TENSOR
REMARK 3 L11: 0.6241 L22: 3.7522
REMARK 3 L33: 0.1224 L12: -1.4286
REMARK 3 L13: 0.1975 L23: -0.2939
REMARK 3 S TENSOR
REMARK 3 S11: 0.4206 S12: 0.1942 S13: -0.2386
REMARK 3 S21: -1.3217 S22: -0.1167 S23: 0.1216
REMARK 3 S31: 0.0576 S32: 0.1338 S33: -0.3039
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 177 A 203
REMARK 3 ORIGIN FOR THE GROUP (A): 52.0379 -17.7517 15.8200
REMARK 3 T TENSOR
REMARK 3 T11: 0.1716 T22: 0.0742
REMARK 3 T33: 0.0848 T12: -0.0092
REMARK 3 T13: -0.0466 T23: 0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 1.1079 L22: 3.8130
REMARK 3 L33: 4.7295 L12: -2.0037
REMARK 3 L13: 1.5836 L23: -2.7589
REMARK 3 S TENSOR
REMARK 3 S11: 0.0189 S12: 0.0094 S13: -0.0755
REMARK 3 S21: -0.1654 S22: 0.0364 S23: 0.2386
REMARK 3 S31: -0.0753 S32: 0.2118 S33: -0.0553
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 204 A 237
REMARK 3 ORIGIN FOR THE GROUP (A): 52.2942 -13.0084 6.6793
REMARK 3 T TENSOR
REMARK 3 T11: 0.2766 T22: 0.0982
REMARK 3 T33: 0.1022 T12: -0.0369
REMARK 3 T13: -0.0030 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 2.4551 L22: 12.2415
REMARK 3 L33: 2.8207 L12: -2.5841
REMARK 3 L13: 1.8327 L23: 0.5622
REMARK 3 S TENSOR
REMARK 3 S11: -0.1669 S12: 0.0803 S13: 0.2606
REMARK 3 S21: -0.6042 S22: 0.0652 S23: 0.1221
REMARK 3 S31: -0.6370 S32: 0.1232 S33: 0.1016
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 6 B 36
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8814 8.9326 23.9932
REMARK 3 T TENSOR
REMARK 3 T11: 1.1157 T22: 1.5012
REMARK 3 T33: 1.5364 T12: 0.3525
REMARK 3 T13: 0.2827 T23: 0.1644
REMARK 3 L TENSOR
REMARK 3 L11: 4.4485 L22: 0.9060
REMARK 3 L33: 6.0395 L12: 1.5479
REMARK 3 L13: -1.3090 L23: -1.3244
REMARK 3 S TENSOR
REMARK 3 S11: -0.2677 S12: -0.2943 S13: 0.2560
REMARK 3 S21: 0.3677 S22: 0.3973 S23: 0.5634
REMARK 3 S31: -1.2030 S32: -1.1199 S33: -0.1296
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 37 B 48
REMARK 3 ORIGIN FOR THE GROUP (A): 35.7332 -3.4469 20.8441
REMARK 3 T TENSOR
REMARK 3 T11: 0.4666 T22: 0.3313
REMARK 3 T33: 0.6467 T12: -0.0998
REMARK 3 T13: 0.0559 T23: 0.0580
REMARK 3 L TENSOR
REMARK 3 L11: 30.1764 L22: 3.8608
REMARK 3 L33: 11.6947 L12: -10.0902
REMARK 3 L13: -2.2322 L23: -1.3862
REMARK 3 S TENSOR
REMARK 3 S11: -0.4372 S12: -0.1652 S13: 0.3287
REMARK 3 S21: 0.1354 S22: 0.0491 S23: -0.0341
REMARK 3 S31: 0.9280 S32: 0.0169 S33: 0.3881
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 49 B 69
REMARK 3 ORIGIN FOR THE GROUP (A): 27.1741 -9.5924 27.5942
REMARK 3 T TENSOR
REMARK 3 T11: 0.9393 T22: 1.0566
REMARK 3 T33: 1.2430 T12: -0.1364
REMARK 3 T13: 0.3079 T23: 0.2065
REMARK 3 L TENSOR
REMARK 3 L11: 0.4604 L22: 1.3909
REMARK 3 L33: 8.4485 L12: -0.6639
REMARK 3 L13: 1.8243 L23: -1.9175
REMARK 3 S TENSOR
REMARK 3 S11: -0.0341 S12: -0.2714 S13: -0.2865
REMARK 3 S21: 0.4340 S22: 0.2498 S23: 1.0311
REMARK 3 S31: 0.7105 S32: -1.3545 S33: -0.2157
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 70 B 90
