HEADER PROTEIN TRANSPORT 20-JUN-14 4TT9
TITLE STRUCTURE OF THE C-TERMINAL SPOA DOMAIN OF SHIGELLA FLEXNERI SPA33
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SURFACE PRESENTATION OF ANTIGENS PROTEIN SPAO;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: SPA33 PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: C-TERMINAL SPOA DOMAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SHIGELLA FLEXNERI;
SOURCE 3 ORGANISM_TAXID: 623;
SOURCE 4 GENE: SPAO, SPA33, CP0152;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 37762;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS T3SS, C-RING, SPOA, FLIN, IMMUNE SYSTEM, PROTEIN TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.MCDOWELL,S.JOHNSON,S.M.LEA
REVDAT 4 20-DEC-23 4TT9 1 REMARK
REVDAT 3 24-FEB-16 4TT9 1 JRNL
REVDAT 2 18-NOV-15 4TT9 1 JRNL
REVDAT 1 24-JUN-15 4TT9 0
JRNL AUTH M.A.MCDOWELL,J.MARCOUX,G.MCVICKER,S.JOHNSON,Y.H.FONG,
JRNL AUTH 2 R.STEVENS,L.A.BOWMAN,M.T.DEGIACOMI,J.YAN,A.WISE,M.E.FRIEDE,
JRNL AUTH 3 J.L.BENESCH,J.E.DEANE,C.M.TANG,C.V.ROBINSON,S.M.LEA
JRNL TITL CHARACTERISATION OF SHIGELLA SPA33 AND THERMOTOGA FLIM/N
JRNL TITL 2 REVEALS A NEW MODEL FOR C-RING ASSEMBLY IN T3SS.
JRNL REF MOL.MICROBIOL. V. 99 749 2016
JRNL REFN ESSN 1365-2958
JRNL PMID 26538516
JRNL DOI 10.1111/MMI.13267
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 13522
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.120
REMARK 3 FREE R VALUE TEST SET COUNT : 1369
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 51.3127 - 4.9595 0.87 1272 161 0.1347 0.1716
REMARK 3 2 4.9595 - 3.9370 0.89 1206 137 0.1156 0.1714
REMARK 3 3 3.9370 - 3.4394 0.89 1215 147 0.1586 0.1754
REMARK 3 4 3.4394 - 3.1250 0.90 1222 132 0.1882 0.2218
REMARK 3 5 3.1250 - 2.9010 0.90 1237 128 0.2164 0.2767
REMARK 3 6 2.9010 - 2.7300 0.90 1200 134 0.2370 0.2462
REMARK 3 7 2.7300 - 2.5933 0.90 1209 123 0.2587 0.3033
REMARK 3 8 2.5933 - 2.4804 0.90 1195 136 0.2916 0.3362
REMARK 3 9 2.4804 - 2.3849 0.89 1208 140 0.3128 0.3597
REMARK 3 10 2.3849 - 2.3026 0.90 1174 127 0.3240 0.3645
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.520
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 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 : 0.007 2323
REMARK 3 ANGLE : 1.030 3124
REMARK 3 CHIRALITY : 0.071 357
REMARK 3 PLANARITY : 0.004 391
REMARK 3 DIHEDRAL : 15.140 854
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 17
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 16 THROUGH 22 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.0475 -13.3752 48.8198
REMARK 3 T TENSOR
REMARK 3 T11: 0.4681 T22: 1.3048
REMARK 3 T33: 0.8499 T12: 0.1541
