HEADER ANTIMICROBIAL PROTEIN 02-MAR-18 6CLU
TITLE STAPHYLOCOCCUS AUREUS DIHYDROPTEROATE SYNTHASE (SADHPS) F17L E208K
TITLE 2 DOUBLE MUTANT STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROPTEROATE SYNTHASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: DHPS,DIHYDROPTEROATE PYROPHOSPHORYLASE;
COMPND 5 EC: 2.5.1.15;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 GENE: FOLP, DPSA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ANTIBIOTIC RESISTANCE MUTATIONS, SULFONAMIDE RESISTANCE,
KEYWDS 2 ANTIMICROBIAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.GAJEWSKI,E.C.GRIFFITH,Y.WU,S.W.WHITE
REVDAT 4 13-MAR-24 6CLU 1 REMARK
REVDAT 3 18-DEC-19 6CLU 1 REMARK
REVDAT 2 20-FEB-19 6CLU 1 REMARK
REVDAT 1 22-AUG-18 6CLU 0
JRNL AUTH E.C.GRIFFITH,M.J.WALLACE,Y.WU,G.KUMAR,S.GAJEWSKI,P.JACKSON,
JRNL AUTH 2 G.A.PHELPS,Z.ZHENG,C.O.ROCK,R.E.LEE,S.W.WHITE
JRNL TITL THE STRUCTURAL AND FUNCTIONAL BASIS FOR RECURRING SULFA DRUG
JRNL TITL 2 RESISTANCE MUTATIONS INSTAPHYLOCOCCUS AUREUSDIHYDROPTEROATE
JRNL TITL 3 SYNTHASE.
JRNL REF FRONT MICROBIOL V. 9 1369 2018
JRNL REFN ESSN 1664-302X
JRNL PMID 30065703
JRNL DOI 10.3389/FMICB.2018.01369
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 48.420
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 73613
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.720
REMARK 3 FREE R VALUE TEST SET COUNT : 2005
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 20.4078 - 4.6834 0.97 5156 150 0.1643 0.1880
REMARK 3 2 4.6834 - 3.7248 0.97 5120 144 0.1408 0.1678
REMARK 3 3 3.7248 - 3.2561 0.97 5160 133 0.1566 0.1713
REMARK 3 4 3.2561 - 2.9594 0.97 5080 140 0.1642 0.1776
REMARK 3 5 2.9594 - 2.7478 0.97 5135 148 0.1812 0.2109
REMARK 3 6 2.7478 - 2.5861 0.97 5099 143 0.1959 0.2129
REMARK 3 7 2.5861 - 2.4568 0.97 5096 141 0.2077 0.2309
REMARK 3 8 2.4568 - 2.3500 0.97 5106 144 0.2162 0.2319
REMARK 3 9 2.3500 - 2.2597 0.97 5085 142 0.2224 0.2537
REMARK 3 10 2.2597 - 2.1818 0.97 5130 144 0.2406 0.2857
REMARK 3 11 2.1818 - 2.1137 0.97 5091 145 0.2689 0.2719
REMARK 3 12 2.1137 - 2.0533 0.97 5114 147 0.2904 0.3119
REMARK 3 13 2.0533 - 1.9993 0.97 5069 141 0.3257 0.3615
REMARK 3 14 1.9993 - 1.9505 0.96 5041 143 0.3928 0.4370
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.430
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.24
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: 0.3200
REMARK 3 OPERATOR: H,-K,-L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.001 7142
REMARK 3 ANGLE : 0.371 9690
REMARK 3 CHIRALITY : 0.040 1182
REMARK 3 PLANARITY : 0.003 1245
REMARK 3 DIHEDRAL : 13.883 4330
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 38
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 90.2239 119.4001 7.9285
REMARK 3 T TENSOR
REMARK 3 T11: 0.2632 T22: 0.3291
REMARK 3 T33: 0.3790 T12: 0.0530
REMARK 3 T13: 0.0122 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 1.7233 L22: 1.7630
REMARK 3 L33: 1.3190 L12: 0.8234
REMARK 3 L13: 0.2435 L23: 0.1231
REMARK 3 S TENSOR
REMARK 3 S11: 0.1634 S12: 0.3846 S13: 0.3066
REMARK 3 S21: 0.1077 S22: -0.1396 S23: -0.4359
REMARK 3 S31: 0.3176 S32: 0.4127 S33: -0.0885
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 26 THROUGH 59 )
REMARK 3 ORIGIN FOR THE GROUP (A): 90.2005 123.4208 3.9821
REMARK 3 T TENSOR
REMARK 3 T11: 0.2296 T22: 0.3064
REMARK 3 T33: 0.3705 T12: 0.0338
REMARK 3 T13: 0.0484 T23: 0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 1.1751 L22: 0.0714
REMARK 3 L33: 1.6611 L12: 0.2776
REMARK 3 L13: 0.0870 L23: -0.1086
REMARK 3 S TENSOR
REMARK 3 S11: -0.0608 S12: 0.0769 S13: 0.2779
REMARK 3 S21: -0.0605 S22: 0.0625 S23: -0.1626
REMARK 3 S31: 0.0799 S32: 0.0925 S33: 0.0650
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 60 THROUGH 74 )
REMARK 3 ORIGIN FOR THE GROUP (A): 92.2094 134.4413 9.3960
REMARK 3 T TENSOR
REMARK 3 T11: 0.2630 T22: 0.3824
REMARK 3 T33: 0.6185 T12: 0.0354
REMARK 3 T13: 0.0229 T23: 0.0344
REMARK 3 L TENSOR
REMARK 3 L11: 0.2952 L22: 1.0846
REMARK 3 L33: 4.3997 L12: 0.2626
REMARK 3 L13: -0.2652 L23: 1.3502
REMARK 3 S TENSOR
REMARK 3 S11: -0.4454 S12: -0.0863 S13: 0.1356
REMARK 3 S21: -0.0500 S22: -0.0557 S23: -0.4769
REMARK 3 S31: -0.1958 S32: 0.2932 S33: 0.0542
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 75 THROUGH 121 )
REMARK 3 ORIGIN FOR THE GROUP (A): 80.2767 133.6721 10.4480
REMARK 3 T TENSOR
REMARK 3 T11: 0.2001 T22: 0.2486
REMARK 3 T33: 0.3561 T12: 0.0470
REMARK 3 T13: 0.0319 T23: 0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 1.1863 L22: 1.1557
REMARK 3 L33: 1.3369 L12: -0.1484
REMARK 3 L13: -0.5746 L23: -0.2115
REMARK 3 S TENSOR
REMARK 3 S11: 0.0671 S12: 0.0443 S13: 0.3566
REMARK 3 S21: -0.0462 S22: -0.0599 S23: -0.2095
REMARK 3 S31: -0.0680 S32: -0.0711 S33: -0.0174
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 122 THROUGH 138 )
REMARK 3 ORIGIN FOR THE GROUP (A): 73.2735 123.2826 20.6815
REMARK 3 T TENSOR
REMARK 3 T11: 0.2328 T22: 0.2196
REMARK 3 T33: 0.2944 T12: 0.0288
REMARK 3 T13: 0.0131 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 1.3745 L22: 1.6274
REMARK 3 L33: 1.5404 L12: 0.1110
REMARK 3 L13: -0.3374 L23: -0.3796
REMARK 3 S TENSOR
REMARK 3 S11: 0.0994 S12: 0.0829 S13: -0.0860
REMARK 3 S21: 0.0756 S22: -0.0282 S23: -0.0476
REMARK 3 S31: 0.1235 S32: -0.0139 S33: -0.0662
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 139 THROUGH 157 )
REMARK 3 ORIGIN FOR THE GROUP (A): 66.2669 125.4631 18.5231
REMARK 3 T TENSOR
REMARK 3 T11: 0.1691 T22: 0.3179
REMARK 3 T33: 0.2547 T12: 0.0406
REMARK 3 T13: 0.0113 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 1.0088 L22: 4.3755
REMARK 3 L33: 1.1257 L12: -0.6767
REMARK 3 L13: -0.1662 L23: -1.5443
REMARK 3 S TENSOR
REMARK 3 S11: -0.0980 S12: -0.0126 S13: 0.1287
REMARK 3 S21: 0.0302 S22: 0.2239 S23: -0.0509
