HEADER IMMUNE SYSTEM/VIRAL PROTEIN 11-NOV-09 2WY3
TITLE STRUCTURE OF THE HCMV UL16-MICB COMPLEX ELUCIDATES SELECT BINDING OF A
TITLE 2 VIRAL IMMUNOEVASIN TO DIVERSE NKG2D LIGANDS
CAVEAT 2WY3 NAG B 1202 HAS WRONG CHIRALITY AT ATOM C1 NAG D 1202 HAS
CAVEAT 2 2WY3 WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MHC CLASS I POLYPEPTIDE-RELATED SEQUENCE B;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: MHC CLASS I HOMOLOG DOMAIN, RESIDUES 24-341;
COMPND 5 SYNONYM: MHC CLASS I POLYPEPTIDE-RELATED SEQUENCE B ALLELE 002, MIC-
COMPND 6 B;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: UNCHARACTERIZED PROTEIN UL16;
COMPND 10 CHAIN: B, D;
COMPND 11 FRAGMENT: RESIDUES 27-184;
COMPND 12 SYNONYM: UL16;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: LUNG;
SOURCE 6 CELL: FIBROBLAST;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21A;
SOURCE 11 OTHER_DETAILS: CDNA OF ALLELE 002 WAS ISOLATED FROM A IMR90 HUMAN
SOURCE 12 LUNG FIBROBLAST LIBRARY;
SOURCE 13 MOL_ID: 2;
SOURCE 14 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 5 STRAIN AD169;
SOURCE 15 ORGANISM_TAXID: 10360;
SOURCE 16 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 17 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 19 EXPRESSION_SYSTEM_CELL_LINE: CHO LEC 3.2.8.1;
SOURCE 20 EXPRESSION_SYSTEM_ORGAN: OVARY;
SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1(-);
SOURCE 22 OTHER_DETAILS: CDNA ISOLATED FROM HCMV STRAIN AD169 GENOME.
KEYWDS IMMUNE SYSTEM-VIRAL PROTEIN COMPLEX, IMMUNE RESPONSE, INNATE
KEYWDS 2 IMMUNITY, STRUCTURAL MIMICRY, IMMUNOGLOBULIN DOMAIN, MEMBRANE,
KEYWDS 3 CYTOLYSIS, ULBP, NKG2D, NK CELL, CELL MEMBRANE, TRANSMEMBRANE, VIRAL
KEYWDS 4 IMMUNE EVASION, NATURAL KILLER CELL, CONVERGENT EVOLUTION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MUELLER,G.ZOCHER,A.STEINLE,T.STEHLE
REVDAT 4 20-DEC-23 2WY3 1 HETSYN
REVDAT 3 29-JUL-20 2WY3 1 CAVEAT COMPND REMARK HETNAM
REVDAT 3 2 1 LINK SITE
REVDAT 2 18-JUN-14 2WY3 1 REMARK VERSN
REVDAT 1 02-FEB-10 2WY3 0
JRNL AUTH S.MULLER,G.ZOCHER,A.STEINLE,T.STEHLE
JRNL TITL STRUCTURE OF THE HCMV UL16-MICB COMPLEX ELUCIDATES SELECT
JRNL TITL 2 BINDING OF A VIRAL IMMUNOEVASIN TO DIVERSE NKG2D LIGANDS.
JRNL REF PLOS PATHOG. V. 6 723 2010
JRNL REFN ISSN 1553-7366
JRNL PMID 20090832
JRNL DOI 10.1371/JOURNAL.PPAT.1000723
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 82271
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4114
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.1051 - 5.5276 0.99 2958 156 0.2309 0.2350
REMARK 3 2 5.5276 - 4.3883 1.00 2799 147 0.1522 0.2027
REMARK 3 3 4.3883 - 3.8339 1.00 2776 147 0.1449 0.1644
REMARK 3 4 3.8339 - 3.4834 0.99 2759 145 0.1451 0.1821
REMARK 3 5 3.4834 - 3.2338 0.99 2733 144 0.1554 0.1996
REMARK 3 6 3.2338 - 3.0432 0.99 2738 144 0.1700 0.1920
REMARK 3 7 3.0432 - 2.8908 1.00 2732 144 0.1807 0.2421
REMARK 3 8 2.8908 - 2.7650 0.99 2718 143 0.1732 0.2300
REMARK 3 9 2.7650 - 2.6585 0.99 2715 143 0.1745 0.2021
REMARK 3 10 2.6585 - 2.5668 0.99 2715 142 0.1766 0.2182
REMARK 3 11 2.5668 - 2.4865 0.99 2693 142 0.1665 0.1864
REMARK 3 12 2.4865 - 2.4155 0.99 2679 141 0.1692 0.2266
REMARK 3 13 2.4155 - 2.3519 0.99 2702 142 0.1695 0.2313
REMARK 3 14 2.3519 - 2.2945 0.99 2690 142 0.1682 0.2216
REMARK 3 15 2.2945 - 2.2423 0.99 2687 141 0.1601 0.2209
REMARK 3 16 2.2423 - 2.1946 0.99 2664 141 0.1616 0.1731
REMARK 3 17 2.1946 - 2.1507 0.99 2673 140 0.1538 0.2003
REMARK 3 18 2.1507 - 2.1101 0.99 2690 142 0.1597 0.1805
REMARK 3 19 2.1101 - 2.0724 0.98 2630 138 0.1659 0.2082
REMARK 3 20 2.0724 - 2.0373 0.99 2684 142 0.1599 0.2124
REMARK 3 21 2.0373 - 2.0045 0.99 2635 138 0.1673 0.1906
REMARK 3 22 2.0045 - 1.9736 0.98 2658 140 0.1727 0.2516
REMARK 3 23 1.9736 - 1.9446 0.98 2628 138 0.1788 0.2068
REMARK 3 24 1.9446 - 1.9172 0.98 2681 141 0.1843 0.2592
REMARK 3 25 1.9172 - 1.8913 0.98 2610 138 0.1844 0.2307
REMARK 3 26 1.8913 - 1.8667 0.97 2615 138 0.1961 0.2275
REMARK 3 27 1.8667 - 1.8434 0.98 2657 139 0.1948 0.2260
REMARK 3 28 1.8434 - 1.8212 0.97 2613 138 0.1983 0.2357
REMARK 3 29 1.8212 - 1.8000 0.98 2625 138 0.2116 0.2195
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 : 0.38
REMARK 3 B_SOL : 56.52
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.020
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.06
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.64470
REMARK 3 B22 (A**2) : -0.56170
REMARK 3 B33 (A**2) : -4.08300
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 : 0.006 5481
REMARK 3 ANGLE : 1.057 7451
REMARK 3 CHIRALITY : 0.077 846
REMARK 3 PLANARITY : 0.004 942
REMARK 3 DIHEDRAL : 14.769 2086
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 26
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 1:25)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4489 48.7049 89.1082
REMARK 3 T TENSOR
REMARK 3 T11: 0.2910 T22: 0.1848
REMARK 3 T33: 0.1416 T12: 0.0002
REMARK 3 T13: -0.0236 T23: -0.0401
REMARK 3 L TENSOR
REMARK 3 L11: 2.6889 L22: 0.3071
REMARK 3 L33: 2.0066 L12: 0.5430
REMARK 3 L13: 1.1172 L23: 0.8275
REMARK 3 S TENSOR
REMARK 3 S11: -0.0071 S12: 0.3072 S13: -0.3937
REMARK 3 S21: -0.1792 S22: 0.2416 S23: -0.1812
REMARK 3 S31: 0.2872 S32: 0.2566 S33: -0.2466
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 26:84)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6056 49.1065 96.4055
REMARK 3 T TENSOR
REMARK 3 T11: 0.2270 T22: 0.1062
REMARK 3 T33: 0.1276 T12: 0.0376
REMARK 3 T13: -0.0194 T23: -0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 1.7158 L22: 1.0711
REMARK 3 L33: 3.2354 L12: 0.6443
REMARK 3 L13: 0.3632 L23: 0.8814
REMARK 3 S TENSOR
REMARK 3 S11: 0.1127 S12: -0.0365 S13: -0.0434
REMARK 3 S21: -0.0369 S22: 0.0196 S23: 0.0138
REMARK 3 S31: 0.2959 S32: 0.1234 S33: -0.1331
