HEADER TRANSFERASE 07-JUN-16 5L84
TITLE STRUCTURE OF THE H959F VARIANT OF THE PPSC DEHYDRATASE DOMAIN FROM
TITLE 2 MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHTHIOCEROL SYNTHESIS POLYKETIDE SYNTHASE TYPE I PPSC;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BETA-KETOACYL-ACYL-CARRIER-PROTEIN SYNTHASE I;
COMPND 5 EC: 2.3.1.41;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: ATCC 25618 / H37RV;
SOURCE 5 GENE: PPSC, RV2933;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS DEHYDRATASE, POLYKETIDE, COMPLEX, TUBERCULOSIS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.FAILLE,S.GAVALDA,L.MOUREY,J.D.PEDELACQ
REVDAT 3 10-JAN-24 5L84 1 REMARK
REVDAT 2 16-OCT-19 5L84 1 REMARK
REVDAT 1 30-AUG-17 5L84 0
JRNL AUTH A.FAILLE,S.GAVALDA,N.SLAMA,C.LHERBET,L.MAVEYRAUD,V.GUILLET,
JRNL AUTH 2 F.LAVAL,A.QUEMARD,L.MOUREY,J.D.PEDELACQ
JRNL TITL INSIGHTS INTO SUBSTRATE MODIFICATION BY DEHYDRATASES FROM
JRNL TITL 2 TYPE I POLYKETIDE SYNTHASES.
JRNL REF J. MOL. BIOL. V. 429 1554 2017
JRNL REFN ESSN 1089-8638
JRNL PMID 28377293
JRNL DOI 10.1016/J.JMB.2017.03.026
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 13625
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.390
REMARK 3 FREE R VALUE TEST SET COUNT : 1279
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 48.2040 - 6.0290 0.98 1471 153 0.1716 0.1929
REMARK 3 2 6.0290 - 4.7868 0.99 1403 146 0.1630 0.1684
REMARK 3 3 4.7868 - 4.1821 1.00 1377 143 0.1350 0.1776
REMARK 3 4 4.1821 - 3.7999 1.00 1363 141 0.1783 0.1997
REMARK 3 5 3.7999 - 3.5276 1.00 1355 142 0.2146 0.2435
REMARK 3 6 3.5276 - 3.3197 0.99 1346 138 0.2361 0.2791
REMARK 3 7 3.3197 - 3.1535 0.99 1357 139 0.2766 0.3281
REMARK 3 8 3.1535 - 3.0162 1.00 1331 138 0.3045 0.3639
REMARK 3 9 3.0162 - 2.9001 1.00 1343 139 0.3447 0.3405
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.010
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 95.27
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 : 0.004 2036
REMARK 3 ANGLE : 0.856 2785
REMARK 3 CHIRALITY : 0.032 341
REMARK 3 PLANARITY : 0.004 365
REMARK 3 DIHEDRAL : 16.049 720
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 926 THROUGH 981 )
REMARK 3 ORIGIN FOR THE GROUP (A): 92.6053 107.7675 9.5077
REMARK 3 T TENSOR
REMARK 3 T11: 0.4211 T22: 0.5578
REMARK 3 T33: 0.4905 T12: -0.0878
REMARK 3 T13: -0.0222 T23: 0.0445
REMARK 3 L TENSOR
REMARK 3 L11: 0.9416 L22: 0.4489
REMARK 3 L33: 0.6004 L12: 0.5076
REMARK 3 L13: -0.4488 L23: 0.1021
REMARK 3 S TENSOR
REMARK 3 S11: 0.1376 S12: 0.3849 S13: -0.0948
REMARK 3 S21: 0.1814 S22: -0.0674 S23: -0.0616
REMARK 3 S31: 0.2647 S32: -0.0166 S33: 0.0188
