| content |
HEADER HYDROLASE 31-MAR-20 6WCX
TITLE FPHF, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
TITLE 2 HYDROLASES F, SUBSTRATE BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE FAMILY PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: PUTATIVE ESTERASE,TRIBUTYRIN ESTERASE;
COMPND 5 EC: 3.1.2.12;
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: EP54_00010, EQ90_02595, HMPREF3211_01237, NCTC10654_02801,
SOURCE 5 NCTC10702_04070, RK64_00235;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: M1366
KEYWDS FPHF, FLUOROPHOSPHONATE-BINDING, SERINE HYDROLASES, HEPTANOATE,
KEYWDS 2 HEPTAN-1-OL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER,P.D.MACE
REVDAT 1 16-SEP-20 6WCX 0
JRNL AUTH M.FELLNER,C.S.LENTZ,S.A.JAMIESON,J.L.BREWSTER,L.CHEN,
JRNL AUTH 2 M.BOGYO,P.D.MACE
JRNL TITL STRUCTURAL BASIS FOR THE INHIBITOR AND SUBSTRATE SPECIFICITY
JRNL TITL 2 OF THE UNIQUE FPH SERINE HYDROLASES OF STAPHYLOCOCCUS
JRNL TITL 3 AUREUS.
JRNL REF ACS INFECT DIS. 2020
JRNL REFN ESSN 2373-8227
JRNL PMID 32865965
JRNL DOI 10.1021/ACSINFECDIS.0C00503
REMARK 2
REMARK 2 RESOLUTION. 2.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18RC1-3769
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) : 2.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.19
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.920
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 23797
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 2067
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 49.1900 - 7.1300 0.99 2704 131 0.2634 0.3178
REMARK 3 2 7.1300 - 5.6600 1.00 2707 159 0.2247 0.2408
REMARK 3 3 5.6600 - 4.9500 1.00 2734 141 0.1818 0.2057
REMARK 3 4 4.9500 - 4.5000 0.99 2713 125 0.1684 0.2254
REMARK 3 5 4.4900 - 4.1700 0.99 2648 151 0.1630 0.1839
REMARK 3 6 4.1700 - 3.9300 0.98 2678 157 0.1896 0.2077
REMARK 3 7 3.9300 - 3.7300 0.99 2711 133 0.2027 0.2642
REMARK 3 8 3.7300 - 3.5700 0.98 2673 144 0.2154 0.2510
REMARK 3 9 3.5700 - 3.4300 0.96 2616 121 0.2218 0.3322
REMARK 3 10 3.4300 - 3.3100 0.97 2631 138 0.2533 0.2820
REMARK 3 11 3.3100 - 3.2100 0.96 2580 130 0.2706 0.3006
REMARK 3 12 3.2100 - 3.1200 0.96 2572 164 0.2927 0.3119
REMARK 3 13 3.1200 - 3.0400 0.95 2620 139 0.2976 0.3483
REMARK 3 14 3.0400 - 2.9600 0.95 2608 117 0.2990 0.3186
REMARK 3 15 2.9600 - 2.8900 0.90 2397 117 0.3048 0.2716
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.830
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.95
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 19
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID -1 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.5093 33.5248 -11.7112
REMARK 3 T TENSOR
REMARK 3 T11: 0.2915 T22: 0.3706
REMARK 3 T33: 0.4584 T12: 0.1166
REMARK 3 T13: 0.0386 T23: 0.0610
REMARK 3 L TENSOR
REMARK 3 L11: 0.5520 L22: 0.4274
REMARK 3 L33: 1.3715 L12: 0.4651
REMARK 3 L13: 0.4292 L23: 0.1461
REMARK 3 S TENSOR
REMARK 3 S11: -0.0583 S12: -0.0986 S13: 0.0045
REMARK 3 S21: -0.0775 S22: 0.0006 S23: -0.1582
REMARK 3 S31: 0.1276 S32: 0.1486 S33: 0.0464
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 25 THROUGH 39 )
REMARK 3 ORIGIN FOR THE GROUP (A): -44.5666 23.3170 -28.1503
REMARK 3 T TENSOR
REMARK 3 T11: 0.8051 T22: 0.3674
REMARK 3 T33: 0.5517 T12: 0.0223
REMARK 3 T13: 0.2069 T23: 0.1114
REMARK 3 L TENSOR
REMARK 3 L11: 0.5831 L22: 1.9194
REMARK 3 L33: 4.0935 L12: -0.4905
REMARK 3 L13: 0.6344 L23: -2.7988
REMARK 3 S TENSOR
REMARK 3 S11: -0.0571 S12: -0.2276 S13: -0.4941
REMARK 3 S21: -0.0242 S22: -0.0143 S23: -0.0954
REMARK 3 S31: 0.6286 S32: -0.1802 S33: 0.0648
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 40 THROUGH 68 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.9556 23.8965 -13.0050
REMARK 3 T TENSOR
REMARK 3 T11: 0.5133 T22: 0.4617
REMARK 3 T33: 0.4220 T12: 0.2635
REMARK 3 T13: 0.0938 T23: 0.1904
REMARK 3 L TENSOR
REMARK 3 L11: 0.6409 L22: 0.8081
REMARK 3 L33: 1.1287 L12: -0.2302
REMARK 3 L13: 0.2049 L23: 0.3033
REMARK 3 S TENSOR
REMARK 3 S11: -0.0288 S12: 0.0455 S13: -0.0761
REMARK 3 S21: 0.1191 S22: 0.0809 S23: -0.0399
REMARK 3 S31: 0.6239 S32: 0.4690 S33: -0.0576
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 69 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): -36.6169 24.4213 -4.1004
REMARK 3 T TENSOR
REMARK 3 T11: 0.3661 T22: 0.3317
REMARK 3 T33: 0.2806 T12: 0.0077
REMARK 3 T13: 0.0274 T23: 0.0982
REMARK 3 L TENSOR
REMARK 3 L11: 0.8358 L22: 0.8997
REMARK 3 L33: 2.1741 L12: 0.3278
REMARK 3 L13: 0.4461 L23: 0.2734
REMARK 3 S TENSOR
REMARK 3 S11: 0.1232 S12: -0.1073 S13: -0.0920
REMARK 3 S21: 0.2442 S22: -0.0866 S23: 0.1369
REMARK 3 S31: 0.5135 S32: -0.0276 S33: -0.0394
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 134 THROUGH 162 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.0588 20.7696 3.8653
REMARK 3 T TENSOR
REMARK 3 T11: 0.4276 T22: 0.5488
REMARK 3 T33: 0.3355 T12: 0.0719
REMARK 3 T13: 0.0258 T23: 0.1506
REMARK 3 L TENSOR
REMARK 3 L11: 1.7376 L22: 2.0470