REMARK 3 T13: 0.1932 T23: 0.4457
REMARK 3 L TENSOR
REMARK 3 L11: 1.1758 L22: 2.8753
REMARK 3 L33: 1.1638 L12: 1.7185
REMARK 3 L13: 0.7563 L23: 1.5752
REMARK 3 S TENSOR
REMARK 3 S11: -0.4318 S12: -0.7934 S13: -0.8849
REMARK 3 S21: 0.1390 S22: -0.4956 S23: -0.4081
REMARK 3 S31: 0.6648 S32: 0.2569 S33: 0.5052
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 23 THROUGH 43 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.2789 5.3828 42.6081
REMARK 3 T TENSOR
REMARK 3 T11: 0.3763 T22: 0.4060
REMARK 3 T33: 0.3747 T12: -0.0078
REMARK 3 T13: -0.0149 T23: -0.1409
REMARK 3 L TENSOR
REMARK 3 L11: 7.3134 L22: 2.4850
REMARK 3 L33: 6.7660 L12: 1.8974
REMARK 3 L13: 1.5735 L23: -1.1636
REMARK 3 S TENSOR
REMARK 3 S11: -0.5177 S12: -0.3178 S13: 0.9485
REMARK 3 S21: 0.1573 S22: 0.1905 S23: 0.2993
REMARK 3 S31: -0.4559 S32: -0.2163 S33: 0.6591
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 44 THROUGH 55 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1745 7.8157 33.1222
REMARK 3 T TENSOR
REMARK 3 T11: 0.4821 T22: 0.4972
REMARK 3 T33: 0.6237 T12: -0.0450
REMARK 3 T13: -0.1324 T23: -0.0933
REMARK 3 L TENSOR
REMARK 3 L11: 3.2815 L22: 2.8184
REMARK 3 L33: 3.0485 L12: 1.0177
REMARK 3 L13: -2.6596 L23: -0.1909
REMARK 3 S TENSOR
REMARK 3 S11: -0.5309 S12: 0.1572 S13: 1.8254
REMARK 3 S21: -0.6885 S22: 0.6044 S23: 0.0458
REMARK 3 S31: -0.0293 S32: 0.0100 S33: 0.1184
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 56 THROUGH 80 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.0113 -1.2206 33.4577
REMARK 3 T TENSOR
REMARK 3 T11: 0.3719 T22: 0.5359
REMARK 3 T33: 0.5267 T12: -0.0232
REMARK 3 T13: 0.1862 T23: -0.0490
REMARK 3 L TENSOR
REMARK 3 L11: 5.3184 L22: 4.7844
REMARK 3 L33: 6.4202 L12: -1.2088
REMARK 3 L13: 1.6841 L23: 1.3646
REMARK 3 S TENSOR
REMARK 3 S11: -0.2550 S12: -0.2172 S13: 0.0425
REMARK 3 S21: -0.2938 S22: -0.4011 S23: -0.2029
REMARK 3 S31: -0.1674 S32: -0.6296 S33: 0.7502
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 81 THROUGH 85 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.7434 1.4770 36.8528
REMARK 3 T TENSOR
REMARK 3 T11: 0.3930 T22: 1.0522
REMARK 3 T33: 0.5576 T12: -0.0881
REMARK 3 T13: 0.0148 T23: 0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 6.1031 L22: 6.6986
REMARK 3 L33: 7.8917 L12: 1.1313
REMARK 3 L13: 6.9380 L23: 1.0271
REMARK 3 S TENSOR
REMARK 3 S11: -0.0591 S12: -0.6160 S13: -1.0302
REMARK 3 S21: -0.0285 S22: -0.1617 S23: -1.3008
REMARK 3 S31: -0.3268 S32: 2.5670 S33: -0.5958
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 16 THROUGH 39 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.0589 -3.1077 44.4822
REMARK 3 T TENSOR
REMARK 3 T11: 0.2993 T22: 0.3716