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 982 THROUGH 1008 )
REMARK 3 ORIGIN FOR THE GROUP (A): 98.4161 110.5753 15.5212
REMARK 3 T TENSOR
REMARK 3 T11: 0.6497 T22: 0.4784
REMARK 3 T33: 0.4983 T12: 0.0077
REMARK 3 T13: -0.0666 T23: 0.0640
REMARK 3 L TENSOR
REMARK 3 L11: 2.7544 L22: 0.6984
REMARK 3 L33: 2.3321 L12: -1.3607
REMARK 3 L13: -2.5722 L23: 1.2624
REMARK 3 S TENSOR
REMARK 3 S11: 0.2470 S12: -0.1739 S13: -0.0284
REMARK 3 S21: -0.1806 S22: -0.0129 S23: -0.0204
REMARK 3 S31: 0.2996 S32: 0.2823 S33: 0.0001
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1009 THROUGH 1029 )
REMARK 3 ORIGIN FOR THE GROUP (A): 102.8446 111.2135 9.2838
REMARK 3 T TENSOR
REMARK 3 T11: 0.4394 T22: 0.5874
REMARK 3 T33: 0.5181 T12: 0.0583
REMARK 3 T13: 0.0021 T23: -0.0223
REMARK 3 L TENSOR
REMARK 3 L11: 0.1574 L22: 0.8225
REMARK 3 L33: 0.1343 L12: 0.3715
REMARK 3 L13: 0.1578 L23: 0.3475
REMARK 3 S TENSOR
REMARK 3 S11: -0.0632 S12: 0.0884 S13: -0.7194
REMARK 3 S21: -0.2257 S22: 0.3941 S23: -0.2241
REMARK 3 S31: -0.1639 S32: -0.0646 S33: -0.0002
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1030 THROUGH 1045 )
REMARK 3 ORIGIN FOR THE GROUP (A): 99.9262 114.5057 6.8644
REMARK 3 T TENSOR
REMARK 3 T11: 0.6361 T22: 0.7113
REMARK 3 T33: 0.6432 T12: 0.0839
REMARK 3 T13: 0.0639 T23: -0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 0.9618 L22: 0.5001
REMARK 3 L33: 0.0826 L12: 0.1158
REMARK 3 L13: -0.2115 L23: 0.1171
REMARK 3 S TENSOR
REMARK 3 S11: 0.3858 S12: 0.5499 S13: 0.4499
REMARK 3 S21: 0.0066 S22: -0.1985 S23: 0.3034
REMARK 3 S31: 0.3835 S32: 1.1040 S33: -0.0024
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1046 THROUGH 1078 )
REMARK 3 ORIGIN FOR THE GROUP (A): 82.2907 119.5181 34.6151
REMARK 3 T TENSOR
REMARK 3 T11: 0.6792 T22: 0.8654
REMARK 3 T33: 0.4494 T12: 0.2128
REMARK 3 T13: 0.0446 T23: 0.1943
REMARK 3 L TENSOR
REMARK 3 L11: 0.0985 L22: 0.2641
REMARK 3 L33: 0.5044 L12: -0.2066
REMARK 3 L13: -0.2232 L23: 0.4774
REMARK 3 S TENSOR
REMARK 3 S11: 0.2480 S12: 0.0725 S13: 0.0173
REMARK 3 S21: 0.0206 S22: 0.0408 S23: 0.4034
REMARK 3 S31: -0.3140 S32: 0.0720 S33: 0.0018
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1079 THROUGH 1098 )
REMARK 3 ORIGIN FOR THE GROUP (A): 76.8141 116.7436 23.0164
REMARK 3 T TENSOR
REMARK 3 T11: 0.6958 T22: 0.8798
REMARK 3 T33: 0.6234 T12: 0.1444
REMARK 3 T13: 0.2427 T23: 0.1906
REMARK 3 L TENSOR
REMARK 3 L11: 0.2742 L22: 0.7884
REMARK 3 L33: 0.4330 L12: 0.1256
REMARK 3 L13: 0.3262 L23: 0.2846
REMARK 3 S TENSOR
REMARK 3 S11: 0.0615 S12: 0.0176 S13: 0.3336
REMARK 3 S21: 0.1127 S22: 0.2259 S23: -0.1134
REMARK 3 S31: 0.2466 S32: -1.2438 S33: 0.1133