REMARK 3 L33: 1.5716 L12: -0.2551
REMARK 3 L13: 0.6805 L23: 0.8569
REMARK 3 S TENSOR
REMARK 3 S11: 0.1367 S12: -0.2055 S13: 0.0614
REMARK 3 S21: 0.0786 S22: -0.0008 S23: -0.3239
REMARK 3 S31: 0.6407 S32: 0.3344 S33: -0.1222
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 163 THROUGH 179 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.4212 24.0790 15.1443
REMARK 3 T TENSOR
REMARK 3 T11: 0.5964 T22: 0.5500
REMARK 3 T33: 0.3637 T12: -0.0896
REMARK 3 T13: -0.0897 T23: 0.0690
REMARK 3 L TENSOR
REMARK 3 L11: 3.0215 L22: 6.5933
REMARK 3 L33: 3.3999 L12: 2.8223
REMARK 3 L13: -3.1625 L23: -3.5437
REMARK 3 S TENSOR
REMARK 3 S11: -0.1571 S12: -0.5054 S13: -0.1010
REMARK 3 S21: 0.6514 S22: -0.0929 S23: -0.3032
REMARK 3 S31: 0.0801 S32: 0.1508 S33: 0.2351
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 180 THROUGH 221 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.2539 9.1892 4.2218
REMARK 3 T TENSOR
REMARK 3 T11: 0.7041 T22: 0.3750
REMARK 3 T33: 0.3897 T12: 0.0736
REMARK 3 T13: -0.0049 T23: 0.1180
REMARK 3 L TENSOR
REMARK 3 L11: 1.8922 L22: 2.2620
REMARK 3 L33: 2.8931 L12: -0.1350
REMARK 3 L13: -0.7343 L23: 0.0388
REMARK 3 S TENSOR
REMARK 3 S11: -0.2822 S12: -0.4864 S13: -0.5375
REMARK 3 S21: 0.2411 S22: -0.0532 S23: -0.2626
REMARK 3 S31: 1.0824 S32: 0.1938 S33: 0.3286
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 222 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.2734 11.4039 -8.7213
REMARK 3 T TENSOR
REMARK 3 T11: 0.5067 T22: 0.3683
REMARK 3 T33: 0.3896 T12: 0.0781
REMARK 3 T13: -0.0092 T23: 0.0718
REMARK 3 L TENSOR
REMARK 3 L11: 1.8544 L22: 2.5106
REMARK 3 L33: 1.9875 L12: 0.6434
REMARK 3 L13: -0.0526 L23: -1.0004
REMARK 3 S TENSOR
REMARK 3 S11: 0.2895 S12: -0.0297 S13: -0.5726
REMARK 3 S21: 0.2214 S22: -0.1771 S23: -0.3154
REMARK 3 S31: 0.5919 S32: 0.3890 S33: -0.0878
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID -1 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.7660 48.5130 -15.0326
REMARK 3 T TENSOR
REMARK 3 T11: 0.2017 T22: 0.4784
REMARK 3 T33: 0.3664 T12: 0.0029
REMARK 3 T13: -0.0046 T23: 0.0430
REMARK 3 L TENSOR
REMARK 3 L11: 1.7649 L22: 2.6081
REMARK 3 L33: 2.7609 L12: 0.2513
REMARK 3 L13: -0.8090 L23: 0.1600
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: 0.3021 S13: -0.2464
REMARK 3 S21: -0.3023 S22: -0.0990 S23: -0.6058
REMARK 3 S31: -0.3098 S32: 0.4585 S33: 0.1003
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 41 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.7618 51.5733 -4.1949
REMARK 3 T TENSOR
REMARK 3 T11: 0.1879 T22: 0.3591
REMARK 3 T33: 0.2771 T12: -0.0453
REMARK 3 T13: -0.0193 T23: 0.0449
REMARK 3 L TENSOR
REMARK 3 L11: 1.1229 L22: 1.1050
REMARK 3 L33: 3.5584 L12: -0.3386
REMARK 3 L13: 0.3529 L23: -0.4096
REMARK 3 S TENSOR
REMARK 3 S11: 0.0280 S12: -0.0575 S13: -0.0809
REMARK 3 S21: 0.0473 S22: -0.1060 S23: -0.1483
REMARK 3 S31: -0.4500 S32: 0.5755 S33: 0.0421
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 134 THROUGH 189 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.9827 53.4287 11.0280
REMARK 3 T TENSOR
REMARK 3 T11: 0.2608 T22: 0.3457
REMARK 3 T33: 0.2464 T12: 0.0333
REMARK 3 T13: 0.0650 T23: 0.0376
REMARK 3 L TENSOR
REMARK 3 L11: 0.8016 L22: 2.6623
REMARK 3 L33: 2.1107 L12: 0.1048
REMARK 3 L13: 1.2859 L23: 0.6153
REMARK 3 S TENSOR
REMARK 3 S11: 0.0737 S12: -0.1243 S13: 0.0561
REMARK 3 S21: 0.1730 S22: 0.1190 S23: 0.1190
REMARK 3 S31: 0.1101 S32: -0.2523 S33: -0.1878
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 190 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.9460 65.2553 1.4560
REMARK 3 T TENSOR
REMARK 3 T11: 0.5519 T22: 0.3674
REMARK 3 T33: 0.3787 T12: 0.0774
REMARK 3 T13: 0.0290 T23: -0.0309
REMARK 3 L TENSOR
REMARK 3 L11: 2.4388 L22: 2.4824
REMARK 3 L33: 4.2635 L12: 0.1430
REMARK 3 L13: 1.1614 L23: 1.1564
REMARK 3 S TENSOR
REMARK 3 S11: -0.0537 S12: -0.3603 S13: 0.4383
REMARK 3 S21: 0.2391 S22: -0.1177 S23: 0.1507
REMARK 3 S31: -0.9164 S32: -0.4961 S33: 0.1843
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID -1 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.6378 43.0879 -17.1989
REMARK 3 T TENSOR
REMARK 3 T11: 0.2249 T22: 0.7009
REMARK 3 T33: 0.4555 T12: 0.0606
REMARK 3 T13: -0.0120 T23: -0.0526
REMARK 3 L TENSOR
REMARK 3 L11: 1.6675 L22: 0.7021
REMARK 3 L33: 1.1777 L12: 0.7023
REMARK 3 L13: -0.4407 L23: 0.0756
REMARK 3 S TENSOR
REMARK 3 S11: 0.1353 S12: -0.5211 S13: -0.0450
REMARK 3 S21: 0.2600 S22: 0.0070 S23: -0.0119
REMARK 3 S31: -0.0841 S32: 0.5732 S33: -0.1044
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 41 THROUGH 146 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1890 35.9850 -29.1858
REMARK 3 T TENSOR
REMARK 3 T11: 0.0471 T22: 0.9816
REMARK 3 T33: 0.3736 T12: 0.2851
REMARK 3 T13: 0.0646 T23: 0.0500
REMARK 3 L TENSOR
REMARK 3 L11: 0.5226 L22: 0.1181
REMARK 3 L33: 0.5575 L12: -0.0957
REMARK 3 L13: 0.0350 L23: 0.1090
REMARK 3 S TENSOR
REMARK 3 S11: 0.0493 S12: -0.1501 S13: 0.0036