REMARK 3 T33: 0.3098 T12: -0.1135
REMARK 3 T13: 0.0799 T23: 0.0610
REMARK 3 L TENSOR
REMARK 3 L11: 2.7309 L22: 3.8900
REMARK 3 L33: 3.6588 L12: -1.6670
REMARK 3 L13: 2.7167 L23: -0.1856
REMARK 3 S TENSOR
REMARK 3 S11: 0.0241 S12: 0.4559 S13: 0.0600
REMARK 3 S21: 0.0521 S22: -0.5107 S23: -0.0162
REMARK 3 S31: 0.0737 S32: -0.0744 S33: 0.5248
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 40 THROUGH 87 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9172 -2.4830 34.9331
REMARK 3 T TENSOR
REMARK 3 T11: 0.3245 T22: 0.3600
REMARK 3 T33: 0.3092 T12: 0.0051
REMARK 3 T13: 0.0017 T23: 0.0331
REMARK 3 L TENSOR
REMARK 3 L11: 4.2664 L22: 3.8046
REMARK 3 L33: 5.3071 L12: 0.9585
REMARK 3 L13: -1.0313 L23: 0.9951
REMARK 3 S TENSOR
REMARK 3 S11: -0.2453 S12: -0.1132 S13: -0.0286
REMARK 3 S21: -0.1542 S22: -0.1393 S23: 0.1293
REMARK 3 S31: 0.2996 S32: 0.2476 S33: 0.3653
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 15 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.2212 -0.4223 7.5971
REMARK 3 T TENSOR
REMARK 3 T11: 0.4354 T22: 0.3714
REMARK 3 T33: 0.3729 T12: 0.0139
REMARK 3 T13: 0.0830 T23: -0.0936
REMARK 3 L TENSOR
REMARK 3 L11: 3.1322 L22: 0.7966
REMARK 3 L33: 3.4735 L12: -0.3502
REMARK 3 L13: -2.4790 L23: -0.8267
REMARK 3 S TENSOR
REMARK 3 S11: -0.3325 S12: -0.1685 S13: -0.7250
REMARK 3 S21: -0.1605 S22: -0.2566 S23: 0.0396
REMARK 3 S31: 0.5485 S32: -0.0158 S33: 0.4391
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 43 THROUGH 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0654 -2.7926 18.4656
REMARK 3 T TENSOR
REMARK 3 T11: 0.3859 T22: 0.2905
REMARK 3 T33: 0.3521 T12: 0.0077
REMARK 3 T13: 0.0344 T23: 0.0401
REMARK 3 L TENSOR
REMARK 3 L11: 9.3607 L22: 4.0898
REMARK 3 L33: 2.3510 L12: 0.0894
REMARK 3 L13: 0.4537 L23: 0.9300
REMARK 3 S TENSOR
REMARK 3 S11: -0.1806 S12: 0.1890 S13: -0.6418
REMARK 3 S21: 0.2431 S22: 0.1518 S23: -0.3378
REMARK 3 S31: 0.5501 S32: 0.0756 S33: 0.1014
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 78 THROUGH 86 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9954 -0.6743 17.0646
REMARK 3 T TENSOR
REMARK 3 T11: 0.4249 T22: 0.7925
REMARK 3 T33: 0.8809 T12: 0.1221
REMARK 3 T13: -0.1247 T23: -0.0351
REMARK 3 L TENSOR
REMARK 3 L11: 9.5365 L22: 6.7453
REMARK 3 L33: 7.5464 L12: -3.6710
REMARK 3 L13: -6.3364 L23: 3.9601
REMARK 3 S TENSOR
REMARK 3 S11: 0.0797 S12: 0.6801 S13: -1.1291
REMARK 3 S21: 0.1926 S22: -0.1936 S23: -1.1820
REMARK 3 S31: 0.0141 S32: 0.4352 S33: 0.0293
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 17 THROUGH 34 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5041 0.8435 7.5185
REMARK 3 T TENSOR
