HEADER IMMUNE SYSTEM 04-DEC-13 4NUX
TITLE STRUCTURE OF RECEPTOR A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-17 RECEPTOR A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEFIR DOMAIN (UNP RESIDUES 376-591);
COMPND 5 SYNONYM: IL-17 RECEPTOR A, IL-17RA, CDW217;
COMPND 6 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: IL17RA, IL17R;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SEFIR DOMAIN, IMMUNE SYSTEM, CYTOKINE, RECEPTOR, AUTOIMMUNE
KEYWDS 2 INFLAMMATORY
EXPDTA X-RAY DIFFRACTION
AUTHOR B.ZHANG,Y.HAN,J.DENG
REVDAT 3 28-FEB-24 4NUX 1 REMARK
REVDAT 2 24-SEP-14 4NUX 1 JRNL
REVDAT 1 14-MAY-14 4NUX 0
JRNL AUTH B.ZHANG,C.LIU,W.QIAN,Y.HAN,X.LI,J.DENG
JRNL TITL STRUCTURE OF THE UNIQUE SEFIR DOMAIN FROM HUMAN INTERLEUKIN
JRNL TITL 2 17 RECEPTOR A REVEALS A COMPOSITE LIGAND-BINDING SITE
JRNL TITL 3 CONTAINING A CONSERVED ALPHA-HELIX FOR ACT1 BINDING AND
JRNL TITL 4 IL-17 SIGNALING.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 1476 2014
JRNL REFN ISSN 0907-4449
JRNL PMID 24816115
JRNL DOI 10.1107/S1399004714005227
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6_289)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.26
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.260
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 3 NUMBER OF REFLECTIONS : 12124
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1220
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 33.2680 - 4.7688 0.99 1402 158 0.1781 0.2152
REMARK 3 2 4.7688 - 3.7868 0.98 1320 149 0.1476 0.1824
REMARK 3 3 3.7868 - 3.3086 0.98 1293 146 0.1745 0.2226
REMARK 3 4 3.3086 - 3.0064 0.96 1285 134 0.1924 0.2663
REMARK 3 5 3.0064 - 2.7910 0.94 1236 141 0.2201 0.2895
REMARK 3 6 2.7910 - 2.6265 0.90 1189 126 0.2161 0.2943
REMARK 3 7 2.6265 - 2.4950 0.89 1168 134 0.2101 0.2833
REMARK 3 8 2.4950 - 2.3864 0.84 1083 130 0.2223 0.3048
REMARK 3 9 2.3864 - 2.2946 0.71 928 102 0.2404 0.3113
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 39.58
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.780
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) : 9.40700
REMARK 3 B22 (A**2) : -3.30920
REMARK 3 B33 (A**2) : -6.09790
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.008 1612
REMARK 3 ANGLE : 1.066 2183
REMARK 3 CHIRALITY : 0.073 233
REMARK 3 PLANARITY : 0.004 283
REMARK 3 DIHEDRAL : 16.285 586
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 376:381)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.2656 54.3339 27.6504
REMARK 3 T TENSOR
REMARK 3 T11: 0.4058 T22: 0.2352
REMARK 3 T33: 0.2659 T12: 0.1371
REMARK 3 T13: -0.1719 T23: 0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 2.2169 L22: 4.0827
REMARK 3 L33: 0.5637 L12: -0.2651
REMARK 3 L13: 0.6756 L23: -1.2924
REMARK 3 S TENSOR
REMARK 3 S11: -0.5499 S12: 0.2440 S13: 0.1826
REMARK 3 S21: -0.2648 S22: 0.4409 S23: -0.1042
REMARK 3 S31: -0.1389 S32: -0.4146 S33: 0.0810
