HEADER TRANSFERASE 11-AUG-15 5D5P
TITLE HCGB FROM METHANOCOCCUS MARIPALUDIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HCGB;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOCOCCUS MARIPALUDIS (STRAIN S2 / LL);
SOURCE 3 ORGANISM_TAXID: 267377;
SOURCE 4 GENE: MMP1497;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET24B
KEYWDS GUANYLYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.FUJISHIRO,U.ERMLER,S.SHIMA
REVDAT 4 10-JAN-24 5D5P 1 REMARK
REVDAT 3 14-JUN-17 5D5P 1 JRNL
REVDAT 2 29-MAR-17 5D5P 1 JRNL
REVDAT 1 26-OCT-16 5D5P 0
JRNL AUTH L.BAI,T.FUJISHIRO,G.HUANG,J.KOCH,A.TAKABAYASHI,M.YOKONO,
JRNL AUTH 2 A.TANAKA,T.XU,X.HU,U.ERMLER,S.SHIMA
JRNL TITL TOWARDS ARTIFICIAL METHANOGENESIS: BIOSYNTHESIS OF THE
JRNL TITL 2 [FE]-HYDROGENASE COFACTOR AND CHARACTERIZATION OF THE
JRNL TITL 3 SEMI-SYNTHETIC HYDROGENASE.
JRNL REF FARADAY DISCUSS. V. 198 37 2017
JRNL REFN ISSN 1359-6640
JRNL PMID 28294213
JRNL DOI 10.1039/C6FD00209A
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.68
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 70402
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3520
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 43.6890 - 4.9685 0.99 2747 144 0.1640 0.1772
REMARK 3 2 4.9685 - 3.9445 0.99 2687 142 0.1371 0.1669
REMARK 3 3 3.9445 - 3.4461 0.99 2674 141 0.1651 0.1716
REMARK 3 4 3.4461 - 3.1311 1.00 2698 142 0.1896 0.2335
REMARK 3 5 3.1311 - 2.9067 1.00 2664 140 0.1913 0.2328
REMARK 3 6 2.9067 - 2.7354 0.99 2680 141 0.1912 0.1976
REMARK 3 7 2.7354 - 2.5984 1.00 2689 141 0.1896 0.2573
REMARK 3 8 2.5984 - 2.4853 1.00 2684 142 0.1845 0.2208
REMARK 3 9 2.4853 - 2.3896 1.00 2678 141 0.1872 0.2036
REMARK 3 10 2.3896 - 2.3072 1.00 2670 140 0.1906 0.2700
REMARK 3 11 2.3072 - 2.2351 1.00 2664 140 0.1895 0.1973
REMARK 3 12 2.2351 - 2.1712 1.00 2709 143 0.1855 0.2431
REMARK 3 13 2.1712 - 2.1140 1.00 2660 140 0.1928 0.2129
REMARK 3 14 2.1140 - 2.0624 1.00 2673 141 0.1992 0.2234
REMARK 3 15 2.0624 - 2.0155 1.00 2665 140 0.2016 0.2069
REMARK 3 16 2.0155 - 1.9727 1.00 2678 141 0.2128 0.2482
REMARK 3 17 1.9727 - 1.9332 1.00 2682 141 0.2139 0.2650
REMARK 3 18 1.9332 - 1.8967 1.00 2656 140 0.2159 0.2608
REMARK 3 19 1.8967 - 1.8628 1.00 2663 140 0.2329 0.2644
REMARK 3 20 1.8628 - 1.8313 1.00 2665 140 0.2428 0.2811
REMARK 3 21 1.8313 - 1.8017 1.00 2700 142 0.2657 0.3142
REMARK 3 22 1.8017 - 1.7740 1.00 2614 138 0.2719 0.3702
REMARK 3 23 1.7740 - 1.7479 0.99 2680 141 0.2699 0.2720
REMARK 3 24 1.7479 - 1.7233 0.99 2646 139 0.2770 0.3283
REMARK 3 25 1.7233 - 1.7000 1.00 2656 140 0.3015 0.3079
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 : 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) : 22.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.49
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.15
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 : 0.011 4783
REMARK 3 ANGLE : 1.351 6465
REMARK 3 CHIRALITY : 0.064 825
