HEADER IMMUNE SYSTEM 29-AUG-17 6ATI
TITLE HLA-DRB1*1402 IN COMPLEX WITH VIMENTIN-64CIT59-71
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: VIMENTIN-64CIT59-71;
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: HOMO SAPIENS;
SOURCE 18 ORGANISM_TAXID: 9606
KEYWDS HLA CLASS II, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.W.SCALLY,Y.T.TING,J.ROSSJOHN
REVDAT 3 29-JUL-20 6ATI 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE
REVDAT 2 18-OCT-17 6ATI 1 JRNL
REVDAT 1 13-SEP-17 6ATI 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. 1.98 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) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.63
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 63283
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 3210
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 33.6339 - 5.6225 1.00 2701 140 0.1970 0.2289
REMARK 3 2 5.6225 - 4.4660 1.00 2662 144 0.1483 0.1799
REMARK 3 3 4.4660 - 3.9025 1.00 2633 142 0.1426 0.1631
REMARK 3 4 3.9025 - 3.5461 1.00 2622 152 0.1731 0.2332
REMARK 3 5 3.5461 - 3.2921 1.00 2618 135 0.1632 0.1937
REMARK 3 6 3.2921 - 3.0982 1.00 2647 120 0.1753 0.2171
REMARK 3 7 3.0982 - 2.9431 1.00 2619 155 0.1788 0.2187
REMARK 3 8 2.9431 - 2.8151 1.00 2616 147 0.1836 0.2126
REMARK 3 9 2.8151 - 2.7068 1.00 2619 128 0.1796 0.2500
REMARK 3 10 2.7068 - 2.6134 1.00 2622 127 0.1955 0.2262
REMARK 3 11 2.6134 - 2.5317 1.00 2621 166 0.1877 0.2501
REMARK 3 12 2.5317 - 2.4594 1.00 2600 138 0.1857 0.2432
REMARK 3 13 2.4594 - 2.3946 1.00 2618 132 0.1859 0.2075
REMARK 3 14 2.3946 - 2.3362 1.00 2628 126 0.1922 0.2404
REMARK 3 15 2.3362 - 2.2831 1.00 2614 161 0.1951 0.2289
REMARK 3 16 2.2831 - 2.2345 0.97 2505 134 0.3747 0.4297
REMARK 3 17 2.2345 - 2.1899 0.99 2580 147 0.2393 0.3019
REMARK 3 18 2.1899 - 2.1485 1.00 2632 131 0.1906 0.2387
REMARK 3 19 2.1485 - 2.1102 1.00 2610 131 0.1878 0.2346
REMARK 3 20 2.1102 - 2.0744 1.00 2599 138 0.2186 0.2558
REMARK 3 21 2.0744 - 2.0410 0.99 2569 150 0.2827 0.3482
REMARK 3 22 2.0410 - 2.0096 1.00 2605 130 0.1946 0.2485
REMARK 3 23 2.0096 - 1.9800 0.98 2533 136 0.1876 0.2390
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) : 21.760
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 6524
REMARK 3 ANGLE : 0.885 8869
REMARK 3 CHIRALITY : 0.037 962
REMARK 3 PLANARITY : 0.004 1157
REMARK 3 DIHEDRAL : 13.169 2361
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 23
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.1055 0.0061 112.7153
REMARK 3 T TENSOR
REMARK 3 T11: 0.0940 T22: 0.0738
REMARK 3 T33: 0.1067 T12: 0.0157
REMARK 3 T13: 0.0088 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 1.0601 L22: 0.3307
REMARK 3 L33: 1.7576 L12: 0.5490
REMARK 3 L13: -0.4381 L23: -0.4602
REMARK 3 S TENSOR
REMARK 3 S11: 0.0394 S12: 0.0338 S13: 0.1473
REMARK 3 S21: 0.0831 S22: 0.0376 S23: 0.0784
REMARK 3 S31: -0.1454 S32: 0.0555 S33: -0.0285
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 46 THROUGH 55 )