REMARK 3 S31: -0.1395 S32: -0.2731 S33: -0.0382
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 158 THROUGH 216 )
REMARK 3 ORIGIN FOR THE GROUP (A): 75.4965 113.8669 15.3862
REMARK 3 T TENSOR
REMARK 3 T11: 0.1790 T22: 0.2068
REMARK 3 T33: 0.2702 T12: 0.0156
REMARK 3 T13: 0.0107 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 1.2551 L22: 1.2559
REMARK 3 L33: 1.0686 L12: 0.3106
REMARK 3 L13: -0.9636 L23: 0.3623
REMARK 3 S TENSOR
REMARK 3 S11: -0.0870 S12: -0.0006 S13: -0.1634
REMARK 3 S21: 0.0659 S22: 0.0706 S23: -0.0156
REMARK 3 S31: 0.0852 S32: -0.0016 S33: 0.0013
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 217 THROUGH 242 )
REMARK 3 ORIGIN FOR THE GROUP (A): 79.7892 109.3720 8.0123
REMARK 3 T TENSOR
REMARK 3 T11: 0.1984 T22: 0.2547
REMARK 3 T33: 0.2916 T12: 0.0365
REMARK 3 T13: 0.0228 T23: -0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 1.6809 L22: 1.5100
REMARK 3 L33: 0.8958 L12: 0.0071
REMARK 3 L13: 0.0898 L23: 0.0286
REMARK 3 S TENSOR
REMARK 3 S11: 0.0354 S12: -0.0497 S13: -0.1325
REMARK 3 S21: -0.1387 S22: -0.0065 S23: -0.1406
REMARK 3 S31: 0.0702 S32: -0.0825 S33: -0.0228
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 243 THROUGH 260 )
REMARK 3 ORIGIN FOR THE GROUP (A): 75.6388 107.8843 -2.3288
REMARK 3 T TENSOR
REMARK 3 T11: 0.3023 T22: 0.2575
REMARK 3 T33: 0.3045 T12: 0.0290
REMARK 3 T13: -0.0109 T23: 0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 3.9926 L22: 1.8314
REMARK 3 L33: 1.6108 L12: 0.9064
REMARK 3 L13: 1.5022 L23: 0.3235
REMARK 3 S TENSOR
REMARK 3 S11: 0.1278 S12: 0.0684 S13: -0.0722
REMARK 3 S21: -0.2632 S22: -0.0158 S23: 0.1822
REMARK 3 S31: 0.0792 S32: -0.0709 S33: -0.0317
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 59 )
REMARK 3 ORIGIN FOR THE GROUP (A): 86.1601 83.5375 -0.5719
REMARK 3 T TENSOR
REMARK 3 T11: 0.2011 T22: 0.2841
REMARK 3 T33: 0.3602 T12: 0.0258
REMARK 3 T13: -0.0002 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 1.1073 L22: 0.4164
REMARK 3 L33: 0.1805 L12: 0.5001
REMARK 3 L13: -0.2165 L23: 0.0781
REMARK 3 S TENSOR
REMARK 3 S11: -0.1351 S12: -0.0139 S13: -0.1229
REMARK 3 S21: -0.0555 S22: 0.0919 S23: -0.0201
REMARK 3 S31: 0.1406 S32: 0.1723 S33: 0.0550
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 60 THROUGH 87 )
REMARK 3 ORIGIN FOR THE GROUP (A): 83.1882 73.8502 -4.8940
REMARK 3 T TENSOR
REMARK 3 T11: 0.2969 T22: 0.2917
REMARK 3 T33: 0.4231 T12: 0.0510
REMARK 3 T13: 0.0629 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 1.4640 L22: 0.9842
REMARK 3 L33: 1.1127 L12: 0.2997
REMARK 3 L13: 0.3576 L23: -0.1608
REMARK 3 S TENSOR
REMARK 3 S11: 0.0629 S12: 0.1298 S13: -0.0442
REMARK 3 S21: -0.2285 S22: -0.0705 S23: -0.3778
REMARK 3 S31: 0.2212 S32: 0.0868 S33: 0.0719
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 88 THROUGH 111 )
REMARK 3 ORIGIN FOR THE GROUP (A): 73.6314 73.0380 -6.2938
REMARK 3 T TENSOR
REMARK 3 T11: 0.3105 T22: 0.2983
REMARK 3 T33: 0.3441 T12: -0.0009
REMARK 3 T13: 0.0331 T23: -0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 1.9124 L22: 1.6296
REMARK 3 L33: 1.1978 L12: -0.5808
REMARK 3 L13: -0.0812 L23: 0.0132
REMARK 3 S TENSOR
REMARK 3 S11: -0.0013 S12: 0.1562 S13: -0.1070
REMARK 3 S21: -0.3635 S22: -0.1037 S23: -0.0686
REMARK 3 S31: 0.0931 S32: -0.0343 S33: 0.0769
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 112 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): 64.4409 83.1234 -3.8602
REMARK 3 T TENSOR
REMARK 3 T11: 0.1641 T22: 0.2240
REMARK 3 T33: 0.2717 T12: 0.0129
REMARK 3 T13: -0.0108 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 1.7056 L22: 2.3814
REMARK 3 L33: 1.0649 L12: 0.5660
REMARK 3 L13: -0.3169 L23: -0.0043
REMARK 3 S TENSOR
REMARK 3 S11: -0.1590 S12: -0.1435 S13: 0.0319
REMARK 3 S21: -0.0785 S22: 0.1062 S23: -0.0474
REMARK 3 S31: 0.0729 S32: -0.0199 S33: 0.0819
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 191 THROUGH 242 )
REMARK 3 ORIGIN FOR THE GROUP (A): 72.8556 93.2488 0.9430
REMARK 3 T TENSOR
REMARK 3 T11: 0.1994 T22: 0.2477
REMARK 3 T33: 0.2689 T12: 0.0162
REMARK 3 T13: -0.0152 T23: -0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 1.4555 L22: 1.4791
REMARK 3 L33: 0.8034 L12: 0.7698
REMARK 3 L13: 0.8996 L23: 0.7909
REMARK 3 S TENSOR
REMARK 3 S11: 0.1760 S12: 0.1217 S13: 0.0196
REMARK 3 S21: -0.0610 S22: -0.1304 S23: 0.1407
REMARK 3 S31: -0.1485 S32: -0.1604 S33: -0.0212
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 243 THROUGH 264 )
REMARK 3 ORIGIN FOR THE GROUP (A): 76.1884 98.8334 11.8471
REMARK 3 T TENSOR
REMARK 3 T11: 0.2150 T22: 0.2491
REMARK 3 T33: 0.3122 T12: 0.0004
REMARK 3 T13: -0.0242 T23: 0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 1.4642 L22: 1.2842
REMARK 3 L33: 2.6576 L12: -1.2738
REMARK 3 L13: -1.7206 L23: 1.6727
REMARK 3 S TENSOR
REMARK 3 S11: 0.0054 S12: 0.0038 S13: -0.3977
REMARK 3 S21: 0.0850 S22: -0.1538 S23: 0.1444
REMARK 3 S31: -0.0600 S32: 0.0042 S33: 0.0788
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 2 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 99.0521 111.4116 -25.9188
REMARK 3 T TENSOR
REMARK 3 T11: 0.3201 T22: 0.1876
REMARK 3 T33: 0.3809 T12: -0.0622
REMARK 3 T13: 0.0193 T23: 0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 1.3329 L22: 2.2150
REMARK 3 L33: 1.3365 L12: -0.3828
REMARK 3 L13: 0.2396 L23: -0.9458
REMARK 3 S TENSOR
REMARK 3 S11: 0.0766 S12: -0.1135 S13: -0.2026
REMARK 3 S21: 0.3635 S22: 0.0016 S23: 0.1223
REMARK 3 S31: -0.0074 S32: 0.0363 S33: 0.0172
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 26 THROUGH 59 )
REMARK 3 ORIGIN FOR THE GROUP (A): 101.8841 105.1905 -24.4436
REMARK 3 T TENSOR
REMARK 3 T11: 0.3524 T22: 0.2124
REMARK 3 T33: 0.4956 T12: -0.0104
REMARK 3 T13: 0.0233 T23: 0.0592
REMARK 3 L TENSOR
REMARK 3 L11: 0.6436 L22: 1.2512
REMARK 3 L33: 0.9718 L12: 0.1193