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 382:396)
REMARK 3 ORIGIN FOR THE GROUP (A): 49.8295 44.7101 39.1276
REMARK 3 T TENSOR
REMARK 3 T11: 0.2025 T22: 0.2380
REMARK 3 T33: 0.1097 T12: 0.0286
REMARK 3 T13: 0.0153 T23: 0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 2.0154 L22: 1.1714
REMARK 3 L33: 0.0021 L12: 0.5861
REMARK 3 L13: 0.0416 L23: 0.1385
REMARK 3 S TENSOR
REMARK 3 S11: 0.1936 S12: -0.3139 S13: 0.0909
REMARK 3 S21: 0.0253 S22: -0.3115 S23: -0.1535
REMARK 3 S31: 0.2864 S32: 0.1623 S33: 0.0238
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 397:414)
REMARK 3 ORIGIN FOR THE GROUP (A): 41.9579 54.1829 36.5390
REMARK 3 T TENSOR
REMARK 3 T11: 0.1390 T22: 0.1005
REMARK 3 T33: 0.1087 T12: 0.0688
REMARK 3 T13: 0.0078 T23: -0.0404
REMARK 3 L TENSOR
REMARK 3 L11: 1.4406 L22: 1.5949
REMARK 3 L33: 2.0264 L12: 0.5079
REMARK 3 L13: 0.3513 L23: 1.6809
REMARK 3 S TENSOR
REMARK 3 S11: 0.2001 S12: -0.1984 S13: 0.2894
REMARK 3 S21: 0.4806 S22: -0.2503 S23: 0.3958
REMARK 3 S31: 0.2135 S32: -0.2771 S33: -0.0091
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 415:425)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.8016 37.7007 34.7849
REMARK 3 T TENSOR
REMARK 3 T11: 0.3052 T22: 0.5798
REMARK 3 T33: 0.4080 T12: -0.0561
REMARK 3 T13: -0.0429 T23: 0.0330
REMARK 3 L TENSOR
REMARK 3 L11: 2.4788 L22: 2.1001
REMARK 3 L33: 4.2862 L12: -1.1506
REMARK 3 L13: -2.2369 L23: -0.5945
REMARK 3 S TENSOR
REMARK 3 S11: -0.3766 S12: -0.8684 S13: 0.1199
REMARK 3 S21: 0.3742 S22: -0.0732 S23: 0.2263
REMARK 3 S31: 0.0523 S32: -1.3368 S33: 0.3929
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 426:434)
REMARK 3 ORIGIN FOR THE GROUP (A): 37.3202 40.5098 25.1182
REMARK 3 T TENSOR
REMARK 3 T11: 0.1998 T22: 0.4711
REMARK 3 T33: 0.2982 T12: 0.0387
REMARK 3 T13: -0.1376 T23: -0.0338
REMARK 3 L TENSOR
REMARK 3 L11: 5.4377 L22: 6.2409
REMARK 3 L33: 2.0730 L12: 0.0284
REMARK 3 L13: -1.4783 L23: -3.1559
REMARK 3 S TENSOR
REMARK 3 S11: -0.3574 S12: 1.0535 S13: -0.8172
REMARK 3 S21: -0.0938 S22: 0.6699 S23: 0.2491
REMARK 3 S31: 0.4438 S32: -0.7925 S33: -0.5711
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 435:445)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.3637 50.7336 22.6003
REMARK 3 T TENSOR
REMARK 3 T11: 0.4822 T22: 0.2384
REMARK 3 T33: 0.2187 T12: 0.0839
REMARK 3 T13: -0.0342 T23: 0.0565
REMARK 3 L TENSOR
REMARK 3 L11: 1.1752 L22: 2.1085
REMARK 3 L33: 1.1895 L12: 0.9672
REMARK 3 L13: 0.2352 L23: 1.2024
REMARK 3 S TENSOR
REMARK 3 S11: -0.5945 S12: 0.0503 S13: 0.1377
REMARK 3 S21: -0.5728 S22: 0.4421 S23: 0.1992
REMARK 3 S31: -0.7821 S32: -0.3089 S33: 0.1977
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 446:460)
REMARK 3 ORIGIN FOR THE GROUP (A): 57.2081 38.2146 28.6682
REMARK 3 T TENSOR
REMARK 3 T11: 0.1586 T22: 0.1458
REMARK 3 T33: 0.2064 T12: 0.0057
