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HEADER HYDROLASE 15-APR-16 5JD5
TITLE CRYSTAL STRUCTURE OF MGS-MILE3, AN ALPHA/BETA HYDROLASE ENZYME FROM
TITLE 2 THE METAGENOME OF PYRENE-PHENANTHRENE ENRICHMENT CULTURE WITH
TITLE 3 SEDIMENT SAMPLE OF MILAZZO HARBOR, ITALY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MGS-MILE3;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P15TV LIC
KEYWDS ALPHA/BETA HYDROLASE, ESTERASE, METAGENOME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.STOGIOS,X.XU,H.CUI,M.MARTINEZ-MARTINEZ,T.N.CHERNIKOVA,
AUTHOR 2 P.N.GOLYSHIN,M.M.YAKIMOV,M.FERRER,A.SAVCHENKO
REVDAT 1 04-MAY-16 5JD5 0
JRNL AUTH M.MARTINEZ-MARTINEZ
JRNL TITL CRYSTAL STRUCTURE OF MGS-MILE3, AN ALPHA/BETA HYDROLASE
JRNL TITL 2 ENZYME FROM THE METAGENOME OF PYRENE-PHENANTHRENE ENRICHMENT
JRNL TITL 3 CULTURE WITH SEDIMENT SAMPLE OF MILAZZO HARBOR, ITALY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.95 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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 103051
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.950
REMARK 3 FREE R VALUE TEST SET COUNT : 2006
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 24.7174 - 4.6862 0.95 7639 154 0.1494 0.1814
REMARK 3 2 4.6862 - 3.7237 0.98 7632 149 0.1429 0.1895
REMARK 3 3 3.7237 - 3.2542 0.95 7380 146 0.1614 0.1886
REMARK 3 4 3.2542 - 2.9572 0.90 6940 130 0.1879 0.2232
REMARK 3 5 2.9572 - 2.7455 0.87 6734 137 0.1970 0.2613
REMARK 3 6 2.7455 - 2.5838 0.88 6687 145 0.2032 0.2626
REMARK 3 7 2.5838 - 2.4545 0.91 6950 140 0.2139 0.2667
REMARK 3 8 2.4545 - 2.3478 0.94 7143 142 0.2159 0.2959
REMARK 3 9 2.3478 - 2.2575 0.94 7174 136 0.2287 0.2773
REMARK 3 10 2.2575 - 2.1796 0.96 7285 145 0.2605 0.3104
REMARK 3 11 2.1796 - 2.1115 0.96 7352 137 0.2509 0.3092
REMARK 3 12 2.1115 - 2.0512 0.97 7359 155 0.2688 0.3366
REMARK 3 13 2.0512 - 1.9972 0.98 7462 146 0.2824 0.2878
REMARK 3 14 1.9972 - 1.9500 0.96 7308 144 0.2958 0.2793
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.270
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 : 0.006 9972
REMARK 3 ANGLE : 0.993 13585
REMARK 3 CHIRALITY : 0.035 1457
REMARK 3 PLANARITY : 0.005 1827
REMARK 3 DIHEDRAL : 11.994 3590
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 5:40)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.6389 47.7257 126.2810
REMARK 3 T TENSOR
REMARK 3 T11: 0.4196 T22: 0.2180
REMARK 3 T33: 0.2601 T12: -0.0772
REMARK 3 T13: -0.1102 T23: 0.0175
REMARK 3 L TENSOR
REMARK 3 L11: 2.0947 L22: 3.4722
REMARK 3 L33: 2.1842 L12: -1.3770
REMARK 3 L13: 1.6214 L23: -1.3670
REMARK 3 S TENSOR
REMARK 3 S11: -0.0763 S12: -0.2772 S13: 0.0010
REMARK 3 S21: 0.4580 S22: 0.1203 S23: 0.0931
REMARK 3 S31: 0.3276 S32: -0.2562 S33: -0.0645
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 41:54)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.3581 68.4708 134.6385
REMARK 3 T TENSOR
REMARK 3 T11: 1.0868 T22: 0.6372
REMARK 3 T33: 0.3843 T12: -0.0232
REMARK 3 T13: 0.0110 T23: -0.0394
REMARK 3 L TENSOR
REMARK 3 L11: 4.1172 L22: 5.8286
REMARK 3 L33: 8.7778 L12: 3.6934
REMARK 3 L13: 0.0412 L23: 0.4870
REMARK 3 S TENSOR
REMARK 3 S11: -0.0478 S12: -1.6879 S13: 0.4661
REMARK 3 S21: 1.7197 S22: -0.2773 S23: 0.2368
REMARK 3 S31: -0.8235 S32: 0.5913 S33: 0.3473
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 55:86)
REMARK 3 ORIGIN FOR THE GROUP (A): 46.6941 76.8379 126.6165
REMARK 3 T TENSOR
REMARK 3 T11: 0.3781 T22: 0.1780
REMARK 3 T33: 0.2021 T12: -0.0002
REMARK 3 T13: -0.1175 T23: -0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 3.5216 L22: 2.1417
REMARK 3 L33: 3.7999 L12: -0.6341
REMARK 3 L13: 1.8176 L23: 0.3211
REMARK 3 S TENSOR
REMARK 3 S11: -0.1103 S12: -0.2326 S13: 0.0823
REMARK 3 S21: 0.6211 S22: 0.1326 S23: -0.1217
REMARK 3 S31: -0.1201 S32: 0.0683 S33: 0.0952
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 87:234)
REMARK 3 ORIGIN FOR THE GROUP (A): 42.1885 68.5072 116.3991
REMARK 3 T TENSOR
REMARK 3 T11: 0.2521 T22: 0.1910
REMARK 3 T33: 0.1935 T12: 0.0075