REMARK 3 L13: 0.2263 L23: 0.0869
REMARK 3 S TENSOR
REMARK 3 S11: -0.0888 S12: -0.1269 S13: -0.4095
REMARK 3 S21: -0.0652 S22: -0.1498 S23: -0.0511
REMARK 3 S31: 0.0102 S32: 0.0426 S33: 0.0494
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 60 THROUGH 74 )
REMARK 3 ORIGIN FOR THE GROUP (A): 113.6606 107.3938 -16.8527
REMARK 3 T TENSOR
REMARK 3 T11: 0.4154 T22: 0.2756
REMARK 3 T33: 0.5142 T12: 0.0354
REMARK 3 T13: -0.0188 T23: 0.0853
REMARK 3 L TENSOR
REMARK 3 L11: 1.3540 L22: 1.3943
REMARK 3 L33: 2.8722 L12: 0.9404
REMARK 3 L13: 1.3700 L23: 1.5323
REMARK 3 S TENSOR
REMARK 3 S11: 0.1621 S12: -0.2833 S13: -0.2112
REMARK 3 S21: 0.3604 S22: -0.1436 S23: -0.0197
REMARK 3 S31: 0.3010 S32: -0.0215 S33: -0.0058
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 75 THROUGH 97 )
REMARK 3 ORIGIN FOR THE GROUP (A): 112.2672 113.1693 -23.0211
REMARK 3 T TENSOR
REMARK 3 T11: 0.2911 T22: 0.2065
REMARK 3 T33: 0.3540 T12: -0.0119
REMARK 3 T13: 0.0091 T23: 0.0817
REMARK 3 L TENSOR
REMARK 3 L11: 1.8681 L22: 2.4970
REMARK 3 L33: 1.5521 L12: 0.1067
REMARK 3 L13: -0.0226 L23: 0.7343
REMARK 3 S TENSOR
REMARK 3 S11: -0.2429 S12: -0.0189 S13: -0.2440
REMARK 3 S21: 0.0926 S22: 0.1659 S23: 0.1427
REMARK 3 S31: -0.0236 S32: 0.3518 S33: 0.1324
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 98 THROUGH 121 )
REMARK 3 ORIGIN FOR THE GROUP (A): 112.8786 122.5908 -21.3512
REMARK 3 T TENSOR
REMARK 3 T11: 0.2949 T22: 0.1789
REMARK 3 T33: 0.3544 T12: -0.0443
REMARK 3 T13: -0.0183 T23: 0.0360
REMARK 3 L TENSOR
REMARK 3 L11: 0.6857 L22: 1.6734
REMARK 3 L33: 1.4438 L12: 0.0112
REMARK 3 L13: -0.4273 L23: 0.4231
REMARK 3 S TENSOR
REMARK 3 S11: -0.0213 S12: -0.0479 S13: -0.2556
REMARK 3 S21: 0.1049 S22: 0.0532 S23: -0.2871
REMARK 3 S31: 0.0511 S32: 0.0476 S33: -0.0194
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 122 THROUGH 138 )
REMARK 3 ORIGIN FOR THE GROUP (A): 104.2176 126.4927 -21.7599
REMARK 3 T TENSOR
REMARK 3 T11: 0.2644 T22: 0.1942
REMARK 3 T33: 0.2890 T12: -0.0440
REMARK 3 T13: -0.0601 T23: 0.0544
REMARK 3 L TENSOR
REMARK 3 L11: 1.4861 L22: 1.8771
REMARK 3 L33: 0.4970 L12: -0.6547
REMARK 3 L13: 0.1440 L23: 0.1629
REMARK 3 S TENSOR
REMARK 3 S11: 0.1655 S12: -0.0412 S13: 0.0312
REMARK 3 S21: -0.1273 S22: 0.0119 S23: 0.0373
REMARK 3 S31: -0.0423 S32: -0.0866 S33: -0.0639
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 139 THROUGH 157 )
REMARK 3 ORIGIN FOR THE GROUP (A): 104.7312 134.5206 -23.1009
REMARK 3 T TENSOR
REMARK 3 T11: 0.3311 T22: 0.1587
REMARK 3 T33: 0.2416 T12: -0.0539
REMARK 3 T13: -0.0386 T23: 0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 4.1534 L22: 1.2793
REMARK 3 L33: 0.7745 L12: -0.7035
REMARK 3 L13: -0.9626 L23: 0.0252
REMARK 3 S TENSOR
REMARK 3 S11: 0.0933 S12: -0.3290 S13: 0.0442
REMARK 3 S21: 0.1335 S22: -0.0417 S23: -0.1561
REMARK 3 S31: -0.1008 S32: 0.1996 S33: -0.0455
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 158 THROUGH 175 )
REMARK 3 ORIGIN FOR THE GROUP (A): 101.6050 125.9535 -23.9409
REMARK 3 T TENSOR
REMARK 3 T11: 0.3243 T22: 0.1877
REMARK 3 T33: 0.2646 T12: -0.0334
REMARK 3 T13: -0.0430 T23: 0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 1.3685 L22: 1.3988
REMARK 3 L33: 0.7986 L12: 0.0777
REMARK 3 L13: -0.1429 L23: 0.1071
REMARK 3 S TENSOR
REMARK 3 S11: -0.1777 S12: -0.2140 S13: -0.3892
REMARK 3 S21: -0.0010 S22: -0.1932 S23: -0.0409
REMARK 3 S31: -0.0501 S32: 0.1875 S33: 0.0654
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 176 THROUGH 192 )
REMARK 3 ORIGIN FOR THE GROUP (A): 90.4380 131.8482 -22.4960
REMARK 3 T TENSOR
REMARK 3 T11: 0.3014 T22: 0.2508
REMARK 3 T33: 0.3346 T12: -0.0585
REMARK 3 T13: 0.0114 T23: -0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 1.3424 L22: 1.1213
REMARK 3 L33: 2.1067 L12: 0.4492
REMARK 3 L13: -0.7386 L23: -0.0672
REMARK 3 S TENSOR
REMARK 3 S11: 0.1248 S12: 0.0423 S13: 0.0028
REMARK 3 S21: 0.0946 S22: -0.0676 S23: 0.2443
REMARK 3 S31: -0.1814 S32: -0.3865 S33: 0.0175
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 193 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): 91.0858 121.4011 -21.3572
REMARK 3 T TENSOR
REMARK 3 T11: 0.3547 T22: 0.2608
REMARK 3 T33: 0.3583 T12: -0.0665
REMARK 3 T13: 0.0360 T23: 0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 1.4993 L22: 0.6495
REMARK 3 L33: 0.7748 L12: 0.1973
REMARK 3 L13: -0.0954 L23: 0.0129
REMARK 3 S TENSOR
REMARK 3 S11: 0.2585 S12: -0.2394 S13: -0.0080
REMARK 3 S21: 0.4335 S22: -0.2164 S23: 0.2517
REMARK 3 S31: -0.0922 S32: 0.0026 S33: -0.0041
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 216 THROUGH 242 )
REMARK 3 ORIGIN FOR THE GROUP (A): 88.3520 117.2691 -24.9778
REMARK 3 T TENSOR
REMARK 3 T11: 0.3058 T22: 0.2159
REMARK 3 T33: 0.2994 T12: -0.0414
REMARK 3 T13: 0.0175 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 1.4889 L22: 2.2190
REMARK 3 L33: 0.7535 L12: 0.0911
REMARK 3 L13: 0.1021 L23: -0.1677
REMARK 3 S TENSOR
REMARK 3 S11: -0.0679 S12: -0.0561 S13: -0.1867
REMARK 3 S21: 0.3052 S22: 0.0428 S23: 0.0067
REMARK 3 S31: -0.0649 S32: -0.0654 S33: 0.0654
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 243 THROUGH 262 )
REMARK 3 ORIGIN FOR THE GROUP (A): 87.1117 116.3370 -37.2421
REMARK 3 T TENSOR
REMARK 3 T11: 0.2192 T22: 0.2530
REMARK 3 T33: 0.3671 T12: -0.0270
REMARK 3 T13: 0.0086 T23: -0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 1.8542 L22: 1.9569
REMARK 3 L33: 3.2708 L12: -0.7221
REMARK 3 L13: 0.8511 L23: -1.0777
REMARK 3 S TENSOR
REMARK 3 S11: -0.1163 S12: 0.2836 S13: -0.0534
REMARK 3 S21: -0.0833 S22: -0.0274 S23: -0.4867
REMARK 3 S31: -0.0382 S32: -0.3021 S33: 0.0607
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 2 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.2755 104.7935 -32.8086
REMARK 3 T TENSOR
REMARK 3 T11: 0.3427 T22: 0.2015