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1099 THROUGH 1124 )
REMARK 3 ORIGIN FOR THE GROUP (A): 84.6539 108.8004 26.9844
REMARK 3 T TENSOR
REMARK 3 T11: 0.7823 T22: 0.4690
REMARK 3 T33: 0.5419 T12: -0.0174
REMARK 3 T13: 0.1841 T23: 0.0399
REMARK 3 L TENSOR
REMARK 3 L11: 0.7379 L22: 0.7979
REMARK 3 L33: 0.5896 L12: 0.5727
REMARK 3 L13: -0.6338 L23: -0.6568
REMARK 3 S TENSOR
REMARK 3 S11: -0.4488 S12: -0.4444 S13: -0.2322
REMARK 3 S21: -0.0818 S22: -0.0237 S23: 0.4939
REMARK 3 S31: 0.2938 S32: 0.3711 S33: -0.0080
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1125 THROUGH 1160 )
REMARK 3 ORIGIN FOR THE GROUP (A): 83.9425 121.9305 25.9345
REMARK 3 T TENSOR
REMARK 3 T11: 0.4393 T22: 0.2977
REMARK 3 T33: 0.7046 T12: 0.0328
REMARK 3 T13: 0.1572 T23: 0.0332
REMARK 3 L TENSOR
REMARK 3 L11: 0.5544 L22: 3.1915
REMARK 3 L33: 1.5301 L12: -1.3427
REMARK 3 L13: -0.6614 L23: 1.4620
REMARK 3 S TENSOR
REMARK 3 S11: -0.3790 S12: -0.2702 S13: 0.4057
REMARK 3 S21: 0.6298 S22: 0.9572 S23: 0.7510
REMARK 3 S31: 0.4540 S32: -0.0039 S33: 0.4896
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1161 THROUGH 1185 )
REMARK 3 ORIGIN FOR THE GROUP (A): 92.0997 114.5132 27.5717
REMARK 3 T TENSOR
REMARK 3 T11: 0.7259 T22: 0.5620
REMARK 3 T33: 0.6085 T12: 0.0014
REMARK 3 T13: 0.0421 T23: 0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 1.7134 L22: 0.1945
REMARK 3 L33: 0.3571 L12: -0.5117
REMARK 3 L13: -0.0640 L23: -0.1436
REMARK 3 S TENSOR
REMARK 3 S11: 0.2827 S12: -0.4023 S13: 0.1432
REMARK 3 S21: 0.3865 S22: 0.0027 S23: 0.2720
REMARK 3 S31: 0.1467 S32: 0.3532 S33: 0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1186 THROUGH 1200 )
REMARK 3 ORIGIN FOR THE GROUP (A): 92.6291 123.8310 28.8464
REMARK 3 T TENSOR
REMARK 3 T11: 0.7618 T22: 0.6058
REMARK 3 T33: 0.7819 T12: -0.0430
REMARK 3 T13: 0.0571 T23: -0.0545
REMARK 3 L TENSOR
REMARK 3 L11: 0.4143 L22: -0.0019
REMARK 3 L33: 0.0917 L12: -0.0024
REMARK 3 L13: 0.2066 L23: -0.0098
REMARK 3 S TENSOR
REMARK 3 S11: 0.3096 S12: -1.0841 S13: 0.2995
REMARK 3 S21: 0.5718 S22: -0.5564 S23: -0.1410
REMARK 3 S31: 0.1991 S32: 0.8245 S33: -0.0225
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1201 THROUGH 1218 )
REMARK 3 ORIGIN FOR THE GROUP (A): 92.2809 117.7249 27.7532
REMARK 3 T TENSOR
REMARK 3 T11: 0.8888 T22: 0.6571
REMARK 3 T33: 0.7799 T12: 0.0585
REMARK 3 T13: 0.0645 T23: 0.0461
REMARK 3 L TENSOR
REMARK 3 L11: 1.1281 L22: 0.5558
REMARK 3 L33: 0.5300 L12: -0.7087
REMARK 3 L13: -0.4772 L23: 0.5089
REMARK 3 S TENSOR
REMARK 3 S11: 0.2718 S12: -0.6702 S13: 0.1948
REMARK 3 S21: 0.6656 S22: 0.4898 S23: 0.2712
REMARK 3 S31: -0.4495 S32: 0.0376 S33: 0.0719