REMARK 3 PLANARITY : 0.008 816
REMARK 3 DIHEDRAL : 11.772 1849
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 23 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8033 -14.1900 36.5571
REMARK 3 T TENSOR
REMARK 3 T11: 0.4498 T22: 0.5759
REMARK 3 T33: 0.5520 T12: 0.0282
REMARK 3 T13: 0.1249 T23: 0.0780
REMARK 3 L TENSOR
REMARK 3 L11: 2.0677 L22: 9.7206
REMARK 3 L33: 4.4756 L12: -2.3437
REMARK 3 L13: -1.9381 L23: -0.2021
REMARK 3 S TENSOR
REMARK 3 S11: 0.0050 S12: -1.1339 S13: -0.9434
REMARK 3 S21: 0.7956 S22: -0.4240 S23: 0.6506
REMARK 3 S31: 0.3641 S32: 0.1535 S33: 0.3376
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 24 THROUGH 67 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.8355 6.2415 23.9587
REMARK 3 T TENSOR
REMARK 3 T11: 0.2229 T22: 0.2217
REMARK 3 T33: 0.2804 T12: 0.0485
REMARK 3 T13: 0.0470 T23: -0.0422
REMARK 3 L TENSOR
REMARK 3 L11: 3.0675 L22: 4.0887
REMARK 3 L33: 6.1994 L12: -0.1055
REMARK 3 L13: -0.4083 L23: -2.2818
REMARK 3 S TENSOR
REMARK 3 S11: 0.0047 S12: -0.2532 S13: 0.3578
REMARK 3 S21: 0.4043 S22: 0.2109 S23: 0.4193
REMARK 3 S31: -0.7525 S32: -0.4305 S33: -0.2358
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 68 THROUGH 158 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1553 -1.3822 15.3276
REMARK 3 T TENSOR
REMARK 3 T11: 0.1385 T22: 0.1517
REMARK 3 T33: 0.1796 T12: 0.0459
REMARK 3 T13: 0.0066 T23: 0.0334
REMARK 3 L TENSOR
REMARK 3 L11: 2.0464 L22: 2.1004
REMARK 3 L33: 3.0725 L12: 0.0221
REMARK 3 L13: -0.2067 L23: 0.7617
REMARK 3 S TENSOR
REMARK 3 S11: 0.0512 S12: 0.0734 S13: 0.2521
REMARK 3 S21: -0.0940 S22: -0.0319 S23: 0.2122
REMARK 3 S31: -0.1701 S32: -0.2872 S33: -0.0207
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.5376 -29.3486 20.3511
REMARK 3 T TENSOR
REMARK 3 T11: 0.4943 T22: 0.2551
REMARK 3 T33: 0.4851 T12: 0.0960
REMARK 3 T13: 0.0968 T23: 0.0700
REMARK 3 L TENSOR
REMARK 3 L11: 6.8348 L22: 2.0410
REMARK 3 L33: 2.0057 L12: 0.9393
REMARK 3 L13: -2.2962 L23: 1.0464
REMARK 3 S TENSOR
REMARK 3 S11: -0.3302 S12: -0.5157 S13: -1.2111
REMARK 3 S21: 0.2659 S22: 0.1301 S23: 0.5885
REMARK 3 S31: 1.1473 S32: -0.0257 S33: 0.1809
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 17 THROUGH 35 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.1681 -27.5140 17.8438
REMARK 3 T TENSOR
REMARK 3 T11: 0.3719 T22: 0.2687
REMARK 3 T33: 0.3003 T12: 0.0889
REMARK 3 T13: -0.0321 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 8.2077 L22: 5.8710
REMARK 3 L33: 2.0088 L12: 0.1698
REMARK 3 L13: -3.9586 L23: -3.4619
REMARK 3 S TENSOR
REMARK 3 S11: -0.2719 S12: -1.0378 S13: -0.4186
REMARK 3 S21: 0.6718 S22: 0.0129 S23: -0.3501
REMARK 3 S31: 0.7797 S32: 0.9032 S33: 0.2738
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 36 THROUGH 67 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.4744 -13.7315 -2.0943
REMARK 3 T TENSOR
REMARK 3 T11: 0.1553 T22: 0.2231
REMARK 3 T33: 0.1152 T12: 0.0288