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 85:139)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6037 57.9598 81.2229
REMARK 3 T TENSOR
REMARK 3 T11: 0.3352 T22: 0.1199
REMARK 3 T33: 0.1256 T12: -0.0179
REMARK 3 T13: -0.0462 T23: -0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 0.9053 L22: 0.1138
REMARK 3 L33: 2.7137 L12: 0.1177
REMARK 3 L13: 1.2535 L23: 1.2403
REMARK 3 S TENSOR
REMARK 3 S11: 0.0040 S12: 0.0278 S13: -0.0015
REMARK 3 S21: -0.3286 S22: 0.0204 S23: 0.0247
REMARK 3 S31: -0.3991 S32: 0.0567 S33: -0.0195
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 140:148)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.3327 57.7851 83.7780
REMARK 3 T TENSOR
REMARK 3 T11: 0.7406 T22: 0.4647
REMARK 3 T33: 0.2017 T12: 0.3628
REMARK 3 T13: -0.0038 T23: -0.0303
REMARK 3 L TENSOR
REMARK 3 L11: 0.9883 L22: -0.1376
REMARK 3 L33: 4.7948 L12: -1.1732
REMARK 3 L13: -1.8183 L23: 7.8656
REMARK 3 S TENSOR
REMARK 3 S11: -0.8795 S12: -0.2022 S13: -0.1913
REMARK 3 S21: 0.6975 S22: 0.5164 S23: 0.5134
REMARK 3 S31: -0.6831 S32: 0.0351 S33: 0.2205
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 152:175)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.5165 64.1703 96.0208
REMARK 3 T TENSOR
REMARK 3 T11: 0.2243 T22: 0.2363
REMARK 3 T33: 0.1868 T12: -0.0281
REMARK 3 T13: -0.0163 T23: -0.0599
REMARK 3 L TENSOR
REMARK 3 L11: 1.7787 L22: 0.8048
REMARK 3 L33: 1.3362 L12: -0.8242
REMARK 3 L13: 0.7502 L23: 0.3966
REMARK 3 S TENSOR
REMARK 3 S11: 0.1100 S12: -0.1483 S13: -0.3218
REMARK 3 S21: -0.2959 S22: -0.0593 S23: 0.1335
REMARK 3 S31: 0.0038 S32: -0.2204 S33: 0.0195
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN C AND RESID 0:17)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0293 24.9910 89.3752
REMARK 3 T TENSOR
REMARK 3 T11: 0.2659 T22: 0.3123
REMARK 3 T33: 0.2121 T12: 0.1700
REMARK 3 T13: -0.0103 T23: 0.0330
REMARK 3 L TENSOR
REMARK 3 L11: 0.8528 L22: 5.6371
REMARK 3 L33: 3.0020 L12: -0.9767
REMARK 3 L13: 0.7748 L23: -2.5257
REMARK 3 S TENSOR
REMARK 3 S11: 0.4579 S12: 0.2689 S13: 0.0963
REMARK 3 S21: -0.5533 S22: -0.5374 S23: 0.4863
REMARK 3 S31: -0.0456 S32: -0.1266 S33: 0.0516
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN C AND RESID 18:37)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3254 27.2093 95.8164
REMARK 3 T TENSOR
REMARK 3 T11: 0.1633 T22: 0.1904
REMARK 3 T33: 0.1970 T12: 0.0874
REMARK 3 T13: -0.0132 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 0.5364 L22: 2.5880
REMARK 3 L33: 3.6097 L12: -0.8794
REMARK 3 L13: 0.9146 L23: -0.6453
REMARK 3 S TENSOR
REMARK 3 S11: 0.1770 S12: 0.0249 S13: 0.4123
REMARK 3 S21: 0.0046 S22: -0.1928 S23: 0.3923
REMARK 3 S31: -0.5289 S32: -0.4796 S33: -0.0549
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN C AND RESID 38:41)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4253 35.2518 94.4403
REMARK 3 T TENSOR
REMARK 3 T11: 0.6160 T22: 0.1847
REMARK 3 T33: 0.8759 T12: -0.1488
REMARK 3 T13: 0.0753 T23: 0.2391
REMARK 3 L TENSOR
REMARK 3 L11: 3.6356 L22: -2.7256
REMARK 3 L33: 4.8784 L12: -3.2351
REMARK 3 L13: -1.4392 L23: -1.9232
REMARK 3 S TENSOR
REMARK 3 S11: 0.3558 S12: 0.3628 S13: 2.6849
REMARK 3 S21: 0.7585 S22: 0.6545 S23: 1.8755
REMARK 3 S31: -1.5707 S32: 0.3584 S33: -0.9222
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN C AND RESID 42:90)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4023 25.0111 94.0344
REMARK 3 T TENSOR
REMARK 3 T11: 0.1639 T22: 0.1724
REMARK 3 T33: 0.1757 T12: 0.0431
REMARK 3 T13: -0.0088 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 3.4111 L22: 1.7014
REMARK 3 L33: -1.8151 L12: -1.1116
REMARK 3 L13: 0.9883 L23: -0.1746
REMARK 3 S TENSOR
REMARK 3 S11: 0.1756 S12: 0.1645 S13: 0.0134
REMARK 3 S21: -0.1504 S22: -0.1236 S23: 0.0769
REMARK 3 S31: -0.1028 S32: 0.1748 S33: -0.0407
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN C AND RESID 91:124)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.1375 14.6064 87.7950
REMARK 3 T TENSOR
REMARK 3 T11: 0.2492 T22: 0.3598
REMARK 3 T33: 0.3021 T12: 0.0385
REMARK 3 T13: -0.1084 T23: -0.0592
REMARK 3 L TENSOR
REMARK 3 L11: 2.0471 L22: 1.7466
REMARK 3 L33: 1.5146 L12: -2.1291
REMARK 3 L13: 0.4192 L23: -0.0066
REMARK 3 S TENSOR
REMARK 3 S11: 0.1946 S12: 0.3299 S13: -0.4139
REMARK 3 S21: -0.2586 S22: -0.2458 S23: 0.7389
REMARK 3 S31: 0.0468 S32: -0.6025 S33: 0.1070
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN C AND RESID 125:139)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6291 15.8069 74.7051
REMARK 3 T TENSOR
REMARK 3 T11: 0.5012 T22: 0.6976
REMARK 3 T33: 0.3326 T12: 0.1917
REMARK 3 T13: -0.2697 T23: -0.1037
REMARK 3 L TENSOR
REMARK 3 L11: 1.5930 L22: 0.6934
REMARK 3 L33: -0.6793 L12: 1.3145
REMARK 3 L13: -1.6339 L23: 0.8656
REMARK 3 S TENSOR
REMARK 3 S11: 0.1266 S12: 0.9610 S13: 0.0196
REMARK 3 S21: -0.7523 S22: 0.2010 S23: 0.3496
REMARK 3 S31: -0.5141 S32: -0.6253 S33: -0.1705
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN C AND RESID 140:156)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.3283 13.1639 76.4897
REMARK 3 T TENSOR
REMARK 3 T11: 0.8517 T22: 0.4663
REMARK 3 T33: 0.0869 T12: 0.2494
REMARK 3 T13: -0.0598 T23: -0.1307
REMARK 3 L TENSOR
REMARK 3 L11: 2.0057 L22: 2.8057
REMARK 3 L33: -5.4536 L12: 0.1444
REMARK 3 L13: 2.1082 L23: -2.6308
REMARK 3 S TENSOR
REMARK 3 S11: 0.4264 S12: 0.7846 S13: -0.6462
REMARK 3 S21: -1.6331 S22: -1.0616 S23: 0.0070
REMARK 3 S31: -0.0596 S32: 0.2664 S33: 0.4342
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN C AND RESID 157:175)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.0768 11.1848 98.0976
REMARK 3 T TENSOR
REMARK 3 T11: 0.1686 T22: 0.2404
REMARK 3 T33: 0.1899 T12: 0.0096
REMARK 3 T13: 0.0022 T23: 0.0273
REMARK 3 L TENSOR
REMARK 3 L11: 0.6801 L22: 1.9751
REMARK 3 L33: 1.5916 L12: -1.3575
REMARK 3 L13: -1.2753 L23: 0.9388