REMARK 3 ORIGIN FOR THE GROUP (A): -40.1083 7.2113 101.0186
REMARK 3 T TENSOR
REMARK 3 T11: 0.1742 T22: 0.2154
REMARK 3 T33: 0.2479 T12: 0.0813
REMARK 3 T13: -0.0184 T23: 0.1246
REMARK 3 L TENSOR
REMARK 3 L11: 1.6214 L22: 2.0511
REMARK 3 L33: 1.6874 L12: -1.0774
REMARK 3 L13: 0.4411 L23: -0.1976
REMARK 3 S TENSOR
REMARK 3 S11: 0.0726 S12: 0.3706 S13: 0.5190
REMARK 3 S21: -0.1447 S22: -0.0724 S23: -0.3187
REMARK 3 S31: -0.2394 S32: -0.0609 S33: 0.1490
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 56 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.6192 -4.2995 123.9769
REMARK 3 T TENSOR
REMARK 3 T11: 0.1417 T22: 0.1111
REMARK 3 T33: 0.1118 T12: 0.0087
REMARK 3 T13: 0.0203 T23: -0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 1.3389 L22: 2.0693
REMARK 3 L33: 3.1321 L12: 0.1147
REMARK 3 L13: -0.0295 L23: -1.5868
REMARK 3 S TENSOR
REMARK 3 S11: 0.0443 S12: -0.1279 S13: 0.2040
REMARK 3 S21: 0.0411 S22: -0.0227 S23: 0.2471
REMARK 3 S31: -0.0903 S32: -0.2264 S33: 0.0107
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 77 THROUGH 87 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.9023 -10.3020 132.5161
REMARK 3 T TENSOR
REMARK 3 T11: 0.1071 T22: 0.0799
REMARK 3 T33: 0.1074 T12: 0.0200
REMARK 3 T13: 0.0114 T23: 0.0391
REMARK 3 L TENSOR
REMARK 3 L11: 3.7487 L22: 0.1097
REMARK 3 L33: 1.3465 L12: 0.2969
REMARK 3 L13: -1.7582 L23: 0.0340
REMARK 3 S TENSOR
REMARK 3 S11: 0.0380 S12: -0.1741 S13: -0.0169
REMARK 3 S21: 0.1214 S22: -0.0828 S23: -0.0705
REMARK 3 S31: 0.0162 S32: -0.0185 S33: 0.0608
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 88 THROUGH 102 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.2881 5.5619 109.7946
REMARK 3 T TENSOR
REMARK 3 T11: 0.1780 T22: 0.2295
REMARK 3 T33: 0.1968 T12: -0.0506
REMARK 3 T13: 0.0052 T23: -0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 1.6303 L22: 1.6740
REMARK 3 L33: 2.7188 L12: 0.1052
REMARK 3 L13: -0.2951 L23: -0.4611
REMARK 3 S TENSOR
REMARK 3 S11: -0.2772 S12: 0.2325 S13: 0.1583
REMARK 3 S21: -0.3603 S22: 0.1990 S23: -0.2100
REMARK 3 S31: -0.0540 S32: 0.1384 S33: 0.0270
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 123 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8871 2.4495 120.1782
REMARK 3 T TENSOR
REMARK 3 T11: 0.1242 T22: 0.0698
REMARK 3 T33: 0.0938 T12: -0.0026
REMARK 3 T13: -0.0132 T23: 0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 1.0525 L22: 0.5915
REMARK 3 L33: 1.0058 L12: 0.6464
REMARK 3 L13: -0.5121 L23: -0.4106
REMARK 3 S TENSOR
REMARK 3 S11: -0.0199 S12: -0.0017 S13: 0.0657
REMARK 3 S21: 0.0314 S22: -0.0114 S23: 0.0117
REMARK 3 S31: -0.0520 S32: 0.0630 S33: 0.0271
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 124 THROUGH 144 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.2238 2.7544 118.2998
REMARK 3 T TENSOR
REMARK 3 T11: 0.1171 T22: 0.0748
REMARK 3 T33: 0.1206 T12: -0.0005
REMARK 3 T13: -0.0012 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 1.2908 L22: 0.4500
REMARK 3 L33: 1.0630 L12: 0.2149