REMARK 3 ORIGIN FOR THE GROUP (A): 27.8503 -9.2535 13.7605
REMARK 3 T TENSOR
REMARK 3 T11: 0.8034 T22: 0.4316
REMARK 3 T33: 0.9184 T12: -0.2622
REMARK 3 T13: -0.0824 T23: 0.0620
REMARK 3 L TENSOR
REMARK 3 L11: 5.9508 L22: 2.2938
REMARK 3 L33: 12.6326 L12: 0.7016
REMARK 3 L13: -4.8529 L23: -2.8998
REMARK 3 S TENSOR
REMARK 3 S11: 0.0721 S12: -0.2332 S13: -0.4505
REMARK 3 S21: -0.1238 S22: 0.2119 S23: 0.3844
REMARK 3 S31: 1.2560 S32: -0.1646 S33: -0.2840
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 99 B 112
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6194 -16.5938 21.1393
REMARK 3 T TENSOR
REMARK 3 T11: 1.1623 T22: 1.2136
REMARK 3 T33: 1.6551 T12: -0.7779
REMARK 3 T13: 0.1741 T23: 0.1257
REMARK 3 L TENSOR
REMARK 3 L11: 0.6060 L22: 3.1921
REMARK 3 L33: 13.9698 L12: -1.3771
REMARK 3 L13: 2.8937 L23: -6.6062
REMARK 3 S TENSOR
REMARK 3 S11: 0.2060 S12: -0.2938 S13: -0.1940
REMARK 3 S21: -0.2991 S22: 0.4141 S23: 0.5306
REMARK 3 S31: 1.0873 S32: -1.1699 S33: -0.6201
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 113 B 130
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9487 0.9368 15.6708
REMARK 3 T TENSOR
REMARK 3 T11: 0.3715 T22: 0.4263
REMARK 3 T33: 0.3894 T12: -0.0769
REMARK 3 T13: 0.0003 T23: 0.0685
REMARK 3 L TENSOR
REMARK 3 L11: 1.1303 L22: 12.0538
REMARK 3 L33: 4.0941 L12: -0.3768
REMARK 3 L13: -0.9753 L23: -1.1308
REMARK 3 S TENSOR
REMARK 3 S11: 0.2193 S12: 0.0641 S13: -0.3138
REMARK 3 S21: 0.1050 S22: 0.0188 S23: 0.8294
REMARK 3 S31: 0.1022 S32: -0.7349 S33: -0.2381
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 131 B 152
REMARK 3 ORIGIN FOR THE GROUP (A): 14.9844 1.6557 11.1328
REMARK 3 T TENSOR
REMARK 3 T11: 0.8350 T22: 1.2691
REMARK 3 T33: 1.2562 T12: -0.0691
REMARK 3 T13: -0.1048 T23: 0.1344
REMARK 3 L TENSOR
REMARK 3 L11: 4.7568 L22: 3.4906
REMARK 3 L33: 3.4949 L12: -1.8224
REMARK 3 L13: 2.6588 L23: 1.3446
REMARK 3 S TENSOR
REMARK 3 S11: -0.2457 S12: -0.6897 S13: -0.2657
REMARK 3 S21: -0.2988 S22: -0.4180 S23: 1.1010
REMARK 3 S31: -0.3796 S32: -0.9947 S33: 0.6637
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 153 B 176
REMARK 3 ORIGIN FOR THE GROUP (A): 38.1116 7.3548 23.0504
REMARK 3 T TENSOR
REMARK 3 T11: 0.7375 T22: 0.9524
REMARK 3 T33: 0.6990 T12: 0.0964
REMARK 3 T13: 0.0643 T23: 0.0782
REMARK 3 L TENSOR
REMARK 3 L11: 8.6201 L22: 1.1692
REMARK 3 L33: 0.4490 L12: 1.9589
REMARK 3 L13: 0.5752 L23: 0.6671
REMARK 3 S TENSOR
REMARK 3 S11: -0.1117 S12: -1.2550 S13: 0.0834
REMARK 3 S21: 0.1322 S22: 0.0757 S23: 0.1418
REMARK 3 S31: 0.0758 S32: 0.1191 S33: 0.0359
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 177 B 203
REMARK 3 ORIGIN FOR THE GROUP (A): 63.3340 4.9499 10.3362
REMARK 3 T TENSOR
REMARK 3 T11: 0.5143 T22: 0.3810
REMARK 3 T33: 0.4756 T12: -0.1480
REMARK 3 T13: 0.0266 T23: -0.1116
REMARK 3 L TENSOR
REMARK 3 L11: 8.3947 L22: 4.5683
REMARK 3 L33: 6.4566 L12: -2.3132
REMARK 3 L13: -0.9095 L23: -0.3999
REMARK 3 S TENSOR