REMARK 3 T33: 0.5306 T12: -0.0291
REMARK 3 T13: 0.0613 T23: -0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.8577 L22: 1.2526
REMARK 3 L33: 0.5797 L12: 0.3283
REMARK 3 L13: 0.2668 L23: -0.1502
REMARK 3 S TENSOR
REMARK 3 S11: -0.0337 S12: 0.0782 S13: -0.4252
REMARK 3 S21: 0.2383 S22: 0.0333 S23: 0.2712
REMARK 3 S31: 0.3387 S32: -0.0661 S33: -0.0314
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 26 THROUGH 39 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.9129 103.0712 -23.2674
REMARK 3 T TENSOR
REMARK 3 T11: 0.5264 T22: 0.2653
REMARK 3 T33: 0.5033 T12: -0.0250
REMARK 3 T13: 0.1455 T23: 0.0723
REMARK 3 L TENSOR
REMARK 3 L11: 2.7251 L22: 2.6994
REMARK 3 L33: 0.9955 L12: 1.9486
REMARK 3 L13: 0.2411 L23: 0.3959
REMARK 3 S TENSOR
REMARK 3 S11: -0.1500 S12: -0.2871 S13: -0.2651
REMARK 3 S21: 0.4679 S22: -0.1386 S23: -0.0251
REMARK 3 S31: 0.4305 S32: 0.0308 S33: 0.0816
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 40 THROUGH 74 )
REMARK 3 ORIGIN FOR THE GROUP (A): 54.8989 105.4060 -32.7593
REMARK 3 T TENSOR
REMARK 3 T11: 0.3476 T22: 0.2793
REMARK 3 T33: 0.7257 T12: -0.0598
REMARK 3 T13: 0.1660 T23: 0.0379
REMARK 3 L TENSOR
REMARK 3 L11: 1.3639 L22: 0.6382
REMARK 3 L33: 0.7496 L12: 0.7052
REMARK 3 L13: -0.1300 L23: 0.3821
REMARK 3 S TENSOR
REMARK 3 S11: -0.1075 S12: -0.0904 S13: -0.7813
REMARK 3 S21: 0.2312 S22: -0.0135 S23: 0.5165
REMARK 3 S31: 0.3194 S32: -0.0629 S33: 0.1297
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 75 THROUGH 97 )
REMARK 3 ORIGIN FOR THE GROUP (A): 52.1815 111.1271 -32.8624
REMARK 3 T TENSOR
REMARK 3 T11: 0.3142 T22: 0.2017
REMARK 3 T33: 0.7282 T12: -0.0501
REMARK 3 T13: 0.1550 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 1.5987 L22: 1.1693
REMARK 3 L33: 2.2716 L12: -0.1557
REMARK 3 L13: 0.5753 L23: -0.2605
REMARK 3 S TENSOR
REMARK 3 S11: -0.0856 S12: -0.2214 S13: 0.0173
REMARK 3 S21: 0.2380 S22: -0.0613 S23: 0.5560
REMARK 3 S31: 0.0287 S32: -0.3029 S33: -0.0056
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 98 THROUGH 138 )
REMARK 3 ORIGIN FOR THE GROUP (A): 56.0092 117.7555 -43.9315
REMARK 3 T TENSOR
REMARK 3 T11: 0.2373 T22: 0.2737
REMARK 3 T33: 0.5010 T12: -0.0139
REMARK 3 T13: 0.0276 T23: -0.0388
REMARK 3 L TENSOR
REMARK 3 L11: 1.5667 L22: 1.5508
REMARK 3 L33: 1.1341 L12: -0.5219
REMARK 3 L13: -0.6396 L23: 0.1026
REMARK 3 S TENSOR
REMARK 3 S11: 0.0623 S12: 0.1279 S13: -0.1879
REMARK 3 S21: 0.0739 S22: -0.0262 S23: 0.5910
REMARK 3 S31: 0.0621 S32: -0.1098 S33: 0.0062
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 139 THROUGH 175 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.6836 123.6526 -44.8076
REMARK 3 T TENSOR
REMARK 3 T11: 0.2557 T22: 0.2324
REMARK 3 T33: 0.3699 T12: -0.0196
REMARK 3 T13: 0.0298 T23: -0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 1.1936 L22: 1.1209
REMARK 3 L33: 0.5112 L12: -0.4305
REMARK 3 L13: -0.2711 L23: -0.2202
REMARK 3 S TENSOR
REMARK 3 S11: 0.1688 S12: 0.0093 S13: -0.1239
REMARK 3 S21: 0.0636 S22: -0.1150 S23: 0.3702
REMARK 3 S31: -0.0995 S32: -0.0963 S33: -0.0630
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 176 THROUGH 192 )
REMARK 3 ORIGIN FOR THE GROUP (A): 74.6589 122.9604 -45.7013
REMARK 3 T TENSOR
REMARK 3 T11: 0.2354 T22: 0.2542
REMARK 3 T33: 0.2872 T12: -0.0041
REMARK 3 T13: 0.0131 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 1.0675 L22: 2.6824
REMARK 3 L33: 1.7098 L12: -1.1535
REMARK 3 L13: -0.8140 L23: 1.3463
REMARK 3 S TENSOR
REMARK 3 S11: -0.0073 S12: -0.0658 S13: -0.0532
REMARK 3 S21: -0.0419 S22: -0.0533 S23: 0.0600
REMARK 3 S31: -0.1247 S32: 0.1594 S33: 0.0397
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 193 THROUGH 203 )
REMARK 3 ORIGIN FOR THE GROUP (A): 68.9686 118.1404 -37.9509
REMARK 3 T TENSOR
REMARK 3 T11: 0.2173 T22: 0.1828
REMARK 3 T33: 0.3828 T12: -0.0282
REMARK 3 T13: 0.0240 T23: -0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 1.5912 L22: 2.3635
REMARK 3 L33: 0.7716 L12: -1.3332
REMARK 3 L13: 0.1688 L23: -0.0914
REMARK 3 S TENSOR
REMARK 3 S11: 0.0252 S12: -0.1693 S13: 0.0714
REMARK 3 S21: -0.0184 S22: 0.1334 S23: -0.1284
REMARK 3 S31: 0.0780 S32: -0.0775 S33: -0.1813
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 204 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): 82.0505 106.8204 -42.6287
REMARK 3 T TENSOR
REMARK 3 T11: 0.3825 T22: 0.2824
REMARK 3 T33: 0.4466 T12: 0.0134
REMARK 3 T13: 0.0529 T23: -0.0457
REMARK 3 L TENSOR
REMARK 3 L11: 0.9121 L22: 3.0925
REMARK 3 L33: 0.8918 L12: -0.4664
REMARK 3 L13: -0.5870 L23: -0.8787
REMARK 3 S TENSOR
REMARK 3 S11: 0.0579 S12: 0.1574 S13: -0.2787
REMARK 3 S21: -0.5151 S22: -0.0838 S23: -0.7861
REMARK 3 S31: 0.3391 S32: 0.0717 S33: -0.0540
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 216 THROUGH 242 )
REMARK 3 ORIGIN FOR THE GROUP (A): 75.9232 114.5755 -34.0822
REMARK 3 T TENSOR
REMARK 3 T11: 0.2434 T22: 0.2160
REMARK 3 T33: 0.2988 T12: -0.0240
REMARK 3 T13: 0.0168 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 1.4803 L22: 1.8355
REMARK 3 L33: 1.3230 L12: 0.2858
REMARK 3 L13: -0.0204 L23: 0.0555
REMARK 3 S TENSOR
REMARK 3 S11: -0.0757 S12: -0.1260 S13: -0.0886
REMARK 3 S21: -0.0889 S22: 0.0735 S23: 0.0532
REMARK 3 S31: 0.0220 S32: 0.0357 S33: -0.0211
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 243 THROUGH 263 )
REMARK 3 ORIGIN FOR THE GROUP (A): 77.7453 122.6389 -23.9845
REMARK 3 T TENSOR
REMARK 3 T11: 0.2940 T22: 0.2149
REMARK 3 T33: 0.3029 T12: -0.0454
REMARK 3 T13: 0.0519 T23: -0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 1.5157 L22: 4.5867
REMARK 3 L33: 0.7086 L12: 1.4753
REMARK 3 L13: 0.4522 L23: 0.9984
REMARK 3 S TENSOR
REMARK 3 S11: 0.0767 S12: -0.1542 S13: 0.2147
REMARK 3 S21: 0.3849 S22: 0.0179 S23: 0.2032
REMARK 3 S31: -0.0661 S32: 0.0736 S33: -0.1121
