HEADER IMMUNE SYSTEM 29-AUG-17 6ATF
TITLE HLA-DRB1*1402 IN COMPLEX WITH VIMENTIN59-71
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;
COMPND 3 CHAIN: A, D;
COMPND 4 FRAGMENT: UNP RESIDUES 26-206;
COMPND 5 SYNONYM: MHC CLASS II ANTIGEN DRA;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: MHC CLASS II ANTIGEN;
COMPND 9 CHAIN: B, E;
COMPND 10 FRAGMENT: UNP RESIDUES 30-219;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: VIMENTIN59-71;
COMPND 14 CHAIN: C, F;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HLA-DRA, HLA-DRA1;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: HLA-DRB1;
SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 18 ORGANISM_TAXID: 32630
KEYWDS HLA CLASS II, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.W.SCALLY,Y.T.TING,J.ROSSJOHN
REVDAT 3 29-JUL-20 6ATF 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 18-OCT-17 6ATF 1 JRNL
REVDAT 1 13-SEP-17 6ATF 0
JRNL AUTH S.W.SCALLY,S.C.LAW,Y.T.TING,J.V.HEEMST,J.SOKOLOVE,
JRNL AUTH 2 A.J.DEUTSCH,E.BRIDIE CLEMENS,A.K.MOUSTAKAS,G.K.PAPADOPOULOS,
JRNL AUTH 3 D.V.WOUDE,I.SMOLIK,C.A.HITCHON,D.B.ROBINSON,E.D.FERUCCI,
JRNL AUTH 4 C.N.BERNSTEIN,X.MENG,V.ANAPARTI,T.HUIZINGA,K.KEDZIERSKA,
JRNL AUTH 5 H.H.REID,S.RAYCHAUDHURI,R.E.TOES,J.ROSSJOHN,H.EL-GABALAWY,
JRNL AUTH 6 R.THOMAS
JRNL TITL MOLECULAR BASIS FOR INCREASED SUSCEPTIBILITY OF INDIGENOUS
JRNL TITL 2 NORTH AMERICANS TO SEROPOSITIVE RHEUMATOID ARTHRITIS.
JRNL REF ANN. RHEUM. DIS. V. 76 1915 2017
JRNL REFN ISSN 1468-2060
JRNL PMID 28801345
JRNL DOI 10.1136/ANNRHEUMDIS-2017-211300
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 72003
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 3632
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 33.4876 - 5.6173 1.00 2697 161 0.1840 0.1813
REMARK 3 2 5.6173 - 4.4619 1.00 2680 136 0.1443 0.1807
REMARK 3 3 4.4619 - 3.8989 1.00 2664 138 0.1351 0.1613
REMARK 3 4 3.8989 - 3.5428 1.00 2622 154 0.1504 0.1718
REMARK 3 5 3.5428 - 3.2891 1.00 2669 134 0.1545 0.1793
REMARK 3 6 3.2891 - 3.0954 1.00 2636 140 0.1623 0.1900
REMARK 3 7 3.0954 - 2.9404 1.00 2655 126 0.1682 0.2424
REMARK 3 8 2.9404 - 2.8125 1.00 2669 139 0.1728 0.1923
REMARK 3 9 2.8125 - 2.7043 1.00 2617 137 0.1724 0.1953
REMARK 3 10 2.7043 - 2.6110 1.00 2635 137 0.1776 0.2138
REMARK 3 11 2.6110 - 2.5294 1.00 2636 154 0.1701 0.2163
REMARK 3 12 2.5294 - 2.4571 1.00 2603 138 0.1779 0.2380
REMARK 3 13 2.4571 - 2.3924 1.00 2628 135 0.1817 0.2258
REMARK 3 14 2.3924 - 2.3341 1.00 2631 138 0.1762 0.2285
REMARK 3 15 2.3341 - 2.2810 1.00 2631 139 0.1723 0.2226
REMARK 3 16 2.2810 - 2.2325 1.00 2606 142 0.1706 0.2027
REMARK 3 17 2.2325 - 2.1879 1.00 2635 144 0.1768 0.2031
REMARK 3 18 2.1879 - 2.1466 1.00 2629 122 0.1775 0.2084
REMARK 3 19 2.1466 - 2.1083 1.00 2599 149 0.1755 0.2180
REMARK 3 20 2.1083 - 2.0725 1.00 2640 156 0.1860 0.2240
REMARK 3 21 2.0725 - 2.0391 1.00 2570 149 0.1913 0.2209
REMARK 3 22 2.0391 - 2.0077 1.00 2627 147 0.1913 0.2327
REMARK 3 23 2.0077 - 1.9782 1.00 2619 138 0.1940 0.2438
REMARK 3 24 1.9782 - 1.9503 0.99 2629 127 0.2069 0.2515
REMARK 3 25 1.9503 - 1.9240 0.99 2590 138 0.2224 0.2449
REMARK 3 26 1.9240 - 1.8990 0.97 2554 114 0.2395 0.2651
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.860
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 : 0.004 6626
REMARK 3 ANGLE : 0.913 9006
REMARK 3 CHIRALITY : 0.037 976
REMARK 3 PLANARITY : 0.004 1173
REMARK 3 DIHEDRAL : 13.950 2416
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 26 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.8748 4.3740 114.3068