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 5L84 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1200000296.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0723
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13660
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 46.125
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 10.47
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.7000
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4OOC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NA/K PO4 1.8 M PH 6.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.87700
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 41.89350
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.89350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 124.31550
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.89350
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.89350
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 41.43850
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.89350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.89350
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 124.31550
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.89350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.89350
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 41.43850
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 82.87700
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 1350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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 900
REMARK 465 GLY A 901
REMARK 465 SER A 902
REMARK 465 SER A 903
REMARK 465 HIS A 904
REMARK 465 HIS A 905
REMARK 465 HIS A 906
REMARK 465 HIS A 907
REMARK 465 HIS A 908
REMARK 465 HIS A 909
REMARK 465 SER A 910
REMARK 465 SER A 911
REMARK 465 GLY A 912
REMARK 465 LEU A 913
REMARK 465 VAL A 914
REMARK 465 PRO A 915
REMARK 465 ARG A 916
REMARK 465 GLY A 917
REMARK 465 SER A 918
REMARK 465 HIS A 919
REMARK 465 MET A 920
REMARK 465 ALA A 921
REMARK 465 TYR A 922
REMARK 465 HIS A 923
REMARK 465 ARG A 924
REMARK 465 PRO A 925
REMARK 465 PRO A 1051
REMARK 465 LEU A 1052
REMARK 465 ASP A 1053
REMARK 465 HIS A 1054
REMARK 465 GLU A 1055
REMARK 465 GLY A 1056
REMARK 465 GLN A 1057
REMARK 465 ARG A 1058
REMARK 465 ARG A 1059
REMARK 465 GLU A 1060
REMARK 465 VAL A 1061
REMARK 465 GLY A 1146
REMARK 465 GLY A 1147
REMARK 465 GLN A 1148
REMARK 465 ASP A 1149
REMARK 465 ALA A 1150
REMARK 465 ARG A 1151
REMARK 465 GLN A 1152
REMARK 465 GLY A 1153
REMARK 465 PRO A 1154
REMARK 465 SER A 1155
REMARK 465 SER A 1156
REMARK 465 ASN A 1157
REMARK 465 SER A 1158