REMARK 3 T13: 0.0661 T23: -0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 3.6211 L22: 0.4766
REMARK 3 L33: 1.9046 L12: 0.4964
REMARK 3 L13: -0.0860 L23: -0.6140
REMARK 3 S TENSOR
REMARK 3 S11: 0.0623 S12: -0.3524 S13: -0.4594
REMARK 3 S21: -0.0362 S22: 0.1202 S23: -0.4857
REMARK 3 S31: 0.3280 S32: 0.0559 S33: -0.0542
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 461:467)
REMARK 3 ORIGIN FOR THE GROUP (A): 56.4978 30.1506 31.9596
REMARK 3 T TENSOR
REMARK 3 T11: 0.1876 T22: 0.1502
REMARK 3 T33: 0.2336 T12: 0.1247
REMARK 3 T13: 0.0199 T23: -0.0671
REMARK 3 L TENSOR
REMARK 3 L11: 5.4235 L22: 0.5908
REMARK 3 L33: 7.3039 L12: -1.2888
REMARK 3 L13: 1.7251 L23: 0.2655
REMARK 3 S TENSOR
REMARK 3 S11: 0.2496 S12: -0.5921 S13: -1.4537
REMARK 3 S21: 0.0821 S22: -0.2700 S23: 0.2325
REMARK 3 S31: 0.6211 S32: -0.1223 S33: 0.3338
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN A AND RESID 468:478)
REMARK 3 ORIGIN FOR THE GROUP (A): 48.3645 34.8782 37.6886
REMARK 3 T TENSOR
REMARK 3 T11: 0.2444 T22: 0.2082
REMARK 3 T33: 0.2198 T12: 0.0151
REMARK 3 T13: -0.0483 T23: 0.0522
REMARK 3 L TENSOR
REMARK 3 L11: 3.3515 L22: 6.8858
REMARK 3 L33: 2.8889 L12: -1.4038
REMARK 3 L13: 0.2882 L23: -2.7616
REMARK 3 S TENSOR
REMARK 3 S11: 0.4790 S12: 0.4205 S13: -0.1843
REMARK 3 S21: 0.3344 S22: -0.0141 S23: 0.1427
REMARK 3 S31: 0.1576 S32: 0.0252 S33: -0.3475
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN A AND RESID 479:493)
REMARK 3 ORIGIN FOR THE GROUP (A): 48.2834 40.9343 19.1642
REMARK 3 T TENSOR
REMARK 3 T11: 0.2514 T22: 0.2579
REMARK 3 T33: 0.1238 T12: 0.0822
REMARK 3 T13: -0.0341 T23: -0.0347
REMARK 3 L TENSOR
REMARK 3 L11: 1.5226 L22: 1.4081
REMARK 3 L33: 2.3197 L12: -0.0328
REMARK 3 L13: -1.2415 L23: 1.4291
REMARK 3 S TENSOR
REMARK 3 S11: 0.2767 S12: 0.4600 S13: -0.3148
REMARK 3 S21: 0.0054 S22: -0.1493 S23: -0.2961
REMARK 3 S31: -0.5377 S32: -0.3142 S33: -0.0344
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN A AND RESID 494:507)
REMARK 3 ORIGIN FOR THE GROUP (A): 52.9383 51.0465 26.4911
REMARK 3 T TENSOR
REMARK 3 T11: 0.1842 T22: 0.1250
REMARK 3 T33: 0.1854 T12: 0.0468
REMARK 3 T13: -0.0130 T23: -0.0240
REMARK 3 L TENSOR
REMARK 3 L11: 1.4453 L22: 1.8928
REMARK 3 L33: 2.3718 L12: 1.6969
REMARK 3 L13: 1.3946 L23: 1.3451
REMARK 3 S TENSOR
REMARK 3 S11: -0.2194 S12: 0.2120 S13: 0.1728
REMARK 3 S21: -0.3934 S22: 0.1255 S23: -0.1765
REMARK 3 S31: -0.4357 S32: 0.3074 S33: 0.1189
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN A AND RESID 508:517)
REMARK 3 ORIGIN FOR THE GROUP (A): 59.2946 45.1478 26.2744
REMARK 3 T TENSOR
REMARK 3 T11: 0.1788 T22: 0.2068
REMARK 3 T33: 0.2666 T12: 0.0909
REMARK 3 T13: -0.0053 T23: -0.0490
REMARK 3 L TENSOR
REMARK 3 L11: 1.5096 L22: 3.7017
REMARK 3 L33: 1.4083 L12: -0.4224
REMARK 3 L13: -1.2383 L23: 0.0341
REMARK 3 S TENSOR
REMARK 3 S11: 0.2304 S12: 0.0635 S13: -0.0412
REMARK 3 S21: -0.3375 S22: -0.6506 S23: 0.1187