REMARK 3 T TENSOR
REMARK 3 T11: 0.0935 T22: 0.0835
REMARK 3 T33: 0.0882 T12: 0.0286
REMARK 3 T13: 0.0063 T23: -0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 2.9374 L22: 1.5101
REMARK 3 L33: 2.3719 L12: 0.1547
REMARK 3 L13: 0.9481 L23: -1.6767
REMARK 3 S TENSOR
REMARK 3 S11: -0.0262 S12: 0.0541 S13: -0.1246
REMARK 3 S21: -0.0183 S22: 0.0161 S23: -0.0145
REMARK 3 S31: 0.0409 S32: -0.0099 S33: 0.0315
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 27 THROUGH 55 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.4942 -5.4391 106.3641
REMARK 3 T TENSOR
REMARK 3 T11: 0.1722 T22: 0.0957
REMARK 3 T33: 0.2074 T12: 0.0014
REMARK 3 T13: 0.0137 T23: -0.0399
REMARK 3 L TENSOR
REMARK 3 L11: 3.4698 L22: 2.9424
REMARK 3 L33: 2.6927 L12: 0.1300
REMARK 3 L13: -1.0495 L23: 1.1705
REMARK 3 S TENSOR
REMARK 3 S11: -0.0435 S12: 0.2013 S13: -0.7121
REMARK 3 S21: 0.0450 S22: 0.0370 S23: -0.1817
REMARK 3 S31: 0.4525 S32: 0.1390 S33: -0.0621
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 56 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 54.8203 4.9213 123.0097
REMARK 3 T TENSOR
REMARK 3 T11: 0.1270 T22: 0.1289
REMARK 3 T33: 0.1248 T12: 0.0108
REMARK 3 T13: -0.0124 T23: 0.0570
REMARK 3 L TENSOR
REMARK 3 L11: 1.2868 L22: 2.0370
REMARK 3 L33: 6.1252 L12: 0.4379
REMARK 3 L13: 0.5256 L23: 2.7864
REMARK 3 S TENSOR
REMARK 3 S11: 0.0271 S12: -0.0391 S13: -0.1392
REMARK 3 S21: 0.1117 S22: -0.0979 S23: -0.0476
REMARK 3 S31: 0.2036 S32: 0.1495 S33: 0.0371
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 77 THROUGH 101 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7839 1.9457 119.2004
REMARK 3 T TENSOR
REMARK 3 T11: 0.1347 T22: 0.0901
REMARK 3 T33: 0.0777 T12: -0.0450
REMARK 3 T13: 0.0271 T23: 0.0517
REMARK 3 L TENSOR
REMARK 3 L11: 3.2149 L22: 1.4552
REMARK 3 L33: 2.0635 L12: 1.0425
REMARK 3 L13: 1.3183 L23: 0.4831
REMARK 3 S TENSOR
REMARK 3 S11: -0.2552 S12: 0.0680 S13: 0.2383
REMARK 3 S21: -0.1145 S22: 0.0671 S23: 0.2984
REMARK 3 S31: 0.0886 S32: -0.1981 S33: 0.1743
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 102 THROUGH 154 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.3496 -2.8826 117.4500
REMARK 3 T TENSOR
REMARK 3 T11: 0.1173 T22: 0.0566
REMARK 3 T33: 0.1011 T12: 0.0068
REMARK 3 T13: 0.0113 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 2.5143 L22: 0.4807
REMARK 3 L33: 2.0489 L12: 1.0677
REMARK 3 L13: 0.0104 L23: 0.2202
REMARK 3 S TENSOR
REMARK 3 S11: -0.0580 S12: 0.0371 S13: -0.0873
REMARK 3 S21: -0.0561 S22: -0.0027 S23: -0.0212
REMARK 3 S31: 0.1388 S32: -0.0963 S33: 0.0341
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 155 THROUGH 166 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.0165 -9.3731 119.6624
REMARK 3 T TENSOR
REMARK 3 T11: 0.2098 T22: 0.2958
REMARK 3 T33: 0.1926 T12: -0.1524
REMARK 3 T13: 0.0246 T23: 0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 1.6990 L22: 2.0348
REMARK 3 L33: 0.8732 L12: 0.6968
REMARK 3 L13: -1.1159 L23: -0.4919
REMARK 3 S TENSOR
REMARK 3 S11: 0.0794 S12: 0.1497 S13: -0.2749
REMARK 3 S21: 0.1937 S22: -0.0055 S23: 0.1109
REMARK 3 S31: 0.4523 S32: -0.6433 S33: -0.0903
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 167 THROUGH 181 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.2619 -0.7732 124.9657
REMARK 3 T TENSOR
REMARK 3 T11: 0.0877 T22: 0.2442
REMARK 3 T33: 0.1169 T12: 0.0010
REMARK 3 T13: 0.0443 T23: 0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 1.6475 L22: 3.2397
REMARK 3 L33: 1.9228 L12: 0.4442
REMARK 3 L13: -1.7281 L23: 0.1619
REMARK 3 S TENSOR
REMARK 3 S11: 0.0908 S12: -0.5505 S13: 0.2290