REMARK 3 S21: -0.0121 S22: 0.2094 S23: -0.1068
REMARK 3 S31: -0.0791 S32: 0.7368 S33: -0.1633
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 147 THROUGH 189 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.8637 31.8343 -47.6272
REMARK 3 T TENSOR
REMARK 3 T11: 0.3487 T22: 0.9529
REMARK 3 T33: 0.3934 T12: 0.1659
REMARK 3 T13: 0.0363 T23: 0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 6.9571 L22: 1.5285
REMARK 3 L33: 0.4198 L12: -2.3312
REMARK 3 L13: 1.3146 L23: -0.0878
REMARK 3 S TENSOR
REMARK 3 S11: 0.0860 S12: 0.1241 S13: -0.5622
REMARK 3 S21: -0.1225 S22: -0.2054 S23: 0.1818
REMARK 3 S31: 0.2716 S32: 1.2468 S33: 0.1338
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 190 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4785 22.4216 -34.1816
REMARK 3 T TENSOR
REMARK 3 T11: 0.4357 T22: 0.8855
REMARK 3 T33: 0.3801 T12: 0.3198
REMARK 3 T13: 0.0031 T23: -0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 1.7592 L22: 0.8655
REMARK 3 L33: 1.4464 L12: 0.1348
REMARK 3 L13: -1.0298 L23: -0.0728
REMARK 3 S TENSOR
REMARK 3 S11: -0.1008 S12: -0.1189 S13: -0.2566
REMARK 3 S21: 0.1636 S22: 0.1423 S23: -0.1345
REMARK 3 S31: 0.0775 S32: 0.0391 S33: -0.0649
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID -1 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.3163 40.9300 -26.8270
REMARK 3 T TENSOR
REMARK 3 T11: 0.2360 T22: 0.4596
REMARK 3 T33: 0.4050 T12: 0.1221
REMARK 3 T13: -0.0071 T23: 0.0560
REMARK 3 L TENSOR
REMARK 3 L11: 0.1335 L22: 0.4457
REMARK 3 L33: 0.8253 L12: 0.1633
REMARK 3 L13: 0.0851 L23: -0.2263
REMARK 3 S TENSOR
REMARK 3 S11: -0.0297 S12: 0.0413 S13: -0.0173
REMARK 3 S21: 0.0867 S22: 0.0027 S23: -0.0784
REMARK 3 S31: 0.0348 S32: 0.0115 S33: 0.0190
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 134 THROUGH 189 )
REMARK 3 ORIGIN FOR THE GROUP (A): -40.0684 50.1260 -44.4771
REMARK 3 T TENSOR
REMARK 3 T11: 0.3650 T22: 0.3765
REMARK 3 T33: 0.3652 T12: 0.1381
REMARK 3 T13: 0.0702 T23: 0.0993
REMARK 3 L TENSOR
REMARK 3 L11: 2.7082 L22: 1.2967
REMARK 3 L33: 1.6709 L12: -0.4757
REMARK 3 L13: 1.0945 L23: 0.3009
REMARK 3 S TENSOR
REMARK 3 S11: -0.0651 S12: 0.1752 S13: 0.2565
REMARK 3 S21: -0.1576 S22: -0.0978 S23: -0.0156
REMARK 3 S31: -0.3685 S32: -0.2702 S33: 0.1502
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 190 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.6283 57.9522 -33.8507
REMARK 3 T TENSOR
REMARK 3 T11: 0.4705 T22: 0.5118
REMARK 3 T33: 0.4557 T12: 0.1982
REMARK 3 T13: -0.0467 T23: 0.0861
REMARK 3 L TENSOR
REMARK 3 L11: 1.6502 L22: 0.6967
REMARK 3 L33: 1.7082 L12: 0.0995
REMARK 3 L13: 1.0748 L23: 0.2090
REMARK 3 S TENSOR
REMARK 3 S11: -0.1340 S12: 0.1665 S13: 0.2370
REMARK 3 S21: -0.1575 S22: 0.0974 S23: 0.2307
REMARK 3 S31: -0.4678 S32: -0.3362 S33: 0.0583
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID -1 THROUGH 42 OR
REMARK 3 RESID 44 THROUGH 55 OR RESID 57 THROUGH
REMARK 3 110 OR (RESID 111 AND (NAME N OR NAME CA
REMARK 3 OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 112 THROUGH 156 OR (RESID 157 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 158 THROUGH 173 OR
REMARK 3 (RESID 174 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 175
REMARK 3 THROUGH 176 OR (RESID 177 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 178 THROUGH 185 OR (RESID 186
REMARK 3 THROUGH 187 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 188 THROUGH 190 OR (RESID 191 THROUGH 192
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 193 THROUGH 199
REMARK 3 OR RESID 201 THROUGH 202 OR (RESID 203
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 204 THROUGH 205
REMARK 3 OR RESID 207 THROUGH 232 OR (RESID 233
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 234 THROUGH 240
REMARK 3 OR (RESID 241 THROUGH 242 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 243 THROUGH 251 OR (RESID 252
REMARK 3 THROUGH 253 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 301))
REMARK 3 SELECTION : (CHAIN B AND (RESID -1 THROUGH 26 OR
REMARK 3 (RESID 27 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 28
REMARK 3 THROUGH 36 OR (RESID 37 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 38 THROUGH 42 OR RESID 44
REMARK 3 THROUGH 55 OR RESID 57 THROUGH 110 OR
REMARK 3 (RESID 111 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 112
REMARK 3 THROUGH 156 OR (RESID 157 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 158 THROUGH 173 OR (RESID 174
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 175 THROUGH 176
REMARK 3 OR (RESID 177 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 178 THROUGH 185 OR (RESID 186 THROUGH 187
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 188 THROUGH 190
REMARK 3 OR (RESID 191 THROUGH 192 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 193 THROUGH 199 OR RESID 201
REMARK 3 THROUGH 202 OR (RESID 203 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 204 THROUGH 205 OR RESID 207
