HEADER TRANSFERASE 24-OCT-13 4NC9
TITLE CRYSTAL STRUCTURE OF PHOSPHATIDYL MANNOSYLTRANSFERASE PIMA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GDP-MANNOSE-DEPENDENT ALPHA-(1-2)-PHOSPHATIDYLINOSITOL
COMPND 3 MANNOSYLTRANSFERASE;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 SYNONYM: ALPHA-MANNOSYLTRANSFERASE, GUANOSINE DIPHOSPHOMANNOSE-
COMPND 6 PHOSPHATIDYL-INOSITOL ALPHA-MANNOSYLTRANSFERASE, PHOSPHATIDYLINOSITOL
COMPND 7 ALPHA-MANNOSYLTRANSFERASE, PI ALPHA-MANNOSYLTRANSFERASE;
COMPND 8 EC: 2.4.1.57;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS;
SOURCE 3 ORGANISM_TAXID: 246196;
SOURCE 4 STRAIN: ATCC 700084 / MC(2)155;
SOURCE 5 GENE: MSMEG_2935, MSMEI_2861, PIMA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A-PIMA
KEYWDS GT-B, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.GIGANTI,D.ALBESA-JOVE,M.BELLINZONI,M.E.GUERIN,P.M.ALZARI
REVDAT 3 20-SEP-23 4NC9 1 SEQADV
REVDAT 2 10-JUN-15 4NC9 1 JRNL
REVDAT 1 12-NOV-14 4NC9 0
JRNL AUTH D.GIGANTI,D.ALBESA-JOVE,S.URRESTI,A.RODRIGO-UNZUETA,
JRNL AUTH 2 M.A.MARTINEZ,N.COMINO,N.BARILONE,M.BELLINZONI,A.CHENAL,
JRNL AUTH 3 M.E.GUERIN,P.M.ALZARI
JRNL TITL SECONDARY STRUCTURE RESHUFFLING MODULATES
JRNL TITL 2 GLYCOSYLTRANSFERASE FUNCTION AT THE MEMBRANE.
JRNL REF NAT.CHEM.BIOL. V. 11 16 2015
JRNL REFN ISSN 1552-4450
JRNL PMID 25402770
JRNL DOI 10.1038/NCHEMBIO.1694
REMARK 2
REMARK 2 RESOLUTION. 3.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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) : 3.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.52
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 29522
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1567
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 43.5249 - 7.0890 0.99 2832 139 0.1854 0.2089
REMARK 3 2 7.0890 - 5.6306 1.00 2732 144 0.2270 0.2734
REMARK 3 3 5.6306 - 4.9200 1.00 2675 172 0.2061 0.2679
REMARK 3 4 4.9200 - 4.4706 1.00 2685 157 0.1859 0.2219
REMARK 3 5 4.4706 - 4.1504 1.00 2703 147 0.1947 0.2742
REMARK 3 6 4.1504 - 3.9059 1.00 2657 139 0.2162 0.2333
REMARK 3 7 3.9059 - 3.7104 1.00 2659 140 0.2336 0.2946
REMARK 3 8 3.7104 - 3.5490 1.00 2671 143 0.2528 0.3005
REMARK 3 9 3.5490 - 3.4124 1.00 2680 130 0.2340 0.2694
REMARK 3 10 3.4124 - 3.2947 1.00 2628 142 0.2563 0.3303
REMARK 3 11 3.2947 - 3.1917 0.97 2597 114 0.3043 0.3447
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.630
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 : 0.005 10424
REMARK 3 ANGLE : 0.903 14222
REMARK 3 CHIRALITY : 0.049 1682
REMARK 3 PLANARITY : 0.004 1868
REMARK 3 DIHEDRAL : 13.151 3563
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 17
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ -1:108)
REMARK 3 ORIGIN FOR THE GROUP (A): 73.9328 22.1150 -19.8132