REMARK 3 T13: 0.0137 T23: -0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 6.6522 L22: 7.7174
REMARK 3 L33: 5.3531 L12: 2.8670
REMARK 3 L13: -0.6513 L23: -0.7128
REMARK 3 S TENSOR
REMARK 3 S11: -0.1859 S12: 0.4985 S13: -0.2615
REMARK 3 S21: -0.4359 S22: 0.1348 S23: -0.3105
REMARK 3 S31: 0.1401 S32: 0.0921 S33: 0.0339
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 68 THROUGH 92 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.6915 -5.2506 6.3675
REMARK 3 T TENSOR
REMARK 3 T11: 0.1841 T22: 0.1847
REMARK 3 T33: 0.1714 T12: 0.0311
REMARK 3 T13: 0.0273 T23: 0.0483
REMARK 3 L TENSOR
REMARK 3 L11: 4.5753 L22: 8.5986
REMARK 3 L33: 5.8889 L12: -0.4757
REMARK 3 L13: 1.0256 L23: 6.8286
REMARK 3 S TENSOR
REMARK 3 S11: 0.1128 S12: 0.3460 S13: 0.3439
REMARK 3 S21: -0.6550 S22: 0.0345 S23: -0.2788
REMARK 3 S31: -0.5584 S32: -0.0753 S33: -0.1395
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 93 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.0711 -8.1352 10.6459
REMARK 3 T TENSOR
REMARK 3 T11: 0.1050 T22: 0.1269
REMARK 3 T33: 0.1256 T12: 0.0171
REMARK 3 T13: -0.0038 T23: 0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 4.3809 L22: 2.1199
REMARK 3 L33: 3.6581 L12: -0.9514
REMARK 3 L13: -1.0203 L23: 0.2661
REMARK 3 S TENSOR
REMARK 3 S11: 0.0028 S12: 0.1329 S13: 0.1783
REMARK 3 S21: -0.1572 S22: 0.1025 S23: -0.3270
REMARK 3 S31: -0.2076 S32: 0.1722 S33: -0.0157
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 138 THROUGH 157 )
REMARK 3 ORIGIN FOR THE GROUP (A): 53.0792 -12.4191 9.1243
REMARK 3 T TENSOR
REMARK 3 T11: 0.1321 T22: 0.2662
REMARK 3 T33: 0.2505 T12: 0.0222
REMARK 3 T13: -0.0092 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 5.1814 L22: 6.9095
REMARK 3 L33: 4.2049 L12: 0.6162
REMARK 3 L13: -0.4154 L23: -0.3416
REMARK 3 S TENSOR
REMARK 3 S11: -0.0326 S12: -0.0436 S13: -0.0662
REMARK 3 S21: -0.1656 S22: -0.1549 S23: -0.8628
REMARK 3 S31: 0.0126 S32: 0.5947 S33: 0.0368
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4699 -8.3389 -3.0795
REMARK 3 T TENSOR
REMARK 3 T11: 0.2203 T22: 0.5243
REMARK 3 T33: 0.2323 T12: -0.0223
REMARK 3 T13: -0.0172 T23: 0.0931
REMARK 3 L TENSOR
REMARK 3 L11: 5.5151 L22: 9.1491
REMARK 3 L33: 8.1966 L12: 0.8071
REMARK 3 L13: -1.0795 L23: 0.7944
REMARK 3 S TENSOR
REMARK 3 S11: -0.1863 S12: 1.3093 S13: 0.3001
REMARK 3 S21: -0.8545 S22: 0.2697 S23: -0.1038
REMARK 3 S31: -0.0270 S32: 0.2363 S33: -0.0616
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 17 THROUGH 67 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2293 -23.1423 7.1564
REMARK 3 T TENSOR
REMARK 3 T11: 0.1141 T22: 0.1813
REMARK 3 T33: 0.1391 T12: 0.0123
REMARK 3 T13: -0.0130 T23: -0.0240
REMARK 3 L TENSOR
REMARK 3 L11: 2.5286 L22: 5.0037
REMARK 3 L33: 4.1034 L12: 0.2088
REMARK 3 L13: 0.0203 L23: -2.7643
REMARK 3 S TENSOR
REMARK 3 S11: -0.0442 S12: 0.2604 S13: -0.0211
REMARK 3 S21: -0.2085 S22: 0.0697 S23: 0.0382
REMARK 3 S31: 0.0535 S32: -0.1554 S33: -0.0591