REMARK 3 THROUGH 215 OR (RESID 216 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 217 THROUGH 227 OR (RESID 228
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 229 THROUGH 232
REMARK 3 OR (RESID 233 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 234 THROUGH 301))
REMARK 3 ATOM PAIRS NUMBER : 4548
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID -1 THROUGH 42 OR
REMARK 3 RESID 44 THROUGH 55 OR RESID 57 THROUGH
REMARK 3 110 OR (RESID 111 AND (NAME N OR NAME CA
REMARK 3 OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 112 THROUGH 156 OR (RESID 157 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 158 THROUGH 173 OR
REMARK 3 (RESID 174 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 175
REMARK 3 THROUGH 176 OR (RESID 177 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 178 THROUGH 185 OR (RESID 186
REMARK 3 THROUGH 187 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 188 THROUGH 190 OR (RESID 191 THROUGH 192
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 193 THROUGH 199
REMARK 3 OR RESID 201 THROUGH 202 OR (RESID 203
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 204 THROUGH 205
REMARK 3 OR RESID 207 THROUGH 232 OR (RESID 233
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 234 THROUGH 240
REMARK 3 OR (RESID 241 THROUGH 242 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 243 THROUGH 251 OR (RESID 252
REMARK 3 THROUGH 253 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 301))
REMARK 3 SELECTION : (CHAIN C AND (RESID -1 THROUGH 26 OR
REMARK 3 (RESID 27 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 28
REMARK 3 THROUGH 36 OR (RESID 37 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 38 THROUGH 42 OR RESID 44
REMARK 3 THROUGH 55 OR RESID 57 THROUGH 168 OR
REMARK 3 (RESID 169 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 170
REMARK 3 THROUGH 173 OR (RESID 174 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 175 THROUGH 185 OR (RESID 186
REMARK 3 THROUGH 187 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 188 THROUGH 191 OR (RESID 192 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 193 THROUGH 199 OR RESID 201
REMARK 3 THROUGH 205 OR RESID 207 THROUGH 215 OR
REMARK 3 (RESID 216 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 217
REMARK 3 THROUGH 232 OR (RESID 233 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 234 THROUGH 240 OR (RESID 241
REMARK 3 THROUGH 242 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 243 THROUGH 251 OR (RESID 252 THROUGH 253
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 301))
REMARK 3 ATOM PAIRS NUMBER : 4548
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID -1 THROUGH 42 OR
REMARK 3 RESID 44 THROUGH 55 OR RESID 57 THROUGH
REMARK 3 110 OR (RESID 111 AND (NAME N OR NAME CA
REMARK 3 OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 112 THROUGH 156 OR (RESID 157 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 158 THROUGH 173 OR
REMARK 3 (RESID 174 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 175
REMARK 3 THROUGH 176 OR (RESID 177 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 178 THROUGH 185 OR (RESID 186
REMARK 3 THROUGH 187 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 188 THROUGH 190 OR (RESID 191 THROUGH 192
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 193 THROUGH 199
REMARK 3 OR RESID 201 THROUGH 202 OR (RESID 203
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 204 THROUGH 205
REMARK 3 OR RESID 207 THROUGH 232 OR (RESID 233
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 234 THROUGH 240
REMARK 3 OR (RESID 241 THROUGH 242 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 243 THROUGH 251 OR (RESID 252
REMARK 3 THROUGH 253 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 301))
REMARK 3 SELECTION : (CHAIN D AND (RESID -1 THROUGH 26 OR
REMARK 3 (RESID 27 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 28
REMARK 3 THROUGH 42 OR RESID 44 THROUGH 55 OR
REMARK 3 RESID 57 THROUGH 110 OR (RESID 111 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 112 THROUGH 156 OR
REMARK 3 (RESID 157 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 158
REMARK 3 THROUGH 168 OR (RESID 169 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 170 THROUGH 190 OR (RESID 191
REMARK 3 THROUGH 192 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 193 THROUGH 199 OR RESID 201 THROUGH 202
REMARK 3 OR (RESID 203 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 204 THROUGH 205 OR RESID 207 THROUGH 215
REMARK 3 OR (RESID 216 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 217 THROUGH 227 OR (RESID 228 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 229 THROUGH 251 OR (RESID 252
REMARK 3 THROUGH 253 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 301))
REMARK 3 ATOM PAIRS NUMBER : 4548
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6WCX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-APR-20.