REMARK 3 S21: 0.0965 S22: -0.2460 S23: 0.3560
REMARK 3 S31: 0.1915 S32: -0.6189 S33: 0.2058
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.5002 14.2851 112.2493
REMARK 3 T TENSOR
REMARK 3 T11: 0.0834 T22: 0.0799
REMARK 3 T33: 0.0847 T12: 0.0050
REMARK 3 T13: -0.0043 T23: 0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 1.4842 L22: 0.8720
REMARK 3 L33: 1.9618 L12: 0.2826
REMARK 3 L13: -0.0362 L23: -0.2674
REMARK 3 S TENSOR
REMARK 3 S11: -0.0324 S12: 0.0721 S13: 0.0438
REMARK 3 S21: 0.0167 S22: -0.0042 S23: -0.0407
REMARK 3 S31: -0.1739 S32: 0.0245 S33: 0.0388
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 90 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6741 7.2527 98.5826
REMARK 3 T TENSOR
REMARK 3 T11: 0.1272 T22: 0.1000
REMARK 3 T33: 0.1116 T12: -0.0290
REMARK 3 T13: -0.0015 T23: -0.0347
REMARK 3 L TENSOR
REMARK 3 L11: 3.3862 L22: 0.9096
REMARK 3 L33: 1.2438 L12: -1.3576
REMARK 3 L13: -0.0069 L23: 0.1976
REMARK 3 S TENSOR
REMARK 3 S11: 0.0278 S12: 0.2289 S13: -0.0740
REMARK 3 S21: -0.0646 S22: -0.0501 S23: 0.1312
REMARK 3 S31: -0.0972 S32: -0.1137 S33: 0.0234
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 3 THROUGH 26 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.8349 35.3216 114.5136
REMARK 3 T TENSOR
REMARK 3 T11: 0.0601 T22: 0.0676
REMARK 3 T33: 0.0806 T12: 0.0131
REMARK 3 T13: -0.0078 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 2.3276 L22: 0.7218
REMARK 3 L33: 6.9659 L12: 0.6905
REMARK 3 L13: -0.5393 L23: 0.1290
REMARK 3 S TENSOR
REMARK 3 S11: -0.0318 S12: 0.0330 S13: 0.1230
REMARK 3 S21: 0.0011 S22: 0.0738 S23: 0.0173
REMARK 3 S31: -0.1886 S32: 0.1387 S33: -0.0124
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 27 THROUGH 55 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.2067 45.1556 106.5348
REMARK 3 T TENSOR
REMARK 3 T11: 0.1603 T22: 0.0883
REMARK 3 T33: 0.1921 T12: 0.0130
REMARK 3 T13: -0.0090 T23: 0.0378
REMARK 3 L TENSOR
REMARK 3 L11: 3.6831 L22: 3.1217
REMARK 3 L33: 3.2826 L12: -0.0203
REMARK 3 L13: 0.9876 L23: -0.9194
REMARK 3 S TENSOR
REMARK 3 S11: 0.0403 S12: 0.1190 S13: 0.6620
REMARK 3 S21: 0.0419 S22: -0.0411 S23: 0.1262
REMARK 3 S31: -0.5050 S32: -0.0877 S33: -0.0428
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 56 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7305 34.7548 123.7334
REMARK 3 T TENSOR
REMARK 3 T11: 0.1141 T22: 0.1287
REMARK 3 T33: 0.1187 T12: 0.0120
REMARK 3 T13: 0.0167 T23: -0.0576
REMARK 3 L TENSOR
REMARK 3 L11: 1.3707 L22: 2.3568
REMARK 3 L33: 6.3124 L12: 0.3844
REMARK 3 L13: -0.6712 L23: -2.8386
REMARK 3 S TENSOR
REMARK 3 S11: -0.0512 S12: -0.1105 S13: 0.1784
REMARK 3 S21: 0.1743 S22: 0.0487 S23: 0.0811
REMARK 3 S31: -0.1556 S32: -0.2789 S33: -0.0244
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 77 THROUGH 101 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.9114 37.7896 119.4162
REMARK 3 T TENSOR
REMARK 3 T11: 0.1068 T22: 0.1283
REMARK 3 T33: 0.0563 T12: -0.0427
REMARK 3 T13: -0.0389 T23: -0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 2.8805 L22: 1.3746
REMARK 3 L33: 1.6637 L12: 0.5629
REMARK 3 L13: -1.3421 L23: -0.2592
REMARK 3 S TENSOR
REMARK 3 S11: -0.2101 S12: 0.1277 S13: -0.2167
REMARK 3 S21: -0.1240 S22: 0.0065 S23: -0.2866
REMARK 3 S31: -0.0596 S32: 0.1414 S33: 0.2011
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 102 THROUGH 154 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.3467 42.5925 117.6392
REMARK 3 T TENSOR
REMARK 3 T11: 0.1415 T22: 0.0659
REMARK 3 T33: 0.0774 T12: -0.0067