REMARK 3 S11: -0.4034 S12: 0.0181 S13: 0.4926
REMARK 3 S21: -0.4909 S22: 0.3258 S23: -1.1506
REMARK 3 S31: -0.9762 S32: 1.1938 S33: 0.0777
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 204 B 237
REMARK 3 ORIGIN FOR THE GROUP (A): 57.2659 3.1247 18.8925
REMARK 3 T TENSOR
REMARK 3 T11: 0.3309 T22: 0.2462
REMARK 3 T33: 0.2606 T12: 0.0362
REMARK 3 T13: -0.0300 T23: -0.1332
REMARK 3 L TENSOR
REMARK 3 L11: 8.7524 L22: 6.9651
REMARK 3 L33: 7.0614 L12: 0.2645
REMARK 3 L13: 3.6486 L23: -0.0293
REMARK 3 S TENSOR
REMARK 3 S11: 0.0135 S12: -0.5962 S13: 0.0900
REMARK 3 S21: 0.1713 S22: 0.1259 S23: -0.5955
REMARK 3 S31: -0.3481 S32: -0.0207 S33: -0.1394
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 3SZT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066857.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.83
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 4.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NOIR-1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19230
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.90
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : 0.05200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 40.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 12.20
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.800
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: SCRWL MODEL OF AHL AND DNA-BINDING DOMAINS OF TRAR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.168 M MAGNESIUM ACETATE, 21.8%
REMARK 280 PEG8000, 0.1 M TRIS, PH 7.83, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 34.98433
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 69.96867
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 69.96867
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 34.98433
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: 4890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 HIS A 2
REMARK 465 ASP A 3
REMARK 465 GLU A 4
REMARK 465 MET B 1
REMARK 465 HIS B 2
REMARK 465 ASP B 3
REMARK 465 GLU B 4
REMARK 465 ARG B 5
REMARK 465 ASN B 91
REMARK 465 GLY B 92
REMARK 465 GLU B 93
REMARK 465 ASP B 94
REMARK 465 PHE B 95
REMARK 465 GLN B 96
REMARK 465 GLU B 97
REMARK 465 ASN B 98
REMARK 465 GLU B 135
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 GLU A 10 CG CD OE1 OE2
REMARK 470 THR A 16 OG1 CG2
REMARK 470 GLU A 19 CG CD OE1 OE2
REMARK 470 GLU A 20 CG CD OE1 OE2
REMARK 470 LEU A 24 CG CD1 CD2
REMARK 470 GLU A 171 CG CD OE1 OE2
REMARK 470 GLU B 10 CG CD OE1 OE2
REMARK 470 LEU B 12 CG CD1 CD2
REMARK 470 GLU B 19 CG CD OE1 OE2
REMARK 470 GLU B 20 CG CD OE1 OE2
REMARK 470 LEU B 24 CG CD1 CD2
REMARK 470 ARG B 79 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 99 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 103 CG CD OE1 OE2
REMARK 470 GLU B 104 CG CD OE1 OE2
REMARK 470 ARG B 111 CG CD NE CZ NH1 NH2
REMARK 470 TRP B 114 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 114 CZ3 CH2