REMARK 3 S TENSOR
REMARK 3 S11: 0.1096 S12: 0.1558 S13: -0.0214
REMARK 3 S21: -0.0954 S22: -0.0911 S23: 0.2126
REMARK 3 S31: -0.1882 S32: -0.4081 S33: -0.0291
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN B AND RESID 27:42)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5299 76.0589 118.4574
REMARK 3 T TENSOR
REMARK 3 T11: 0.2270 T22: 0.3284
REMARK 3 T33: 0.2399 T12: 0.0293
REMARK 3 T13: 0.0668 T23: -0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 2.7475 L22: -0.0862
REMARK 3 L33: 0.3396 L12: -0.7001
REMARK 3 L13: 1.0779 L23: 0.7838
REMARK 3 S TENSOR
REMARK 3 S11: -0.1155 S12: -0.8508 S13: 0.1734
REMARK 3 S21: 0.0881 S22: 0.1047 S23: 0.2170
REMARK 3 S31: -0.2862 S32: -0.0314 S33: 0.0769
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN B AND RESID 43:55)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7058 72.6158 116.0115
REMARK 3 T TENSOR
REMARK 3 T11: 0.2091 T22: 0.1571
REMARK 3 T33: 0.1373 T12: -0.0350
REMARK 3 T13: -0.0110 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 2.0060 L22: 0.8513
REMARK 3 L33: -0.9697 L12: -0.5234
REMARK 3 L13: -0.4256 L23: -1.8134
REMARK 3 S TENSOR
REMARK 3 S11: -0.3002 S12: -0.2610 S13: -0.0905
REMARK 3 S21: 0.2179 S22: 0.2111 S23: -0.0387
REMARK 3 S31: 0.0046 S32: 0.2311 S33: 0.0946
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN B AND RESID 56:87)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3533 73.4336 108.1887
REMARK 3 T TENSOR
REMARK 3 T11: 0.1043 T22: 0.1263
REMARK 3 T33: 0.1578 T12: -0.0048
REMARK 3 T13: -0.0102 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 1.1717 L22: 1.3318
REMARK 3 L33: 1.0497 L12: 0.1319
REMARK 3 L13: 0.0080 L23: -0.1755
REMARK 3 S TENSOR
REMARK 3 S11: 0.0520 S12: 0.0392 S13: -0.0571
REMARK 3 S21: -0.0062 S22: -0.0222 S23: 0.1337
REMARK 3 S31: -0.1225 S32: -0.0754 S33: -0.0283
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN B AND RESID 88:115)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8959 76.3535 101.9661
REMARK 3 T TENSOR
REMARK 3 T11: 0.1398 T22: 0.1495
REMARK 3 T33: 0.1527 T12: 0.0066
REMARK 3 T13: -0.0452 T23: 0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 0.8391 L22: 1.5820
REMARK 3 L33: 2.3379 L12: -0.5023
REMARK 3 L13: 0.8989 L23: -0.1141
REMARK 3 S TENSOR
REMARK 3 S11: -0.1162 S12: 0.1655 S13: 0.1391
REMARK 3 S21: -0.2366 S22: 0.0734 S23: 0.3370
REMARK 3 S31: -0.3171 S32: -0.3017 S33: 0.0661
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN B AND RESID 116:134)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8806 69.4122 101.1327
REMARK 3 T TENSOR
REMARK 3 T11: 0.1843 T22: 0.1596
REMARK 3 T33: 0.1357 T12: -0.0401
REMARK 3 T13: -0.0019 T23: -0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 1.1902 L22: 0.7451
REMARK 3 L33: 0.3664 L12: 0.3190
REMARK 3 L13: 0.0733 L23: 0.3264
REMARK 3 S TENSOR
REMARK 3 S11: -0.1296 S12: 0.3278 S13: 0.0007
REMARK 3 S21: -0.2421 S22: 0.1854 S23: 0.0367
REMARK 3 S31: -0.0739 S32: -0.1077 S33: -0.0308
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN B AND RESID 135:156)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0727 72.8926 114.0179
REMARK 3 T TENSOR
REMARK 3 T11: 0.1313 T22: 0.1552
REMARK 3 T33: 0.1492 T12: -0.0207
REMARK 3 T13: 0.0202 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 1.4279 L22: 0.0718
REMARK 3 L33: 0.5308 L12: -1.4770
REMARK 3 L13: 1.2360 L23: 0.0422
REMARK 3 S TENSOR
REMARK 3 S11: -0.0967 S12: -0.3020 S13: -0.1796
REMARK 3 S21: 0.0297 S22: 0.0110 S23: 0.0321
REMARK 3 S31: -0.0350 S32: -0.1157 S33: 0.0730
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN B AND RESID 157:163)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.0469 73.3152 97.3377
REMARK 3 T TENSOR
REMARK 3 T11: 0.4953 T22: 0.3583
REMARK 3 T33: 0.3404 T12: -0.0097
REMARK 3 T13: 0.1599 T23: -0.0742
REMARK 3 L TENSOR
REMARK 3 L11: 2.6214 L22: 1.0766
REMARK 3 L33: 3.2589 L12: 0.7342
REMARK 3 L13: -4.7546 L23: 1.6973
REMARK 3 S TENSOR
REMARK 3 S11: -0.6843 S12: 0.6194 S13: -0.6603
REMARK 3 S21: -0.1881 S22: 0.0241 S23: -0.3250
REMARK 3 S31: 1.4227 S32: 0.0316 S33: 0.6826
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN D AND RESID 27:43)
REMARK 3 ORIGIN FOR THE GROUP (A): 49.8055 -0.9898 92.0453
REMARK 3 T TENSOR
REMARK 3 T11: 0.1074 T22: 0.3269
REMARK 3 T33: 0.2765 T12: 0.0431
REMARK 3 T13: 0.0495 T23: 0.0233
REMARK 3 L TENSOR
REMARK 3 L11: -2.9221 L22: 1.7600
REMARK 3 L33: 3.6676 L12: -1.6743
REMARK 3 L13: 1.9112 L23: -0.8058
REMARK 3 S TENSOR
REMARK 3 S11: 0.0929 S12: 0.0912 S13: 0.1656
REMARK 3 S21: -0.2869 S22: -0.0044 S23: -0.3762
REMARK 3 S31: 0.2301 S32: 0.9695 S33: -0.0586
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN D AND RESID 44:52)
REMARK 3 ORIGIN FOR THE GROUP (A): 42.4083 1.4841 105.5265
REMARK 3 T TENSOR
REMARK 3 T11: 0.2076 T22: 0.1714
REMARK 3 T33: 0.2382 T12: -0.0064
REMARK 3 T13: -0.0762 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.6731 L22: 1.5970
REMARK 3 L33: 0.8232 L12: -0.6486
REMARK 3 L13: -0.0478 L23: 0.9960
REMARK 3 S TENSOR
REMARK 3 S11: 0.0248 S12: -0.1876 S13: 0.1639
REMARK 3 S21: 0.1676 S22: 0.0881 S23: -0.6090
REMARK 3 S31: 0.2215 S32: 0.3354 S33: -0.0621
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN D AND RESID 53:84)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7048 3.2491 97.0874
REMARK 3 T TENSOR
REMARK 3 T11: 0.1510 T22: 0.0950
REMARK 3 T33: 0.1132 T12: -0.0019
REMARK 3 T13: 0.0342 T23: -0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.5326 L22: 0.6001
REMARK 3 L33: 1.2252 L12: 0.2778
REMARK 3 L13: -0.0207 L23: 0.3008
REMARK 3 S TENSOR
REMARK 3 S11: 0.0427 S12: -0.0078 S13: 0.0143
REMARK 3 S21: -0.0688 S22: 0.0313 S23: -0.0154
REMARK 3 S31: -0.0937 S32: -0.0316 S33: -0.0638
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN D AND RESID 85:110)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.8088 -3.9913 89.5712