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 68 THROUGH 92 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.7383 -20.6438 21.7269
REMARK 3 T TENSOR
REMARK 3 T11: 0.1946 T22: 0.1996
REMARK 3 T33: 0.1733 T12: -0.0200
REMARK 3 T13: -0.0217 T23: 0.0565
REMARK 3 L TENSOR
REMARK 3 L11: 4.0334 L22: 4.9242
REMARK 3 L33: 8.8187 L12: -0.8390
REMARK 3 L13: -0.1310 L23: 6.4668
REMARK 3 S TENSOR
REMARK 3 S11: 0.0758 S12: -0.4543 S13: -0.3850
REMARK 3 S21: 0.5340 S22: -0.0074 S23: -0.0722
REMARK 3 S31: 0.7135 S32: -0.1302 S33: -0.0563
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 93 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.4084 -17.3736 18.0261
REMARK 3 T TENSOR
REMARK 3 T11: 0.1358 T22: 0.1759
REMARK 3 T33: 0.1475 T12: -0.0156
REMARK 3 T13: -0.0175 T23: 0.0295
REMARK 3 L TENSOR
REMARK 3 L11: 2.1817 L22: 4.3677
REMARK 3 L33: 4.9295 L12: 1.1460
REMARK 3 L13: 0.6533 L23: 1.0270
REMARK 3 S TENSOR
REMARK 3 S11: -0.0019 S12: -0.0526 S13: -0.0607
REMARK 3 S21: 0.2365 S22: -0.0858 S23: 0.2584
REMARK 3 S31: 0.1855 S32: -0.5990 S33: 0.0988
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 138 THROUGH 157 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0060 -20.0227 13.0137
REMARK 3 T TENSOR
REMARK 3 T11: 0.1783 T22: 0.2772
REMARK 3 T33: 0.2743 T12: -0.0231
REMARK 3 T13: -0.0166 T23: 0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 7.2090 L22: 7.9471
REMARK 3 L33: 2.0422 L12: 0.0207
REMARK 3 L13: -0.6657 L23: -4.8148
REMARK 3 S TENSOR
REMARK 3 S11: 0.1733 S12: 0.0805 S13: -0.1448
REMARK 3 S21: 0.1578 S22: 0.3084 S23: 0.7653
REMARK 3 S31: 0.1329 S32: -1.0430 S33: -0.4582
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 15 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.0979 10.3637 15.9030
REMARK 3 T TENSOR
REMARK 3 T11: 0.4087 T22: 0.3174
REMARK 3 T33: 0.5368 T12: -0.0127
REMARK 3 T13: 0.0258 T23: 0.0440
REMARK 3 L TENSOR
REMARK 3 L11: 2.0486 L22: 2.0420
REMARK 3 L33: 9.6694 L12: 0.1422
REMARK 3 L13: 1.1877 L23: 0.7990
REMARK 3 S TENSOR
REMARK 3 S11: -0.0107 S12: 0.3014 S13: 1.2558
REMARK 3 S21: 0.4194 S22: -0.0465 S23: 0.3921
REMARK 3 S31: -1.1950 S32: 0.1467 S33: 0.0311
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 16 THROUGH 35 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.5443 9.0540 17.4554
REMARK 3 T TENSOR
REMARK 3 T11: 0.3691 T22: 0.3351
REMARK 3 T33: 0.4026 T12: -0.0602
REMARK 3 T13: 0.0360 T23: -0.0239
REMARK 3 L TENSOR
REMARK 3 L11: 9.1761 L22: 6.1994
REMARK 3 L33: 2.0108 L12: 1.3838
REMARK 3 L13: 3.1460 L23: -1.2463
REMARK 3 S TENSOR
REMARK 3 S11: -0.2098 S12: 1.2062 S13: 0.2972
REMARK 3 S21: -0.6241 S22: 0.2036 S23: -0.3533
REMARK 3 S31: -0.9406 S32: 0.7814 S33: 0.0078
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 36 THROUGH 67 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.0511 -4.7862 38.2686
REMARK 3 T TENSOR
REMARK 3 T11: 0.2080 T22: 0.2647
REMARK 3 T33: 0.1777 T12: 0.0024