REMARK 3 L13: 0.5796 L23: 0.1418
REMARK 3 S TENSOR
REMARK 3 S11: -0.1334 S12: 0.1818 S13: 0.0619
REMARK 3 S21: -0.0922 S22: 0.0531 S23: 0.2542
REMARK 3 S31: -0.1557 S32: 0.0770 S33: 0.0559
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 145 THROUGH 160 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.3963 7.4127 115.0413
REMARK 3 T TENSOR
REMARK 3 T11: 0.1855 T22: 0.1157
REMARK 3 T33: 0.1390 T12: -0.0380
REMARK 3 T13: 0.0065 T23: -0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 0.8149 L22: 0.7299
REMARK 3 L33: 1.1378 L12: -0.2380
REMARK 3 L13: -0.3490 L23: -0.1756
REMARK 3 S TENSOR
REMARK 3 S11: 0.0479 S12: -0.0359 S13: 0.2284
REMARK 3 S21: 0.0591 S22: 0.0233 S23: -0.1054
REMARK 3 S31: -0.1586 S32: 0.1467 S33: -0.0405
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 161 THROUGH 181 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.2846 2.4545 124.6195
REMARK 3 T TENSOR
REMARK 3 T11: 0.1590 T22: 0.1919
REMARK 3 T33: 0.1144 T12: -0.0447
REMARK 3 T13: -0.0162 T23: -0.0276
REMARK 3 L TENSOR
REMARK 3 L11: 1.2209 L22: 1.2878
REMARK 3 L33: 0.6121 L12: 0.7242
REMARK 3 L13: 0.0406 L23: -0.3983
REMARK 3 S TENSOR
REMARK 3 S11: 0.1493 S12: -0.4512 S13: 0.0488
REMARK 3 S21: 0.1154 S22: -0.1451 S23: -0.0727
REMARK 3 S31: -0.0203 S32: 0.3462 S33: 0.0453
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.3219 -13.5975 112.5581
REMARK 3 T TENSOR
REMARK 3 T11: 0.0729 T22: 0.0969
REMARK 3 T33: 0.0901 T12: 0.0151
REMARK 3 T13: 0.0029 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 0.9556 L22: 0.7149
REMARK 3 L33: 0.8842 L12: 0.3476
REMARK 3 L13: -0.2031 L23: -0.0802
REMARK 3 S TENSOR
REMARK 3 S11: -0.0308 S12: 0.1379 S13: 0.0098
REMARK 3 S21: -0.0127 S22: 0.0333 S23: 0.0519
REMARK 3 S31: 0.1303 S32: -0.0778 S33: -0.0151
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 90 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.3379 -6.6536 98.9496
REMARK 3 T TENSOR
REMARK 3 T11: 0.1061 T22: 0.1318
REMARK 3 T33: 0.1295 T12: -0.0038
REMARK 3 T13: 0.0049 T23: 0.0343
REMARK 3 L TENSOR
REMARK 3 L11: 1.8735 L22: 0.8244
REMARK 3 L33: 1.0063 L12: -0.7327
REMARK 3 L13: -0.2218 L23: -0.1591
REMARK 3 S TENSOR
REMARK 3 S11: 0.0368 S12: 0.2373 S13: 0.0625
REMARK 3 S21: -0.0579 S22: -0.1065 S23: -0.1742
REMARK 3 S31: 0.0568 S32: 0.1365 S33: 0.0516
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 3 THROUGH 55 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8496 -40.0802 110.3617
REMARK 3 T TENSOR
REMARK 3 T11: 0.1012 T22: 0.0892
REMARK 3 T33: 0.1459 T12: 0.0229
REMARK 3 T13: -0.0082 T23: -0.0280
REMARK 3 L TENSOR
REMARK 3 L11: 1.4373 L22: 0.6418
REMARK 3 L33: 2.0256 L12: 0.2181
REMARK 3 L13: 0.1504 L23: 0.1513
REMARK 3 S TENSOR
REMARK 3 S11: -0.0056 S12: 0.1523 S13: -0.2378
REMARK 3 S21: -0.0720 S22: -0.0218 S23: -0.1166
REMARK 3 S31: 0.2906 S32: 0.0777 S33: 0.0570
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 56 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.6161 -34.3416 123.8958