REMARK 3 T13: -0.1126 T23: -0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 0.7471 L22: 1.0979
REMARK 3 L33: 1.1913 L12: -0.1074
REMARK 3 L13: 0.0848 L23: 0.3632
REMARK 3 S TENSOR
REMARK 3 S11: -0.0320 S12: -0.0782 S13: 0.0485
REMARK 3 S21: 0.2277 S22: -0.0091 S23: -0.0295
REMARK 3 S31: -0.0874 S32: -0.0664 S33: 0.0489
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 235:321)
REMARK 3 ORIGIN FOR THE GROUP (A): 46.4246 58.4572 112.1875
REMARK 3 T TENSOR
REMARK 3 T11: 0.1874 T22: 0.1442
REMARK 3 T33: 0.2045 T12: 0.0030
REMARK 3 T13: -0.1132 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.7810 L22: 2.1358
REMARK 3 L33: 2.8878 L12: 0.2269
REMARK 3 L13: 0.6574 L23: -0.1729
REMARK 3 S TENSOR
REMARK 3 S11: -0.0494 S12: -0.0439 S13: -0.0635
REMARK 3 S21: 0.2280 S22: 0.0112 S23: -0.1535
REMARK 3 S31: 0.0117 S32: -0.0422 S33: 0.0029
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN B AND RESID 4:44)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.8544 78.0657 41.3118
REMARK 3 T TENSOR
REMARK 3 T11: 0.2996 T22: 0.2897
REMARK 3 T33: 0.2218 T12: 0.1035
REMARK 3 T13: -0.0752 T23: 0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 1.6906 L22: 5.2556
REMARK 3 L33: 1.2438 L12: 2.1215
REMARK 3 L13: -1.1291 L23: -1.1284
REMARK 3 S TENSOR
REMARK 3 S11: -0.0828 S12: 0.3657 S13: 0.1796
REMARK 3 S21: -0.4123 S22: 0.1691 S23: 0.3464
REMARK 3 S31: -0.1610 S32: -0.0534 S33: -0.0871
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 45:59)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.0493 61.1040 31.6180
REMARK 3 T TENSOR
REMARK 3 T11: 0.8744 T22: 0.6637
REMARK 3 T33: 0.3333 T12: 0.1729
REMARK 3 T13: -0.1706 T23: -0.1165
REMARK 3 L TENSOR
REMARK 3 L11: 7.2026 L22: 7.2274
REMARK 3 L33: 2.2334 L12: 6.0285
REMARK 3 L13: -3.4233 L23: -4.0164
REMARK 3 S TENSOR
REMARK 3 S11: -0.1989 S12: 1.0705 S13: -0.2380
REMARK 3 S21: -1.2926 S22: 0.1505 S23: -0.3433
REMARK 3 S31: -0.0365 S32: -0.4691 S33: 0.0376
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 60:233)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.1654 57.4191 49.9655
REMARK 3 T TENSOR
REMARK 3 T11: 0.1847 T22: 0.1714
REMARK 3 T33: 0.1851 T12: 0.0086
REMARK 3 T13: -0.0719 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 0.2567 L22: 1.4450
REMARK 3 L33: 1.3296 L12: 0.0679
REMARK 3 L13: -0.0497 L23: 0.3791
REMARK 3 S TENSOR
REMARK 3 S11: 0.0036 S12: 0.0579 S13: -0.0554
REMARK 3 S21: -0.0229 S22: -0.0171 S23: -0.0209
REMARK 3 S31: 0.0956 S32: 0.0242 S33: 0.0188
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 234:301)
REMARK 3 ORIGIN FOR THE GROUP (A): 42.5667 69.2400 57.5841
REMARK 3 T TENSOR
REMARK 3 T11: 0.2251 T22: 0.1081
REMARK 3 T33: 0.1638 T12: 0.0027
REMARK 3 T13: -0.0881 T23: -0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 1.9812 L22: 2.7183
REMARK 3 L33: 3.8747 L12: 0.4010
REMARK 3 L13: -0.9103 L23: -0.7866
REMARK 3 S TENSOR
REMARK 3 S11: -0.0039 S12: 0.0068 S13: -0.0397
REMARK 3 S21: -0.1452 S22: 0.0408 S23: -0.0040
REMARK 3 S31: 0.0869 S32: 0.0126 S33: -0.0308
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 302:321)
REMARK 3 ORIGIN FOR THE GROUP (A): 57.7577 67.8942 49.0669
REMARK 3 T TENSOR
REMARK 3 T11: 0.2267 T22: 0.2999
REMARK 3 T33: 0.2754 T12: -0.0007
REMARK 3 T13: -0.0349 T23: -0.0396
REMARK 3 L TENSOR
REMARK 3 L11: 5.2171 L22: 4.2740
REMARK 3 L33: 7.4284 L12: -2.8281
REMARK 3 L13: 2.3220 L23: -5.3878
REMARK 3 S TENSOR
REMARK 3 S11: -0.1175 S12: -0.0049 S13: 0.0488
REMARK 3 S21: 0.0013 S22: 0.0026 S23: -0.5758
REMARK 3 S31: -0.1377 S32: 0.5142 S33: 0.0949
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN C AND RESID 6:36)
REMARK 3 ORIGIN FOR THE GROUP (A): 48.1380 52.9868 83.5405
REMARK 3 T TENSOR
REMARK 3 T11: 0.2590 T22: 0.1368
REMARK 3 T33: 0.2138 T12: -0.0269
REMARK 3 T13: -0.0688 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 2.8929 L22: 3.7759
REMARK 3 L33: 2.8291 L12: 0.3525
REMARK 3 L13: -1.6252 L23: -0.5174
REMARK 3 S TENSOR
REMARK 3 S11: 0.0089 S12: 0.0525 S13: 0.2782
REMARK 3 S21: 0.0416 S22: -0.0953 S23: -0.2232
REMARK 3 S31: -0.2282 S32: 0.6101 S33: 0.1718