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 6CLU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1000232842.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979430
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 684630
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 46.622
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.99
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM NITRATE, AND 20% PEG 3350,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
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,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 88.11300
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 132.16950
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 44.05650
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 -23
REMARK 465 GLY A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 GLY A -9
REMARK 465 HIS A -8
REMARK 465 ILE A -7
REMARK 465 GLU A -6
REMARK 465 GLY A -5
REMARK 465 ARG A -4
REMARK 465 HIS A -3
REMARK 465 MET A -2
REMARK 465 LEU A -1
REMARK 465 GLU A 0
REMARK 465 MET A 1
REMARK 465 THR A 51
REMARK 465 ARG A 52
REMARK 465 PRO A 53
REMARK 465 GLY A 54
REMARK 465 HIS A 55
REMARK 465 GLU A 56
REMARK 465 ASN A 261
REMARK 465 ALA A 262
REMARK 465 ARG A 263
REMARK 465 HIS A 264
REMARK 465 ASN A 265
REMARK 465 PHE A 266
REMARK 465 SER A 267
REMARK 465 MET B -23
REMARK 465 GLY B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 SER B -11
REMARK 465 SER B -10
REMARK 465 GLY B -9
REMARK 465 HIS B -8
REMARK 465 ILE B -7
REMARK 465 GLU B -6
REMARK 465 GLY B -5
REMARK 465 ARG B -4
REMARK 465 HIS B -3
REMARK 465 MET B -2
REMARK 465 LEU B -1
REMARK 465 GLU B 0
REMARK 465 MET B 1
REMARK 465 THR B 13
REMARK 465 PRO B 14
REMARK 465 ASP B 15
REMARK 465 SER B 16
REMARK 465 LEU B 17
REMARK 465 SER B 18
REMARK 465 ASP B 19
REMARK 465 GLY B 20
REMARK 465 GLY B 21
REMARK 465 LYS B 22
REMARK 465 PHE B 23
REMARK 465 ASN B 24
REMARK 465 GLY B 48
REMARK 465 VAL B 49
REMARK 465 SER B 50
REMARK 465 THR B 51
REMARK 465 ARG B 52
REMARK 465 PRO B 53
REMARK 465 GLY B 54
REMARK 465 HIS B 55
REMARK 465 GLU B 56
REMARK 465 MET B 57
REMARK 465 GLY B 131
REMARK 465 ASN B 132
REMARK 465 GLY B 133
REMARK 465 ASN B 134
REMARK 465 ARG B 135
REMARK 465 ASP B 136
REMARK 465 GLU B 137
REMARK 465 ALA B 173
REMARK 465 LYS B 174
REMARK 465 THR B 200
REMARK 465 SER B 201
REMARK 465 ARG B 202
REMARK 465 LYS B 203
REMARK 465 ARG B 204
REMARK 465 PHE B 205
REMARK 465 THR B 206
REMARK 465 LYS B 207
REMARK 465 LYS B 208
REMARK 465 MET B 209
REMARK 465 MET B 210
REMARK 465 GLY B 211
REMARK 465 TYR B 212
REMARK 465 ASP B 213
REMARK 465 THR B 214
REMARK 465 THR B 215
REMARK 465 PRO B 216
REMARK 465 VAL B 217
REMARK 465 GLU B 218
REMARK 465 ARG B 219
REMARK 465 ASN B 265
REMARK 465 PHE B 266
REMARK 465 SER B 267
REMARK 465 MET C -23
REMARK 465 GLY C -22
REMARK 465 HIS C -21
REMARK 465 HIS C -20
REMARK 465 HIS C -19
REMARK 465 HIS C -18
REMARK 465 HIS C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 SER C -11
REMARK 465 SER C -10
REMARK 465 GLY C -9
REMARK 465 HIS C -8
REMARK 465 ILE C -7
REMARK 465 GLU C -6
REMARK 465 GLY C -5
REMARK 465 ARG C -4
REMARK 465 HIS C -3
REMARK 465 MET C -2
REMARK 465 LEU C -1
REMARK 465 GLU C 0
REMARK 465 MET C 1
REMARK 465 THR C 13
REMARK 465 PRO C 14
REMARK 465 ASP C 15
REMARK 465 SER C 16
REMARK 465 LEU C 17
REMARK 465 SER C 18
REMARK 465 ASP C 19
REMARK 465 GLY C 20
REMARK 465 GLY C 21
REMARK 465 LYS C 22
REMARK 465 PHE C 23
REMARK 465 ASN C 24
REMARK 465 GLY C 48
REMARK 465 VAL C 49
REMARK 465 SER C 50
REMARK 465 THR C 51
REMARK 465 ARG C 52
REMARK 465 PRO C 53
REMARK 465 GLY C 54
REMARK 465 HIS C 55
REMARK 465 GLU C 56
REMARK 465 MET C 57
REMARK 465 ASN C 132
REMARK 465 GLY C 133
REMARK 465 ASN C 134
REMARK 465 ARG C 135
REMARK 465 ASP C 136
REMARK 465 GLY C 211
REMARK 465 TYR C 212
REMARK 465 ASP C 213
REMARK 465 THR C 214
REMARK 465 ARG C 263
REMARK 465 HIS C 264
REMARK 465 ASN C 265
REMARK 465 PHE C 266
REMARK 465 SER C 267
REMARK 465 MET D -23
REMARK 465 GLY D -22
REMARK 465 HIS D -21
REMARK 465 HIS D -20
REMARK 465 HIS D -19
REMARK 465 HIS D -18
REMARK 465 HIS D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 SER D -11
REMARK 465 SER D -10
REMARK 465 GLY D -9
REMARK 465 HIS D -8
REMARK 465 ILE D -7
REMARK 465 GLU D -6
REMARK 465 GLY D -5
REMARK 465 ARG D -4
REMARK 465 HIS D -3
REMARK 465 MET D -2
REMARK 465 LEU D -1
REMARK 465 GLU D 0
REMARK 465 MET D 1
REMARK 465 VAL D 49
REMARK 465 SER D 50
REMARK 465 THR D 51
REMARK 465 ARG D 52
REMARK 465 PRO D 53
REMARK 465 GLY D 54
REMARK 465 HIS D 55
REMARK 465 GLU D 56
REMARK 465 MET D 57
REMARK 465 ILE D 58
REMARK 465 THR D 59
REMARK 465 HIS D 264
REMARK 465 ASN D 265
REMARK 465 PHE D 266
REMARK 465 SER D 267
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 THR A 2 OG1 CG2
REMARK 470 SER A 18 OG
REMARK 470 ASP A 19 CG OD1 OD2
REMARK 470 LYS A 22 CG CD CE NZ
REMARK 470 GLU A 27 CG CD OE1 OE2
REMARK 470 LYS A 34 CG CD CE NZ
REMARK 470 MET A 57 CG SD CE
REMARK 470 GLU A 61 CG CD OE1 OE2
REMARK 470 GLU A 62 CG CD OE1 OE2
REMARK 470 LYS A 207 CG CD CE NZ
REMARK 470 LYS A 208 CG CD CE NZ
REMARK 470 ASP A 213 CG OD1 OD2
REMARK 470 GLU A 258 CG CD OE1 OE2
REMARK 470 THR B 2 OG1 CG2
REMARK 470 LYS B 5 CG CD CE NZ
REMARK 470 ASN B 11 CG OD1 ND2
REMARK 470 VAL B 12 CG1 CG2
REMARK 470 GLU B 27 CG CD OE1 OE2
REMARK 470 LYS B 34 CG CD CE NZ
REMARK 470 ILE B 58 CG1 CG2 CD1
REMARK 470 GLU B 61 CG CD OE1 OE2
REMARK 470 GLU B 62 CG CD OE1 OE2
REMARK 470 ARG B 66 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 96 CG CD CE NZ
REMARK 470 HIS B 112 CG ND1 CD2 CE1 NE2
REMARK 470 GLN B 116 CG CD OE1 NE2
REMARK 470 LYS B 120 CG CD CE NZ
REMARK 470 ARG B 176 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 178 CG CD OE1 OE2
REMARK 470 GLU B 181 CG CD OE1 OE2