REMARK 3 S31: -0.0262 S32: 0.5425 S33: 0.3379
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN A AND RESID 518:529)
REMARK 3 ORIGIN FOR THE GROUP (A): 56.5141 55.9925 27.7180
REMARK 3 T TENSOR
REMARK 3 T11: 0.3362 T22: 0.2993
REMARK 3 T33: 0.2100 T12: 0.0220
REMARK 3 T13: 0.1209 T23: 0.1415
REMARK 3 L TENSOR
REMARK 3 L11: 1.6142 L22: 1.3769
REMARK 3 L33: 5.9372 L12: -0.8796
REMARK 3 L13: 1.6175 L23: 0.2414
REMARK 3 S TENSOR
REMARK 3 S11: -0.4698 S12: 0.3575 S13: 0.2568
REMARK 3 S21: -0.0124 S22: -0.4768 S23: -0.3123
REMARK 3 S31: -0.1733 S32: 0.7644 S33: 0.5268
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN A AND RESID 530:534)
REMARK 3 ORIGIN FOR THE GROUP (A): 50.2476 62.8143 27.3409
REMARK 3 T TENSOR
REMARK 3 T11: 0.8505 T22: 0.1528
REMARK 3 T33: 0.2953 T12: 0.0489
REMARK 3 T13: 0.0247 T23: 0.0633
REMARK 3 L TENSOR
REMARK 3 L11: 4.0389 L22: 5.2992
REMARK 3 L33: 8.3099 L12: 1.8691
REMARK 3 L13: 2.7180 L23: 3.8848
REMARK 3 S TENSOR
REMARK 3 S11: 0.0604 S12: -0.0757 S13: 0.7664
REMARK 3 S21: -0.9305 S22: -1.0394 S23: -0.3633
REMARK 3 S31: -2.1923 S32: -0.1212 S33: 0.7330
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN A AND RESID 535:539)
REMARK 3 ORIGIN FOR THE GROUP (A): 44.8814 61.1834 23.4223
REMARK 3 T TENSOR
REMARK 3 T11: 0.3675 T22: 0.2071
REMARK 3 T33: 0.2565 T12: 0.0468
REMARK 3 T13: 0.1066 T23: 0.0686
REMARK 3 L TENSOR
REMARK 3 L11: 3.6659 L22: 0.6443
REMARK 3 L33: 9.8303 L12: 0.1979
REMARK 3 L13: -3.2961 L23: -0.6056
REMARK 3 S TENSOR
REMARK 3 S11: -0.5098 S12: 0.3917 S13: -0.2321
REMARK 3 S21: -0.7089 S22: -0.1033 S23: -0.5082
REMARK 3 S31: 0.4630 S32: -0.5267 S33: 0.5863
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN A AND RESID 540:560)
REMARK 3 ORIGIN FOR THE GROUP (A): 52.5260 65.6303 36.9091
REMARK 3 T TENSOR
REMARK 3 T11: 0.3704 T22: -0.0247
REMARK 3 T33: 0.3359 T12: -0.0360
REMARK 3 T13: 0.1148 T23: -0.0648
REMARK 3 L TENSOR
REMARK 3 L11: 2.8603 L22: 4.4087
REMARK 3 L33: 2.1874 L12: 0.2291
REMARK 3 L13: -0.2054 L23: 1.5766
REMARK 3 S TENSOR
REMARK 3 S11: 0.4271 S12: -0.6036 S13: 0.6123
REMARK 3 S21: 0.6854 S22: -0.2363 S23: -1.1140
REMARK 3 S31: 0.5589 S32: 0.3946 S33: -0.4851
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN A AND RESID 561:576)
REMARK 3 ORIGIN FOR THE GROUP (A): 53.7165 55.1098 45.1963
REMARK 3 T TENSOR
REMARK 3 T11: 0.2768 T22: 0.2087
REMARK 3 T33: 0.1070 T12: -0.0621
REMARK 3 T13: -0.0652 T23: -0.0426
REMARK 3 L TENSOR
REMARK 3 L11: 1.8244 L22: 1.8564
REMARK 3 L33: 1.8252 L12: -0.2391
REMARK 3 L13: 1.3542 L23: -1.2856
REMARK 3 S TENSOR
REMARK 3 S11: -0.1884 S12: -0.4791 S13: 0.5524
REMARK 3 S21: 0.8965 S22: 0.0181 S23: -0.4164
REMARK 3 S31: -0.6268 S32: -0.0391 S33: 0.3362
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN A AND RESID 577:582)
REMARK 3 ORIGIN FOR THE GROUP (A): 62.8093 42.9893 47.9093
REMARK 3 T TENSOR
REMARK 3 T11: 0.2742 T22: 0.3083