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN C AND RESID 37:54)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.4229 44.4915 74.0957
REMARK 3 T TENSOR
REMARK 3 T11: 0.6252 T22: 0.6188
REMARK 3 T33: 0.3390 T12: -0.0986
REMARK 3 T13: -0.1968 T23: -0.0478
REMARK 3 L TENSOR
REMARK 3 L11: 3.1643 L22: 6.4385
REMARK 3 L33: 4.5486 L12: -1.5348
REMARK 3 L13: -0.5227 L23: 0.1968
REMARK 3 S TENSOR
REMARK 3 S11: -0.1996 S12: 0.8923 S13: -0.1033
REMARK 3 S21: -1.4589 S22: -0.0554 S23: 0.2290
REMARK 3 S31: -0.0105 S32: -0.5693 S33: 0.2470
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN C AND RESID 55:191)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.7795 29.2322 90.6549
REMARK 3 T TENSOR
REMARK 3 T11: 0.3415 T22: 0.2539
REMARK 3 T33: 0.2903 T12: -0.0974
REMARK 3 T13: -0.1075 T23: -0.0237
REMARK 3 L TENSOR
REMARK 3 L11: 0.8221 L22: 1.4658
REMARK 3 L33: 1.7991 L12: -0.3157
REMARK 3 L13: -0.1330 L23: 0.4236
REMARK 3 S TENSOR
REMARK 3 S11: -0.0213 S12: 0.0901 S13: -0.1107
REMARK 3 S21: -0.0754 S22: -0.0494 S23: 0.2216
REMARK 3 S31: 0.4733 S32: -0.2735 S33: 0.0532
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN C AND RESID 192:283)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.1978 47.2826 96.6367
REMARK 3 T TENSOR
REMARK 3 T11: 0.1522 T22: 0.2199
REMARK 3 T33: 0.2426 T12: -0.0358
REMARK 3 T13: -0.1151 T23: -0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 0.3086 L22: 2.1804
REMARK 3 L33: 2.6856 L12: 0.0753
REMARK 3 L13: -0.2339 L23: -0.1599
REMARK 3 S TENSOR
REMARK 3 S11: -0.0721 S12: 0.0169 S13: 0.0540
REMARK 3 S21: 0.1031 S22: -0.0087 S23: 0.2234
REMARK 3 S31: 0.0216 S32: -0.2613 S33: 0.0470
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN C AND RESID 284:320)
REMARK 3 ORIGIN FOR THE GROUP (A): 48.2752 38.2362 91.3600
REMARK 3 T TENSOR
REMARK 3 T11: 0.2405 T22: 0.1863
REMARK 3 T33: 0.2372 T12: -0.0409
REMARK 3 T13: -0.1132 T23: -0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 2.0208 L22: 4.0238
REMARK 3 L33: 1.1652 L12: 0.0517
REMARK 3 L13: -1.3589 L23: 0.6942
REMARK 3 S TENSOR
REMARK 3 S11: -0.0677 S12: 0.1150 S13: 0.0090
REMARK 3 S21: -0.0483 S22: 0.0592 S23: -0.3963
REMARK 3 S31: 0.3959 S32: 0.1568 S33: -0.0417
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN D AND RESID 5:37)
REMARK 3 ORIGIN FOR THE GROUP (A): 47.8758 74.8255 83.6150
REMARK 3 T TENSOR
REMARK 3 T11: 0.3183 T22: 0.1407
REMARK 3 T33: 0.2683 T12: 0.0221
REMARK 3 T13: -0.1701 T23: -0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 6.3018 L22: 1.8250
REMARK 3 L33: 6.2562 L12: -0.5901
REMARK 3 L13: -1.2774 L23: 1.0822
REMARK 3 S TENSOR
REMARK 3 S11: -0.0375 S12: 0.0849 S13: -0.3702
REMARK 3 S21: -0.1423 S22: 0.0491 S23: -0.0484
REMARK 3 S31: 0.2350 S32: 0.4527 S33: -0.0736
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN D AND RESID 38:54)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.2766 83.4493 93.6916
REMARK 3 T TENSOR
REMARK 3 T11: 0.4612 T22: 0.4778
REMARK 3 T33: 0.3401 T12: 0.0445
REMARK 3 T13: -0.1266 T23: -0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 4.0163 L22: 8.2036
REMARK 3 L33: 5.8350 L12: 2.0751
REMARK 3 L13: 3.4706 L23: 2.2888
REMARK 3 S TENSOR
REMARK 3 S11: -0.2623 S12: -0.5302 S13: -0.0999
REMARK 3 S21: 1.4559 S22: 0.3681 S23: -0.6348
REMARK 3 S31: -0.6700 S32: 0.3985 S33: -0.1070
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN D AND RESID 55:179)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1419 98.4254 78.7236
REMARK 3 T TENSOR
REMARK 3 T11: 0.3140 T22: 0.1557
REMARK 3 T33: 0.2385 T12: 0.0533
REMARK 3 T13: -0.0910 T23: -0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 1.4631 L22: 2.4144
REMARK 3 L33: 1.3964 L12: 1.3366
REMARK 3 L13: -0.3524 L23: 0.5224
REMARK 3 S TENSOR
REMARK 3 S11: 0.0372 S12: -0.0201 S13: 0.2172
REMARK 3 S21: 0.0380 S22: -0.0754 S23: 0.1070
REMARK 3 S31: -0.3179 S32: -0.0621 S33: 0.0132
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN D AND RESID 180:283)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.6116 82.4015 69.9333
REMARK 3 T TENSOR