REMARK 3 T TENSOR
REMARK 3 T11: 0.2053 T22: 0.0948
REMARK 3 T33: 0.1366 T12: -0.0243
REMARK 3 T13: 0.0153 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 1.1007 L22: 0.1575
REMARK 3 L33: 1.2993 L12: -0.0803
REMARK 3 L13: -0.4560 L23: -0.0435
REMARK 3 S TENSOR
REMARK 3 S11: -0.0221 S12: 0.0349 S13: -0.1870
REMARK 3 S21: -0.3151 S22: 0.0557 S23: -0.0466
REMARK 3 S31: 0.2766 S32: 0.0490 S33: -0.0196
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (CHAIN D AND RESID 111:117)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.5499 11.6383 85.8770
REMARK 3 T TENSOR
REMARK 3 T11: 0.1869 T22: 0.0954
REMARK 3 T33: 0.1038 T12: -0.0130
REMARK 3 T13: 0.0174 T23: 0.0231
REMARK 3 L TENSOR
REMARK 3 L11: 0.6846 L22: -0.3312
REMARK 3 L33: 4.9040 L12: -0.6137
REMARK 3 L13: -1.3456 L23: -3.3558
REMARK 3 S TENSOR
REMARK 3 S11: 0.2004 S12: 0.1406 S13: 0.1737
REMARK 3 S21: 0.0144 S22: -0.2273 S23: -0.0640
REMARK 3 S31: -0.5918 S32: -0.0893 S33: 0.0051
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: (CHAIN D AND RESID 118:159)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.5493 2.3663 98.0176
REMARK 3 T TENSOR
REMARK 3 T11: 0.0901 T22: 0.0774
REMARK 3 T33: 0.1036 T12: -0.0185
REMARK 3 T13: 0.0113 T23: 0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 0.4297 L22: 0.6788
REMARK 3 L33: 0.9761 L12: -0.5033
REMARK 3 L13: 0.1099 L23: 0.4571
REMARK 3 S TENSOR
REMARK 3 S11: 0.0421 S12: -0.0025 S13: -0.0179
REMARK 3 S21: -0.0310 S22: 0.0083 S23: -0.0205
REMARK 3 S31: 0.0462 S32: 0.0039 S33: -0.0483
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CHAIN A RESIDUES 149-151 AND 176- -181
REMARK 3 ARE DISORDERED. CHAIN B 164-184 ARE DISORDERED. CHAIN C RESIDUES
REMARK 3 148-149 AND 176-181 ARE DISORDERED. CHAIN D RESIDUES 160-184 ARE
REMARK 3 DISORDERED. MET0 IN CHAIN A IS NOT PART OF THE MATURE EUCARYOTIC
REMARK 3 MICB SEQUENCE BUT AN E.COLI ARTEFACT. MET140 IN CHAIN A AND
REMARK 3 CHAIN C WAS MODELLED AS AN ALANINE IN BOTH CASES
REMARK 4
REMARK 4 2WY3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-NOV-09.
REMARK 100 THE DEPOSITION ID IS D_1290039566.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-AUG-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0013
REMARK 200 MONOCHROMATOR : DCCM
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 82272
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.440
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 8.900
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.49000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.440
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1JE6
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M SODIUM
REMARK 280 CACODYLATE PH 6.5, 25 % PEG 8000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 29.06000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.40000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.08500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 73.40000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.06000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.08500
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 5.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A 149
REMARK 465 ALA A 150
REMARK 465 MET A 151
REMARK 465 VAL A 176
REMARK 465 ALA A 177
REMARK 465 ILE A 178
REMARK 465 ARG A 179
REMARK 465 ARG A 180
REMARK 465 THR A 181
REMARK 465 VAL A 182
REMARK 465 PRO A 183
REMARK 465 PRO A 184
REMARK 465 MET A 185
REMARK 465 VAL A 186
REMARK 465 ASN A 187
REMARK 465 VAL A 188
REMARK 465 THR A 189
REMARK 465 CYS A 190
REMARK 465 SER A 191
REMARK 465 GLU A 192
REMARK 465 VAL A 193
REMARK 465 SER A 194
REMARK 465 GLU A 195
REMARK 465 GLY A 196
REMARK 465 ASN A 197
REMARK 465 ILE A 198
REMARK 465 THR A 199
REMARK 465 VAL A 200
REMARK 465 THR A 201
REMARK 465 CYS A 202
REMARK 465 ARG A 203
REMARK 465 ALA A 204
REMARK 465 SER A 205
REMARK 465 SER A 206
REMARK 465 PHE A 207
REMARK 465 TYR A 208
REMARK 465 PRO A 209
REMARK 465 ARG A 210
REMARK 465 ASN A 211
REMARK 465 ILE A 212
REMARK 465 THR A 213
REMARK 465 LEU A 214
REMARK 465 THR A 215
REMARK 465 TRP A 216
REMARK 465 ARG A 217
REMARK 465 GLN A 218
REMARK 465 ASP A 219
REMARK 465 GLY A 220
REMARK 465 VAL A 221
REMARK 465 SER A 222
REMARK 465 LEU A 223
REMARK 465 SER A 224
REMARK 465 HIS A 225
REMARK 465 ASN A 226
REMARK 465 THR A 227
REMARK 465 GLN A 228
REMARK 465 GLN A 229
REMARK 465 TRP A 230
REMARK 465 GLY A 231
REMARK 465 ASP A 232
REMARK 465 VAL A 233
REMARK 465 LEU A 234
REMARK 465 PRO A 235
REMARK 465 ASP A 236
REMARK 465 GLY A 237
REMARK 465 ASN A 238
REMARK 465 GLY A 239
REMARK 465 THR A 240
REMARK 465 TYR A 241
REMARK 465 GLN A 242
REMARK 465 THR A 243
REMARK 465 TRP A 244
REMARK 465 VAL A 245
REMARK 465 ALA A 246
REMARK 465 THR A 247
REMARK 465 ARG A 248
REMARK 465 ILE A 249
REMARK 465 ARG A 250
REMARK 465 GLN A 251
REMARK 465 GLY A 252
REMARK 465 GLU A 253
REMARK 465 GLU A 254
REMARK 465 GLN A 255
REMARK 465 ARG A 256
REMARK 465 PHE A 257
REMARK 465 THR A 258
REMARK 465 CYS A 259
REMARK 465 TYR A 260
REMARK 465 MET A 261
REMARK 465 GLU A 262
REMARK 465 HIS A 263
REMARK 465 SER A 264
REMARK 465 GLY A 265
REMARK 465 ASN A 266
REMARK 465 HIS A 267
REMARK 465 GLY A 268
REMARK 465 THR A 269
REMARK 465 HIS A 270
REMARK 465 PRO A 271
REMARK 465 VAL A 272
REMARK 465 PRO A 273
REMARK 465 SER A 274
REMARK 465 GLY A 275
REMARK 465 LYS A 276
REMARK 465 VAL A 277
REMARK 465 LEU A 278
REMARK 465 VAL A 279
REMARK 465 LEU A 280
REMARK 465 GLN A 281
REMARK 465 SER A 282
REMARK 465 GLN A 283
REMARK 465 ARG A 284
REMARK 465 THR A 285
REMARK 465 ASP A 286
REMARK 465 PHE A 287
REMARK 465 PRO A 288
REMARK 465 TYR A 289
REMARK 465 VAL A 290
REMARK 465 SER A 291
REMARK 465 ALA A 292
REMARK 465 ALA A 293
REMARK 465 MET A 294
REMARK 465 PRO A 295