REMARK 3 T13: -0.0402 T23: -0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 9.0274 L22: 4.8334
REMARK 3 L33: 6.4605 L12: -0.7025
REMARK 3 L13: -1.0749 L23: 0.1306
REMARK 3 S TENSOR
REMARK 3 S11: 0.0332 S12: -0.4366 S13: -0.3340
REMARK 3 S21: 0.3996 S22: -0.0520 S23: -0.2675
REMARK 3 S31: 0.1051 S32: 0.3840 S33: -0.0097
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 68 THROUGH 157 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.9717 -10.3895 26.6912
REMARK 3 T TENSOR
REMARK 3 T11: 0.1710 T22: 0.1953
REMARK 3 T33: 0.1450 T12: 0.0213
REMARK 3 T13: -0.0315 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 2.9604 L22: 4.1023
REMARK 3 L33: 2.8095 L12: 0.8653
REMARK 3 L13: 0.3452 L23: 0.7581
REMARK 3 S TENSOR
REMARK 3 S11: 0.0376 S12: -0.3404 S13: -0.1194
REMARK 3 S21: 0.2945 S22: 0.0062 S23: -0.3211
REMARK 3 S31: 0.1994 S32: 0.2213 S33: -0.0353
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND SEGID AA
REMARK 3 SELECTION : CHAIN B AND SEGID BA
REMARK 3 ATOM PAIRS NUMBER : 2916
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND SEGID AA
REMARK 3 SELECTION : CHAIN C AND SEGID CA
REMARK 3 ATOM PAIRS NUMBER : 2916
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND SEGID AA
REMARK 3 SELECTION : CHAIN D AND SEGID DA
REMARK 3 ATOM PAIRS NUMBER : 2916
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5D5P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000212708.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-AUG-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 10.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : A DOUBLE CRYSTAL SI(111)
REMARK 200 MONOCHROMETOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70410
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.0800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.73000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.550
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3WB1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CAPS (PH 10.5), 0.2 M NACL, 20 %
REMARK 280 (W/V) PEG8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 281K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 36.27000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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: 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: 4030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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 LYS A 159
REMARK 465 LEU A 160
REMARK 465 GLU A 161
REMARK 465 HIS A 162
REMARK 465 HIS A 163
REMARK 465 HIS A 164
REMARK 465 HIS A 165
REMARK 465 HIS A 166
REMARK 465 HIS A 167
REMARK 465 MET B 1
REMARK 465 LYS B 158
REMARK 465 LYS B 159
REMARK 465 LEU B 160
REMARK 465 GLU B 161
REMARK 465 HIS B 162
REMARK 465 HIS B 163
REMARK 465 HIS B 164
REMARK 465 HIS B 165
REMARK 465 HIS B 166
REMARK 465 HIS B 167
REMARK 465 LYS C 158
REMARK 465 LYS C 159
REMARK 465 LEU C 160
REMARK 465 GLU C 161