REMARK 3 T11: 0.3709 T22: 0.3749
REMARK 3 T33: 0.3968 T12: 0.0118
REMARK 3 T13: 0.0517 T23: 0.0829
REMARK 3 L TENSOR
REMARK 3 L11: 4.4849 L22: 0.6433
REMARK 3 L33: 6.9973 L12: -0.3659
REMARK 3 L13: 0.9881 L23: 2.0631
REMARK 3 S TENSOR
REMARK 3 S11: -0.4486 S12: 0.1260 S13: 0.2188
REMARK 3 S21: 0.0064 S22: -0.2632 S23: 0.3263
REMARK 3 S31: 0.3467 S32: -0.3445 S33: 0.8461
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 35 THROUGH 43 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9854 7.0296 14.8370
REMARK 3 T TENSOR
REMARK 3 T11: 0.5803 T22: 1.0134
REMARK 3 T33: 0.5853 T12: -0.0865
REMARK 3 T13: -0.0109 T23: 0.4241
REMARK 3 L TENSOR
REMARK 3 L11: 2.8648 L22: 3.8301
REMARK 3 L33: 8.7609 L12: 1.6102
REMARK 3 L13: -3.9061 L23: 0.9231
REMARK 3 S TENSOR
REMARK 3 S11: -0.3365 S12: -1.2407 S13: -0.9276
REMARK 3 S21: 0.3817 S22: 0.0934 S23: -0.2004
REMARK 3 S31: 0.7265 S32: 0.0127 S33: -0.5647
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 44 THROUGH 48 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9641 6.6765 23.2685
REMARK 3 T TENSOR
REMARK 3 T11: 0.5593 T22: 1.0572
REMARK 3 T33: 0.4909 T12: 0.1813
REMARK 3 T13: -0.1449 T23: 0.2004
REMARK 3 L TENSOR
REMARK 3 L11: 3.0761 L22: 4.4755
REMARK 3 L33: 5.1323 L12: -1.4072
REMARK 3 L13: 3.9737 L23: -1.8229
REMARK 3 S TENSOR
REMARK 3 S11: -0.1699 S12: 1.0671 S13: 0.7815
REMARK 3 S21: -1.1260 S22: -0.3694 S23: 0.0315
REMARK 3 S31: -0.9621 S32: 0.5156 S33: 0.5955
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 49 THROUGH 53 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7942 7.9973 23.7708
REMARK 3 T TENSOR
REMARK 3 T11: 0.7520 T22: 0.9672
REMARK 3 T33: 0.5819 T12: 0.3007
REMARK 3 T13: -0.3735 T23: -0.3472
REMARK 3 L TENSOR
REMARK 3 L11: 3.6322 L22: 5.1737
REMARK 3 L33: 6.6233 L12: 4.3287
REMARK 3 L13: -4.9039 L23: -5.8453
REMARK 3 S TENSOR
REMARK 3 S11: -0.6202 S12: -1.4371 S13: 1.5846
REMARK 3 S21: 0.3965 S22: -0.2979 S23: 0.2090
REMARK 3 S31: -0.9115 S32: -0.2028 S33: 0.2589
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 54 THROUGH 62 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.0501 3.5225 11.4273
REMARK 3 T TENSOR
REMARK 3 T11: 0.3422 T22: 0.4047
REMARK 3 T33: 0.3912 T12: 0.0906
REMARK 3 T13: 0.0435 T23: 0.0564
REMARK 3 L TENSOR
REMARK 3 L11: 8.5344 L22: 6.0022
REMARK 3 L33: 7.3880 L12: -2.0958
REMARK 3 L13: -0.6305 L23: 4.1048
REMARK 3 S TENSOR
REMARK 3 S11: 0.0238 S12: 0.5948 S13: 0.1533
REMARK 3 S21: -0.5631 S22: -0.4159 S23: 0.6575
REMARK 3 S31: -1.1119 S32: -0.5385 S33: 0.2733
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 63 THROUGH 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.9169 -0.5507 18.0048