REMARK 3 T13: -0.0067 T23: -0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 2.5030 L22: 0.5633
REMARK 3 L33: 1.6464 L12: 0.7740
REMARK 3 L13: 0.0125 L23: -0.2977
REMARK 3 S TENSOR
REMARK 3 S11: -0.0738 S12: 0.0658 S13: 0.0776
REMARK 3 S21: -0.0863 S22: -0.0070 S23: 0.0076
REMARK 3 S31: -0.2345 S32: 0.0466 S33: 0.0522
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 155 THROUGH 181 )
REMARK 3 ORIGIN FOR THE GROUP (A): 52.9306 44.0000 122.6793
REMARK 3 T TENSOR
REMARK 3 T11: 0.1455 T22: 0.2504
REMARK 3 T33: 0.1219 T12: -0.0741
REMARK 3 T13: -0.0201 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 2.7808 L22: 2.9815
REMARK 3 L33: 2.1483 L12: 1.6257
REMARK 3 L13: -0.2312 L23: -0.5502
REMARK 3 S TENSOR
REMARK 3 S11: 0.2056 S12: -0.4220 S13: -0.0500
REMARK 3 S21: 0.1365 S22: -0.2842 S23: -0.2508
REMARK 3 S31: -0.3550 S32: 0.6931 S33: 0.0959
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 2 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6225 24.9498 114.8585
REMARK 3 T TENSOR
REMARK 3 T11: 0.0666 T22: 0.0834
REMARK 3 T33: 0.0769 T12: 0.0062
REMARK 3 T13: 0.0049 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 1.2263 L22: 1.1205
REMARK 3 L33: 2.2714 L12: 0.0271
REMARK 3 L13: -0.0206 L23: 0.2678
REMARK 3 S TENSOR
REMARK 3 S11: -0.0064 S12: 0.0203 S13: -0.0719
REMARK 3 S21: -0.0153 S22: 0.0069 S23: -0.0317
REMARK 3 S31: 0.0632 S32: 0.0538 S33: -0.0115
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 52 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4904 26.0611 108.9023
REMARK 3 T TENSOR
REMARK 3 T11: 0.0875 T22: 0.0981
REMARK 3 T33: 0.0820 T12: 0.0132
REMARK 3 T13: -0.0046 T23: -0.0296
REMARK 3 L TENSOR
REMARK 3 L11: 2.4708 L22: 1.9143
REMARK 3 L33: 2.6823 L12: 1.1179
REMARK 3 L13: -1.2133 L23: -0.6971
REMARK 3 S TENSOR
REMARK 3 S11: -0.0561 S12: 0.2325 S13: -0.0353
REMARK 3 S21: 0.0439 S22: 0.0604 S23: 0.1401
REMARK 3 S31: 0.1647 S32: -0.2314 S33: 0.0246
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 90 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.9331 32.6263 98.6132
REMARK 3 T TENSOR
REMARK 3 T11: 0.1244 T22: 0.1182
REMARK 3 T33: 0.1141 T12: -0.0253
REMARK 3 T13: 0.0046 T23: 0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 3.2446 L22: 0.9146
REMARK 3 L33: 0.9269 L12: -1.5301
REMARK 3 L13: 0.0310 L23: -0.2779
REMARK 3 S TENSOR
REMARK 3 S11: 0.0487 S12: 0.3019 S13: 0.1171
REMARK 3 S21: -0.0514 S22: -0.0914 S23: -0.1469
REMARK 3 S31: 0.0791 S32: 0.0915 S33: 0.0393
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 13 )
REMARK 3 ORIGIN FOR THE GROUP (A): 56.2762 6.7543 113.7522
REMARK 3 T TENSOR
REMARK 3 T11: 0.1107 T22: 0.1055
REMARK 3 T33: 0.1149 T12: 0.0222
REMARK 3 T13: -0.0143 T23: 0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 3.0257 L22: 2.9951
REMARK 3 L33: 5.4895 L12: 1.6338
REMARK 3 L13: 2.7332 L23: 3.2107
REMARK 3 S TENSOR
REMARK 3 S11: -0.0230 S12: 0.1596 S13: -0.2537
REMARK 3 S21: 0.1848 S22: 0.2620 S23: -0.3039
REMARK 3 S31: 0.0713 S32: 0.4030 S33: -0.2565
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1 THROUGH 13 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4243 32.9560 113.9199
REMARK 3 T TENSOR
REMARK 3 T11: 0.1178 T22: 0.1190
REMARK 3 T33: 0.1236 T12: 0.0195
REMARK 3 T13: 0.0411 T23: -0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 2.1334 L22: 1.7834
REMARK 3 L33: 3.2018 L12: 0.7958
REMARK 3 L13: -1.1652 L23: -1.6368
REMARK 3 S TENSOR
REMARK 3 S11: 0.1157 S12: 0.0531 S13: 0.2743
REMARK 3 S21: 0.3078 S22: 0.1703 S23: 0.3597
REMARK 3 S31: -0.2924 S32: -0.2484 S33: -0.3016