REMARK 3 T33: 0.2528 T12: -0.0961
REMARK 3 T13: -0.1464 T23: 0.0674
REMARK 3 L TENSOR
REMARK 3 L11: 9.2244 L22: 5.1160
REMARK 3 L33: 4.0150 L12: 6.6720
REMARK 3 L13: -6.0730 L23: -4.3102
REMARK 3 S TENSOR
REMARK 3 S11: 0.7888 S12: -0.4729 S13: 0.2064
REMARK 3 S21: 1.2402 S22: -0.2650 S23: 0.4634
REMARK 3 S31: 0.1863 S32: 0.0052 S33: -0.3308
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN A AND RESID 583:586)
REMARK 3 ORIGIN FOR THE GROUP (A): 61.1949 37.0771 41.6224
REMARK 3 T TENSOR
REMARK 3 T11: 0.3401 T22: 0.2900
REMARK 3 T33: 0.3169 T12: 0.0623
REMARK 3 T13: 0.0785 T23: -0.0370
REMARK 3 L TENSOR
REMARK 3 L11: 7.5492 L22: 4.8976
REMARK 3 L33: 4.1421 L12: -4.4085
REMARK 3 L13: -3.0786 L23: 4.3806
REMARK 3 S TENSOR
REMARK 3 S11: 0.5745 S12: -0.5337 S13: -0.1536
REMARK 3 S21: -0.8185 S22: 1.0662 S23: -0.8728
REMARK 3 S31: -0.1217 S32: 0.7197 S33: -1.3322
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN A AND RESID 587:591)
REMARK 3 ORIGIN FOR THE GROUP (A): 56.2648 29.6189 40.8538
REMARK 3 T TENSOR
REMARK 3 T11: 0.3985 T22: 0.2017
REMARK 3 T33: 0.1948 T12: -0.0274
REMARK 3 T13: -0.0456 T23: 0.0816
REMARK 3 L TENSOR
REMARK 3 L11: 3.2021 L22: 7.7099
REMARK 3 L33: 4.3592 L12: -2.2727
REMARK 3 L13: -1.1178 L23: 5.7027
REMARK 3 S TENSOR
REMARK 3 S11: 0.4734 S12: 0.3923 S13: 0.6435
REMARK 3 S21: 0.9636 S22: -0.5551 S23: -0.9653
REMARK 3 S31: 1.6836 S32: -0.3599 S33: 0.3398
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 4NUX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1000083686.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13104
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.300
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 5%PEG6000, PH 6.0,
REMARK 280 EVAPORATION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 27.71650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 27.71650
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 38.12800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 68.06500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 38.12800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 68.06500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 27.71650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 38.12800
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 68.06500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 27.71650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 38.12800
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 68.06500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 HIS A 471
REMARK 465 GLY A 472
REMARK 465 LYS A 473
REMARK 465 PRO A 474
REMARK 465 VAL A 475
REMARK 465 GLY A 476
REMARK 465 MET A 541
REMARK 465 PHE A 542
REMARK 465 GLN A 543
REMARK 465 PRO A 544
REMARK 465 GLY A 545
REMARK 465 ARG A 546
REMARK 465 MET A 547
REMARK 465 HIS A 548
REMARK 465 ARG A 549
REMARK 465 VAL A 550