REMARK 3 T TENSOR
REMARK 3 T11: 0.1357 T22: 0.1374
REMARK 3 T33: 0.1557 T12: 0.0216
REMARK 3 T13: -0.0162 T23: 0.0495
REMARK 3 L TENSOR
REMARK 3 L11: 1.1336 L22: 2.2615
REMARK 3 L33: 3.2639 L12: 0.1667
REMARK 3 L13: 0.0828 L23: 1.8958
REMARK 3 S TENSOR
REMARK 3 S11: 0.0411 S12: -0.1111 S13: -0.2400
REMARK 3 S21: 0.0386 S22: -0.0917 S23: -0.1988
REMARK 3 S31: 0.0729 S32: 0.1866 S33: 0.0306
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 77 THROUGH 101 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.7578 -37.0848 119.5760
REMARK 3 T TENSOR
REMARK 3 T11: 0.1160 T22: 0.1060
REMARK 3 T33: 0.0879 T12: -0.0006
REMARK 3 T13: 0.0189 T23: 0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 1.9550 L22: 0.8391
REMARK 3 L33: 1.5047 L12: 0.5270
REMARK 3 L13: 1.0954 L23: 0.2577
REMARK 3 S TENSOR
REMARK 3 S11: -0.1291 S12: 0.0804 S13: 0.1266
REMARK 3 S21: -0.0746 S22: 0.0415 S23: 0.1824
REMARK 3 S31: 0.0767 S32: -0.0735 S33: 0.0517
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 102 THROUGH 154 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.2048 -41.9362 117.8734
REMARK 3 T TENSOR
REMARK 3 T11: 0.1173 T22: 0.0645
REMARK 3 T33: 0.1146 T12: 0.0063
REMARK 3 T13: 0.0051 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 1.0780 L22: 0.3308
REMARK 3 L33: 0.9524 L12: 0.1048
REMARK 3 L13: -0.0142 L23: 0.3008
REMARK 3 S TENSOR
REMARK 3 S11: -0.0009 S12: 0.0326 S13: -0.0363
REMARK 3 S21: 0.0105 S22: -0.0327 S23: -0.1229
REMARK 3 S31: 0.1015 S32: -0.0479 S33: 0.0273
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 155 THROUGH 181 )
REMARK 3 ORIGIN FOR THE GROUP (A): -47.6717 -42.9924 122.8989
REMARK 3 T TENSOR
REMARK 3 T11: 0.1434 T22: 0.1671
REMARK 3 T33: 0.1565 T12: -0.0460
REMARK 3 T13: 0.0191 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 3.0422 L22: 1.4579
REMARK 3 L33: 2.1115 L12: 1.4022
REMARK 3 L13: 1.6402 L23: 1.0444
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: -0.5027 S13: 0.0202
REMARK 3 S21: 0.0713 S22: -0.2030 S23: 0.1865
REMARK 3 S31: 0.1213 S32: -0.5320 S33: 0.1296
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 2 THROUGH 32 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.9535 -27.2585 114.2080
REMARK 3 T TENSOR
REMARK 3 T11: 0.0921 T22: 0.0953
REMARK 3 T33: 0.1056 T12: 0.0177
REMARK 3 T13: -0.0099 T23: 0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 0.9737 L22: 0.5663
REMARK 3 L33: 2.3452 L12: 0.1607
REMARK 3 L13: 0.0599 L23: -0.1730
REMARK 3 S TENSOR
REMARK 3 S11: 0.0034 S12: 0.0336 S13: -0.0019
REMARK 3 S21: -0.0051 S22: 0.1266 S23: -0.0142
REMARK 3 S31: -0.0512 S32: -0.2503 S33: -0.1994
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 33 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7610 -23.5691 111.7220
REMARK 3 T TENSOR
REMARK 3 T11: 0.0766 T22: 0.0828
REMARK 3 T33: 0.0790 T12: 0.0078
REMARK 3 T13: -0.0008 T23: 0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 1.2665 L22: 0.7371
REMARK 3 L33: 0.8395 L12: 0.2545
REMARK 3 L13: -0.0905 L23: -0.2140