REMARK 3 T11: 0.2073 T22: 0.1717
REMARK 3 T33: 0.1969 T12: 0.0174
REMARK 3 T13: -0.0948 T23: -0.0193
REMARK 3 L TENSOR
REMARK 3 L11: 0.6139 L22: 2.0615
REMARK 3 L33: 2.2896 L12: 0.2890
REMARK 3 L13: -0.0109 L23: -0.2680
REMARK 3 S TENSOR
REMARK 3 S11: 0.0482 S12: 0.0173 S13: 0.0089
REMARK 3 S21: -0.0603 S22: -0.0528 S23: 0.1314
REMARK 3 S31: -0.1720 S32: -0.1476 S33: -0.0112
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN D AND RESID 284:321)
REMARK 3 ORIGIN FOR THE GROUP (A): 48.3763 89.9068 76.0409
REMARK 3 T TENSOR
REMARK 3 T11: 0.3075 T22: 0.2239
REMARK 3 T33: 0.2333 T12: -0.0622
REMARK 3 T13: -0.0941 T23: -0.0273
REMARK 3 L TENSOR
REMARK 3 L11: 3.7546 L22: 2.5515
REMARK 3 L33: 2.0606 L12: -0.0971
REMARK 3 L13: 0.9424 L23: 2.1272
REMARK 3 S TENSOR
REMARK 3 S11: 0.0010 S12: -0.1671 S13: 0.1566
REMARK 3 S21: 0.2885 S22: -0.0723 S23: -0.3762
REMARK 3 S31: -0.3992 S32: 0.2995 S33: 0.0647
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 5JD5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220347.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 103264
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 24.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.6300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.57400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.160
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: 2WIR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5, 0.2 M SODIUM
REMARK 280 ACETATE, 30% (W/V) PEG4K, 1/70 CHYMOTRYPSIN. CRYOPROTECTANT:
REMARK 280 PARATONE-N OIL., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 45.83400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.83500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.58000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.83500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.83400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.58000
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, 3, 4, 5, 6
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 MET A 1
REMARK 465 SER A 2
REMARK 465 GLY A 3
REMARK 465 ASP A 4
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLY B 3
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLY C 3
REMARK 465 ASP C 4
REMARK 465 ASN C 5
REMARK 465 ASP C 321
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 GLY D 3
REMARK 465 ASP D 4
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 B 1010 O HOH D 883 1.87
REMARK 500 O HOH D 631 O HOH D 766 2.06
REMARK 500 O HOH D 529 O HOH D 680 2.08
REMARK 500 O HOH C 401 O HOH C 715 2.19
REMARK 500 O HOH D 729 O HOH D 778 2.19
REMARK 500 O HOH D 590 O HOH D 701 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH C 853 O HOH D 834 1545 2.18
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 PRO A 56 -38.26 -38.69
REMARK 500 GLN A 108 42.15 -151.38
REMARK 500 OAS A 169 -118.91 50.21
REMARK 500 PHE A 198 62.47 26.56
REMARK 500 TRP A 205 115.81 78.76
REMARK 500 ILE A 219 -53.62 66.27
REMARK 500 ASP A 264 56.07 -106.89
REMARK 500 GLN B 108 43.47 -148.39
REMARK 500 OAS B 169 -110.53 68.65
REMARK 500 PHE B 198 62.41 23.46
REMARK 500 TRP B 205 118.69 77.53
REMARK 500 ILE B 219 -52.09 69.38
REMARK 500 ASP B 264 53.00 -105.45
REMARK 500 GLN C 108 44.43 -150.32
REMARK 500 OAS C 169 -115.64 55.75
REMARK 500 PHE C 198 64.58 21.28
REMARK 500 TRP C 205 116.22 76.66
REMARK 500 ILE C 219 -56.08 66.82
REMARK 500 ASP C 264 52.00 -104.76
REMARK 500 GLN D 108 45.31 -151.04
REMARK 500 OAS D 169 -119.34 56.03
REMARK 500 PHE D 198 63.42 22.49
REMARK 500 TRP D 205 117.31 76.52
REMARK 500 ILE D 219 -53.26 67.23
REMARK 500 ASP D 264 50.72 -104.74
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 A1024 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A1025 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A1026 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A1027 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH A1028 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH A1029 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH A1030 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A1031 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH A1032 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH A1035 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH A1037 DISTANCE = 6.84 ANGSTROMS