REMARK 100 THE DEPOSITION ID IS D_1000248052.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAR-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.954
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23922
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.890
REMARK 200 RESOLUTION RANGE LOW (A) : 49.190
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 9.100
REMARK 200 R MERGE (I) : 0.22300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 1.13700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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 2.8.3
REMARK 200 STARTING MODEL: 6VH9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4 UL ~8.0 MG/ML FPHF (10 MM HEPES PH
REMARK 280 7.5, 10 MM NACL) WERE MIXED WITH 0.07 UL LIGAND SOLUTION (~0.5
REMARK 280 MM 4-METHYLUMBELLIFERYL HEPTANOATE IN 100% DMSO) AND 0.4 UL OF
REMARK 280 RESERVOIR SOLUTION. SITTING DROP RESERVOIR CONTAINED 50 UL OF
REMARK 280 0.8 M SODIUM FORMATE, 0.1 M TRIS PH 7.5, 10 % W/V PEG 8000 AND
REMARK 280 10 % W/V PEG 1000. CRYSTALS WERE SOAKED FOR ~15 SECONDS IN 75%
REMARK 280 RESERVOIR SOLUTION AND 25% GLYCEROL PRIOR TO FREEZING IN LIQUID
REMARK 280 NITROGEN, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 151.57067
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 303.14133
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 227.35600
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 378.92667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 75.78533
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 151.57067
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 303.14133
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 378.92667
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 227.35600
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 75.78533
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: 2990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
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: 3150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 404 LIES ON A SPECIAL POSITION.
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 GLN A 27 CG CD OE1 NE2
REMARK 470 LYS A 37 CG CD CE NZ
REMARK 470 ASN A 169 CG OD1 ND2
REMARK 470 LYS A 192 CG CD CE NZ
REMARK 470 ASP A 216 CG OD1 OD2
REMARK 470 GLU A 228 CG CD OE1 OE2
REMARK 470 ASP A 253 CG OD1 OD2
REMARK 470 ASN B 169 CG OD1 ND2
REMARK 470 GLN B 241 CG CD OE1 NE2
REMARK 470 ASN B 252 CG OD1 ND2
REMARK 470 ASP B 253 CG OD1 OD2
REMARK 470 LYS C 111 CG CD CE NZ
REMARK 470 GLU C 157 CG CD OE1 OE2
REMARK 470 GLU C 177 CG CD OE1 OE2
REMARK 470 ASP C 191 CG OD1 OD2
REMARK 470 LYS C 203 CG CD CE NZ
REMARK 470 GLU C 228 CG CD OE1 OE2
REMARK 470 LYS D 37 CG CD CE NZ
REMARK 470 LYS D 174 CG CD CE NZ
REMARK 470 GLU D 177 CG CD OE1 OE2
REMARK 470 LYS D 186 CG CD CE NZ
REMARK 470 ASP D 233 CG OD1 OD2
REMARK 470 GLN D 241 CG CD OE1 NE2
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 OG SER D 121 OAB HE4 D 301 2.08
REMARK 500 OG SER C 121 OAB HE4 C 301 2.12
REMARK 500 OG SER A 121 OAB HE4 A 301 2.12
REMARK 500 OG SER D 121 CAF HE4 D 301 2.17
REMARK 500 OG SER B 121 OAB HE4 B 301 2.19
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 SER A 49 -6.15 81.73
REMARK 500 ASP A 51 -157.06 -153.80
REMARK 500 SER A 60 57.87 -117.63
REMARK 500 ASP A 78 -129.67 62.97
REMARK 500 SER A 121 -106.67 55.63
REMARK 500 ASP A 229 -158.60 -119.82
REMARK 500 SER B 49 -14.27 81.72
REMARK 500 ASP B 51 -159.81 -153.80
REMARK 500 SER B 60 60.93 -117.86
REMARK 500 ASP B 78 -128.26 64.04
REMARK 500 SER B 121 -106.79 54.86
REMARK 500 ASP B 229 -156.19 -117.49
REMARK 500 SER C 49 -5.17 78.86
REMARK 500 ASP C 51 -158.78 -152.24
REMARK 500 SER C 60 50.28 -113.96
REMARK 500 ASP C 78 -131.39 63.96
REMARK 500 SER C 121 -110.57 53.51
REMARK 500 ASP C 229 -153.41 -110.18
REMARK 500 ASP C 233 -166.67 -123.09
REMARK 500 SER D 49 -6.37 77.95
REMARK 500 ASP D 51 -157.50 -150.77