REMARK 3 S TENSOR
REMARK 3 S11: -0.0688 S12: 0.0939 S13: 0.0101
REMARK 3 S21: 0.0268 S22: 0.0228 S23: -0.0076
REMARK 3 S31: -0.1127 S32: 0.1237 S33: 0.0472
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 90 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): -51.6550 -33.5556 100.1849
REMARK 3 T TENSOR
REMARK 3 T11: 0.1213 T22: 0.1347
REMARK 3 T33: 0.0931 T12: -0.0144
REMARK 3 T13: 0.0071 T23: -0.0386
REMARK 3 L TENSOR
REMARK 3 L11: 2.1178 L22: 1.1892
REMARK 3 L33: 1.0283 L12: -0.7685
REMARK 3 L13: 0.0397 L23: 0.3110
REMARK 3 S TENSOR
REMARK 3 S11: -0.0680 S12: -0.1150 S13: -0.0156
REMARK 3 S21: 0.0828 S22: 0.0058 S23: 0.1413
REMARK 3 S31: -0.0031 S32: -0.0298 S33: 0.0349
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 134 THROUGH 162 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.9790 -29.8886 102.5154
REMARK 3 T TENSOR
REMARK 3 T11: 0.1029 T22: 0.1233
REMARK 3 T33: 0.1137 T12: -0.0065
REMARK 3 T13: 0.0046 T23: -0.0193
REMARK 3 L TENSOR
REMARK 3 L11: 1.8836 L22: 0.8480
REMARK 3 L33: 0.6673 L12: -0.3793
REMARK 3 L13: -0.1227 L23: 0.2887
REMARK 3 S TENSOR
REMARK 3 S11: 0.0762 S12: 0.1408 S13: 0.0386
REMARK 3 S21: -0.1110 S22: -0.1050 S23: 0.1181
REMARK 3 S31: -0.0657 S32: -0.1314 S33: -0.0045
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 163 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): -57.2397 -31.3381 92.9271
REMARK 3 T TENSOR
REMARK 3 T11: 0.1473 T22: 0.2531
REMARK 3 T33: 0.1291 T12: -0.0138
REMARK 3 T13: -0.0106 T23: -0.0690
REMARK 3 L TENSOR
REMARK 3 L11: 1.3338 L22: 0.3668
REMARK 3 L33: 0.5863 L12: -0.5521
REMARK 3 L13: -0.5260 L23: 0.3233
REMARK 3 S TENSOR
REMARK 3 S11: 0.0631 S12: 0.7307 S13: -0.1565
REMARK 3 S21: -0.1221 S22: -0.1095 S23: 0.1805
REMARK 3 S31: -0.0275 S32: -0.3288 S33: 0.0770
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 13 )
REMARK 3 ORIGIN FOR THE GROUP (A): -51.1724 -6.3076 114.0171
REMARK 3 T TENSOR
REMARK 3 T11: 0.0786 T22: 0.0924
REMARK 3 T33: 0.1510 T12: 0.0466
REMARK 3 T13: 0.0115 T23: 0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 1.0497 L22: 2.0754
REMARK 3 L33: 2.0453 L12: 0.5181
REMARK 3 L13: -0.1655 L23: -0.7793
REMARK 3 S TENSOR
REMARK 3 S11: 0.0399 S12: 0.0948 S13: 0.1921
REMARK 3 S21: 0.1281 S22: -0.0540 S23: 0.3626
REMARK 3 S31: -0.1746 S32: -0.1802 S33: -0.3828
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1 THROUGH 13 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.0340 -32.3731 113.9223
REMARK 3 T TENSOR
REMARK 3 T11: 0.1316 T22: 0.1010
REMARK 3 T33: 0.1471 T12: 0.0367
REMARK 3 T13: -0.0286 T23: -0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 0.6058 L22: 1.5213
REMARK 3 L33: 2.4202 L12: 0.7781
REMARK 3 L13: 0.5392 L23: 1.6993
REMARK 3 S TENSOR
REMARK 3 S11: -0.0059 S12: 0.0463 S13: -0.1206
REMARK 3 S21: 0.1929 S22: -0.0009 S23: -0.2377
REMARK 3 S31: 0.2619 S32: 0.1569 S33: -0.0290
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 6ATI 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_1000229814.