REMARK 465 HIS C 162
REMARK 465 HIS C 163
REMARK 465 HIS C 164
REMARK 465 HIS C 165
REMARK 465 HIS C 166
REMARK 465 HIS C 167
REMARK 465 LYS D 158
REMARK 465 LYS D 159
REMARK 465 LEU D 160
REMARK 465 GLU D 161
REMARK 465 HIS D 162
REMARK 465 HIS D 163
REMARK 465 HIS D 164
REMARK 465 HIS D 165
REMARK 465 HIS D 166
REMARK 465 HIS D 167
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 OD1 ASP A 62 O HOH A 201 2.07
REMARK 500 NH1 ARG B 101 OE2 GLU B 145 2.14
REMARK 500 OD2 ASP D 22 O HOH D 201 2.14
REMARK 500 O HOH A 211 O HOH C 215 2.16
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 ASP A 62 64.88 -105.33
REMARK 500 PHE D 20 -111.04 -117.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BRC RELATED DB: PDB
REMARK 900 RELATED ID: 3WB0 RELATED DB: PDB
REMARK 900 RELATED ID: 3WB1 RELATED DB: PDB
REMARK 900 RELATED ID: 3WB2 RELATED DB: PDB
DBREF 5D5P A 1 159 UNP Q6LX55 Q6LX55_METMP 1 159
DBREF 5D5P B 1 159 UNP Q6LX55 Q6LX55_METMP 1 159
DBREF 5D5P C 1 159 UNP Q6LX55 Q6LX55_METMP 1 159
DBREF 5D5P D 1 159 UNP Q6LX55 Q6LX55_METMP 1 159
SEQADV 5D5P LEU A 160 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P GLU A 161 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS A 162 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS A 163 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS A 164 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS A 165 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS A 166 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS A 167 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P LEU B 160 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P GLU B 161 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS B 162 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS B 163 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS B 164 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS B 165 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS B 166 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS B 167 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P LEU C 160 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P GLU C 161 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS C 162 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS C 163 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS C 164 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS C 165 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS C 166 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS C 167 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P LEU D 160 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P GLU D 161 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS D 162 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS D 163 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS D 164 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS D 165 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS D 166 UNP Q6LX55 EXPRESSION TAG