REMARK 465 SER A 1219
REMARK 465 GLY A 1220
REMARK 465 SER A 1221
REMARK 465 GLY A 1222
REMARK 465 GLY A 1223
REMARK 465 SER A 1224
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 954 -113.03 60.96
REMARK 500 GLN A 988 -171.99 -175.15
REMARK 500 LEU A 997 112.92 -162.61
REMARK 500 SER A1033 25.36 -146.81
REMARK 500 ALA A1064 66.93 -69.70
REMARK 500 ASP A1065 50.68 -143.80
REMARK 500 GLN A1085 72.02 -101.70
REMARK 500 LEU A1144 -71.65 -91.74
REMARK 500 VAL A1164 -7.37 -140.32
REMARK 500 VAL A1179 -20.78 -141.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4OOC RELATED DB: PDB
REMARK 900 WILD-TYPE DH
REMARK 900 RELATED ID: 5I0K RELATED DB: PDB
REMARK 900 H959F VARIANT IN COMPLEX WITH C4:1-COA
REMARK 900 RELATED ID: 5NJI RELATED DB: PDB
REMARK 900 H959F VARIANT IN COMPLEX WITH C12:1-COA
DBREF 5L84 A 921 1222 UNP P96202 PPSC_MYCTU 921 1222
SEQADV 5L84 MET A 900 UNP P96202 INITIATING METHIONINE
SEQADV 5L84 GLY A 901 UNP P96202 EXPRESSION TAG
SEQADV 5L84 SER A 902 UNP P96202 EXPRESSION TAG
SEQADV 5L84 SER A 903 UNP P96202 EXPRESSION TAG
SEQADV 5L84 HIS A 904 UNP P96202 EXPRESSION TAG
SEQADV 5L84 HIS A 905 UNP P96202 EXPRESSION TAG
SEQADV 5L84 HIS A 906 UNP P96202 EXPRESSION TAG
SEQADV 5L84 HIS A 907 UNP P96202 EXPRESSION TAG
SEQADV 5L84 HIS A 908 UNP P96202 EXPRESSION TAG
SEQADV 5L84 HIS A 909 UNP P96202 EXPRESSION TAG
SEQADV 5L84 SER A 910 UNP P96202 EXPRESSION TAG
SEQADV 5L84 SER A 911 UNP P96202 EXPRESSION TAG
SEQADV 5L84 GLY A 912 UNP P96202 EXPRESSION TAG
SEQADV 5L84 LEU A 913 UNP P96202 EXPRESSION TAG
SEQADV 5L84 VAL A 914 UNP P96202 EXPRESSION TAG
SEQADV 5L84 PRO A 915 UNP P96202 EXPRESSION TAG
SEQADV 5L84 ARG A 916 UNP P96202 EXPRESSION TAG
SEQADV 5L84 GLY A 917 UNP P96202 EXPRESSION TAG
SEQADV 5L84 SER A 918 UNP P96202 EXPRESSION TAG
SEQADV 5L84 HIS A 919 UNP P96202 EXPRESSION TAG
SEQADV 5L84 MET A 920 UNP P96202 EXPRESSION TAG
SEQADV 5L84 PHE A 959 UNP P96202 HIS 959 ENGINEERED MUTATION
SEQADV 5L84 GLY A 1223 UNP P96202 EXPRESSION TAG
SEQADV 5L84 SER A 1224 UNP P96202 EXPRESSION TAG
SEQRES 1 A 325 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 325 LEU VAL PRO ARG GLY SER HIS MET ALA TYR HIS ARG PRO
SEQRES 3 A 325 ASP THR HIS PRO LEU LEU GLY VAL GLY VAL THR ASP PRO
SEQRES 4 A 325 THR ASN GLY THR ARG VAL TRP GLU SER GLU LEU ASP PRO
SEQRES 5 A 325 ASP LEU LEU TRP LEU ALA ASP PHE VAL ILE ASP ASP LEU
SEQRES 6 A 325 VAL VAL LEU PRO GLY ALA ALA TYR ALA GLU ILE ALA LEU
SEQRES 7 A 325 ALA ALA ALA THR ASP THR PHE ALA VAL GLU GLN ASP GLN
SEQRES 8 A 325 PRO TRP MET ILE SER GLU LEU ASP LEU ARG GLN MET LEU
SEQRES 9 A 325 HIS VAL THR PRO GLY THR VAL LEU VAL THR THR LEU THR