REMARK 3 T TENSOR
REMARK 3 T11: 0.8255 T22: 0.7846
REMARK 3 T33: 0.8914 T12: -0.0643
REMARK 3 T13: 0.2175 T23: 0.1897
REMARK 3 L TENSOR
REMARK 3 L11: 6.4723 L22: 3.8197
REMARK 3 L33: 4.5320 L12: 0.3252
REMARK 3 L13: 0.0282 L23: -0.5526
REMARK 3 S TENSOR
REMARK 3 S11: 0.2736 S12: 0.8531 S13: 1.4287
REMARK 3 S21: -0.7228 S22: -0.2823 S23: -0.8062
REMARK 3 S31: -0.8439 S32: 1.1771 S33: 0.0729
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 109:157)
REMARK 3 ORIGIN FOR THE GROUP (A): 59.6742 11.8410 -21.8362
REMARK 3 T TENSOR
REMARK 3 T11: 0.5246 T22: 0.4197
REMARK 3 T33: 0.5149 T12: 0.1212
REMARK 3 T13: 0.0178 T23: 0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 4.2141 L22: 3.7981
REMARK 3 L33: 6.0066 L12: -0.0958
REMARK 3 L13: 4.3014 L23: -1.1590
REMARK 3 S TENSOR
REMARK 3 S11: 0.3920 S12: 0.4626 S13: -0.1824
REMARK 3 S21: -0.0449 S22: -0.0969 S23: -0.0642
REMARK 3 S31: -0.0580 S32: 0.2086 S33: -0.3380
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 158:203)
REMARK 3 ORIGIN FOR THE GROUP (A): 68.4760 16.8958 5.3069
REMARK 3 T TENSOR
REMARK 3 T11: 0.6181 T22: 0.6540
REMARK 3 T33: 0.7367 T12: -0.1413
REMARK 3 T13: 0.1026 T23: -0.1686
REMARK 3 L TENSOR
REMARK 3 L11: 2.0174 L22: 3.8109
REMARK 3 L33: 3.4330 L12: -0.9242
REMARK 3 L13: -0.7964 L23: 1.3220
REMARK 3 S TENSOR
REMARK 3 S11: -0.0038 S12: -0.7543 S13: 0.6998
REMARK 3 S21: 0.5399 S22: -0.0309 S23: -0.0229
REMARK 3 S31: -0.2206 S32: 0.3305 S33: 0.0864
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 204:276)
REMARK 3 ORIGIN FOR THE GROUP (A): 63.7208 24.2853 15.3866
REMARK 3 T TENSOR
REMARK 3 T11: 1.0377 T22: 0.8998
REMARK 3 T33: 0.9713 T12: -0.0589
REMARK 3 T13: 0.0258 T23: -0.4344
REMARK 3 L TENSOR
REMARK 3 L11: 6.4725 L22: 3.8417
REMARK 3 L33: 3.2142 L12: -0.8621
REMARK 3 L13: -2.5761 L23: 0.6340
REMARK 3 S TENSOR
REMARK 3 S11: 0.2302 S12: -1.3527 S13: 1.4531
REMARK 3 S21: 1.0347 S22: -0.0627 S23: 0.2394
REMARK 3 S31: -0.8115 S32: 0.2578 S33: -0.1067
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 277:347)
REMARK 3 ORIGIN FOR THE GROUP (A): 62.8861 8.5573 10.8357
REMARK 3 T TENSOR
REMARK 3 T11: 0.8484 T22: 0.5038
REMARK 3 T33: 0.5495 T12: -0.0689
REMARK 3 T13: 0.1386 T23: -0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 9.3368 L22: 6.9942
REMARK 3 L33: 4.3198 L12: -2.2774
REMARK 3 L13: -1.3383 L23: -0.2069
REMARK 3 S TENSOR
REMARK 3 S11: -0.4261 S12: -0.5834 S13: -0.8951
REMARK 3 S21: 1.2667 S22: 0.1608 S23: 0.5613
REMARK 3 S31: 0.5693 S32: -0.2568 S33: 0.0642
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 348:375)
REMARK 3 ORIGIN FOR THE GROUP (A): 74.8891 7.3166 -21.0281
REMARK 3 T TENSOR
REMARK 3 T11: 0.6799 T22: 0.8899
REMARK 3 T33: 0.7173 T12: 0.1337
REMARK 3 T13: 0.1170 T23: -0.0238
REMARK 3 L TENSOR