REMARK 465 GLY A 551
REMARK 465 GLU A 552
REMARK 465 LEU A 553
REMARK 465 SER A 554
REMARK 465 GLY A 555
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 376 CG CD CE NZ
REMARK 480 GLN A 418 CG
REMARK 480 ARG A 431 NE CZ NH1 NH2
REMARK 480 ARG A 466 NE CZ NH1 NH2
REMARK 480 LYS A 491 CE NZ
REMARK 480 ALA A 519 CB
REMARK 480 ASP A 527 OD1 OD2
REMARK 480 ARG A 528 NE CZ NH1 NH2
REMARK 480 PHE A 534 CD2 CE2 CZ
REMARK 480 ARG A 560 CG CD NE CZ NH1 NH2
REMARK 480 ARG A 565 CD NE CZ NH1 NH2
REMARK 480 ARG A 580 CG CD NE CZ NH1 NH2
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 HIS A 388 149.25 179.31
REMARK 500 ASP A 538 71.22 59.24
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4NUX A 376 591 UNP Q96F46 I17RA_HUMAN 376 591
SEQRES 1 A 216 LYS PRO ARG LYS VAL TRP ILE ILE TYR SER ALA ASP HIS
SEQRES 2 A 216 PRO LEU TYR VAL ASP VAL VAL LEU LYS PHE ALA GLN PHE
SEQRES 3 A 216 LEU LEU THR ALA CYS GLY THR GLU VAL ALA LEU ASP LEU
SEQRES 4 A 216 LEU GLU GLU GLN ALA ILE SER GLU ALA GLY VAL MET THR
SEQRES 5 A 216 TRP VAL GLY ARG GLN LYS GLN GLU MET VAL GLU SER ASN
SEQRES 6 A 216 SER LYS ILE ILE VAL LEU CYS SER ARG GLY THR ARG ALA
SEQRES 7 A 216 LYS TRP GLN ALA LEU LEU GLY ARG GLY ALA PRO VAL ARG
SEQRES 8 A 216 LEU ARG CYS ASP HIS GLY LYS PRO VAL GLY ASP LEU PHE
SEQRES 9 A 216 THR ALA ALA MET ASN MET ILE LEU PRO ASP PHE LYS ARG
SEQRES 10 A 216 PRO ALA CYS PHE GLY THR TYR VAL VAL CYS TYR PHE SER
SEQRES 11 A 216 GLU VAL SER CYS ASP GLY ASP VAL PRO ASP LEU PHE GLY
SEQRES 12 A 216 ALA ALA PRO ARG TYR PRO LEU MET ASP ARG PHE GLU GLU
SEQRES 13 A 216 VAL TYR PHE ARG ILE GLN ASP LEU GLU MET PHE GLN PRO
SEQRES 14 A 216 GLY ARG MET HIS ARG VAL GLY GLU LEU SER GLY ASP ASN
SEQRES 15 A 216 TYR LEU ARG SER PRO GLY GLY ARG GLN LEU ARG ALA ALA
SEQRES 16 A 216 LEU ASP ARG PHE ARG ASP TRP GLN VAL ARG CYS PRO ASP
SEQRES 17 A 216 TRP PHE GLU CYS GLU ASN LEU TYR
FORMUL 2 HOH *54(H2 O)
HELIX 1 1 HIS A 388 GLY A 407 1 20
HELIX 2 2 LEU A 412 LEU A 415 5 4
HELIX 3 3 GLU A 416 ALA A 423 1 8
HELIX 4 4 GLY A 424 SER A 439 1 16
HELIX 5 5 SER A 448 LEU A 459 1 12
HELIX 6 6 LEU A 478 LEU A 487 1 10
HELIX 7 7 PRO A 488 GLY A 497 5 10
HELIX 8 8 CYS A 509 VAL A 513 5 5
HELIX 9 9 ARG A 528 ASP A 538 1 11
HELIX 10 10 ASP A 556 SER A 561 5 6
HELIX 11 11 GLY A 563 CYS A 581 1 19
HELIX 12 12 ASP A 583 ASN A 589 1 7
SHEET 1 A 5 GLU A 409 ALA A 411 0
SHEET 2 A 5 LYS A 379 ILE A 383 1 N VAL A 380 O ALA A 411
SHEET 3 A 5 LYS A 442 LEU A 446 1 O LEU A 446 N ILE A 383
SHEET 4 A 5 TYR A 499 PHE A 504 1 O VAL A 500 N ILE A 443
SHEET 5 A 5 ARG A 522 LEU A 525 1 O TYR A 523 N VAL A 501
CISPEP 1 LEU A 525 MET A 526 0 5.34
CRYST1 76.256 136.130 55.433 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013114 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007346 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018040 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