REMARK 525 HOH A1038 DISTANCE = 7.15 ANGSTROMS
REMARK 525 HOH A1040 DISTANCE = 8.59 ANGSTROMS
REMARK 525 HOH B 999 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH B1000 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH B1001 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH B1002 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH B1003 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH B1004 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH B1005 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH B1006 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH B1007 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH B1008 DISTANCE = 7.09 ANGSTROMS
REMARK 525 HOH B1009 DISTANCE = 7.22 ANGSTROMS
REMARK 525 HOH B1010 DISTANCE = 8.63 ANGSTROMS
REMARK 525 HOH C 872 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH C 873 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH C 874 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH C 875 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH C 876 DISTANCE = 6.18 ANGSTROMS
REMARK 525 HOH C 877 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH C 878 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH C 879 DISTANCE = 6.89 ANGSTROMS
REMARK 525 HOH C 880 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH C 881 DISTANCE = 7.14 ANGSTROMS
REMARK 525 HOH D 873 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH D 875 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH D 876 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH D 877 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH D 878 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH D 879 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH D 880 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH D 881 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH D 882 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH D 883 DISTANCE = 7.96 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLU B 168 and OAS B
REMARK 800 169
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide OAS B 169 and ALA B
REMARK 800 170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLU C 168 and OAS C
REMARK 800 169
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide OAS C 169 and ALA C
REMARK 800 170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLU D 168 and OAS D
REMARK 800 169
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide OAS D 169 and ALA D
REMARK 800 170
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JD3 RELATED DB: PDB
REMARK 900 RELATED ID: 5JD4 RELATED DB: PDB
REMARK 900 RELATED ID: 5JD6 RELATED DB: PDB
DBREF 5JD5 A 1 321 PDB 5JD5 5JD5 1 321
DBREF 5JD5 B 1 321 PDB 5JD5 5JD5 1 321
DBREF 5JD5 C 1 321 PDB 5JD5 5JD5 1 321
DBREF 5JD5 D 1 321 PDB 5JD5 5JD5 1 321
SEQRES 1 A 321 MET SER GLY ASP ASN PRO PHE ASP PRO GLU LEU TYR LYS
SEQRES 2 A 321 ASP ALA ALA VAL SER ALA GLU THR ARG ALA LEU ASN THR
SEQRES 3 A 321 ALA LEU ILE ASP LEU LEU GLU THR SER ASP ASP ASN TRP
SEQRES 4 A 321 ASP ILE GLY VAL GLU GLU ALA ARG ALA ARG ARG ASP ARG
SEQRES 5 A 321 GLY GLU GLY PRO PHE PRO ALA VAL PRO LYS SER PRO ARG
SEQRES 6 A 321 ALA ARG THR ILE GLN ILE PRO GLY LYS GLY GLY ASP ILE
SEQRES 7 A 321 ALA LEU ARG ILE ILE ALA PRO GLU THR PRO LYS GLY VAL
SEQRES 8 A 321 TYR LEU HIS PHE HIS GLY GLY GLY TRP VAL PHE GLY SER
SEQRES 9 A 321 ALA ASP GLY GLN ASP PRO MET LEU GLU ARG ILE SER ASP
SEQRES 10 A 321 THR THR GLY LEU VAL CYS VAL SER VAL GLU TYR ARG LEU
SEQRES 11 A 321 ALA PRO GLU HIS PRO TYR PRO ALA GLY PRO ASP ASP CYS
SEQRES 12 A 321 GLU SER ALA ALA LEU TRP LEU VAL GLU ASN ALA LYS ARG
SEQRES 13 A 321 GLU PHE GLY THR ASP LEU LEU THR ILE GLY GLY GLU OAS
SEQRES 14 A 321 ALA GLY GLY HIS LEU ALA ALA VAL THR LEU LEU ARG MET
SEQRES 15 A 321 ARG ASP ARG HIS GLY PHE THR GLY PHE ALA GLY ALA ASN