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 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63444
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 33.629
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
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 : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
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 : 4.300
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 (%): 52.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
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 38.43500
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: 7960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: 7910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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 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 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 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 B 52 CG CD OE1 OE2
REMARK 470 ARG B 55 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 109 CG CD1 CD2
REMARK 470 GLU D 158 CG CD OE1 OE2
REMARK 470 LEU E 109 CG CD1 CD2
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 HOH A 788 O HOH E 306 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 GLN B 34 -2.27 72.67
REMARK 500 THR B 90 -70.58 -125.13
REMARK 500 HIS B 112 100.05 -59.00
REMARK 500 GLN E 34 -0.04 73.59
REMARK 500 THR E 90 -71.36 -124.33
REMARK 500 HIS E 112 99.92 -58.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 400 DISTANCE = 6.35 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6ATF RELATED DB: PDB
DBREF 6ATI A 1 181 UNP P01903 DRA_HUMAN 26 206
DBREF1 6ATI B 1 190 UNP A0A0A1I7H6_HUMAN
DBREF2 6ATI B A0A0A1I7H6 30 219
DBREF 6ATI D 1 181 UNP P01903 DRA_HUMAN 26 206
DBREF1 6ATI E 1 190 UNP A0A0A1I7H6_HUMAN
DBREF2 6ATI E A0A0A1I7H6 30 219
DBREF 6ATI C 1 13 PDB 6ATI 6ATI 1 13
DBREF 6ATI F 1 13 PDB 6ATI 6ATI 1 13
SEQADV 6ATI THR A 182 UNP P01903 EXPRESSION TAG
SEQADV 6ATI SER A 183 UNP P01903 EXPRESSION TAG
SEQADV 6ATI GLY A 184 UNP P01903 EXPRESSION TAG
SEQADV 6ATI ASP A 185 UNP P01903 EXPRESSION TAG
SEQADV 6ATI ASP A 186 UNP P01903 EXPRESSION TAG
SEQADV 6ATI ASP A 187 UNP P01903 EXPRESSION TAG
SEQADV 6ATI ASP A 188 UNP P01903 EXPRESSION TAG
SEQADV 6ATI LYS A 189 UNP P01903 EXPRESSION TAG
SEQADV 6ATI GLY B -1 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATI SER B 0 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATI THR B 191 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATI GLY B 192 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATI GLY B 193 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATI ASP B 194 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATI ASP B 195 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATI ASP B 196 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATI ASP B 197 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATI LYS B 198 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATI THR D 182 UNP P01903 EXPRESSION TAG