SEQRES 10 A 325 GLY ASP GLU GLN ARG CYS GLN VAL GLU ILE ARG THR ARG
SEQRES 11 A 325 SER GLY SER SER GLY TRP THR THR HIS ALA THR ALA THR
SEQRES 12 A 325 VAL ALA ARG ALA GLU PRO LEU ALA PRO LEU ASP HIS GLU
SEQRES 13 A 325 GLY GLN ARG ARG GLU VAL THR THR ALA ASP LEU GLU ASP
SEQRES 14 A 325 GLN LEU ASP PRO ASP ASP LEU TYR GLN ARG LEU ARG GLY
SEQRES 15 A 325 ALA GLY GLN GLN HIS GLY PRO ALA PHE GLN GLY ILE VAL
SEQRES 16 A 325 GLY LEU ALA VAL THR GLN ALA GLY VAL ALA ARG ALA GLN
SEQRES 17 A 325 VAL ARG LEU PRO ALA SER ALA ARG THR GLY SER ARG GLU
SEQRES 18 A 325 PHE MET LEU HIS PRO VAL MET MET ASP ILE ALA LEU GLN
SEQRES 19 A 325 THR LEU GLY ALA THR ARG THR ALA THR ASP LEU ALA GLY
SEQRES 20 A 325 GLY GLN ASP ALA ARG GLN GLY PRO SER SER ASN SER ALA
SEQRES 21 A 325 LEU VAL VAL PRO VAL ARG PHE ALA GLY VAL HIS VAL TYR
SEQRES 22 A 325 GLY ASP ILE THR ARG GLY VAL ARG ALA VAL GLY SER LEU
SEQRES 23 A 325 ALA ALA ALA GLY ASP ARG LEU VAL GLY GLU VAL VAL LEU
SEQRES 24 A 325 THR ASP ALA ASN GLY GLN PRO LEU LEU VAL VAL ASP GLU
SEQRES 25 A 325 VAL GLU MET ALA VAL LEU GLY SER GLY SER GLY GLY SER
HELIX 1 AA1 TRP A 955 ASP A 958 5 4
HELIX 2 AA2 PRO A 968 PHE A 984 1 17
HELIX 3 AA3 ASP A 1071 LEU A 1079 1 9
HELIX 4 AA4 GLY A 1087 GLN A 1091 5 5
HELIX 5 AA5 PRO A 1111 ARG A 1115 5 5
HELIX 6 AA6 GLY A 1117 PHE A 1121 5 5
HELIX 7 AA7 HIS A 1124 THR A 1134 1 11
HELIX 8 AA8 LEU A 1135 ALA A 1137 5 3
HELIX 9 AA9 THR A 1138 ASP A 1143 1 6
HELIX 10 AB1 ASP A 1174 THR A 1176 5 3
SHEET 1 AA113 VAL A 933 THR A 936 0
SHEET 2 AA113 ARG A 943 LEU A 949 -1 O VAL A 944 N VAL A 935
SHEET 3 AA113 THR A1009 GLY A1017 -1 O LEU A1011 N SER A 947
SHEET 4 AA113 ARG A1021 ARG A1029 -1 O ARG A1027 N VAL A1012
SHEET 5 AA113 TRP A1035 ARG A1045 -1 O ALA A1041 N VAL A1024
SHEET 6 AA113 TRP A 992 LEU A 999 -1 N MET A 993 O ALA A1044
SHEET 7 AA113 VAL A1161 VAL A1171 -1 O VAL A1164 N LEU A 999
SHEET 8 AA113 PRO A1205 VAL A1216 -1 O VAL A1208 N HIS A1170
SHEET 9 AA113 LEU A1192 ASP A1200 -1 N LEU A1198 O LEU A1206
SHEET 10 AA113 GLY A1178 LEU A1185 -1 N SER A1184 O GLU A1195
SHEET 11 AA113 ALA A1104 VAL A1108 -1 N ALA A1106 O ALA A1181
SHEET 12 AA113 ILE A1093 VAL A1098 -1 N GLY A1095 O GLN A1107
SHEET 13 AA113 ASP A1068 LEU A1070 -1 N LEU A1070 O LEU A1096
SHEET 1 AA2 2 VAL A 960 ILE A 961 0
SHEET 2 AA2 2 LEU A 964 VAL A 965 -1 O LEU A 964 N ILE A 961
CRYST1 83.787 83.787 165.754 90.00 90.00 90.00 P 43 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011935 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011935 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006033 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