REMARK 470 GLU B 221 CG CD OE1 OE2
REMARK 470 VAL B 222 CG1 CG2
REMARK 470 LYS B 251 CG CD CE NZ
REMARK 470 GLU B 258 CG CD OE1 OE2
REMARK 470 HIS B 264 CG ND1 CD2 CE1 NE2
REMARK 470 THR C 2 OG1 CG2
REMARK 470 GLU C 27 CG CD OE1 OE2
REMARK 470 ARG C 32 CG CD NE CZ NH1 NH2
REMARK 470 ILE C 58 CG1 CG2 CD1
REMARK 470 GLU C 61 CG CD OE1 OE2
REMARK 470 GLU C 62 CG CD OE1 OE2
REMARK 470 ARG C 66 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 116 CG CD OE1 NE2
REMARK 470 GLU C 137 CG CD OE1 OE2
REMARK 470 ARG C 176 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 204 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 207 CG CD CE NZ
REMARK 470 LYS C 208 CG CD CE NZ
REMARK 470 MET C 210 CG SD CE
REMARK 470 THR C 215 OG1 CG2
REMARK 470 LYS C 251 CG CD CE NZ
REMARK 470 ASN C 261 CG OD1 ND2
REMARK 470 THR D 2 OG1 CG2
REMARK 470 GLU D 27 CG CD OE1 OE2
REMARK 470 VAL D 60 CG1 CG2
REMARK 470 GLU D 61 CG CD OE1 OE2
REMARK 470 GLU D 62 CG CD OE1 OE2
REMARK 470 LEU D 64 CG CD1 CD2
REMARK 470 GLU D 72 CG CD OE1 OE2
REMARK 470 LYS D 80 CG CD CE NZ
REMARK 470 ARG D 87 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 89 CG CD OE1 OE2
REMARK 470 LYS D 96 CG CD CE NZ
REMARK 470 LYS D 120 CG CD CE NZ
REMARK 470 ASN D 134 CG OD1 ND2
REMARK 470 GLU D 137 CG CD OE1 OE2
REMARK 470 LYS D 208 CG CD CE NZ
REMARK 470 ASP D 213 CG OD1 OD2
REMARK 470 LYS D 251 CG CD CE NZ
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 ASP A 19 -140.94 62.98
REMARK 500 ARG A 202 13.72 59.30
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6CLU A 1 267 UNP O05701 DHPS_STAAU 1 267
DBREF 6CLU B 1 267 UNP O05701 DHPS_STAAU 1 267
DBREF 6CLU C 1 267 UNP O05701 DHPS_STAAU 1 267
DBREF 6CLU D 1 267 UNP O05701 DHPS_STAAU 1 267
SEQADV 6CLU MET A -23 UNP O05701 INITIATING METHIONINE
SEQADV 6CLU GLY A -22 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS A -21 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS A -20 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS A -19 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS A -18 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS A -17 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS A -16 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS A -15 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS A -14 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS A -13 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS A -12 UNP O05701 EXPRESSION TAG
SEQADV 6CLU SER A -11 UNP O05701 EXPRESSION TAG
SEQADV 6CLU SER A -10 UNP O05701 EXPRESSION TAG
SEQADV 6CLU GLY A -9 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS A -8 UNP O05701 EXPRESSION TAG
SEQADV 6CLU ILE A -7 UNP O05701 EXPRESSION TAG
SEQADV 6CLU GLU A -6 UNP O05701 EXPRESSION TAG
SEQADV 6CLU GLY A -5 UNP O05701 EXPRESSION TAG
SEQADV 6CLU ARG A -4 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS A -3 UNP O05701 EXPRESSION TAG
SEQADV 6CLU MET A -2 UNP O05701 EXPRESSION TAG
SEQADV 6CLU LEU A -1 UNP O05701 EXPRESSION TAG
SEQADV 6CLU GLU A 0 UNP O05701 EXPRESSION TAG
SEQADV 6CLU LEU A 17 UNP O05701 PHE 17 ENGINEERED MUTATION
SEQADV 6CLU LYS A 208 UNP O05701 GLU 208 ENGINEERED MUTATION
SEQADV 6CLU MET B -23 UNP O05701 INITIATING METHIONINE
SEQADV 6CLU GLY B -22 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS B -21 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS B -20 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS B -19 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS B -18 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS B -17 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS B -16 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS B -15 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS B -14 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS B -13 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS B -12 UNP O05701 EXPRESSION TAG
SEQADV 6CLU SER B -11 UNP O05701 EXPRESSION TAG
SEQADV 6CLU SER B -10 UNP O05701 EXPRESSION TAG
SEQADV 6CLU GLY B -9 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS B -8 UNP O05701 EXPRESSION TAG
SEQADV 6CLU ILE B -7 UNP O05701 EXPRESSION TAG
SEQADV 6CLU GLU B -6 UNP O05701 EXPRESSION TAG
SEQADV 6CLU GLY B -5 UNP O05701 EXPRESSION TAG
SEQADV 6CLU ARG B -4 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS B -3 UNP O05701 EXPRESSION TAG
SEQADV 6CLU MET B -2 UNP O05701 EXPRESSION TAG
SEQADV 6CLU LEU B -1 UNP O05701 EXPRESSION TAG
SEQADV 6CLU GLU B 0 UNP O05701 EXPRESSION TAG
SEQADV 6CLU LEU B 17 UNP O05701 PHE 17 ENGINEERED MUTATION
SEQADV 6CLU LYS B 208 UNP O05701 GLU 208 ENGINEERED MUTATION
SEQADV 6CLU MET C -23 UNP O05701 INITIATING METHIONINE
SEQADV 6CLU GLY C -22 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS C -21 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS C -20 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS C -19 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS C -18 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS C -17 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS C -16 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS C -15 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS C -14 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS C -13 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS C -12 UNP O05701 EXPRESSION TAG
SEQADV 6CLU SER C -11 UNP O05701 EXPRESSION TAG
SEQADV 6CLU SER C -10 UNP O05701 EXPRESSION TAG
SEQADV 6CLU GLY C -9 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS C -8 UNP O05701 EXPRESSION TAG
SEQADV 6CLU ILE C -7 UNP O05701 EXPRESSION TAG
SEQADV 6CLU GLU C -6 UNP O05701 EXPRESSION TAG
SEQADV 6CLU GLY C -5 UNP O05701 EXPRESSION TAG
SEQADV 6CLU ARG C -4 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS C -3 UNP O05701 EXPRESSION TAG