SEQADV 6ATI SER D 183 UNP P01903 EXPRESSION TAG
SEQADV 6ATI GLY D 184 UNP P01903 EXPRESSION TAG
SEQADV 6ATI ASP D 185 UNP P01903 EXPRESSION TAG
SEQADV 6ATI ASP D 186 UNP P01903 EXPRESSION TAG
SEQADV 6ATI ASP D 187 UNP P01903 EXPRESSION TAG
SEQADV 6ATI ASP D 188 UNP P01903 EXPRESSION TAG
SEQADV 6ATI LYS D 189 UNP P01903 EXPRESSION TAG
SEQADV 6ATI GLY E -1 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATI SER E 0 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATI THR E 191 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATI GLY E 192 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATI GLY E 193 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATI ASP E 194 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATI ASP E 195 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATI ASP E 196 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATI ASP E 197 UNP A0A0A1I7H EXPRESSION TAG
SEQADV 6ATI 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 CIR SER SER ALA VAL ARG LEU ARG
SEQRES 1 F 13 GLY VAL TYR ALA THR CIR SER SER ALA VAL ARG LEU ARG
HET CIR C 6 11
HET CIR F 6 11
HET NAG A 500 14
HET NAG A 501 14
HET NAG D 500 14
HET NAG D 501 14
HETNAM CIR CITRULLINE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
FORMUL 5 CIR 2(C6 H13 N3 O3)
FORMUL 7 NAG 4(C8 H15 N O6)
FORMUL 11 HOH *896(H2 O)
HELIX 1 AA1 GLU A 47 ALA A 52 1 6
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 GLU D 47 ALA D 52 1 6
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 CYS B 15 N ILE A 7
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 2 SER A 53 PHE A 54 0
SHEET 2 AA2 2 VAL C 2 TYR C 3 1 O TYR C 3 N SER A 53
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 LEU A 151 N LEU A 105
SHEET 4 AA3 4 SER A 133 GLU A 134 -1 N SER A 133 O TYR A 150
SHEET 1 AA4 4 GLU A 88 THR A 93 0
SHEET 2 AA4 4 ASN A 103 PHE A 112 -1 O ILE A 106 N LEU A 92
SHEET 3 AA4 4 PHE A 145 PHE A 153 -1 O LEU A 151 N LEU A 105
SHEET 4 AA4 4 LEU A 138 PRO A 139 -1 N LEU A 138 O ARG A 146
SHEET 1 AA5 4 LYS A 126 VAL A 128 0
SHEET 2 AA5 4 ASN A 118 ARG A 123 -1 N ARG A 123 O LYS A 126
SHEET 3 AA5 4 TYR A 161 GLU A 166 -1 O ARG A 164 N THR A 120
SHEET 4 AA5 4 LEU A 174 TRP A 178 -1 O TRP A 178 N TYR A 161
SHEET 1 AA6 4 LYS B 98 SER B 104 0
SHEET 2 AA6 4 LEU B 114 PHE B 122 -1 O LEU B 114 N SER B 104
SHEET 3 AA6 4 PHE B 155 GLU B 162 -1 O THR B 157 N VAL B 119
SHEET 4 AA6 4 VAL B 142 SER B 144 -1 N VAL B 143 O MET B 160
SHEET 1 AA7 4 LYS B 98 SER B 104 0
SHEET 2 AA7 4 LEU B 114 PHE B 122 -1 O LEU B 114 N SER B 104
SHEET 3 AA7 4 PHE B 155 GLU B 162 -1 O THR B 157 N VAL B 119
SHEET 4 AA7 4 ILE B 148 HIS B 149 -1 N ILE B 148 O GLN B 156
SHEET 1 AA8 4 GLN B 136 GLU B 138 0
SHEET 2 AA8 4 GLU B 128 ARG B 133 -1 N TRP B 131 O GLU B 138
SHEET 3 AA8 4 VAL B 170 GLU B 176 -1 O GLN B 174 N ARG B 130