SEQADV 5D5P HIS D 167 UNP Q6LX55 EXPRESSION TAG
SEQRES 1 A 167 MET ASN ILE GLU ASN THR ILE LYS SER ALA TYR GLU GLU
SEQRES 2 A 167 SER LEU ASN ASN ALA ARG PHE GLY ASP LYS ILE GLU GLU
SEQRES 3 A 167 ILE ASP ALA ILE GLN SER THR ILE LYS SER ALA LYS ASN
SEQRES 4 A 167 VAL THR VAL ALA THR SER ASN GLU LYS LYS PHE LYS VAL
SEQRES 5 A 167 VAL SER ASP ILE ILE SER ARG ILE THR ASP ALA ASN ILE
SEQRES 6 A 167 SER MET LEU GLU ILE PRO THR ASN SER ALA ASP LEU THR
SEQRES 7 A 167 ARG MET PRO ALA LEU ASN LYS GLY LEU ILE ALA VAL ASP
SEQRES 8 A 167 SER SER ASP ALA ASP LEU ILE ILE THR ARG GLY ARG LEU
SEQRES 9 A 167 GLY ILE PRO GLY SER GLY SER LEU LEU LEU ILE MET ASP
SEQRES 10 A 167 LYS LYS GLY ARG ILE LEU THR GLY SER VAL SER PRO SER
SEQRES 11 A 167 SER ILE ILE HIS LYS ASN PRO ILE ASP LYS THR VAL GLU
SEQRES 12 A 167 LEU GLU LEU ILE THR ALA LEU GLU ARG ILE GLY ILE VAL
SEQRES 13 A 167 VAL LYS LYS LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 167 MET ASN ILE GLU ASN THR ILE LYS SER ALA TYR GLU GLU
SEQRES 2 B 167 SER LEU ASN ASN ALA ARG PHE GLY ASP LYS ILE GLU GLU
SEQRES 3 B 167 ILE ASP ALA ILE GLN SER THR ILE LYS SER ALA LYS ASN
SEQRES 4 B 167 VAL THR VAL ALA THR SER ASN GLU LYS LYS PHE LYS VAL
SEQRES 5 B 167 VAL SER ASP ILE ILE SER ARG ILE THR ASP ALA ASN ILE
SEQRES 6 B 167 SER MET LEU GLU ILE PRO THR ASN SER ALA ASP LEU THR
SEQRES 7 B 167 ARG MET PRO ALA LEU ASN LYS GLY LEU ILE ALA VAL ASP
SEQRES 8 B 167 SER SER ASP ALA ASP LEU ILE ILE THR ARG GLY ARG LEU
SEQRES 9 B 167 GLY ILE PRO GLY SER GLY SER LEU LEU LEU ILE MET ASP
SEQRES 10 B 167 LYS LYS GLY ARG ILE LEU THR GLY SER VAL SER PRO SER
SEQRES 11 B 167 SER ILE ILE HIS LYS ASN PRO ILE ASP LYS THR VAL GLU
SEQRES 12 B 167 LEU GLU LEU ILE THR ALA LEU GLU ARG ILE GLY ILE VAL
SEQRES 13 B 167 VAL LYS LYS LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 167 MET ASN ILE GLU ASN THR ILE LYS SER ALA TYR GLU GLU
SEQRES 2 C 167 SER LEU ASN ASN ALA ARG PHE GLY ASP LYS ILE GLU GLU
SEQRES 3 C 167 ILE ASP ALA ILE GLN SER THR ILE LYS SER ALA LYS ASN
SEQRES 4 C 167 VAL THR VAL ALA THR SER ASN GLU LYS LYS PHE LYS VAL
SEQRES 5 C 167 VAL SER ASP ILE ILE SER ARG ILE THR ASP ALA ASN ILE
SEQRES 6 C 167 SER MET LEU GLU ILE PRO THR ASN SER ALA ASP LEU THR
SEQRES 7 C 167 ARG MET PRO ALA LEU ASN LYS GLY LEU ILE ALA VAL ASP
SEQRES 8 C 167 SER SER ASP ALA ASP LEU ILE ILE THR ARG GLY ARG LEU
SEQRES 9 C 167 GLY ILE PRO GLY SER GLY SER LEU LEU LEU ILE MET ASP
SEQRES 10 C 167 LYS LYS GLY ARG ILE LEU THR GLY SER VAL SER PRO SER
SEQRES 11 C 167 SER ILE ILE HIS LYS ASN PRO ILE ASP LYS THR VAL GLU
SEQRES 12 C 167 LEU GLU LEU ILE THR ALA LEU GLU ARG ILE GLY ILE VAL
SEQRES 13 C 167 VAL LYS LYS LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 167 MET ASN ILE GLU ASN THR ILE LYS SER ALA TYR GLU GLU
SEQRES 2 D 167 SER LEU ASN ASN ALA ARG PHE GLY ASP LYS ILE GLU GLU
SEQRES 3 D 167 ILE ASP ALA ILE GLN SER THR ILE LYS SER ALA LYS ASN