REMARK 3 T TENSOR
REMARK 3 T11: 0.1703 T22: 0.3021
REMARK 3 T33: 0.3937 T12: -0.0297
REMARK 3 T13: 0.0754 T23: -0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 5.9110 L22: 9.2009
REMARK 3 L33: 9.0948 L12: 1.1504
REMARK 3 L13: -0.4850 L23: -3.8247
REMARK 3 S TENSOR
REMARK 3 S11: 0.1627 S12: -0.2208 S13: -0.2809
REMARK 3 S21: 0.4556 S22: -0.6312 S23: 0.5008
REMARK 3 S31: 0.2427 S32: 0.8511 S33: 0.7336
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 78 THROUGH 86 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.5436 1.8538 13.5634
REMARK 3 T TENSOR
REMARK 3 T11: 0.2528 T22: 0.5182
REMARK 3 T33: 0.5320 T12: -0.0333
REMARK 3 T13: 0.0779 T23: -0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 6.6527 L22: 5.3764
REMARK 3 L33: 5.8030 L12: -0.1030
REMARK 3 L13: 4.0066 L23: 3.5222
REMARK 3 S TENSOR
REMARK 3 S11: -0.4190 S12: -0.2025 S13: 0.1246
REMARK 3 S21: 0.0578 S22: -0.5612 S23: 0.3086
REMARK 3 S31: -0.2941 S32: -0.6230 S33: 1.0245
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 4TT9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000202249.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE, AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13523
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 51.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.77000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: 1YAB, 1O9Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% (V/V) ISOPROPANOL, 0.1 M NA HEPES
REMARK 280 PH7.0, 10% (W/V) PEG 4000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 13.91000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8060 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 GLU A 208
REMARK 465 SER A 209
REMARK 465 GLU A 210
REMARK 465 HIS A 211
REMARK 465 THR A 212
REMARK 465 GLU A 213
REMARK 465 VAL A 214
REMARK 465 SER A 215
REMARK 465 LEU A 216
REMARK 465 ALA A 217
REMARK 465 LEU A 218
REMARK 465 PHE A 219
REMARK 465 ASN A 220
REMARK 465 VAL A 291
REMARK 465 LYS A 292
REMARK 465 GLU A 293
REMARK 465 GLU B 208
REMARK 465 SER B 209
REMARK 465 GLU B 210
REMARK 465 HIS B 211
REMARK 465 THR B 212
REMARK 465 GLU B 213
REMARK 465 VAL B 214
REMARK 465 SER B 215
REMARK 465 LEU B 216
REMARK 465 ALA B 217
REMARK 465 LEU B 218
REMARK 465 PHE B 219
REMARK 465 ASN B 220
REMARK 465 GLU B 293
REMARK 465 GLU C 208
REMARK 465 SER C 209
REMARK 465 GLU C 210
REMARK 465 HIS C 211
REMARK 465 THR C 212
REMARK 465 GLU C 213
REMARK 465 VAL C 214
REMARK 465 SER C 215
REMARK 465 LEU C 216
REMARK 465 ALA C 217
REMARK 465 LEU C 218
REMARK 465 PHE C 219
REMARK 465 LYS C 292
REMARK 465 GLU C 293
REMARK 465 GLU D 208
REMARK 465 SER D 209