SEQADV 6CLU MET C -2 UNP O05701 EXPRESSION TAG
SEQADV 6CLU LEU C -1 UNP O05701 EXPRESSION TAG
SEQADV 6CLU GLU C 0 UNP O05701 EXPRESSION TAG
SEQADV 6CLU LEU C 17 UNP O05701 PHE 17 ENGINEERED MUTATION
SEQADV 6CLU LYS C 208 UNP O05701 GLU 208 ENGINEERED MUTATION
SEQADV 6CLU MET D -23 UNP O05701 INITIATING METHIONINE
SEQADV 6CLU GLY D -22 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS D -21 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS D -20 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS D -19 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS D -18 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS D -17 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS D -16 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS D -15 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS D -14 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS D -13 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS D -12 UNP O05701 EXPRESSION TAG
SEQADV 6CLU SER D -11 UNP O05701 EXPRESSION TAG
SEQADV 6CLU SER D -10 UNP O05701 EXPRESSION TAG
SEQADV 6CLU GLY D -9 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS D -8 UNP O05701 EXPRESSION TAG
SEQADV 6CLU ILE D -7 UNP O05701 EXPRESSION TAG
SEQADV 6CLU GLU D -6 UNP O05701 EXPRESSION TAG
SEQADV 6CLU GLY D -5 UNP O05701 EXPRESSION TAG
SEQADV 6CLU ARG D -4 UNP O05701 EXPRESSION TAG
SEQADV 6CLU HIS D -3 UNP O05701 EXPRESSION TAG
SEQADV 6CLU MET D -2 UNP O05701 EXPRESSION TAG
SEQADV 6CLU LEU D -1 UNP O05701 EXPRESSION TAG
SEQADV 6CLU GLU D 0 UNP O05701 EXPRESSION TAG
SEQADV 6CLU LEU D 17 UNP O05701 PHE 17 ENGINEERED MUTATION
SEQADV 6CLU LYS D 208 UNP O05701 GLU 208 ENGINEERED MUTATION
SEQRES 1 A 291 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 A 291 SER GLY HIS ILE GLU GLY ARG HIS MET LEU GLU MET THR
SEQRES 3 A 291 LYS THR LYS ILE MET GLY ILE LEU ASN VAL THR PRO ASP
SEQRES 4 A 291 SER LEU SER ASP GLY GLY LYS PHE ASN ASN VAL GLU SER
SEQRES 5 A 291 ALA VAL THR ARG VAL LYS ALA MET MET ASP GLU GLY ALA
SEQRES 6 A 291 ASP ILE ILE ASP VAL GLY GLY VAL SER THR ARG PRO GLY
SEQRES 7 A 291 HIS GLU MET ILE THR VAL GLU GLU GLU LEU ASN ARG VAL
SEQRES 8 A 291 LEU PRO VAL VAL GLU ALA ILE VAL GLY PHE ASP VAL LYS
SEQRES 9 A 291 ILE SER VAL ASP THR PHE ARG SER GLU VAL ALA GLU ALA
SEQRES 10 A 291 CYS LEU LYS LEU GLY VAL ASP ILE ILE ASN ASP GLN TRP
SEQRES 11 A 291 ALA GLY LEU TYR ASP HIS ARG MET PHE GLN VAL VAL ALA
SEQRES 12 A 291 LYS TYR ASP ALA GLU ILE VAL LEU MET HIS ASN GLY ASN
SEQRES 13 A 291 GLY ASN ARG ASP GLU PRO VAL VAL GLU GLU MET LEU THR
SEQRES 14 A 291 SER LEU LEU ALA GLN ALA HIS GLN ALA LYS ILE ALA GLY
SEQRES 15 A 291 ILE PRO SER ASN LYS ILE TRP LEU ASP PRO GLY ILE GLY
SEQRES 16 A 291 PHE ALA LYS THR ARG ASN GLU GLU ALA GLU VAL MET ALA
SEQRES 17 A 291 ARG LEU ASP GLU LEU VAL ALA THR GLU TYR PRO VAL LEU
SEQRES 18 A 291 LEU ALA THR SER ARG LYS ARG PHE THR LYS LYS MET MET
SEQRES 19 A 291 GLY TYR ASP THR THR PRO VAL GLU ARG ASP GLU VAL THR
SEQRES 20 A 291 ALA ALA THR THR ALA TYR GLY ILE MET LYS GLY VAL ARG
SEQRES 21 A 291 ALA VAL ARG VAL HIS ASN VAL GLU LEU ASN ALA LYS LEU
SEQRES 22 A 291 ALA LYS GLY ILE ASP PHE LEU LYS GLU ASN GLU ASN ALA
SEQRES 23 A 291 ARG HIS ASN PHE SER
SEQRES 1 B 291 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 B 291 SER GLY HIS ILE GLU GLY ARG HIS MET LEU GLU MET THR
SEQRES 3 B 291 LYS THR LYS ILE MET GLY ILE LEU ASN VAL THR PRO ASP
SEQRES 4 B 291 SER LEU SER ASP GLY GLY LYS PHE ASN ASN VAL GLU SER
SEQRES 5 B 291 ALA VAL THR ARG VAL LYS ALA MET MET ASP GLU GLY ALA
SEQRES 6 B 291 ASP ILE ILE ASP VAL GLY GLY VAL SER THR ARG PRO GLY
SEQRES 7 B 291 HIS GLU MET ILE THR VAL GLU GLU GLU LEU ASN ARG VAL
SEQRES 8 B 291 LEU PRO VAL VAL GLU ALA ILE VAL GLY PHE ASP VAL LYS
SEQRES 9 B 291 ILE SER VAL ASP THR PHE ARG SER GLU VAL ALA GLU ALA
SEQRES 10 B 291 CYS LEU LYS LEU GLY VAL ASP ILE ILE ASN ASP GLN TRP
SEQRES 11 B 291 ALA GLY LEU TYR ASP HIS ARG MET PHE GLN VAL VAL ALA
SEQRES 12 B 291 LYS TYR ASP ALA GLU ILE VAL LEU MET HIS ASN GLY ASN
SEQRES 13 B 291 GLY ASN ARG ASP GLU PRO VAL VAL GLU GLU MET LEU THR
SEQRES 14 B 291 SER LEU LEU ALA GLN ALA HIS GLN ALA LYS ILE ALA GLY
SEQRES 15 B 291 ILE PRO SER ASN LYS ILE TRP LEU ASP PRO GLY ILE GLY
SEQRES 16 B 291 PHE ALA LYS THR ARG ASN GLU GLU ALA GLU VAL MET ALA
SEQRES 17 B 291 ARG LEU ASP GLU LEU VAL ALA THR GLU TYR PRO VAL LEU
SEQRES 18 B 291 LEU ALA THR SER ARG LYS ARG PHE THR LYS LYS MET MET
SEQRES 19 B 291 GLY TYR ASP THR THR PRO VAL GLU ARG ASP GLU VAL THR
SEQRES 20 B 291 ALA ALA THR THR ALA TYR GLY ILE MET LYS GLY VAL ARG
SEQRES 21 B 291 ALA VAL ARG VAL HIS ASN VAL GLU LEU ASN ALA LYS LEU
SEQRES 22 B 291 ALA LYS GLY ILE ASP PHE LEU LYS GLU ASN GLU ASN ALA
SEQRES 23 B 291 ARG HIS ASN PHE SER
SEQRES 1 C 291 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 C 291 SER GLY HIS ILE GLU GLY ARG HIS MET LEU GLU MET THR
SEQRES 3 C 291 LYS THR LYS ILE MET GLY ILE LEU ASN VAL THR PRO ASP
SEQRES 4 C 291 SER LEU SER ASP GLY GLY LYS PHE ASN ASN VAL GLU SER
SEQRES 5 C 291 ALA VAL THR ARG VAL LYS ALA MET MET ASP GLU GLY ALA
SEQRES 6 C 291 ASP ILE ILE ASP VAL GLY GLY VAL SER THR ARG PRO GLY
SEQRES 7 C 291 HIS GLU MET ILE THR VAL GLU GLU GLU LEU ASN ARG VAL
SEQRES 8 C 291 LEU PRO VAL VAL GLU ALA ILE VAL GLY PHE ASP VAL LYS
SEQRES 9 C 291 ILE SER VAL ASP THR PHE ARG SER GLU VAL ALA GLU ALA
SEQRES 10 C 291 CYS LEU LYS LEU GLY VAL ASP ILE ILE ASN ASP GLN TRP
SEQRES 11 C 291 ALA GLY LEU TYR ASP HIS ARG MET PHE GLN VAL VAL ALA
SEQRES 12 C 291 LYS TYR ASP ALA GLU ILE VAL LEU MET HIS ASN GLY ASN
SEQRES 13 C 291 GLY ASN ARG ASP GLU PRO VAL VAL GLU GLU MET LEU THR
SEQRES 14 C 291 SER LEU LEU ALA GLN ALA HIS GLN ALA LYS ILE ALA GLY
SEQRES 15 C 291 ILE PRO SER ASN LYS ILE TRP LEU ASP PRO GLY ILE GLY
SEQRES 16 C 291 PHE ALA LYS THR ARG ASN GLU GLU ALA GLU VAL MET ALA