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 6ATF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1000229810.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.3
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) : .95370
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72027
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 33.482
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 4MCY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG 3350, 0.2M POTASSIUM NITRATE,
REMARK 280 0.1M BIS-TRIS-PROPANE PH 7.3, VAPOR DIFFUSION, HANGING 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 38.88500
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, G
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, H
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 ILE A 1
REMARK 465 LYS A 2
REMARK 465 SER A 183
REMARK 465 GLY A 184
REMARK 465 ASP A 185
REMARK 465 ASP A 186
REMARK 465 ASP A 187
REMARK 465 ASP A 188
REMARK 465 LYS A 189
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 GLY B 1
REMARK 465 THR B 191
REMARK 465 GLY B 192
REMARK 465 GLY B 193
REMARK 465 ASP B 194
REMARK 465 ASP B 195
REMARK 465 ASP B 196
REMARK 465 ASP B 197
REMARK 465 LYS B 198
REMARK 465 ILE D 1
REMARK 465 LYS D 2
REMARK 465 THR D 182
REMARK 465 SER D 183
REMARK 465 GLY D 184
REMARK 465 ASP D 185
REMARK 465 ASP D 186
REMARK 465 ASP D 187
REMARK 465 ASP D 188
REMARK 465 LYS D 189
REMARK 465 GLY E -1
REMARK 465 SER E 0
REMARK 465 GLY E 1
REMARK 465 THR E 191
REMARK 465 GLY E 192
REMARK 465 GLY E 193
REMARK 465 ASP E 194
REMARK 465 ASP E 195
REMARK 465 ASP E 196
REMARK 465 ASP E 197
REMARK 465 LYS E 198
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 71 CG CD OE1 OE2
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 GLN B 34 -10.44 75.77
REMARK 500 TYR B 78 -61.05 -121.83
REMARK 500 THR B 90 -72.39 -123.12
REMARK 500 ASN B 113 22.24 -140.38
REMARK 500 GLN E 34 -10.71 75.89
REMARK 500 TYR E 78 -61.54 -121.59
REMARK 500 THR E 90 -73.03 -122.67
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6ATF A 1 181 UNP P01903 DRA_HUMAN 26 206
DBREF1 6ATF B 1 190 UNP A0A0A1I7H6_HUMAN
DBREF2 6ATF B A0A0A1I7H6 30 219
DBREF 6ATF D 1 181 UNP P01903 DRA_HUMAN 26 206
DBREF1 6ATF E 1 190 UNP A0A0A1I7H6_HUMAN
DBREF2 6ATF E A0A0A1I7H6 30 219
DBREF 6ATF C 1 13 PDB 6ATF 6ATF 1 13
DBREF 6ATF F 1 13 PDB 6ATF 6ATF 1 13
SEQADV 6ATF THR A 182 UNP P01903 EXPRESSION TAG
SEQADV 6ATF SER A 183 UNP P01903 EXPRESSION TAG
SEQADV 6ATF GLY A 184 UNP P01903 EXPRESSION TAG
SEQADV 6ATF ASP A 185 UNP P01903 EXPRESSION TAG
SEQADV 6ATF ASP A 186 UNP P01903 EXPRESSION TAG
SEQADV 6ATF ASP A 187 UNP P01903 EXPRESSION TAG
SEQADV 6ATF ASP A 188 UNP P01903 EXPRESSION TAG
SEQADV 6ATF LYS A 189 UNP P01903 EXPRESSION TAG
SEQADV 6ATF GLY B -1 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATF SER B 0 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATF THR B 191 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATF GLY B 192 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATF GLY B 193 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATF ASP B 194 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATF ASP B 195 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATF ASP B 196 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATF ASP B 197 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATF LYS B 198 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATF THR D 182 UNP P01903 EXPRESSION TAG
SEQADV 6ATF SER D 183 UNP P01903 EXPRESSION TAG
SEQADV 6ATF GLY D 184 UNP P01903 EXPRESSION TAG