REMARK 465 GLU D 210
REMARK 465 HIS D 211
REMARK 465 THR D 212
REMARK 465 GLU D 213
REMARK 465 VAL D 214
REMARK 465 SER D 215
REMARK 465 LEU D 216
REMARK 465 ALA D 217
REMARK 465 LEU D 218
REMARK 465 PHE D 219
REMARK 465 ASN D 220
REMARK 465 TYR D 221
REMARK 465 GLU D 279
REMARK 465 ASP D 280
REMARK 465 LYS D 292
REMARK 465 GLU D 293
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O LEU B 275 O HOH B 407 2.09
REMARK 500 OH TYR D 245 O2 EDO D 301 2.11
REMARK 500 OE1 GLU C 274 O HOH C 408 2.11
REMARK 500 O SER A 287 O HOH A 301 2.15
REMARK 500 OE1 GLU D 274 O HOH D 401 2.15
REMARK 500 OG SER B 287 O HOH B 408 2.17
REMARK 500 N ASN C 220 O HOH C 418 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 249 23.39 45.43
REMARK 500 PRO A 254 78.80 -69.91
REMARK 500 ASP A 255 -177.71 65.82
REMARK 500 ASP A 256 -35.80 76.73
REMARK 500 HIS A 260 60.86 -117.18
REMARK 500 VAL A 270 -71.98 -90.52
REMARK 500 ASP A 280 17.88 59.84
REMARK 500 ASN B 248 29.31 47.21
REMARK 500 ASP B 280 -4.80 61.69
REMARK 500 ASP C 255 -10.46 67.67
REMARK 500 ASP C 280 81.66 53.37
REMARK 500 TRP C 289 93.40 -163.77
REMARK 500 THR D 238 -161.77 -71.49
REMARK 500 ASN D 248 29.09 48.67
REMARK 500 ASN D 266 20.00 56.15
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 EDO B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 301
DBREF 4TT9 A 208 293 UNP P0A1K9 SPAO_SHIFL 208 293
DBREF 4TT9 B 208 293 UNP P0A1K9 SPAO_SHIFL 208 293
DBREF 4TT9 C 208 293 UNP P0A1K9 SPAO_SHIFL 208 293
DBREF 4TT9 D 208 293 UNP P0A1K9 SPAO_SHIFL 208 293
SEQRES 1 A 86 GLU SER GLU HIS THR GLU VAL SER LEU ALA LEU PHE ASN
SEQRES 2 A 86 TYR ASP ASP ILE ASN VAL LYS VAL ASP PHE ILE LEU LEU
SEQRES 3 A 86 GLU LYS ASN MET THR ILE ASN GLU LEU LYS MET TYR VAL
SEQRES 4 A 86 GLU ASN GLU LEU PHE LYS PHE PRO ASP ASP ILE VAL LYS
SEQRES 5 A 86 HIS VAL ASN ILE LYS VAL ASN GLY SER LEU VAL GLY HIS
SEQRES 6 A 86 GLY GLU LEU VAL SER ILE GLU ASP GLY TYR GLY ILE GLU
SEQRES 7 A 86 ILE SER SER TRP MET VAL LYS GLU
SEQRES 1 B 86 GLU SER GLU HIS THR GLU VAL SER LEU ALA LEU PHE ASN
SEQRES 2 B 86 TYR ASP ASP ILE ASN VAL LYS VAL ASP PHE ILE LEU LEU
SEQRES 3 B 86 GLU LYS ASN MET THR ILE ASN GLU LEU LYS MET TYR VAL
SEQRES 4 B 86 GLU ASN GLU LEU PHE LYS PHE PRO ASP ASP ILE VAL LYS
SEQRES 5 B 86 HIS VAL ASN ILE LYS VAL ASN GLY SER LEU VAL GLY HIS
SEQRES 6 B 86 GLY GLU LEU VAL SER ILE GLU ASP GLY TYR GLY ILE GLU
SEQRES 7 B 86 ILE SER SER TRP MET VAL LYS GLU
SEQRES 1 C 86 GLU SER GLU HIS THR GLU VAL SER LEU ALA LEU PHE ASN
SEQRES 2 C 86 TYR ASP ASP ILE ASN VAL LYS VAL ASP PHE ILE LEU LEU
SEQRES 3 C 86 GLU LYS ASN MET THR ILE ASN GLU LEU LYS MET TYR VAL