SEQRES 16 A 321 LEU VAL PHE GLY ALA PHE ASP LEU ARG TRP THR PRO SER
SEQRES 17 A 321 ALA ARG SER TYR GLY ASN ASP ARG TYR LEU ILE LEU ARG
SEQRES 18 A 321 THR LEU ASP LEU GLU LYS PHE ASP ALA CYS PHE LEU PRO
SEQRES 19 A 321 GLU ASN VAL ASP ARG ALA ASP PRO ASP ILE SER PRO LEU
SEQRES 20 A 321 MET ALA ASN LEU HIS ASP MET PRO PRO ALA LEU PHE THR
SEQRES 21 A 321 VAL GLY THR ASP ASP ALA LEU LEU ASP ASP SER LEU PHE
SEQRES 22 A 321 MET HIS ALA ARG TRP ALA ALA ALA GLY ASN GLU ALA GLU
SEQRES 23 A 321 LEU ALA VAL TYR PRO GLY GLY ALA HIS GLY PHE VAL ALA
SEQRES 24 A 321 PHE PRO GLY ALA LEU ALA ALA SER ALA VAL GLN ARG MET
SEQRES 25 A 321 ASP ALA PHE LEU LYS ARG PHE THR ASP
SEQRES 1 B 321 MET SER GLY ASP ASN PRO PHE ASP PRO GLU LEU TYR LYS
SEQRES 2 B 321 ASP ALA ALA VAL SER ALA GLU THR ARG ALA LEU ASN THR
SEQRES 3 B 321 ALA LEU ILE ASP LEU LEU GLU THR SER ASP ASP ASN TRP
SEQRES 4 B 321 ASP ILE GLY VAL GLU GLU ALA ARG ALA ARG ARG ASP ARG
SEQRES 5 B 321 GLY GLU GLY PRO PHE PRO ALA VAL PRO LYS SER PRO ARG
SEQRES 6 B 321 ALA ARG THR ILE GLN ILE PRO GLY LYS GLY GLY ASP ILE
SEQRES 7 B 321 ALA LEU ARG ILE ILE ALA PRO GLU THR PRO LYS GLY VAL
SEQRES 8 B 321 TYR LEU HIS PHE HIS GLY GLY GLY TRP VAL PHE GLY SER
SEQRES 9 B 321 ALA ASP GLY GLN ASP PRO MET LEU GLU ARG ILE SER ASP
SEQRES 10 B 321 THR THR GLY LEU VAL CYS VAL SER VAL GLU TYR ARG LEU
SEQRES 11 B 321 ALA PRO GLU HIS PRO TYR PRO ALA GLY PRO ASP ASP CYS
SEQRES 12 B 321 GLU SER ALA ALA LEU TRP LEU VAL GLU ASN ALA LYS ARG
SEQRES 13 B 321 GLU PHE GLY THR ASP LEU LEU THR ILE GLY GLY GLU OAS
SEQRES 14 B 321 ALA GLY GLY HIS LEU ALA ALA VAL THR LEU LEU ARG MET
SEQRES 15 B 321 ARG ASP ARG HIS GLY PHE THR GLY PHE ALA GLY ALA ASN
SEQRES 16 B 321 LEU VAL PHE GLY ALA PHE ASP LEU ARG TRP THR PRO SER
SEQRES 17 B 321 ALA ARG SER TYR GLY ASN ASP ARG TYR LEU ILE LEU ARG
SEQRES 18 B 321 THR LEU ASP LEU GLU LYS PHE ASP ALA CYS PHE LEU PRO
SEQRES 19 B 321 GLU ASN VAL ASP ARG ALA ASP PRO ASP ILE SER PRO LEU
SEQRES 20 B 321 MET ALA ASN LEU HIS ASP MET PRO PRO ALA LEU PHE THR
SEQRES 21 B 321 VAL GLY THR ASP ASP ALA LEU LEU ASP ASP SER LEU PHE
SEQRES 22 B 321 MET HIS ALA ARG TRP ALA ALA ALA GLY ASN GLU ALA GLU
SEQRES 23 B 321 LEU ALA VAL TYR PRO GLY GLY ALA HIS GLY PHE VAL ALA
SEQRES 24 B 321 PHE PRO GLY ALA LEU ALA ALA SER ALA VAL GLN ARG MET
SEQRES 25 B 321 ASP ALA PHE LEU LYS ARG PHE THR ASP
SEQRES 1 C 321 MET SER GLY ASP ASN PRO PHE ASP PRO GLU LEU TYR LYS
SEQRES 2 C 321 ASP ALA ALA VAL SER ALA GLU THR ARG ALA LEU ASN THR
SEQRES 3 C 321 ALA LEU ILE ASP LEU LEU GLU THR SER ASP ASP ASN TRP
SEQRES 4 C 321 ASP ILE GLY VAL GLU GLU ALA ARG ALA ARG ARG ASP ARG
SEQRES 5 C 321 GLY GLU GLY PRO PHE PRO ALA VAL PRO LYS SER PRO ARG
SEQRES 6 C 321 ALA ARG THR ILE GLN ILE PRO GLY LYS GLY GLY ASP ILE
SEQRES 7 C 321 ALA LEU ARG ILE ILE ALA PRO GLU THR PRO LYS GLY VAL
SEQRES 8 C 321 TYR LEU HIS PHE HIS GLY GLY GLY TRP VAL PHE GLY SER
SEQRES 9 C 321 ALA ASP GLY GLN ASP PRO MET LEU GLU ARG ILE SER ASP
SEQRES 10 C 321 THR THR GLY LEU VAL CYS VAL SER VAL GLU TYR ARG LEU
SEQRES 11 C 321 ALA PRO GLU HIS PRO TYR PRO ALA GLY PRO ASP ASP CYS
SEQRES 12 C 321 GLU SER ALA ALA LEU TRP LEU VAL GLU ASN ALA LYS ARG
SEQRES 13 C 321 GLU PHE GLY THR ASP LEU LEU THR ILE GLY GLY GLU OAS
SEQRES 14 C 321 ALA GLY GLY HIS LEU ALA ALA VAL THR LEU LEU ARG MET
SEQRES 15 C 321 ARG ASP ARG HIS GLY PHE THR GLY PHE ALA GLY ALA ASN
SEQRES 16 C 321 LEU VAL PHE GLY ALA PHE ASP LEU ARG TRP THR PRO SER
SEQRES 17 C 321 ALA ARG SER TYR GLY ASN ASP ARG TYR LEU ILE LEU ARG
SEQRES 18 C 321 THR LEU ASP LEU GLU LYS PHE ASP ALA CYS PHE LEU PRO
SEQRES 19 C 321 GLU ASN VAL ASP ARG ALA ASP PRO ASP ILE SER PRO LEU
SEQRES 20 C 321 MET ALA ASN LEU HIS ASP MET PRO PRO ALA LEU PHE THR
SEQRES 21 C 321 VAL GLY THR ASP ASP ALA LEU LEU ASP ASP SER LEU PHE
SEQRES 22 C 321 MET HIS ALA ARG TRP ALA ALA ALA GLY ASN GLU ALA GLU
SEQRES 23 C 321 LEU ALA VAL TYR PRO GLY GLY ALA HIS GLY PHE VAL ALA
SEQRES 24 C 321 PHE PRO GLY ALA LEU ALA ALA SER ALA VAL GLN ARG MET
SEQRES 25 C 321 ASP ALA PHE LEU LYS ARG PHE THR ASP