SEQADV 6ATF ASP D 185 UNP P01903 EXPRESSION TAG
SEQADV 6ATF ASP D 186 UNP P01903 EXPRESSION TAG
SEQADV 6ATF ASP D 187 UNP P01903 EXPRESSION TAG
SEQADV 6ATF ASP D 188 UNP P01903 EXPRESSION TAG
SEQADV 6ATF LYS D 189 UNP P01903 EXPRESSION TAG
SEQADV 6ATF GLY E -1 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATF SER E 0 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATF THR E 191 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATF GLY E 192 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATF GLY E 193 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATF ASP E 194 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATF ASP E 195 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATF ASP E 196 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATF ASP E 197 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATF LYS E 198 UNP A0A0A1I7H EXPRESSION TAG
SEQRES 1 A 189 ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES 2 A 189 LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES 3 A 189 ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES 4 A 189 GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES 5 A 189 SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES 6 A 189 ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES 7 A 189 TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES 8 A 189 LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES 9 A 189 LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES 10 A 189 ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES 11 A 189 GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES 12 A 189 LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES 13 A 189 THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 A 189 LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP THR
SEQRES 15 A 189 SER GLY ASP ASP ASP ASP LYS
SEQRES 1 B 200 GLY SER GLY ASP THR ARG PRO ARG PHE LEU GLU TYR SER
SEQRES 2 B 200 THR SER GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL
SEQRES 3 B 200 ARG PHE LEU GLU ARG TYR PHE HIS ASN GLN GLU GLU ASN
SEQRES 4 B 200 VAL ARG PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL
SEQRES 5 B 200 THR GLU LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER
SEQRES 6 B 200 GLN LYS ASP LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP
SEQRES 7 B 200 THR TYR CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE
SEQRES 8 B 200 THR VAL GLN ARG ARG VAL HIS PRO LYS VAL THR VAL TYR
SEQRES 9 B 200 PRO SER LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU
SEQRES 10 B 200 VAL CYS SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU
SEQRES 11 B 200 VAL ARG TRP PHE ARG ASN GLY GLN GLU GLU LYS THR GLY
SEQRES 12 B 200 VAL VAL SER THR GLY LEU ILE HIS ASN GLY ASP TRP THR
SEQRES 13 B 200 PHE GLN THR LEU VAL MET LEU GLU THR VAL PRO ARG SER
SEQRES 14 B 200 GLY GLU VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL
SEQRES 15 B 200 THR SER PRO LEU THR VAL GLU TRP ARG ALA THR GLY GLY
SEQRES 16 B 200 ASP ASP ASP ASP LYS
SEQRES 1 D 189 ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES 2 D 189 LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES 3 D 189 ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES 4 D 189 GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES 5 D 189 SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES 6 D 189 ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES 7 D 189 TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES 8 D 189 LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES 9 D 189 LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES 10 D 189 ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES 11 D 189 GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES 12 D 189 LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES 13 D 189 THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 D 189 LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP THR