SEQRES 17 C 291 ARG LEU ASP GLU LEU VAL ALA THR GLU TYR PRO VAL LEU
SEQRES 18 C 291 LEU ALA THR SER ARG LYS ARG PHE THR LYS LYS MET MET
SEQRES 19 C 291 GLY TYR ASP THR THR PRO VAL GLU ARG ASP GLU VAL THR
SEQRES 20 C 291 ALA ALA THR THR ALA TYR GLY ILE MET LYS GLY VAL ARG
SEQRES 21 C 291 ALA VAL ARG VAL HIS ASN VAL GLU LEU ASN ALA LYS LEU
SEQRES 22 C 291 ALA LYS GLY ILE ASP PHE LEU LYS GLU ASN GLU ASN ALA
SEQRES 23 C 291 ARG HIS ASN PHE SER
SEQRES 1 D 291 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 D 291 SER GLY HIS ILE GLU GLY ARG HIS MET LEU GLU MET THR
SEQRES 3 D 291 LYS THR LYS ILE MET GLY ILE LEU ASN VAL THR PRO ASP
SEQRES 4 D 291 SER LEU SER ASP GLY GLY LYS PHE ASN ASN VAL GLU SER
SEQRES 5 D 291 ALA VAL THR ARG VAL LYS ALA MET MET ASP GLU GLY ALA
SEQRES 6 D 291 ASP ILE ILE ASP VAL GLY GLY VAL SER THR ARG PRO GLY
SEQRES 7 D 291 HIS GLU MET ILE THR VAL GLU GLU GLU LEU ASN ARG VAL
SEQRES 8 D 291 LEU PRO VAL VAL GLU ALA ILE VAL GLY PHE ASP VAL LYS
SEQRES 9 D 291 ILE SER VAL ASP THR PHE ARG SER GLU VAL ALA GLU ALA
SEQRES 10 D 291 CYS LEU LYS LEU GLY VAL ASP ILE ILE ASN ASP GLN TRP
SEQRES 11 D 291 ALA GLY LEU TYR ASP HIS ARG MET PHE GLN VAL VAL ALA
SEQRES 12 D 291 LYS TYR ASP ALA GLU ILE VAL LEU MET HIS ASN GLY ASN
SEQRES 13 D 291 GLY ASN ARG ASP GLU PRO VAL VAL GLU GLU MET LEU THR
SEQRES 14 D 291 SER LEU LEU ALA GLN ALA HIS GLN ALA LYS ILE ALA GLY
SEQRES 15 D 291 ILE PRO SER ASN LYS ILE TRP LEU ASP PRO GLY ILE GLY
SEQRES 16 D 291 PHE ALA LYS THR ARG ASN GLU GLU ALA GLU VAL MET ALA
SEQRES 17 D 291 ARG LEU ASP GLU LEU VAL ALA THR GLU TYR PRO VAL LEU
SEQRES 18 D 291 LEU ALA THR SER ARG LYS ARG PHE THR LYS LYS MET MET
SEQRES 19 D 291 GLY TYR ASP THR THR PRO VAL GLU ARG ASP GLU VAL THR
SEQRES 20 D 291 ALA ALA THR THR ALA TYR GLY ILE MET LYS GLY VAL ARG
SEQRES 21 D 291 ALA VAL ARG VAL HIS ASN VAL GLU LEU ASN ALA LYS LEU
SEQRES 22 D 291 ALA LYS GLY ILE ASP PHE LEU LYS GLU ASN GLU ASN ALA
SEQRES 23 D 291 ARG HIS ASN PHE SER
FORMUL 5 HOH *197(H2 O)
HELIX 1 AA1 ASN A 25 GLY A 40 1 16
HELIX 2 AA2 THR A 59 VAL A 75 1 17
HELIX 3 AA3 ARG A 87 LEU A 97 1 11
HELIX 4 AA4 ARG A 113 TYR A 121 1 9
HELIX 5 AA5 PRO A 138 GLY A 158 1 21
HELIX 6 AA6 PRO A 160 ASN A 162 5 3
HELIX 7 AA7 THR A 175 ARG A 185 1 11
HELIX 8 AA8 ARG A 185 ALA A 191 1 7
HELIX 9 AA9 LYS A 203 MET A 210 1 8
HELIX 10 AB1 PRO A 216 GLU A 218 5 3
HELIX 11 AB2 ARG A 219 GLY A 234 1 16
HELIX 12 AB3 ASN A 242 GLU A 260 1 19
HELIX 13 AB4 VAL B 26 GLY B 40 1 15
HELIX 14 AB5 THR B 59 VAL B 75 1 17
HELIX 15 AB6 ARG B 87 GLY B 98 1 12
HELIX 16 AB7 ARG B 113 TYR B 121 1 9
HELIX 17 AB8 VAL B 139 GLY B 158 1 20
HELIX 18 AB9 PRO B 160 ASN B 162 5 3
HELIX 19 AC1 ARG B 176 ARG B 185 1 10
HELIX 20 AC2 ARG B 185 ALA B 191 1 7
HELIX 21 AC3 VAL B 222 GLY B 234 1 13
HELIX 22 AC4 ASN B 242 ARG B 263 1 22
HELIX 23 AC5 VAL C 26 GLY C 40 1 15
HELIX 24 AC6 THR C 59 VAL C 75 1 17
HELIX 25 AC7 ARG C 87 GLY C 98 1 12
HELIX 26 AC8 HIS C 112 TYR C 121 1 10
HELIX 27 AC9 PRO C 138 GLY C 158 1 21
HELIX 28 AD1 PRO C 160 ASN C 162 5 3
HELIX 29 AD2 THR C 175 ARG C 185 1 11
HELIX 30 AD3 ARG C 185 ALA C 191 1 7
HELIX 31 AD4 LYS C 203 MET C 210 1 8
HELIX 32 AD5 PRO C 216 GLU C 218 5 3
HELIX 33 AD6 ARG C 219 GLY C 234 1 16
HELIX 34 AD7 ASN C 242 ALA C 262 1 21
HELIX 35 AD8 ASN D 25 GLY D 40 1 16
HELIX 36 AD9 GLU D 61 VAL D 75 1 15
HELIX 37 AE1 ARG D 87 GLY D 98 1 12
HELIX 38 AE2 ARG D 113 TYR D 121 1 9
HELIX 39 AE3 PRO D 138 GLY D 158 1 21
HELIX 40 AE4 PRO D 160 ASN D 162 5 3
HELIX 41 AE5 THR D 175 ALA D 184 1 10
HELIX 42 AE6 ARG D 185 ALA D 191 1 7
HELIX 43 AE7 LYS D 203 GLY D 211 1 9
HELIX 44 AE8 THR D 215 GLU D 218 5 4
HELIX 45 AE9 ARG D 219 GLY D 234 1 16
HELIX 46 AF1 ASN D 242 ARG D 263 1 22
SHEET 1 AA1 8 ILE A 164 ASP A 167 0
SHEET 2 AA1 8 GLU A 124 MET A 128 1 N LEU A 127 O TRP A 165
SHEET 3 AA1 8 ILE A 101 ASP A 104 1 N ILE A 102 O VAL A 126
SHEET 4 AA1 8 LYS A 80 ASP A 84 1 N VAL A 83 O ASN A 103
SHEET 5 AA1 8 ILE A 43 VAL A 46 1 N ILE A 44 O SER A 82
SHEET 6 AA1 8 LYS A 5 LEU A 10 1 N GLY A 8 O ASP A 45
SHEET 7 AA1 8 ALA A 237 VAL A 240 1 O VAL A 238 N MET A 7
SHEET 8 AA1 8 LEU A 197 LEU A 198 1 N LEU A 198 O ARG A 239
SHEET 1 AA2 8 ILE B 164 ASP B 167 0
SHEET 2 AA2 8 GLU B 124 MET B 128 1 N LEU B 127 O TRP B 165
SHEET 3 AA2 8 ILE B 101 ASP B 104 1 N ILE B 102 O VAL B 126
SHEET 4 AA2 8 LYS B 80 ASP B 84 1 N VAL B 83 O ASN B 103
SHEET 5 AA2 8 ILE B 43 VAL B 46 1 N VAL B 46 O SER B 82
SHEET 6 AA2 8 LYS B 5 LEU B 10 1 N GLY B 8 O ILE B 43
SHEET 7 AA2 8 ALA B 237 VAL B 240 1 O VAL B 238 N MET B 7
SHEET 8 AA2 8 LEU B 197 LEU B 198 1 N LEU B 198 O ALA B 237
SHEET 1 AA3 8 ILE C 164 ASP C 167 0
SHEET 2 AA3 8 GLU C 124 MET C 128 1 N LEU C 127 O TRP C 165
SHEET 3 AA3 8 ILE C 101 ASP C 104 1 N ILE C 102 O VAL C 126
SHEET 4 AA3 8 LYS C 80 ASP C 84 1 N VAL C 83 O ASN C 103
SHEET 5 AA3 8 ILE C 43 VAL C 46 1 N VAL C 46 O SER C 82
SHEET 6 AA3 8 LYS C 5 LEU C 10 1 N GLY C 8 O ILE C 43
SHEET 7 AA3 8 ALA C 237 VAL C 240 1 O VAL C 238 N MET C 7
SHEET 8 AA3 8 LEU C 197 LEU C 198 1 N LEU C 198 O ALA C 237
SHEET 1 AA4 8 ILE D 164 ASP D 167 0
SHEET 2 AA4 8 GLU D 124 MET D 128 1 N ILE D 125 O TRP D 165
SHEET 3 AA4 8 ILE D 101 ASP D 104 1 N ILE D 102 O VAL D 126
SHEET 4 AA4 8 LYS D 80 ASP D 84 1 N ILE D 81 O ILE D 101
SHEET 5 AA4 8 ILE D 43 VAL D 46 1 N ILE D 44 O SER D 82
SHEET 6 AA4 8 LYS D 5 LEU D 10 1 N GLY D 8 O ILE D 43
SHEET 7 AA4 8 ALA D 237 VAL D 240 1 O VAL D 238 N MET D 7
SHEET 8 AA4 8 LEU D 197 LEU D 198 1 N LEU D 198 O ARG D 239
CRYST1 76.636 76.636 176.226 90.00 90.00 90.00 P 43 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 0.013049 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013049 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005675 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