SEQRES 1 D 321 MET SER GLY ASP ASN PRO PHE ASP PRO GLU LEU TYR LYS
SEQRES 2 D 321 ASP ALA ALA VAL SER ALA GLU THR ARG ALA LEU ASN THR
SEQRES 3 D 321 ALA LEU ILE ASP LEU LEU GLU THR SER ASP ASP ASN TRP
SEQRES 4 D 321 ASP ILE GLY VAL GLU GLU ALA ARG ALA ARG ARG ASP ARG
SEQRES 5 D 321 GLY GLU GLY PRO PHE PRO ALA VAL PRO LYS SER PRO ARG
SEQRES 6 D 321 ALA ARG THR ILE GLN ILE PRO GLY LYS GLY GLY ASP ILE
SEQRES 7 D 321 ALA LEU ARG ILE ILE ALA PRO GLU THR PRO LYS GLY VAL
SEQRES 8 D 321 TYR LEU HIS PHE HIS GLY GLY GLY TRP VAL PHE GLY SER
SEQRES 9 D 321 ALA ASP GLY GLN ASP PRO MET LEU GLU ARG ILE SER ASP
SEQRES 10 D 321 THR THR GLY LEU VAL CYS VAL SER VAL GLU TYR ARG LEU
SEQRES 11 D 321 ALA PRO GLU HIS PRO TYR PRO ALA GLY PRO ASP ASP CYS
SEQRES 12 D 321 GLU SER ALA ALA LEU TRP LEU VAL GLU ASN ALA LYS ARG
SEQRES 13 D 321 GLU PHE GLY THR ASP LEU LEU THR ILE GLY GLY GLU OAS
SEQRES 14 D 321 ALA GLY GLY HIS LEU ALA ALA VAL THR LEU LEU ARG MET
SEQRES 15 D 321 ARG ASP ARG HIS GLY PHE THR GLY PHE ALA GLY ALA ASN
SEQRES 16 D 321 LEU VAL PHE GLY ALA PHE ASP LEU ARG TRP THR PRO SER
SEQRES 17 D 321 ALA ARG SER TYR GLY ASN ASP ARG TYR LEU ILE LEU ARG
SEQRES 18 D 321 THR LEU ASP LEU GLU LYS PHE ASP ALA CYS PHE LEU PRO
SEQRES 19 D 321 GLU ASN VAL ASP ARG ALA ASP PRO ASP ILE SER PRO LEU
SEQRES 20 D 321 MET ALA ASN LEU HIS ASP MET PRO PRO ALA LEU PHE THR
SEQRES 21 D 321 VAL GLY THR ASP ASP ALA LEU LEU ASP ASP SER LEU PHE
SEQRES 22 D 321 MET HIS ALA ARG TRP ALA ALA ALA GLY ASN GLU ALA GLU
SEQRES 23 D 321 LEU ALA VAL TYR PRO GLY GLY ALA HIS GLY PHE VAL ALA
SEQRES 24 D 321 PHE PRO GLY ALA LEU ALA ALA SER ALA VAL GLN ARG MET
SEQRES 25 D 321 ASP ALA PHE LEU LYS ARG PHE THR ASP
HET OAS A 169 9
HET OAS B 169 9
HET OAS C 169 9
HET OAS D 169 9
HET CL A 401 1
HET CL B 401 1
HETNAM OAS O-ACETYLSERINE
HETNAM CL CHLORIDE ION
FORMUL 1 OAS 4(C5 H9 N O4)
FORMUL 5 CL 2(CL 1-)
FORMUL 7 HOH *2009(H2 O)
HELIX 1 AA1 ASP A 8 VAL A 17 5 10
HELIX 2 AA2 SER A 18 SER A 35 1 18
HELIX 3 AA3 ASP A 37 GLY A 42 1 6
HELIX 4 AA4 GLY A 42 ARG A 52 1 11
HELIX 5 AA5 GLN A 108 GLY A 120 1 13
HELIX 6 AA6 PRO A 137 GLY A 159 1 23
HELIX 7 AA7 OAS A 169 GLY A 187 1 19
HELIX 8 AA8 THR A 206 TYR A 212 1 7
HELIX 9 AA9 ARG A 221 LEU A 233 1 13
HELIX 10 AB1 SER A 245 ALA A 249 5 5
HELIX 11 AB2 LEU A 267 ALA A 281 1 15
HELIX 12 AB3 GLY A 296 PHE A 300 5 5
HELIX 13 AB4 GLY A 302 PHE A 319 1 18
HELIX 14 AB5 ASP B 8 VAL B 17 5 10
HELIX 15 AB6 SER B 18 SER B 35 1 18
HELIX 16 AB7 ASP B 37 GLY B 42 1 6
HELIX 17 AB8 GLY B 42 ARG B 52 1 11
HELIX 18 AB9 GLN B 108 GLY B 120 1 13
HELIX 19 AC1 PRO B 137 GLY B 159 1 23
HELIX 20 AC2 OAS B 169 GLY B 187 1 19
HELIX 21 AC3 THR B 206 TYR B 212 1 7
HELIX 22 AC4 ARG B 221 LEU B 233 1 13
HELIX 23 AC5 SER B 245 ALA B 249 5 5
HELIX 24 AC6 LEU B 267 ALA B 281 1 15
HELIX 25 AC7 GLY B 296 PHE B 300 5 5
HELIX 26 AC8 GLY B 302 ARG B 318 1 17
HELIX 27 AC9 PHE B 319 ASP B 321 5 3
HELIX 28 AD1 ASP C 8 VAL C 17 5 10
HELIX 29 AD2 SER C 18 SER C 35 1 18
HELIX 30 AD3 ASP C 37 GLY C 42 1 6
HELIX 31 AD4 GLY C 42 ARG C 52 1 11
HELIX 32 AD5 GLN C 108 GLY C 120 1 13
HELIX 33 AD6 PRO C 137 GLY C 159 1 23
HELIX 34 AD7 OAS C 169 HIS C 186 1 18
HELIX 35 AD8 THR C 206 TYR C 212 1 7
HELIX 36 AD9 ARG C 221 LEU C 233 1 13
HELIX 37 AE1 SER C 245 ALA C 249 5 5
HELIX 38 AE2 LEU C 267 ALA C 281 1 15
HELIX 39 AE3 GLY C 296 PHE C 300 5 5
HELIX 40 AE4 GLY C 302 ARG C 318 1 17
HELIX 41 AE5 ASP D 8 VAL D 17 5 10
HELIX 42 AE6 SER D 18 SER D 35 1 18
HELIX 43 AE7 ASP D 37 GLY D 42 1 6
HELIX 44 AE8 GLY D 42 ARG D 52 1 11
HELIX 45 AE9 GLN D 108 GLY D 120 1 13
HELIX 46 AF1 PRO D 137 GLY D 159 1 23
HELIX 47 AF2 OAS D 169 GLY D 187 1 19
HELIX 48 AF3 THR D 206 TYR D 212 1 7
HELIX 49 AF4 ARG D 221 LEU D 233 1 13
HELIX 50 AF5 SER D 245 ALA D 249 5 5
HELIX 51 AF6 LEU D 267 ALA D 281 1 15
HELIX 52 AF7 GLY D 296 PHE D 300 5 5
HELIX 53 AF8 GLY D 302 PHE D 319 1 18
SHEET 1 AA1 8 ARG A 67 GLY A 73 0
SHEET 2 AA1 8 GLY A 76 ILE A 83 -1 O ILE A 82 N ARG A 67
SHEET 3 AA1 8 VAL A 122 VAL A 126 -1 O SER A 125 N ARG A 81
SHEET 4 AA1 8 VAL A 91 PHE A 95 1 N HIS A 94 O VAL A 124