REMARK 470 THR B 140 OG1 CG2
REMARK 470 ILE B 142 CG1 CG2 CD1
REMARK 470 GLU B 144 CG CD OE1 OE2
REMARK 470 LYS B 145 CG CD CE NZ
REMARK 470 ILE B 152 CG1 CG2 CD1
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 PHE A 34 -169.67 -110.33
REMARK 500 GLU A 35 -39.24 -134.16
REMARK 500 ALA A 49 97.21 -161.61
REMARK 500 TYR A 85 19.14 -152.00
REMARK 500 GLU A 135 100.79 68.29
REMARK 500 PRO A 166 -77.55 -31.84
REMARK 500 SER B 13 -7.69 -57.55
REMARK 500 ASN B 31 1.90 -59.98
REMARK 500 ALA B 49 73.54 -167.63
REMARK 500 SER B 56 -146.86 -157.70
REMARK 500 ASN B 57 14.88 -160.13
REMARK 500 ARG B 111 -18.31 -143.60
REMARK 500 SER B 133 68.37 -105.64
REMARK 500 LEU B 143 0.79 -57.90
REMARK 500 PRO B 166 -71.46 -43.31
REMARK 500 VAL B 169 75.90 -116.91
REMARK 500 THR B 177 155.23 -48.20
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 OHN A 238
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OHN B 239
DBREF 3SZT A 1 237 UNP Q9RMS5 Q9RMS5_PSEAE 1 237
DBREF 3SZT B 1 237 UNP Q9RMS5 Q9RMS5_PSEAE 1 237
SEQRES 1 A 237 MET HIS ASP GLU ARG GLU GLY TYR LEU GLU ILE LEU SER
SEQRES 2 A 237 ARG ILE THR THR GLU GLU GLU PHE PHE SER LEU VAL LEU
SEQRES 3 A 237 GLU ILE CYS GLY ASN TYR GLY PHE GLU PHE PHE SER PHE
SEQRES 4 A 237 GLY ALA ARG ALA PRO PHE PRO LEU THR ALA PRO LYS TYR
SEQRES 5 A 237 HIS PHE LEU SER ASN TYR PRO GLY GLU TRP LYS SER ARG
SEQRES 6 A 237 TYR ILE SER GLU ASP TYR THR SER ILE ASP PRO ILE VAL
SEQRES 7 A 237 ARG HIS GLY LEU LEU GLU TYR THR PRO LEU ILE TRP ASN
SEQRES 8 A 237 GLY GLU ASP PHE GLN GLU ASN ARG PHE PHE TRP GLU GLU
SEQRES 9 A 237 ALA LEU HIS HIS GLY ILE ARG HIS GLY TRP SER ILE PRO
SEQRES 10 A 237 VAL ARG GLY LYS TYR GLY LEU ILE SER MET LEU SER LEU
SEQRES 11 A 237 VAL ARG SER SER GLU SER ILE ALA ALA THR GLU ILE LEU
SEQRES 12 A 237 GLU LYS GLU SER PHE LEU LEU TRP ILE THR SER MET LEU
SEQRES 13 A 237 GLN ALA THR PHE GLY ASP LEU LEU ALA PRO ARG ILE VAL
SEQRES 14 A 237 PRO GLU SER ASN VAL ARG LEU THR ALA ARG GLU THR GLU
SEQRES 15 A 237 MET LEU LYS TRP THR ALA VAL GLY LYS THR TYR GLY GLU
SEQRES 16 A 237 ILE GLY LEU ILE LEU SER ILE ASP GLN ARG THR VAL LYS
SEQRES 17 A 237 PHE HIS ILE VAL ASN ALA MET ARG LYS LEU ASN SER SER
SEQRES 18 A 237 ASN LYS ALA GLU ALA THR MET LYS ALA TYR ALA ILE GLY
SEQRES 19 A 237 LEU LEU ASN
SEQRES 1 B 237 MET HIS ASP GLU ARG GLU GLY TYR LEU GLU ILE LEU SER
SEQRES 2 B 237 ARG ILE THR THR GLU GLU GLU PHE PHE SER LEU VAL LEU
SEQRES 3 B 237 GLU ILE CYS GLY ASN TYR GLY PHE GLU PHE PHE SER PHE
SEQRES 4 B 237 GLY ALA ARG ALA PRO PHE PRO LEU THR ALA PRO LYS TYR
SEQRES 5 B 237 HIS PHE LEU SER ASN TYR PRO GLY GLU TRP LYS SER ARG
SEQRES 6 B 237 TYR ILE SER GLU ASP TYR THR SER ILE ASP PRO ILE VAL
SEQRES 7 B 237 ARG HIS GLY LEU LEU GLU TYR THR PRO LEU ILE TRP ASN
SEQRES 8 B 237 GLY GLU ASP PHE GLN GLU ASN ARG PHE PHE TRP GLU GLU
SEQRES 9 B 237 ALA LEU HIS HIS GLY ILE ARG HIS GLY TRP SER ILE PRO
SEQRES 10 B 237 VAL ARG GLY LYS TYR GLY LEU ILE SER MET LEU SER LEU