SEQRES 15 D 189 SER GLY ASP ASP ASP ASP LYS
SEQRES 1 E 200 GLY SER GLY ASP THR ARG PRO ARG PHE LEU GLU TYR SER
SEQRES 2 E 200 THR SER GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL
SEQRES 3 E 200 ARG PHE LEU GLU ARG TYR PHE HIS ASN GLN GLU GLU ASN
SEQRES 4 E 200 VAL ARG PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL
SEQRES 5 E 200 THR GLU LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER
SEQRES 6 E 200 GLN LYS ASP LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP
SEQRES 7 E 200 THR TYR CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE
SEQRES 8 E 200 THR VAL GLN ARG ARG VAL HIS PRO LYS VAL THR VAL TYR
SEQRES 9 E 200 PRO SER LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU
SEQRES 10 E 200 VAL CYS SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU
SEQRES 11 E 200 VAL ARG TRP PHE ARG ASN GLY GLN GLU GLU LYS THR GLY
SEQRES 12 E 200 VAL VAL SER THR GLY LEU ILE HIS ASN GLY ASP TRP THR
SEQRES 13 E 200 PHE GLN THR LEU VAL MET LEU GLU THR VAL PRO ARG SER
SEQRES 14 E 200 GLY GLU VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL
SEQRES 15 E 200 THR SER PRO LEU THR VAL GLU TRP ARG ALA THR GLY GLY
SEQRES 16 E 200 ASP ASP ASP ASP LYS
SEQRES 1 C 13 GLY VAL TYR ALA THR ARG SER SER ALA VAL ARG LEU ARG
SEQRES 1 F 13 GLY VAL TYR ALA THR ARG SER SER ALA VAL ARG LEU ARG
HET NAG G 1 14
HET NAG G 2 14
HET NAG H 1 14
HET NAG H 2 14
HET NAG A 500 14
HET EDO B 201 4
HET EDO B 202 4
HET EDO B 203 4
HET EDO B 204 4
HET PGE B 205 10
HET PGE B 206 10
HET NAG D 500 14
HET EDO E 201 4
HET EDO E 202 4
HET EDO E 203 4
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 7 NAG 6(C8 H15 N O6)
FORMUL 10 EDO 7(C2 H6 O2)
FORMUL 14 PGE 2(C6 H14 O4)
FORMUL 20 HOH *1017(H2 O)
HELIX 1 AA1 LEU A 45 PHE A 51 5 7
HELIX 2 AA2 GLU A 55 SER A 77 1 23
HELIX 3 AA3 THR B 51 LEU B 53 5 3
HELIX 4 AA4 GLY B 54 SER B 63 1 10
HELIX 5 AA5 GLN B 64 ALA B 73 1 10
HELIX 6 AA6 ALA B 73 TYR B 78 1 6
HELIX 7 AA7 TYR B 78 GLU B 87 1 10
HELIX 8 AA8 SER B 88 THR B 90 5 3
HELIX 9 AA9 LEU D 45 PHE D 51 5 7
HELIX 10 AB1 GLU D 55 SER D 77 1 23
HELIX 11 AB2 THR E 51 LEU E 53 5 3
HELIX 12 AB3 GLY E 54 SER E 63 1 10
HELIX 13 AB4 GLN E 64 ALA E 73 1 10
HELIX 14 AB5 ALA E 73 TYR E 78 1 6
HELIX 15 AB6 TYR E 78 GLU E 87 1 10
HELIX 16 AB7 SER E 88 THR E 90 5 3
SHEET 1 AA1 8 GLU A 40 TRP A 43 0
SHEET 2 AA1 8 ASP A 29 ASP A 35 -1 N HIS A 33 O VAL A 42
SHEET 3 AA1 8 SER A 19 PHE A 26 -1 N PHE A 26 O ASP A 29
SHEET 4 AA1 8 HIS A 5 ASN A 15 -1 N ILE A 8 O ASP A 25
SHEET 5 AA1 8 PHE B 7 PHE B 18 -1 O PHE B 17 N HIS A 5
SHEET 6 AA1 8 ARG B 23 HIS B 32 -1 O LEU B 27 N GLU B 14
SHEET 7 AA1 8 GLU B 35 ASP B 41 -1 O PHE B 40 N GLU B 28
SHEET 8 AA1 8 TYR B 47 ALA B 49 -1 O ARG B 48 N ARG B 39
SHEET 1 AA2 4 GLU A 88 THR A 93 0
SHEET 2 AA2 4 ASN A 103 PHE A 112 -1 O ILE A 106 N LEU A 92
SHEET 3 AA2 4 PHE A 145 PHE A 153 -1 O LYS A 147 N ILE A 109
SHEET 4 AA2 4 SER A 133 GLU A 134 -1 N SER A 133 O TYR A 150
SHEET 1 AA3 4 GLU A 88 THR A 93 0
SHEET 2 AA3 4 ASN A 103 PHE A 112 -1 O ILE A 106 N LEU A 92
SHEET 3 AA3 4 PHE A 145 PHE A 153 -1 O LYS A 147 N ILE A 109
SHEET 4 AA3 4 LEU A 138 PRO A 139 -1 N LEU A 138 O ARG A 146
SHEET 1 AA4 4 LYS A 126 VAL A 128 0