SEQRES 4 D 167 VAL THR VAL ALA THR SER ASN GLU LYS LYS PHE LYS VAL
SEQRES 5 D 167 VAL SER ASP ILE ILE SER ARG ILE THR ASP ALA ASN ILE
SEQRES 6 D 167 SER MET LEU GLU ILE PRO THR ASN SER ALA ASP LEU THR
SEQRES 7 D 167 ARG MET PRO ALA LEU ASN LYS GLY LEU ILE ALA VAL ASP
SEQRES 8 D 167 SER SER ASP ALA ASP LEU ILE ILE THR ARG GLY ARG LEU
SEQRES 9 D 167 GLY ILE PRO GLY SER GLY SER LEU LEU LEU ILE MET ASP
SEQRES 10 D 167 LYS LYS GLY ARG ILE LEU THR GLY SER VAL SER PRO SER
SEQRES 11 D 167 SER ILE ILE HIS LYS ASN PRO ILE ASP LYS THR VAL GLU
SEQRES 12 D 167 LEU GLU LEU ILE THR ALA LEU GLU ARG ILE GLY ILE VAL
SEQRES 13 D 167 VAL LYS LYS LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 5 HOH *359(H2 O)
HELIX 1 AA1 ASN A 2 ASN A 16 1 15
HELIX 2 AA2 LYS A 23 SER A 36 1 14
HELIX 3 AA3 ASN A 46 SER A 58 1 13
HELIX 4 AA4 THR A 72 THR A 78 5 7
HELIX 5 AA5 MET A 80 SER A 93 1 14
HELIX 6 AA6 PRO A 137 ARG A 152 1 16
HELIX 7 AA7 ILE B 3 ASN B 16 1 14
HELIX 8 AA8 LYS B 23 SER B 36 1 14
HELIX 9 AA9 ASN B 46 SER B 58 1 13
HELIX 10 AB1 THR B 72 THR B 78 5 7
HELIX 11 AB2 MET B 80 SER B 93 1 14
HELIX 12 AB3 PRO B 137 ARG B 152 1 16
HELIX 13 AB4 ASN C 2 ASN C 16 1 15
HELIX 14 AB5 LYS C 23 SER C 36 1 14
HELIX 15 AB6 ASN C 46 SER C 58 1 13
HELIX 16 AB7 THR C 72 THR C 78 5 7
HELIX 17 AB8 MET C 80 SER C 93 1 14
HELIX 18 AB9 PRO C 137 ARG C 152 1 16
HELIX 19 AC1 ASN D 2 ASN D 16 1 15
HELIX 20 AC2 LYS D 23 SER D 36 1 14
HELIX 21 AC3 ASN D 46 SER D 58 1 13
HELIX 22 AC4 THR D 72 THR D 78 5 7
HELIX 23 AC5 MET D 80 SER D 93 1 14
HELIX 24 AC6 PRO D 137 ARG D 152 1 16
SHEET 1 AA1 5 ASN A 64 MET A 67 0
SHEET 2 AA1 5 ASN A 39 ALA A 43 1 N VAL A 40 O SER A 66
SHEET 3 AA1 5 LEU A 97 ARG A 103 1 O ILE A 99 N ALA A 43
SHEET 4 AA1 5 SER A 111 ASP A 117 -1 O LEU A 112 N GLY A 102
SHEET 5 AA1 5 ILE A 122 SER A 128 -1 O LEU A 123 N ILE A 115
SHEET 1 AA2 5 ASN B 64 MET B 67 0
SHEET 2 AA2 5 ASN B 39 VAL B 42 1 N VAL B 40 O ASN B 64
SHEET 3 AA2 5 LEU B 97 ARG B 103 1 O LEU B 97 N THR B 41
SHEET 4 AA2 5 SER B 111 ASP B 117 -1 O MET B 116 N ILE B 98
SHEET 5 AA2 5 ILE B 122 SER B 128 -1 O SER B 126 N LEU B 113
SHEET 1 AA3 5 ASN C 64 MET C 67 0
SHEET 2 AA3 5 ASN C 39 VAL C 42 1 N VAL C 40 O ASN C 64
SHEET 3 AA3 5 LEU C 97 ARG C 103 1 O LEU C 97 N THR C 41
SHEET 4 AA3 5 SER C 111 ASP C 117 -1 O LEU C 112 N GLY C 102
SHEET 5 AA3 5 ILE C 122 SER C 128 -1 O SER C 126 N LEU C 113
SHEET 1 AA4 5 ASN D 64 MET D 67 0
SHEET 2 AA4 5 ASN D 39 VAL D 42 1 N VAL D 40 O ASN D 64
SHEET 3 AA4 5 LEU D 97 ARG D 103 1 O LEU D 97 N THR D 41
SHEET 4 AA4 5 SER D 111 ASP D 117 -1 O MET D 116 N ILE D 98
SHEET 5 AA4 5 ILE D 122 SER D 128 -1 O LEU D 123 N ILE D 115
CRYST1 64.120 72.540 70.980 90.00 99.09 90.00 P 1 21 1 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 0.015596 0.000000 0.002496 0.00000
SCALE2 0.000000 0.013785 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014268 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