SEQRES 11 B 237 VAL ARG SER SER GLU SER ILE ALA ALA THR GLU ILE LEU
SEQRES 12 B 237 GLU LYS GLU SER PHE LEU LEU TRP ILE THR SER MET LEU
SEQRES 13 B 237 GLN ALA THR PHE GLY ASP LEU LEU ALA PRO ARG ILE VAL
SEQRES 14 B 237 PRO GLU SER ASN VAL ARG LEU THR ALA ARG GLU THR GLU
SEQRES 15 B 237 MET LEU LYS TRP THR ALA VAL GLY LYS THR TYR GLY GLU
SEQRES 16 B 237 ILE GLY LEU ILE LEU SER ILE ASP GLN ARG THR VAL LYS
SEQRES 17 B 237 PHE HIS ILE VAL ASN ALA MET ARG LYS LEU ASN SER SER
SEQRES 18 B 237 ASN LYS ALA GLU ALA THR MET LYS ALA TYR ALA ILE GLY
SEQRES 19 B 237 LEU LEU ASN
HET OHN A 238 21
HET NA B 238 1
HET OHN B 239 21
HETNAM OHN N-3-OXO-DODECANOYL-L-HOMOSERINE LACTONE
HETNAM NA SODIUM ION
FORMUL 3 OHN 2(C16 H27 N O4)
FORMUL 4 NA NA 1+
FORMUL 6 HOH *20(H2 O)
HELIX 1 1 GLY A 7 ILE A 15 1 9
HELIX 2 2 THR A 17 TYR A 32 1 16
HELIX 3 3 PRO A 59 GLU A 69 1 11
HELIX 4 4 ASP A 70 ILE A 74 5 5
HELIX 5 5 ASP A 75 GLU A 84 1 10
HELIX 6 6 ASN A 98 HIS A 108 1 11
HELIX 7 7 LYS A 121 GLY A 123 5 3
HELIX 8 8 ALA A 138 VAL A 169 1 32
HELIX 9 9 PRO A 170 VAL A 174 5 5
HELIX 10 10 THR A 177 VAL A 189 1 13
HELIX 11 11 THR A 192 SER A 201 1 10
HELIX 12 12 ASP A 203 LEU A 218 1 16
HELIX 13 13 ASN A 222 ILE A 233 1 12
HELIX 14 14 TYR B 8 SER B 13 1 6
HELIX 15 15 THR B 17 ASN B 31 1 15
HELIX 16 16 PRO B 59 GLU B 69 1 11
HELIX 17 17 ASP B 70 ILE B 74 5 5
HELIX 18 18 ASP B 75 GLU B 84 1 10
HELIX 19 19 ARG B 99 HIS B 107 1 9
HELIX 20 20 LYS B 121 GLY B 123 5 3
HELIX 21 21 ALA B 138 VAL B 169 1 32
HELIX 22 22 PRO B 170 VAL B 174 5 5
HELIX 23 23 THR B 177 VAL B 189 1 13
HELIX 24 24 THR B 192 SER B 201 1 10
HELIX 25 25 ASP B 203 LEU B 218 1 16
HELIX 26 26 ASN B 222 GLY B 234 1 13
SHEET 1 A 5 TYR A 52 SER A 56 0
SHEET 2 A 5 PHE A 36 ARG A 42 -1 N PHE A 39 O LEU A 55
SHEET 3 A 5 ILE A 125 ARG A 132 -1 O VAL A 131 N PHE A 36
SHEET 4 A 5 HIS A 112 ARG A 119 -1 N VAL A 118 O SER A 126
SHEET 5 A 5 LEU A 88 ASN A 91 -1 N LEU A 88 O SER A 115
SHEET 1 B 5 TYR B 52 LEU B 55 0
SHEET 2 B 5 PHE B 39 ARG B 42 -1 N PHE B 39 O LEU B 55
SHEET 3 B 5 ILE B 125 ARG B 132 -1 O ILE B 125 N ARG B 42
SHEET 4 B 5 HIS B 112 ARG B 119 -1 N HIS B 112 O ARG B 132
SHEET 5 B 5 LEU B 88 TRP B 90 -1 N LEU B 88 O SER B 115
CISPEP 1 PHE A 45 PRO A 46 0 -4.24
CISPEP 2 PHE B 45 PRO B 46 0 -1.40
SITE 1 AC1 12 SER A 38 GLY A 40 TYR A 58 TRP A 62
SITE 2 AC1 12 TYR A 66 ASP A 75 LEU A 82 TRP A 90
SITE 3 AC1 12 TRP A 102 ALA A 105 ILE A 125 HOH A 246
SITE 1 AC2 19 SER B 38 GLY B 40 ALA B 41 TYR B 52
SITE 2 AC2 19 PHE B 54 TYR B 58 TRP B 62 TYR B 66
SITE 3 AC2 19 ASP B 75 ILE B 77 VAL B 78 GLY B 81
SITE 4 AC2 19 LEU B 82 TRP B 90 TRP B 102 ILE B 110
SITE 5 AC2 19 SER B 126 MET B 127 SER B 129
CRYST1 94.862 94.862 104.953 90.00 90.00 120.00 P 31 2 1 12
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 0.010542 0.006086 0.000000 0.00000
SCALE2 0.000000 0.012172 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009528 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