REMARK 500 SER D 60 54.51 -113.68
REMARK 500 ASP D 78 -133.43 63.19
REMARK 500 SER D 121 -110.53 53.45
REMARK 500 ASP D 229 -153.94 -111.46
REMARK 500 ASP D 233 -166.30 -122.38
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 HE4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HE4 B 301 and SER B
REMARK 800 121
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HE4 C 301 and SER C
REMARK 800 121
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HE4 D 301 and SER D
REMARK 800 121
DBREF1 6WCX A 2 253 UNP A0A0D6GS23_STAAU
DBREF2 6WCX A A0A0D6GS23 2 253
DBREF1 6WCX B 2 253 UNP A0A0D6GS23_STAAU
DBREF2 6WCX B A0A0D6GS23 2 253
DBREF1 6WCX C 2 253 UNP A0A0D6GS23_STAAU
DBREF2 6WCX C A0A0D6GS23 2 253
DBREF1 6WCX D 2 253 UNP A0A0D6GS23_STAAU
DBREF2 6WCX D A0A0D6GS23 2 253
SEQADV 6WCX GLY A -1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6WCX PRO A 0 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6WCX GLY A 1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6WCX GLY B -1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6WCX PRO B 0 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6WCX GLY B 1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6WCX GLY C -1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6WCX PRO C 0 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6WCX GLY C 1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6WCX GLY D -1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6WCX PRO D 0 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6WCX GLY D 1 UNP A0A0D6GS2 EXPRESSION TAG
SEQRES 1 A 255 GLY PRO GLY ALA TYR ILE SER LEU ASN TYR HIS SER PRO
SEQRES 2 A 255 THR ILE GLY MET HIS GLN ASN LEU THR VAL ILE LEU PRO
SEQRES 3 A 255 GLU ASP GLN SER PHE PHE ASN SER ASP THR THR VAL LYS
SEQRES 4 A 255 PRO LEU LYS THR LEU MET LEU LEU HIS GLY LEU SER SER
SEQRES 5 A 255 ASP GLU THR THR TYR MET ARG TYR THR SER ILE GLU ARG
SEQRES 6 A 255 TYR ALA ASN GLU HIS LYS LEU ALA VAL ILE MET PRO ASN
SEQRES 7 A 255 VAL ASP HIS SER ALA TYR ALA ASN MET ALA TYR GLY HIS
SEQRES 8 A 255 SER TYR TYR ASP TYR ILE LEU GLU VAL TYR ASP TYR VAL
SEQRES 9 A 255 HIS GLN ILE PHE PRO LEU SER LYS LYS ARG ASP ASP ASN
SEQRES 10 A 255 PHE ILE ALA GLY HIS SER MET GLY GLY TYR GLY THR ILE
SEQRES 11 A 255 LYS PHE ALA LEU THR GLN GLY ASP LYS PHE ALA LYS ALA
SEQRES 12 A 255 VAL PRO LEU SER ALA VAL PHE GLU ALA GLN ASN LEU MET
SEQRES 13 A 255 ASP LEU GLU TRP ASN ASP PHE SER LYS GLU ALA ILE ILE
SEQRES 14 A 255 GLY ASN LEU SER SER VAL LYS GLY THR GLU HIS ASP PRO
SEQRES 15 A 255 TYR TYR LEU LEU ASP LYS ALA VAL ALA GLU ASP LYS GLN
SEQRES 16 A 255 ILE PRO LYS LEU LEU ILE MET CYS GLY LYS GLN ASP PHE
SEQRES 17 A 255 LEU TYR GLN ASP ASN LEU ASP PHE ILE ASP TYR LEU SER
SEQRES 18 A 255 ARG ILE ASN VAL PRO TYR GLN PHE GLU ASP GLY PRO GLY
SEQRES 19 A 255 ASP HIS ASP TYR ALA TYR TRP ASP GLN ALA ILE LYS ARG
SEQRES 20 A 255 ALA ILE THR TRP MET VAL ASN ASP
SEQRES 1 B 255 GLY PRO GLY ALA TYR ILE SER LEU ASN TYR HIS SER PRO
SEQRES 2 B 255 THR ILE GLY MET HIS GLN ASN LEU THR VAL ILE LEU PRO
SEQRES 3 B 255 GLU ASP GLN SER PHE PHE ASN SER ASP THR THR VAL LYS
SEQRES 4 B 255 PRO LEU LYS THR LEU MET LEU LEU HIS GLY LEU SER SER
SEQRES 5 B 255 ASP GLU THR THR TYR MET ARG TYR THR SER ILE GLU ARG
SEQRES 6 B 255 TYR ALA ASN GLU HIS LYS LEU ALA VAL ILE MET PRO ASN
SEQRES 7 B 255 VAL ASP HIS SER ALA TYR ALA ASN MET ALA TYR GLY HIS
SEQRES 8 B 255 SER TYR TYR ASP TYR ILE LEU GLU VAL TYR ASP TYR VAL
SEQRES 9 B 255 HIS GLN ILE PHE PRO LEU SER LYS LYS ARG ASP ASP ASN
SEQRES 10 B 255 PHE ILE ALA GLY HIS SER MET GLY GLY TYR GLY THR ILE
SEQRES 11 B 255 LYS PHE ALA LEU THR GLN GLY ASP LYS PHE ALA LYS ALA
SEQRES 12 B 255 VAL PRO LEU SER ALA VAL PHE GLU ALA GLN ASN LEU MET
SEQRES 13 B 255 ASP LEU GLU TRP ASN ASP PHE SER LYS GLU ALA ILE ILE
SEQRES 14 B 255 GLY ASN LEU SER SER VAL LYS GLY THR GLU HIS ASP PRO
SEQRES 15 B 255 TYR TYR LEU LEU ASP LYS ALA VAL ALA GLU ASP LYS GLN