REMARK 465 CYS A 296
REMARK 465 PHE A 297
REMARK 465 VAL A 298
REMARK 465 ILE A 299
REMARK 465 ILE A 300
REMARK 465 ILE A 301
REMARK 465 ILE A 302
REMARK 465 LEU A 303
REMARK 465 CYS A 304
REMARK 465 VAL A 305
REMARK 465 PRO A 306
REMARK 465 CYS A 307
REMARK 465 CYS A 308
REMARK 465 LYS A 309
REMARK 465 LYS A 310
REMARK 465 LYS A 311
REMARK 465 THR A 312
REMARK 465 SER A 313
REMARK 465 ALA A 314
REMARK 465 ALA A 315
REMARK 465 GLU A 316
REMARK 465 GLY A 317
REMARK 465 PRO A 318
REMARK 465 ARG B 164
REMARK 465 PRO B 165
REMARK 465 PRO B 166
REMARK 465 GLY B 167
REMARK 465 SER B 168
REMARK 465 GLY B 169
REMARK 465 LEU B 170
REMARK 465 ALA B 171
REMARK 465 LYS B 172
REMARK 465 HIS B 173
REMARK 465 PRO B 174
REMARK 465 SER B 175
REMARK 465 VAL B 176
REMARK 465 SER B 177
REMARK 465 ALA B 178
REMARK 465 ASP B 179
REMARK 465 GLU B 180
REMARK 465 GLU B 181
REMARK 465 LEU B 182
REMARK 465 SER B 183
REMARK 465 ALA B 184
REMARK 465 MET C 0
REMARK 465 LYS C 81
REMARK 465 ASP C 82
REMARK 465 GLN C 83
REMARK 465 LYS C 84
REMARK 465 GLY C 85
REMARK 465 GLY C 86
REMARK 465 GLU C 148
REMARK 465 ASP C 149
REMARK 465 VAL C 176
REMARK 465 ALA C 177
REMARK 465 ILE C 178
REMARK 465 ARG C 179
REMARK 465 ARG C 180
REMARK 465 THR C 181
REMARK 465 VAL C 182
REMARK 465 PRO C 183
REMARK 465 PRO C 184
REMARK 465 MET C 185
REMARK 465 VAL C 186
REMARK 465 ASN C 187
REMARK 465 VAL C 188
REMARK 465 THR C 189
REMARK 465 CYS C 190
REMARK 465 SER C 191
REMARK 465 GLU C 192
REMARK 465 VAL C 193
REMARK 465 SER C 194
REMARK 465 GLU C 195
REMARK 465 GLY C 196
REMARK 465 ASN C 197
REMARK 465 ILE C 198
REMARK 465 THR C 199
REMARK 465 VAL C 200
REMARK 465 THR C 201
REMARK 465 CYS C 202
REMARK 465 ARG C 203
REMARK 465 ALA C 204
REMARK 465 SER C 205
REMARK 465 SER C 206
REMARK 465 PHE C 207
REMARK 465 TYR C 208
REMARK 465 PRO C 209
REMARK 465 ARG C 210
REMARK 465 ASN C 211
REMARK 465 ILE C 212
REMARK 465 THR C 213
REMARK 465 LEU C 214
REMARK 465 THR C 215
REMARK 465 TRP C 216
REMARK 465 ARG C 217
REMARK 465 GLN C 218
REMARK 465 ASP C 219
REMARK 465 GLY C 220
REMARK 465 VAL C 221
REMARK 465 SER C 222
REMARK 465 LEU C 223
REMARK 465 SER C 224
REMARK 465 HIS C 225
REMARK 465 ASN C 226
REMARK 465 THR C 227
REMARK 465 GLN C 228
REMARK 465 GLN C 229
REMARK 465 TRP C 230
REMARK 465 GLY C 231
REMARK 465 ASP C 232
REMARK 465 VAL C 233
REMARK 465 LEU C 234
REMARK 465 PRO C 235
REMARK 465 ASP C 236
REMARK 465 GLY C 237
REMARK 465 ASN C 238
REMARK 465 GLY C 239
REMARK 465 THR C 240
REMARK 465 TYR C 241
REMARK 465 GLN C 242
REMARK 465 THR C 243
REMARK 465 TRP C 244
REMARK 465 VAL C 245
REMARK 465 ALA C 246
REMARK 465 THR C 247
REMARK 465 ARG C 248
REMARK 465 ILE C 249
REMARK 465 ARG C 250
REMARK 465 GLN C 251
REMARK 465 GLY C 252
REMARK 465 GLU C 253
REMARK 465 GLU C 254
REMARK 465 GLN C 255
REMARK 465 ARG C 256
REMARK 465 PHE C 257
REMARK 465 THR C 258
REMARK 465 CYS C 259
REMARK 465 TYR C 260
REMARK 465 MET C 261
REMARK 465 GLU C 262
REMARK 465 HIS C 263
REMARK 465 SER C 264
REMARK 465 GLY C 265
REMARK 465 ASN C 266
REMARK 465 HIS C 267
REMARK 465 GLY C 268
REMARK 465 THR C 269
REMARK 465 HIS C 270
REMARK 465 PRO C 271
REMARK 465 VAL C 272
REMARK 465 PRO C 273
REMARK 465 SER C 274
REMARK 465 GLY C 275
REMARK 465 LYS C 276
REMARK 465 VAL C 277
REMARK 465 LEU C 278
REMARK 465 VAL C 279
REMARK 465 LEU C 280
REMARK 465 GLN C 281
REMARK 465 SER C 282
REMARK 465 GLN C 283
REMARK 465 ARG C 284
REMARK 465 THR C 285
REMARK 465 ASP C 286
REMARK 465 PHE C 287
REMARK 465 PRO C 288
REMARK 465 TYR C 289
REMARK 465 VAL C 290
REMARK 465 SER C 291
REMARK 465 ALA C 292
REMARK 465 ALA C 293
REMARK 465 MET C 294
REMARK 465 PRO C 295
REMARK 465 CYS C 296
REMARK 465 PHE C 297
REMARK 465 VAL C 298
REMARK 465 ILE C 299
REMARK 465 ILE C 300
REMARK 465 ILE C 301
REMARK 465 ILE C 302
REMARK 465 LEU C 303
REMARK 465 CYS C 304
REMARK 465 VAL C 305
REMARK 465 PRO C 306
REMARK 465 CYS C 307
REMARK 465 CYS C 308
REMARK 465 LYS C 309
REMARK 465 LYS C 310
REMARK 465 LYS C 311
REMARK 465 THR C 312
REMARK 465 SER C 313
REMARK 465 ALA C 314
REMARK 465 ALA C 315
REMARK 465 GLU C 316
REMARK 465 GLY C 317
REMARK 465 PRO C 318
REMARK 465 SER D 160
REMARK 465 LEU D 161
REMARK 465 TYR D 162
REMARK 465 PRO D 163
REMARK 465 ARG D 164
REMARK 465 PRO D 165
REMARK 465 PRO D 166
REMARK 465 GLY D 167
REMARK 465 SER D 168
REMARK 465 GLY D 169
REMARK 465 LEU D 170
REMARK 465 ALA D 171
REMARK 465 LYS D 172
REMARK 465 HIS D 173
REMARK 465 PRO D 174
REMARK 465 SER D 175
REMARK 465 VAL D 176
REMARK 465 SER D 177
REMARK 465 ALA D 178
REMARK 465 ASP D 179
REMARK 465 GLU D 180
REMARK 465 GLU D 181
REMARK 465 LEU D 182
REMARK 465 SER D 183
REMARK 465 ALA D 184
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 16 CB CG CD OE1 OE2
REMARK 470 MET A 140 CG SD CE
REMARK 470 GLU C 1 CG CD OE1 OE2
REMARK 470 GLU C 16 CB CG CD OE1 OE2
REMARK 470 MET C 140 CG SD CE
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS D 38 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 CYS D 143 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 16 -0.11 83.91
REMARK 500 GLN B 111 73.38 -152.13
REMARK 500 GLU C 16 4.75 83.52
REMARK 500 HIS C 79 58.41 -98.38
REMARK 500 SER C 102 -3.70 79.85
REMARK 500 GLN C 125 -3.31 74.77
REMARK 500 ASN D 84 105.71 -163.08
REMARK 500 GLN D 111 73.23 -151.38
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 D2004 DISTANCE = 6.11 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PEU A 1176
REMARK 610 PEU C 1176
REMARK 610 PEU D 1160
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JE6 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE MHC CLASS I HOMOLOG MICB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE UNIPROT ACCESSION NUMBER Q29980 DOES NOT PROVIDE THE
REMARK 999 CORRECT AMINO ACID SEQUENCE OF THE MICB ALLELE 002.