SHEET 2 AA4 4 ASN A 118 ARG A 123 -1 N ARG A 123 O LYS A 126
SHEET 3 AA4 4 TYR A 161 GLU A 166 -1 O ARG A 164 N THR A 120
SHEET 4 AA4 4 LEU A 174 TRP A 178 -1 O TRP A 178 N TYR A 161
SHEET 1 AA5 4 LYS B 98 SER B 104 0
SHEET 2 AA5 4 LEU B 114 PHE B 122 -1 O VAL B 116 N TYR B 102
SHEET 3 AA5 4 PHE B 155 GLU B 162 -1 O THR B 157 N VAL B 119
SHEET 4 AA5 4 VAL B 142 SER B 144 -1 N VAL B 143 O MET B 160
SHEET 1 AA6 4 LYS B 98 SER B 104 0
SHEET 2 AA6 4 LEU B 114 PHE B 122 -1 O VAL B 116 N TYR B 102
SHEET 3 AA6 4 PHE B 155 GLU B 162 -1 O THR B 157 N VAL B 119
SHEET 4 AA6 4 ILE B 148 HIS B 149 -1 N ILE B 148 O GLN B 156
SHEET 1 AA7 4 GLN B 136 GLU B 138 0
SHEET 2 AA7 4 GLU B 128 ARG B 133 -1 N ARG B 133 O GLN B 136
SHEET 3 AA7 4 VAL B 170 GLU B 176 -1 O GLN B 174 N ARG B 130
SHEET 4 AA7 4 LEU B 184 ARG B 189 -1 O TRP B 188 N TYR B 171
SHEET 1 AA8 8 GLU D 40 TRP D 43 0
SHEET 2 AA8 8 ASP D 29 ASP D 35 -1 N HIS D 33 O VAL D 42
SHEET 3 AA8 8 SER D 19 PHE D 26 -1 N PHE D 26 O ASP D 29
SHEET 4 AA8 8 HIS D 5 ASN D 15 -1 N ILE D 8 O ASP D 25
SHEET 5 AA8 8 PHE E 7 PHE E 18 -1 O PHE E 17 N HIS D 5
SHEET 6 AA8 8 ARG E 23 HIS E 32 -1 O PHE E 31 N TYR E 10
SHEET 7 AA8 8 GLU E 35 ASP E 41 -1 O PHE E 40 N GLU E 28
SHEET 8 AA8 8 TYR E 47 ALA E 49 -1 O ARG E 48 N ARG E 39
SHEET 1 AA9 4 GLU D 88 THR D 93 0
SHEET 2 AA9 4 ASN D 103 PHE D 112 -1 O ILE D 106 N LEU D 92
SHEET 3 AA9 4 PHE D 145 PHE D 153 -1 O LEU D 151 N LEU D 105
SHEET 4 AA9 4 SER D 133 GLU D 134 -1 N SER D 133 O TYR D 150
SHEET 1 AB1 4 GLU D 88 THR D 93 0
SHEET 2 AB1 4 ASN D 103 PHE D 112 -1 O ILE D 106 N LEU D 92
SHEET 3 AB1 4 PHE D 145 PHE D 153 -1 O LEU D 151 N LEU D 105
SHEET 4 AB1 4 LEU D 138 PRO D 139 -1 N LEU D 138 O ARG D 146
SHEET 1 AB2 4 LYS D 126 VAL D 128 0
SHEET 2 AB2 4 ASN D 118 ARG D 123 -1 N ARG D 123 O LYS D 126
SHEET 3 AB2 4 TYR D 161 GLU D 166 -1 O ARG D 164 N THR D 120
SHEET 4 AB2 4 LEU D 174 TRP D 178 -1 O TRP D 178 N TYR D 161
SHEET 1 AB3 4 LYS E 98 SER E 104 0
SHEET 2 AB3 4 LEU E 114 PHE E 122 -1 O VAL E 116 N TYR E 102
SHEET 3 AB3 4 PHE E 155 GLU E 162 -1 O LEU E 161 N LEU E 115
SHEET 4 AB3 4 VAL E 142 SER E 144 -1 N VAL E 143 O MET E 160
SHEET 1 AB4 4 LYS E 98 SER E 104 0
SHEET 2 AB4 4 LEU E 114 PHE E 122 -1 O VAL E 116 N TYR E 102
SHEET 3 AB4 4 PHE E 155 GLU E 162 -1 O LEU E 161 N LEU E 115
SHEET 4 AB4 4 ILE E 148 HIS E 149 -1 N ILE E 148 O GLN E 156
SHEET 1 AB5 4 GLN E 136 GLU E 138 0
SHEET 2 AB5 4 GLU E 128 ARG E 133 -1 N TRP E 131 O GLU E 138
SHEET 3 AB5 4 VAL E 170 GLU E 176 -1 O GLN E 174 N ARG E 130
SHEET 4 AB5 4 LEU E 184 ARG E 189 -1 O TRP E 188 N TYR E 171
SSBOND 1 CYS A 107 CYS A 163 1555 1555 2.03
SSBOND 2 CYS B 15 CYS B 79 1555 1555 2.05
SSBOND 3 CYS B 117 CYS B 173 1555 1555 2.02
SSBOND 4 CYS D 107 CYS D 163 1555 1555 2.03
SSBOND 5 CYS E 15 CYS E 79 1555 1555 2.06
SSBOND 6 CYS E 117 CYS E 173 1555 1555 2.04
LINK ND2 ASN A 78 C1 NAG A 500 1555 1555 1.45
LINK ND2 ASN A 118 C1 NAG G 1 1555 1555 1.44
LINK ND2 ASN D 78 C1 NAG D 500 1555 1555 1.45
LINK ND2 ASN D 118 C1 NAG H 1 1555 1555 1.43
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.43
CISPEP 1 ASN A 15 PRO A 16 0 2.03
CISPEP 2 THR A 113 PRO A 114 0 0.32
CISPEP 3 TYR B 123 PRO B 124 0 4.77
CISPEP 4 ASN D 15 PRO D 16 0 1.91
CISPEP 5 THR D 113 PRO D 114 0 -0.35
CISPEP 6 TYR E 123 PRO E 124 0 4.06
CRYST1 66.980 77.770 94.540 90.00 109.52 90.00 P 1 21 1 4
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 0.014930 0.000000 0.005293 0.00000
SCALE2 0.000000 0.012858 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011223 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