SEQRES 16 B 255 ILE PRO LYS LEU LEU ILE MET CYS GLY LYS GLN ASP PHE
SEQRES 17 B 255 LEU TYR GLN ASP ASN LEU ASP PHE ILE ASP TYR LEU SER
SEQRES 18 B 255 ARG ILE ASN VAL PRO TYR GLN PHE GLU ASP GLY PRO GLY
SEQRES 19 B 255 ASP HIS ASP TYR ALA TYR TRP ASP GLN ALA ILE LYS ARG
SEQRES 20 B 255 ALA ILE THR TRP MET VAL ASN ASP
SEQRES 1 C 255 GLY PRO GLY ALA TYR ILE SER LEU ASN TYR HIS SER PRO
SEQRES 2 C 255 THR ILE GLY MET HIS GLN ASN LEU THR VAL ILE LEU PRO
SEQRES 3 C 255 GLU ASP GLN SER PHE PHE ASN SER ASP THR THR VAL LYS
SEQRES 4 C 255 PRO LEU LYS THR LEU MET LEU LEU HIS GLY LEU SER SER
SEQRES 5 C 255 ASP GLU THR THR TYR MET ARG TYR THR SER ILE GLU ARG
SEQRES 6 C 255 TYR ALA ASN GLU HIS LYS LEU ALA VAL ILE MET PRO ASN
SEQRES 7 C 255 VAL ASP HIS SER ALA TYR ALA ASN MET ALA TYR GLY HIS
SEQRES 8 C 255 SER TYR TYR ASP TYR ILE LEU GLU VAL TYR ASP TYR VAL
SEQRES 9 C 255 HIS GLN ILE PHE PRO LEU SER LYS LYS ARG ASP ASP ASN
SEQRES 10 C 255 PHE ILE ALA GLY HIS SER MET GLY GLY TYR GLY THR ILE
SEQRES 11 C 255 LYS PHE ALA LEU THR GLN GLY ASP LYS PHE ALA LYS ALA
SEQRES 12 C 255 VAL PRO LEU SER ALA VAL PHE GLU ALA GLN ASN LEU MET
SEQRES 13 C 255 ASP LEU GLU TRP ASN ASP PHE SER LYS GLU ALA ILE ILE
SEQRES 14 C 255 GLY ASN LEU SER SER VAL LYS GLY THR GLU HIS ASP PRO
SEQRES 15 C 255 TYR TYR LEU LEU ASP LYS ALA VAL ALA GLU ASP LYS GLN
SEQRES 16 C 255 ILE PRO LYS LEU LEU ILE MET CYS GLY LYS GLN ASP PHE
SEQRES 17 C 255 LEU TYR GLN ASP ASN LEU ASP PHE ILE ASP TYR LEU SER
SEQRES 18 C 255 ARG ILE ASN VAL PRO TYR GLN PHE GLU ASP GLY PRO GLY
SEQRES 19 C 255 ASP HIS ASP TYR ALA TYR TRP ASP GLN ALA ILE LYS ARG
SEQRES 20 C 255 ALA ILE THR TRP MET VAL ASN ASP
SEQRES 1 D 255 GLY PRO GLY ALA TYR ILE SER LEU ASN TYR HIS SER PRO
SEQRES 2 D 255 THR ILE GLY MET HIS GLN ASN LEU THR VAL ILE LEU PRO
SEQRES 3 D 255 GLU ASP GLN SER PHE PHE ASN SER ASP THR THR VAL LYS
SEQRES 4 D 255 PRO LEU LYS THR LEU MET LEU LEU HIS GLY LEU SER SER
SEQRES 5 D 255 ASP GLU THR THR TYR MET ARG TYR THR SER ILE GLU ARG
SEQRES 6 D 255 TYR ALA ASN GLU HIS LYS LEU ALA VAL ILE MET PRO ASN
SEQRES 7 D 255 VAL ASP HIS SER ALA TYR ALA ASN MET ALA TYR GLY HIS
SEQRES 8 D 255 SER TYR TYR ASP TYR ILE LEU GLU VAL TYR ASP TYR VAL
SEQRES 9 D 255 HIS GLN ILE PHE PRO LEU SER LYS LYS ARG ASP ASP ASN
SEQRES 10 D 255 PHE ILE ALA GLY HIS SER MET GLY GLY TYR GLY THR ILE
SEQRES 11 D 255 LYS PHE ALA LEU THR GLN GLY ASP LYS PHE ALA LYS ALA
SEQRES 12 D 255 VAL PRO LEU SER ALA VAL PHE GLU ALA GLN ASN LEU MET
SEQRES 13 D 255 ASP LEU GLU TRP ASN ASP PHE SER LYS GLU ALA ILE ILE
SEQRES 14 D 255 GLY ASN LEU SER SER VAL LYS GLY THR GLU HIS ASP PRO
SEQRES 15 D 255 TYR TYR LEU LEU ASP LYS ALA VAL ALA GLU ASP LYS GLN
SEQRES 16 D 255 ILE PRO LYS LEU LEU ILE MET CYS GLY LYS GLN ASP PHE
SEQRES 17 D 255 LEU TYR GLN ASP ASN LEU ASP PHE ILE ASP TYR LEU SER
SEQRES 18 D 255 ARG ILE ASN VAL PRO TYR GLN PHE GLU ASP GLY PRO GLY
SEQRES 19 D 255 ASP HIS ASP TYR ALA TYR TRP ASP GLN ALA ILE LYS ARG
SEQRES 20 D 255 ALA ILE THR TRP MET VAL ASN ASP
HET HE4 A 301 8
HET HE4 B 301 8
HET HE4 C 301 8
HET HE4 D 301 8
HETNAM HE4 HEPTAN-1-OL
FORMUL 5 HE4 4(C7 H16 O)
FORMUL 9 HOH *17(H2 O)
HELIX 1 AA1 ASP A 26 ASN A 31 5 6
HELIX 2 AA2 THR A 53 THR A 59 1 7
HELIX 3 AA3 SER A 60 HIS A 68 1 9
HELIX 4 AA4 SER A 90 PHE A 106 1 17
HELIX 5 AA5 LYS A 111 ASP A 113 5 3
HELIX 6 AA6 SER A 121 GLN A 134 1 14
HELIX 7 AA7 GLU A 149 ASP A 155 1 7
HELIX 8 AA8 SER A 162 GLY A 168 1 7
HELIX 9 AA9 ASP A 179 GLU A 190 1 12
HELIX 10 AB1 LEU A 207 ILE A 221 1 15
HELIX 11 AB2 ASP A 235 ASN A 252 1 18
HELIX 12 AB3 ASP B 26 ASN B 31 5 6
HELIX 13 AB4 THR B 53 THR B 59 1 7
HELIX 14 AB5 SER B 60 HIS B 68 1 9
HELIX 15 AB6 SER B 90 PHE B 106 1 17
HELIX 16 AB7 LYS B 111 ASP B 113 5 3
HELIX 17 AB8 SER B 121 GLN B 134 1 14
HELIX 18 AB9 ALA B 150 ASP B 155 1 6
HELIX 19 AC1 SER B 162 GLY B 168 1 7
HELIX 20 AC2 ASP B 179 GLU B 190 1 12
HELIX 21 AC3 LEU B 207 ILE B 221 1 15