SHEET 5 AA1 8 LEU A 163 GLU A 168 1 O THR A 164 N LEU A 93
SHEET 6 AA1 8 PHE A 191 VAL A 197 1 O ALA A 192 N LEU A 163
SHEET 7 AA1 8 ALA A 257 ASP A 264 1 O LEU A 258 N ALA A 194
SHEET 8 AA1 8 ALA A 285 ALA A 294 1 O GLU A 286 N PHE A 259
SHEET 1 AA2 8 ARG B 67 GLY B 73 0
SHEET 2 AA2 8 GLY B 76 ILE B 83 -1 O ILE B 82 N ARG B 67
SHEET 3 AA2 8 VAL B 122 GLU B 127 -1 O SER B 125 N ARG B 81
SHEET 4 AA2 8 VAL B 91 PHE B 95 1 N HIS B 94 O VAL B 124
SHEET 5 AA2 8 LEU B 163 GLU B 168 1 O THR B 164 N VAL B 91
SHEET 6 AA2 8 PHE B 191 VAL B 197 1 O ALA B 192 N LEU B 163
SHEET 7 AA2 8 ALA B 257 ASP B 264 1 O LEU B 258 N ALA B 194
SHEET 8 AA2 8 ALA B 285 ALA B 294 1 O ALA B 288 N PHE B 259
SHEET 1 AA3 8 ARG C 67 GLY C 73 0
SHEET 2 AA3 8 GLY C 76 ILE C 83 -1 O ILE C 78 N ILE C 71
SHEET 3 AA3 8 VAL C 122 VAL C 126 -1 O CYS C 123 N ILE C 83
SHEET 4 AA3 8 VAL C 91 PHE C 95 1 N HIS C 94 O VAL C 124
SHEET 5 AA3 8 LEU C 163 GLU C 168 1 O THR C 164 N VAL C 91
SHEET 6 AA3 8 PHE C 191 VAL C 197 1 O ALA C 192 N LEU C 163
SHEET 7 AA3 8 ALA C 257 ASP C 264 1 O LEU C 258 N ALA C 194
SHEET 8 AA3 8 ALA C 285 ALA C 294 1 O ALA C 288 N PHE C 259
SHEET 1 AA4 8 ARG D 67 GLY D 73 0
SHEET 2 AA4 8 GLY D 76 ILE D 83 -1 O ILE D 82 N ARG D 67
SHEET 3 AA4 8 VAL D 122 VAL D 126 -1 O SER D 125 N ARG D 81
SHEET 4 AA4 8 VAL D 91 PHE D 95 1 N TYR D 92 O VAL D 124
SHEET 5 AA4 8 LEU D 163 GLU D 168 1 O THR D 164 N LEU D 93
SHEET 6 AA4 8 PHE D 191 VAL D 197 1 O ALA D 192 N LEU D 163
SHEET 7 AA4 8 ALA D 257 ASP D 264 1 O LEU D 258 N ALA D 194
SHEET 8 AA4 8 ALA D 285 ALA D 294 1 O ALA D 288 N PHE D 259
LINK C GLU A 168 N OAS A 169 1555 1555 1.33
LINK C OAS A 169 N ALA A 170 1555 1555 1.33
LINK C GLU B 168 N OAS B 169 1555 1555 1.26
LINK C OAS B 169 N ALA B 170 1555 1555 1.43
LINK C GLU C 168 N OAS C 169 1555 1555 1.32
LINK C OAS C 169 N ALA C 170 1555 1555 1.32
LINK C GLU D 168 N OAS D 169 1555 1555 1.34
LINK C OAS D 169 N ALA D 170 1555 1555 1.30
CISPEP 1 ALA A 131 PRO A 132 0 -0.17
CISPEP 2 TYR A 136 PRO A 137 0 4.86
CISPEP 3 ALA B 131 PRO B 132 0 -0.62
CISPEP 4 TYR B 136 PRO B 137 0 5.29
CISPEP 5 ALA C 131 PRO C 132 0 1.38
CISPEP 6 TYR C 136 PRO C 137 0 3.20
CISPEP 7 ASN D 5 PRO D 6 0 -9.16
CISPEP 8 ALA D 131 PRO D 132 0 -2.22
CISPEP 9 TYR D 136 PRO D 137 0 4.12
SITE 1 AC1 3 ALA A 15 THR A 68 HOH A 942
SITE 1 AC2 2 ARG B 204 ARG D 210
SITE 1 AC3 18 HIS B 94 PHE B 95 GLY B 97 GLY B 98
SITE 2 AC3 18 GLY B 99 GLY B 167 ALA B 170 GLY B 171
SITE 3 AC3 18 GLY B 172 HIS B 173 VAL B 197 PHE B 198
SITE 4 AC3 18 GLY B 199 ALA B 200 HIS B 295 HOH B 547
SITE 5 AC3 18 HOH B 648 HOH B 653
SITE 1 AC4 13 GLY B 98 GLY B 99 TRP B 100 GLU B 168
SITE 2 AC4 13 GLY B 171 GLY B 172 HIS B 173 LEU B 174
SITE 3 AC4 13 VAL B 197 PHE B 198 GLY B 199 ALA B 200
SITE 4 AC4 13 HIS B 295
SITE 1 AC5 18 HIS C 94 PHE C 95 GLY C 97 GLY C 98
SITE 2 AC5 18 GLY C 99 GLY C 167 ALA C 170 GLY C 171
SITE 3 AC5 18 GLY C 172 HIS C 173 VAL C 197 PHE C 198
SITE 4 AC5 18 GLY C 199 ALA C 200 HIS C 295 HOH C 423
SITE 5 AC5 18 HOH C 531 HOH C 584
SITE 1 AC6 13 GLY C 98 GLY C 99 TRP C 100 GLU C 168
SITE 2 AC6 13 GLY C 171 GLY C 172 HIS C 173 LEU C 174
SITE 3 AC6 13 VAL C 197 PHE C 198 GLY C 199 ALA C 200
SITE 4 AC6 13 HIS C 295
SITE 1 AC7 17 HIS D 94 PHE D 95 GLY D 97 GLY D 98
SITE 2 AC7 17 GLY D 99 GLY D 167 ALA D 170 GLY D 171
SITE 3 AC7 17 GLY D 172 HIS D 173 VAL D 197 PHE D 198
SITE 4 AC7 17 GLY D 199 ALA D 200 HIS D 295 HOH D 432
SITE 5 AC7 17 HOH D 544
SITE 1 AC8 13 GLY D 98 GLY D 99 TRP D 100 GLU D 168
SITE 2 AC8 13 GLY D 171 GLY D 172 HIS D 173 LEU D 174
SITE 3 AC8 13 VAL D 197 PHE D 198 GLY D 199 ALA D 200
SITE 4 AC8 13 HIS D 295
CRYST1 91.668 97.160 167.670 90.00 90.00 90.00 P 21 21 21 16
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 0.010909 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010292 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005964 0.00000
TER 2436 ASP A 321
TER 4874 ASP B 321
TER 7292 THR C 320
TER 9719 ASP D 321
MASTER 745 0 6 53 32 0 29 611707 4 44 100
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