SHEET 4 AA8 4 LEU B 184 ARG B 189 -1 O LEU B 184 N VAL B 175
SHEET 1 AA9 8 GLU D 40 TRP D 43 0
SHEET 2 AA9 8 ASP D 29 ASP D 35 -1 N HIS D 33 O VAL D 42
SHEET 3 AA9 8 SER D 19 PHE D 26 -1 N PHE D 26 O ASP D 29
SHEET 4 AA9 8 HIS D 5 ASN D 15 -1 N ILE D 8 O ASP D 25
SHEET 5 AA9 8 PHE E 7 PHE E 18 -1 O PHE E 17 N HIS D 5
SHEET 6 AA9 8 ARG E 23 HIS E 32 -1 O LEU E 27 N GLU E 14
SHEET 7 AA9 8 GLU E 35 ASP E 41 -1 O PHE E 40 N GLU E 28
SHEET 8 AA9 8 TYR E 47 ALA E 49 -1 O ARG E 48 N ARG E 39
SHEET 1 AB1 2 SER D 53 PHE D 54 0
SHEET 2 AB1 2 VAL F 2 TYR F 3 1 O TYR F 3 N SER D 53
SHEET 1 AB2 4 GLU D 88 THR D 93 0
SHEET 2 AB2 4 ASN D 103 PHE D 112 -1 O ILE D 106 N LEU D 92
SHEET 3 AB2 4 PHE D 145 PHE D 153 -1 O LEU D 151 N LEU D 105
SHEET 4 AB2 4 SER D 133 GLU D 134 -1 N SER D 133 O TYR D 150
SHEET 1 AB3 4 GLU D 88 THR D 93 0
SHEET 2 AB3 4 ASN D 103 PHE D 112 -1 O ILE D 106 N LEU D 92
SHEET 3 AB3 4 PHE D 145 PHE D 153 -1 O LEU D 151 N LEU D 105
SHEET 4 AB3 4 LEU D 138 PRO D 139 -1 N LEU D 138 O ARG D 146
SHEET 1 AB4 4 LYS D 126 VAL D 128 0
SHEET 2 AB4 4 ASN D 118 ARG D 123 -1 N ARG D 123 O LYS D 126
SHEET 3 AB4 4 TYR D 161 GLU D 166 -1 O ARG D 164 N THR D 120
SHEET 4 AB4 4 LEU D 174 TRP D 178 -1 O TRP D 178 N TYR D 161
SHEET 1 AB5 4 LYS E 98 SER E 104 0
SHEET 2 AB5 4 LEU E 114 PHE E 122 -1 O LEU E 114 N SER E 104
SHEET 3 AB5 4 PHE E 155 GLU E 162 -1 O THR E 157 N VAL E 119
SHEET 4 AB5 4 VAL E 142 SER E 144 -1 N VAL E 143 O MET E 160
SHEET 1 AB6 4 LYS E 98 SER E 104 0
SHEET 2 AB6 4 LEU E 114 PHE E 122 -1 O LEU E 114 N SER E 104
SHEET 3 AB6 4 PHE E 155 GLU E 162 -1 O THR E 157 N VAL E 119
SHEET 4 AB6 4 ILE E 148 HIS E 149 -1 N ILE E 148 O GLN E 156
SHEET 1 AB7 4 GLN E 136 GLU E 138 0
SHEET 2 AB7 4 GLU E 128 ARG E 133 -1 N TRP E 131 O GLU E 138
SHEET 3 AB7 4 VAL E 170 GLU E 176 -1 O GLN E 174 N ARG E 130
SHEET 4 AB7 4 LEU E 184 ARG E 189 -1 O LEU E 184 N VAL E 175
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 2.03
SSBOND 4 CYS D 107 CYS D 163 1555 1555 2.04
SSBOND 5 CYS E 15 CYS E 79 1555 1555 2.04
SSBOND 6 CYS E 117 CYS E 173 1555 1555 2.02
LINK ND2 ASN A 78 C1 NAG A 500 1555 1555 1.45
LINK ND2 ASN A 118 C1 NAG A 501 1555 1555 1.44
LINK ND2 ASN D 78 C1 NAG D 500 1555 1555 1.44
LINK ND2 ASN D 118 C1 NAG D 501 1555 1555 1.44
LINK C THR C 5 N2 CIR C 6 1555 1555 1.43
LINK C1 CIR C 6 N SER C 7 1555 1555 1.43
LINK C THR F 5 N2 CIR F 6 1555 1555 1.43
LINK C1 CIR F 6 N SER F 7 1555 1555 1.43
CISPEP 1 ASN A 15 PRO A 16 0 2.20
CISPEP 2 THR A 113 PRO A 114 0 -1.15
CISPEP 3 TYR B 123 PRO B 124 0 3.51
CISPEP 4 ASN D 15 PRO D 16 0 2.40
CISPEP 5 THR D 113 PRO D 114 0 -0.50
CISPEP 6 TYR E 123 PRO E 124 0 2.99
CRYST1 67.270 76.870 94.910 90.00 109.68 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 0.014865 0.000000 0.005317 0.00000
SCALE2 0.000000 0.013009 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011190 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