HELIX 22 AC4 ASP B 235 VAL B 251 1 17
HELIX 23 AC5 ASP C 26 ASN C 31 5 6
HELIX 24 AC6 THR C 53 THR C 59 1 7
HELIX 25 AC7 SER C 60 LYS C 69 1 10
HELIX 26 AC8 SER C 90 PHE C 106 1 17
HELIX 27 AC9 LYS C 111 ASP C 113 5 3
HELIX 28 AD1 SER C 121 GLN C 134 1 14
HELIX 29 AD2 ALA C 150 ASP C 155 1 6
HELIX 30 AD3 SER C 162 GLY C 168 1 7
HELIX 31 AD4 ASP C 179 GLU C 190 1 12
HELIX 32 AD5 LEU C 207 ILE C 221 1 15
HELIX 33 AD6 ASP C 235 ASN C 252 1 18
HELIX 34 AD7 ASP D 26 ASN D 31 5 6
HELIX 35 AD8 THR D 53 THR D 59 1 7
HELIX 36 AD9 SER D 60 LYS D 69 1 10
HELIX 37 AE1 SER D 90 PHE D 106 1 17
HELIX 38 AE2 LYS D 111 ASP D 113 5 3
HELIX 39 AE3 SER D 121 GLN D 134 1 14
HELIX 40 AE4 GLY D 135 PHE D 138 5 4
HELIX 41 AE5 GLU D 149 ASP D 155 1 7
HELIX 42 AE6 SER D 162 GLY D 168 1 7
HELIX 43 AE7 ASP D 179 GLU D 190 1 12
HELIX 44 AE8 LEU D 207 ILE D 221 1 15
HELIX 45 AE9 ASP D 235 ASN D 252 1 18
SHEET 1 AA116 GLN A 226 GLU A 228 0
SHEET 2 AA116 LYS A 196 MET A 200 1 N ILE A 199 O GLN A 226
SHEET 3 AA116 LYS A 140 LEU A 144 1 N ALA A 141 O LYS A 196
SHEET 4 AA116 ASN A 115 HIS A 120 1 N GLY A 119 O LEU A 144
SHEET 5 AA116 LYS A 40 LEU A 45 1 N MET A 43 O ALA A 118
SHEET 6 AA116 LEU A 70 PRO A 75 1 O ILE A 73 N LEU A 42
SHEET 7 AA116 MET A 15 PRO A 24 -1 N THR A 20 O MET A 74
SHEET 8 AA116 GLY A 1 SER A 10 -1 N ILE A 4 O VAL A 21
SHEET 9 AA116 GLY D 1 SER D 10 -1 O ASN D 7 N TYR A 3
SHEET 10 AA116 MET D 15 PRO D 24 -1 O LEU D 23 N ALA D 2
SHEET 11 AA116 LEU D 70 MET D 74 -1 O MET D 74 N THR D 20
SHEET 12 AA116 LYS D 40 LEU D 45 1 N LEU D 44 O ILE D 73
SHEET 13 AA116 ASN D 115 HIS D 120 1 O PHE D 116 N THR D 41
SHEET 14 AA116 LYS D 140 LEU D 144 1 O LEU D 144 N GLY D 119
SHEET 15 AA116 LYS D 196 MET D 200 1 O LYS D 196 N ALA D 141
SHEET 16 AA116 GLN D 226 GLU D 228 1 O GLN D 226 N ILE D 199
SHEET 1 AA216 GLN B 226 GLU B 228 0
SHEET 2 AA216 LYS B 196 MET B 200 1 N ILE B 199 O GLN B 226
SHEET 3 AA216 LYS B 140 LEU B 144 1 N ALA B 141 O LYS B 196
SHEET 4 AA216 ASN B 115 HIS B 120 1 N GLY B 119 O LEU B 144
SHEET 5 AA216 LYS B 40 LEU B 45 1 N THR B 41 O PHE B 116
SHEET 6 AA216 LEU B 70 MET B 74 1 O ALA B 71 N LEU B 42
SHEET 7 AA216 MET B 15 PRO B 24 -1 N ILE B 22 O VAL B 72
SHEET 8 AA216 GLY B 1 SER B 10 -1 N LEU B 6 O LEU B 19
SHEET 9 AA216 GLY C 1 SER C 10 -1 O ASN C 7 N TYR B 3
SHEET 10 AA216 MET C 15 PRO C 24 -1 O LEU C 23 N ALA C 2
SHEET 11 AA216 LEU C 70 MET C 74 -1 O MET C 74 N THR C 20
SHEET 12 AA216 LYS C 40 LEU C 45 1 N LYS C 40 O ALA C 71
SHEET 13 AA216 ASN C 115 HIS C 120 1 O ALA C 118 N LEU C 45
SHEET 14 AA216 LYS C 140 LEU C 144 1 O VAL C 142 N ILE C 117
SHEET 15 AA216 LYS C 196 MET C 200 1 O LYS C 196 N ALA C 141
SHEET 16 AA216 GLN C 226 GLU C 228 1 O GLN C 226 N ILE C 199
LINK OG SER A 121 CAD HE4 A 301 1555 1555 1.38
LINK OG SER B 121 CAD HE4 B 301 1555 1555 1.38
LINK OG SER C 121 CAD HE4 C 301 1555 1555 1.37
LINK OG SER D 121 CAD HE4 D 301 1555 1555 1.38
SITE 1 AC1 6 GLY A 47 LEU A 48 SER A 121 MET A 122
SITE 2 AC1 6 ASN A 152 HIS A 234
SITE 1 AC2 13 LEU B 48 HIS B 120 MET B 122 GLY B 123
SITE 2 AC2 13 GLY B 124 TYR B 125 LEU B 144 SER B 145
SITE 3 AC2 13 ALA B 146 VAL B 147 ASN B 152 LEU B 207
SITE 4 AC2 13 HIS B 234
SITE 1 AC3 12 GLY C 47 LEU C 48 HIS C 120 MET C 122
SITE 2 AC3 12 GLY C 123 GLY C 124 TYR C 125 LEU C 144
SITE 3 AC3 12 SER C 145 VAL C 147 ASN C 152 HIS C 234
SITE 1 AC4 13 GLY D 47 LEU D 48 HIS D 120 MET D 122
SITE 2 AC4 13 GLY D 123 GLY D 124 TYR D 125 LEU D 144
SITE 3 AC4 13 SER D 145 ALA D 146 VAL D 147 ASN D 152
SITE 4 AC4 13 HIS D 234
CRYST1 86.957 86.957 454.712 90.00 90.00 120.00 P 61 2 2 48
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 0.011500 0.006639 0.000000 0.00000
SCALE2 0.000000 0.013279 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002199 0.00000
TER 2059 ASP A 253
TER 4122 ASP B 253
TER 6178 ASP C 253
TER 8223 ASP D 253
MASTER 839 0 4 45 32 0 13 6 8201 4 36 80
END |