REMARK 999 THIS CAN BE FOUND UNDER AAB71642 IN PUBMED PROTEIN SEARCH.
REMARK 999 ONLY THE ALPHA1 AND ALPHA2 DOMAINS (RESIDUES 1-181) OF THE
REMARK 999 ECTODOMAIN (1-276) WAS EXPRESSED. THIS IS A FRAGMENT OF THE
REMARK 999 FULL LENGTH PROTEIN (RESIDUES 1-318).
REMARK 999
REMARK 999 SEQUENCE OF UNCHARACTERIZED PROTEIN UL16
REMARK 999 CAN ALSO BE FOUND UNDER NP_039950 IN THE PUBMED PROTEIN
REMARK 999 SEARCH. ONLY THE ECTODOMAIN (RESIDUES 1-184) WAS
REMARK 999 EXPRESSED. THIS IS A FRAGMENT OF THE FULL LENGTH PROTEIN (
REMARK 999 1-230). DUE TO CLEAVAGE OF THE SIGNAL PEPTIDE (RESIDUES 1-
REMARK 999 26) THE MATURE UL16 PROTEIN USED FOR CRYSTALLIZATION
REMARK 999 CONSISTS OF RESIDUES 27-184.
DBREF 2WY3 A 0 0 PDB 2WY3 2WY3 0 0
DBREF 2WY3 A 1 318 UNP Q29980 MICB_HUMAN 24 341
DBREF 2WY3 B 27 184 UNP P16757 UL16P_HCMVA 27 184
DBREF 2WY3 C 0 0 PDB 2WY3 2WY3 0 0
DBREF 2WY3 C 1 318 UNP Q29980 MICB_HUMAN 24 341
DBREF 2WY3 D 27 184 UNP P16757 UL16P_HCMVA 27 184
SEQADV 2WY3 GLU A 57 UNP Q29980 LYS 80 CONFLICT
SEQADV 2WY3 ASN A 113 UNP Q29980 ASP 136 CONFLICT
SEQADV 2WY3 GLU C 57 UNP Q29980 LYS 80 CONFLICT
SEQADV 2WY3 ASN C 113 UNP Q29980 ASP 136 CONFLICT
SEQRES 1 A 319 MET GLU PRO HIS SER LEU ARG TYR ASN LEU MET VAL LEU
SEQRES 2 A 319 SER GLN ASP GLU SER VAL GLN SER GLY PHE LEU ALA GLU
SEQRES 3 A 319 GLY HIS LEU ASP GLY GLN PRO PHE LEU ARG TYR ASP ARG
SEQRES 4 A 319 GLN LYS ARG ARG ALA LYS PRO GLN GLY GLN TRP ALA GLU
SEQRES 5 A 319 ASP VAL LEU GLY ALA GLU THR TRP ASP THR GLU THR GLU
SEQRES 6 A 319 ASP LEU THR GLU ASN GLY GLN ASP LEU ARG ARG THR LEU
SEQRES 7 A 319 THR HIS ILE LYS ASP GLN LYS GLY GLY LEU HIS SER LEU
SEQRES 8 A 319 GLN GLU ILE ARG VAL CYS GLU ILE HIS GLU ASP SER SER
SEQRES 9 A 319 THR ARG GLY SER ARG HIS PHE TYR TYR ASN GLY GLU LEU
SEQRES 10 A 319 PHE LEU SER GLN ASN LEU GLU THR GLN GLU SER THR VAL
SEQRES 11 A 319 PRO GLN SER SER ARG ALA GLN THR LEU ALA MET ASN VAL
SEQRES 12 A 319 THR ASN PHE TRP LYS GLU ASP ALA MET LYS THR LYS THR
SEQRES 13 A 319 HIS TYR ARG ALA MET GLN ALA ASP CYS LEU GLN LYS LEU
SEQRES 14 A 319 GLN ARG TYR LEU LYS SER GLY VAL ALA ILE ARG ARG THR
SEQRES 15 A 319 VAL PRO PRO MET VAL ASN VAL THR CYS SER GLU VAL SER
SEQRES 16 A 319 GLU GLY ASN ILE THR VAL THR CYS ARG ALA SER SER PHE
SEQRES 17 A 319 TYR PRO ARG ASN ILE THR LEU THR TRP ARG GLN ASP GLY
SEQRES 18 A 319 VAL SER LEU SER HIS ASN THR GLN GLN TRP GLY ASP VAL
SEQRES 19 A 319 LEU PRO ASP GLY ASN GLY THR TYR GLN THR TRP VAL ALA
SEQRES 20 A 319 THR ARG ILE ARG GLN GLY GLU GLU GLN ARG PHE THR CYS
SEQRES 21 A 319 TYR MET GLU HIS SER GLY ASN HIS GLY THR HIS PRO VAL
SEQRES 22 A 319 PRO SER GLY LYS VAL LEU VAL LEU GLN SER GLN ARG THR
SEQRES 23 A 319 ASP PHE PRO TYR VAL SER ALA ALA MET PRO CYS PHE VAL
SEQRES 24 A 319 ILE ILE ILE ILE LEU CYS VAL PRO CYS CYS LYS LYS LYS
SEQRES 25 A 319 THR SER ALA ALA GLU GLY PRO
SEQRES 1 B 158 VAL ASP LEU GLY SER LYS SER SER ASN SER THR CYS ARG
SEQRES 2 B 158 LEU ASN VAL THR GLU LEU ALA SER ILE HIS PRO GLY GLU
SEQRES 3 B 158 THR TRP THR LEU HIS GLY MET CYS ILE SER ILE CYS TYR
SEQRES 4 B 158 TYR GLU ASN VAL THR GLU ASP GLU ILE ILE GLY VAL ALA
SEQRES 5 B 158 PHE THR TRP GLN HIS ASN GLU SER VAL VAL ASP LEU TRP
SEQRES 6 B 158 LEU TYR GLN ASN ASP THR VAL ILE ARG ASN PHE SER ASP
SEQRES 7 B 158 ILE THR THR ASN ILE LEU GLN ASP GLY LEU LYS MET ARG
SEQRES 8 B 158 THR VAL PRO VAL THR LYS LEU TYR THR SER ARG MET VAL
SEQRES 9 B 158 THR ASN LEU THR VAL GLY ARG TYR ASP CYS LEU ARG CYS
SEQRES 10 B 158 GLU ASN GLY THR THR LYS ILE ILE GLU ARG LEU TYR VAL
SEQRES 11 B 158 ARG LEU GLY SER LEU TYR PRO ARG PRO PRO GLY SER GLY
SEQRES 12 B 158 LEU ALA LYS HIS PRO SER VAL SER ALA ASP GLU GLU LEU
SEQRES 13 B 158 SER ALA
SEQRES 1 C 319 MET GLU PRO HIS SER LEU ARG TYR ASN LEU MET VAL LEU
SEQRES 2 C 319 SER GLN ASP GLU SER VAL GLN SER GLY PHE LEU ALA GLU
SEQRES 3 C 319 GLY HIS LEU ASP GLY GLN PRO PHE LEU ARG TYR ASP ARG
SEQRES 4 C 319 GLN LYS ARG ARG ALA LYS PRO GLN GLY GLN TRP ALA GLU
SEQRES 5 C 319 ASP VAL LEU GLY ALA GLU THR TRP ASP THR GLU THR GLU