SEQRES 4 C 86 GLU ASN GLU LEU PHE LYS PHE PRO ASP ASP ILE VAL LYS
SEQRES 5 C 86 HIS VAL ASN ILE LYS VAL ASN GLY SER LEU VAL GLY HIS
SEQRES 6 C 86 GLY GLU LEU VAL SER ILE GLU ASP GLY TYR GLY ILE GLU
SEQRES 7 C 86 ILE SER SER TRP MET VAL LYS GLU
SEQRES 1 D 86 GLU SER GLU HIS THR GLU VAL SER LEU ALA LEU PHE ASN
SEQRES 2 D 86 TYR ASP ASP ILE ASN VAL LYS VAL ASP PHE ILE LEU LEU
SEQRES 3 D 86 GLU LYS ASN MET THR ILE ASN GLU LEU LYS MET TYR VAL
SEQRES 4 D 86 GLU ASN GLU LEU PHE LYS PHE PRO ASP ASP ILE VAL LYS
SEQRES 5 D 86 HIS VAL ASN ILE LYS VAL ASN GLY SER LEU VAL GLY HIS
SEQRES 6 D 86 GLY GLU LEU VAL SER ILE GLU ASP GLY TYR GLY ILE GLU
SEQRES 7 D 86 ILE SER SER TRP MET VAL LYS GLU
HET EDO B 301 4
HET EDO C 301 4
HET EDO C 302 4
HET EDO D 301 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 EDO 4(C2 H6 O2)
FORMUL 9 HOH *65(H2 O)
HELIX 1 AA1 ILE A 239 ASN A 248 1 10
HELIX 2 AA2 ILE B 239 MET B 244 1 6
HELIX 3 AA3 ILE C 239 ASN C 248 1 10
HELIX 4 AA4 ILE D 239 MET D 244 1 6
SHEET 1 AA110 LEU A 250 PHE A 253 0
SHEET 2 AA110 TYR B 282 TRP B 289 -1 O ILE B 284 N PHE A 251
SHEET 3 AA110 SER B 268 SER B 277 -1 N GLU B 274 O GLU B 285
SHEET 4 AA110 VAL B 261 VAL B 265 -1 N VAL B 261 O GLY B 273
SHEET 5 AA110 ASN B 225 THR B 238 -1 N ASP B 229 O LYS B 264
SHEET 6 AA110 ASN A 225 THR A 238 -1 N LEU A 233 O PHE B 230
SHEET 7 AA110 VAL A 261 VAL A 265 -1 O ASN A 262 N ILE A 231
SHEET 8 AA110 SER A 268 ILE A 278 -1 O SER A 268 N VAL A 265
SHEET 9 AA110 GLY A 281 SER A 288 -1 O GLY A 281 N ILE A 278
SHEET 10 AA110 LEU B 250 LYS B 252 -1 O PHE B 251 N ILE A 284
SHEET 1 AA210 LEU C 250 PHE C 253 0
SHEET 2 AA210 TYR D 282 TRP D 289 -1 O TYR D 282 N PHE C 253
SHEET 3 AA210 SER D 268 VAL D 276 -1 N VAL D 276 O GLY D 283
SHEET 4 AA210 VAL D 261 VAL D 265 -1 N VAL D 265 O SER D 268
SHEET 5 AA210 ASN D 225 MET D 237 -1 N ASP D 229 O LYS D 264
SHEET 6 AA210 VAL C 226 THR C 238 -1 N LEU C 232 O PHE D 230
SHEET 7 AA210 VAL C 261 VAL C 265 -1 O ASN C 262 N ILE C 231
SHEET 8 AA210 SER C 268 VAL C 276 -1 O VAL C 270 N ILE C 263
SHEET 9 AA210 GLY C 283 SER C 288 -1 O GLU C 285 N GLU C 274
SHEET 10 AA210 LEU D 250 LYS D 252 -1 O PHE D 251 N ILE C 284
SITE 1 AC1 5 PHE A 230 LYS B 235 TYR B 245 PHE B 251
SITE 2 AC1 5 PHE B 253
SITE 1 AC2 2 TYR C 282 LEU D 275
SITE 1 AC3 3 LYS A 252 ILE B 278 GLU C 279
SITE 1 AC4 5 PHE C 230 LYS D 235 TYR D 245 PHE D 251
SITE 2 AC4 5 PHE D 253
CRYST1 51.300 27.820 104.440 90.00 90.03 90.00 P 1 21 1 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 0.019493 0.000000 0.000010 0.00000
SCALE2 0.000000 0.035945 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009575 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