SEQRES 6 C 319 ASP LEU THR GLU ASN GLY GLN ASP LEU ARG ARG THR LEU
SEQRES 7 C 319 THR HIS ILE LYS ASP GLN LYS GLY GLY LEU HIS SER LEU
SEQRES 8 C 319 GLN GLU ILE ARG VAL CYS GLU ILE HIS GLU ASP SER SER
SEQRES 9 C 319 THR ARG GLY SER ARG HIS PHE TYR TYR ASN GLY GLU LEU
SEQRES 10 C 319 PHE LEU SER GLN ASN LEU GLU THR GLN GLU SER THR VAL
SEQRES 11 C 319 PRO GLN SER SER ARG ALA GLN THR LEU ALA MET ASN VAL
SEQRES 12 C 319 THR ASN PHE TRP LYS GLU ASP ALA MET LYS THR LYS THR
SEQRES 13 C 319 HIS TYR ARG ALA MET GLN ALA ASP CYS LEU GLN LYS LEU
SEQRES 14 C 319 GLN ARG TYR LEU LYS SER GLY VAL ALA ILE ARG ARG THR
SEQRES 15 C 319 VAL PRO PRO MET VAL ASN VAL THR CYS SER GLU VAL SER
SEQRES 16 C 319 GLU GLY ASN ILE THR VAL THR CYS ARG ALA SER SER PHE
SEQRES 17 C 319 TYR PRO ARG ASN ILE THR LEU THR TRP ARG GLN ASP GLY
SEQRES 18 C 319 VAL SER LEU SER HIS ASN THR GLN GLN TRP GLY ASP VAL
SEQRES 19 C 319 LEU PRO ASP GLY ASN GLY THR TYR GLN THR TRP VAL ALA
SEQRES 20 C 319 THR ARG ILE ARG GLN GLY GLU GLU GLN ARG PHE THR CYS
SEQRES 21 C 319 TYR MET GLU HIS SER GLY ASN HIS GLY THR HIS PRO VAL
SEQRES 22 C 319 PRO SER GLY LYS VAL LEU VAL LEU GLN SER GLN ARG THR
SEQRES 23 C 319 ASP PHE PRO TYR VAL SER ALA ALA MET PRO CYS PHE VAL
SEQRES 24 C 319 ILE ILE ILE ILE LEU CYS VAL PRO CYS CYS LYS LYS LYS
SEQRES 25 C 319 THR SER ALA ALA GLU GLY PRO
SEQRES 1 D 158 VAL ASP LEU GLY SER LYS SER SER ASN SER THR CYS ARG
SEQRES 2 D 158 LEU ASN VAL THR GLU LEU ALA SER ILE HIS PRO GLY GLU
SEQRES 3 D 158 THR TRP THR LEU HIS GLY MET CYS ILE SER ILE CYS TYR
SEQRES 4 D 158 TYR GLU ASN VAL THR GLU ASP GLU ILE ILE GLY VAL ALA
SEQRES 5 D 158 PHE THR TRP GLN HIS ASN GLU SER VAL VAL ASP LEU TRP
SEQRES 6 D 158 LEU TYR GLN ASN ASP THR VAL ILE ARG ASN PHE SER ASP
SEQRES 7 D 158 ILE THR THR ASN ILE LEU GLN ASP GLY LEU LYS MET ARG
SEQRES 8 D 158 THR VAL PRO VAL THR LYS LEU TYR THR SER ARG MET VAL
SEQRES 9 D 158 THR ASN LEU THR VAL GLY ARG TYR ASP CYS LEU ARG CYS
SEQRES 10 D 158 GLU ASN GLY THR THR LYS ILE ILE GLU ARG LEU TYR VAL
SEQRES 11 D 158 ARG LEU GLY SER LEU TYR PRO ARG PRO PRO GLY SER GLY
SEQRES 12 D 158 LEU ALA LYS HIS PRO SER VAL SER ALA ASP GLU GLU LEU
SEQRES 13 D 158 SER ALA
MODRES 2WY3 ASN B 41 ASN GLYCOSYLATION SITE
MODRES 2WY3 ASN B 68 ASN GLYCOSYLATION SITE
MODRES 2WY3 ASN B 84 ASN GLYCOSYLATION SITE
MODRES 2WY3 ASN B 95 ASN GLYCOSYLATION SITE
MODRES 2WY3 ASN B 101 ASN GLYCOSYLATION SITE
MODRES 2WY3 ASN B 132 ASN GLYCOSYLATION SITE
MODRES 2WY3 ASN D 41 ASN GLYCOSYLATION SITE
MODRES 2WY3 ASN D 68 ASN GLYCOSYLATION SITE
MODRES 2WY3 ASN D 84 ASN GLYCOSYLATION SITE
MODRES 2WY3 ASN D 95 ASN GLYCOSYLATION SITE
MODRES 2WY3 ASN D 101 ASN GLYCOSYLATION SITE
MODRES 2WY3 ASN D 132 ASN GLYCOSYLATION SITE
HET PEU A1176 19
HET ACT A1177 4
HET ACT B1164 4
HET NAG B1201 14
HET NAG B1202 28
HET NAG B1203 14
HET NAG B1204 14
HET NAG B1205 14
HET NAG B1206 14
HET PEU C1176 17
HET ACT C1177 4
HET PEU D1160 13
HET NAG D1201 14
HET NAG D1202 28
HET NAG D1203 14
HET NAG D1204 14
HET NAG D1205 14
HET NAG D1206 14
HETNAM PEU 2,5,8,11,14,17,20,23,26,29,32,35,38,41,44,47,50,53,56,
HETNAM 2 PEU 59,62,65,68,71,74,77,80-HEPTACOSAOXADOOCTACONTAN-82-OL
HETNAM ACT ACETATE ION
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETSYN PEU PEG 8000
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 5 PEU 3(C55 H112 O28)
FORMUL 6 ACT 3(C2 H3 O2 1-)
FORMUL 8 NAG 12(C8 H15 N O6)
FORMUL 23 HOH *639(H2 O)
HELIX 1 1 GLY A 47 VAL A 53 1 7
HELIX 2 2 ALA A 56 HIS A 79 1 24
HELIX 3 3 SER A 132 GLU A 148 1 17
HELIX 4 4 LYS A 152 GLY A 175 1 24
HELIX 5 5 ASN B 41 ILE B 48 5 8
HELIX 6 6 GLY C 47 VAL C 53 1 7
HELIX 7 7 ALA C 56 HIS C 79 1 24
HELIX 8 8 SER C 132 TRP C 146 1 15
HELIX 9 9 LYS C 152 GLY C 175 1 24
HELIX 10 10 ASN D 41 ILE D 48 5 8
SHEET 1 AA 2 SER A 17 VAL A 18 0
SHEET 2 AA 2 HIS A 3 GLN A 14 -1 O GLN A 14 N SER A 17
SHEET 1 AB 5 ARG A 42 PRO A 45 0
SHEET 2 AB 5 GLN A 31 ASP A 37 -1 O ARG A 35 N LYS A 44
SHEET 3 AB 5 LEU A 23 LEU A 28 -1 O ALA A 24 N TYR A 36
SHEET 4 AB 5 HIS A 3 GLN A 14 -1 O ARG A 6 N HIS A 27
SHEET 5 AB 5 SER A 17 VAL A 18 -1 O SER A 17 N GLN A 14
SHEET 1 AC 8 ARG A 42 PRO A 45 0
SHEET 2 AC 8 GLN A 31 ASP A 37 -1 O ARG A 35 N LYS A 44
SHEET 3 AC 8 LEU A 23 LEU A 28 -1 O ALA A 24 N TYR A 36
SHEET 4 AC 8 HIS A 3 GLN A 14 -1 O ARG A 6 N HIS A 27
SHEET 5 AC 8 LEU A 87 ILE A 98 -1 O HIS A 88 N SER A 13
SHEET 6 AC 8 THR A 104 TYR A 112 -1 O ARG A 105 N GLU A 97
SHEET 7 AC 8 GLU A 115 ASN A 121 -1 O GLU A 115 N TYR A 112
SHEET 8 AC 8 SER A 127 THR A 128 -1 O THR A 128 N SER A 119
SHEET 1 BA 2 ASP B 28 SER B 31 0
SHEET 2 BA 2 SER B 36 ARG B 39 -1 O SER B 36 N SER B 31
SHEET 1 BB 6 THR B 53 HIS B 57 0
SHEET 2 BB 6 THR B 147 ARG B 157 1 O ARG B 153 N TRP B 54
SHEET 3 BB 6 GLY B 136 GLU B 144 -1 O GLY B 136 N VAL B 156
SHEET 4 BB 6 ILE B 75 TRP B 81 -1 O GLY B 76 N LEU B 141
SHEET 5 BB 6 VAL B 88 GLN B 94 -1 O ASP B 89 N PHE B 79
SHEET 6 BB 6 THR B 97 ARG B 100 -1 O THR B 97 N GLN B 94
SHEET 1 BC 3 CYS B 60 GLU B 67 0
SHEET 2 BC 3 VAL B 121 ARG B 128 -1 O THR B 122 N TYR B 66
SHEET 3 BC 3 ASN B 108 LYS B 115 -1 N ILE B 109 O SER B 127
SHEET 1 CA 2 SER C 17 VAL C 18 0
SHEET 2 CA 2 HIS C 3 GLN C 14 -1 O GLN C 14 N SER C 17
SHEET 1 CB 5 ARG C 42 PRO C 45 0
SHEET 2 CB 5 GLN C 31 ASP C 37 -1 O ARG C 35 N LYS C 44
SHEET 3 CB 5 LEU C 23 LEU C 28 -1 O ALA C 24 N TYR C 36
SHEET 4 CB 5 HIS C 3 GLN C 14 -1 O ARG C 6 N HIS C 27
SHEET 5 CB 5 SER C 17 VAL C 18 -1 O SER C 17 N GLN C 14
SHEET 1 CC 8 ARG C 42 PRO C 45 0
SHEET 2 CC 8 GLN C 31 ASP C 37 -1 O ARG C 35 N LYS C 44
SHEET 3 CC 8 LEU C 23 LEU C 28 -1 O ALA C 24 N TYR C 36
SHEET 4 CC 8 HIS C 3 GLN C 14 -1 O ARG C 6 N HIS C 27
SHEET 5 CC 8 HIS C 88 ILE C 98 -1 O HIS C 88 N SER C 13
SHEET 6 CC 8 THR C 104 TYR C 112 -1 O ARG C 105 N GLU C 97
SHEET 7 CC 8 GLU C 115 ASN C 121 -1 O GLU C 115 N TYR C 112
SHEET 8 CC 8 SER C 127 THR C 128 -1 O THR C 128 N SER C 119
SHEET 1 DA 2 ASP D 28 SER D 31 0
SHEET 2 DA 2 SER D 36 ARG D 39 -1 O SER D 36 N SER D 31
SHEET 1 DB 6 THR D 53 HIS D 57 0
SHEET 2 DB 6 THR D 147 ARG D 157 1 O ARG D 153 N TRP D 54
SHEET 3 DB 6 GLY D 136 GLU D 144 -1 O GLY D 136 N VAL D 156
SHEET 4 DB 6 ILE D 75 TRP D 81 -1 O GLY D 76 N LEU D 141
SHEET 5 DB 6 VAL D 88 GLN D 94 -1 O ASP D 89 N PHE D 79
SHEET 6 DB 6 THR D 97 ARG D 100 -1 O THR D 97 N GLN D 94
SHEET 1 DC 3 ILE D 61 GLU D 67 0
SHEET 2 DC 3 VAL D 121 ARG D 128 -1 O THR D 122 N TYR D 66
SHEET 3 DC 3 ASN D 108 LYS D 115 -1 N ILE D 109 O SER D 127
SSBOND 1 CYS A 96 CYS A 164 1555 1555 2.06
SSBOND 2 CYS B 38 CYS B 143 1555 1555 2.04
SSBOND 3 CYS B 64 CYS B 140 1555 1555 2.00
SSBOND 4 CYS C 96 CYS C 164 1555 1555 2.06
SSBOND 5 CYS D 38 CYS D 143 1555 1555 2.05
SSBOND 6 CYS D 64 CYS D 140 1555 1555 2.02
LINK ND2 ASN B 41 C1 NAG B1201 1555 1555 1.44
LINK ND2AASN B 68 C1 ANAG B1202 1555 1555 1.45
LINK ND2BASN B 68 C1 BNAG B1202 1555 1555 1.44
LINK ND2 ASN B 84 C1 NAG B1203 1555 1555 1.44
LINK ND2 ASN B 95 C1 NAG B1204 1555 1555 1.44
LINK ND2 ASN B 101 C1 NAG B1205 1555 1555 1.45
LINK ND2 ASN B 132 C1 NAG B1206 1555 1555 1.45
LINK ND2 ASN D 41 C1 NAG D1201 1555 1555 1.44
LINK ND2BASN D 68 C1 BNAG D1202 1555 1555 1.45
LINK ND2AASN D 68 C1 ANAG D1202 1555 1555 1.44
LINK ND2 ASN D 84 C1 NAG D1203 1555 1555 1.45
LINK ND2 ASN D 95 C1 NAG D1204 1555 1555 1.45
LINK ND2 ASN D 101 C1 NAG D1205 1555 1555 1.45
LINK ND2 ASN D 132 C1 NAG D1206 1555 1555 1.45
CRYST1 58.120 104.170 146.800 90.00 90.00 90.00 P 21 21 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 0.017206 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009600 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006812 0.00000
MTRIX1 1 -0.507600 -0.028430 0.861100 -50.64000 1
MTRIX2 1 0.028940 -0.999500 -0.015930 75.60000 1
MTRIX3 1 0.861100 0.016840 0.508200 28.66000 1
MTRIX1 2 -0.507200 -0.030880 0.861200 -50.73000 1
MTRIX2 2 0.024850 -0.999500 -0.021200 76.22000 1
MTRIX3 2 0.861400 0.010650 0.507700 28.81000 1
(ATOM LINES ARE NOT SHOWN.)
END