REMARK 3 L11: 4.6624 L22: 5.9481
REMARK 3 L33: 8.1249 L12: 0.6177
REMARK 3 L13: 0.9123 L23: -3.1458
REMARK 3 S TENSOR
REMARK 3 S11: 0.3573 S12: 1.3546 S13: -0.3454
REMARK 3 S21: -0.7240 S22: -0.1064 S23: -0.1630
REMARK 3 S31: -0.0571 S32: 0.7841 S33: -0.6190
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ -1:130)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.8331 2.5596 -37.2700
REMARK 3 T TENSOR
REMARK 3 T11: 0.9317 T22: 0.6690
REMARK 3 T33: 0.6575 T12: 0.2153
REMARK 3 T13: -0.1765 T23: -0.2603
REMARK 3 L TENSOR
REMARK 3 L11: 4.9745 L22: 4.5815
REMARK 3 L33: 4.3002 L12: -0.3229
REMARK 3 L13: -0.7055 L23: -0.9371
REMARK 3 S TENSOR
REMARK 3 S11: 0.3818 S12: 1.1569 S13: -0.9735
REMARK 3 S21: -0.8892 S22: -0.3259 S23: 0.1961
REMARK 3 S31: 0.8228 S32: -0.0193 S33: 0.0239
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 131:163)
REMARK 3 ORIGIN FOR THE GROUP (A): 53.5707 25.6814 -46.0117
REMARK 3 T TENSOR
REMARK 3 T11: 0.7430 T22: 0.7848
REMARK 3 T33: 0.9130 T12: 0.2278
REMARK 3 T13: 0.0474 T23: 0.1196
REMARK 3 L TENSOR
REMARK 3 L11: 1.5326 L22: 9.0511
REMARK 3 L33: 1.0850 L12: -0.0790
REMARK 3 L13: 0.9279 L23: -2.0817
REMARK 3 S TENSOR
REMARK 3 S11: -0.0172 S12: 0.3640 S13: 0.3442
REMARK 3 S21: -0.3172 S22: -0.1705 S23: -0.0659
REMARK 3 S31: 0.6156 S32: 0.6314 S33: -0.2219
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 164:329)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3670 -4.2467 -8.1433
REMARK 3 T TENSOR
REMARK 3 T11: 1.1569 T22: 0.7383
REMARK 3 T33: 1.1148 T12: 0.1328
REMARK 3 T13: 0.2538 T23: 0.2180
REMARK 3 L TENSOR
REMARK 3 L11: 1.6719 L22: 5.6748
REMARK 3 L33: 3.6816 L12: 1.0876
REMARK 3 L13: -0.7202 L23: -3.3915
REMARK 3 S TENSOR
REMARK 3 S11: -0.2261 S12: -0.5353 S13: -0.8693
REMARK 3 S21: 0.6880 S22: 0.1743 S23: 0.4427
REMARK 3 S31: 0.6837 S32: -0.1124 S33: 0.1417
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 330:373)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7153 13.7049 -24.4152
REMARK 3 T TENSOR
REMARK 3 T11: 0.7700 T22: 0.5389
REMARK 3 T33: 0.6852 T12: 0.1321
REMARK 3 T13: -0.0161 T23: 0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 4.0618 L22: 3.1217
REMARK 3 L33: 5.0968 L12: -0.1917
REMARK 3 L13: -1.7699 L23: -0.8759
REMARK 3 S TENSOR
REMARK 3 S11: 0.3744 S12: 0.3752 S13: -0.0460
REMARK 3 S21: 0.1168 S22: -0.1428 S23: 0.5118
REMARK 3 S31: -0.7847 S32: -0.4189 S33: -0.6610
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ -2:108)
REMARK 3 ORIGIN FOR THE GROUP (A): 69.3224 -24.6997 -5.9574
REMARK 3 T TENSOR
REMARK 3 T11: 0.7368 T22: 0.4644
REMARK 3 T33: 0.6982 T12: 0.0478
REMARK 3 T13: 0.2045 T23: 0.1241
REMARK 3 L TENSOR
REMARK 3 L11: 6.9719 L22: 7.0573
REMARK 3 L33: 5.6850 L12: 1.9855
REMARK 3 L13: 0.6391 L23: 0.0755
REMARK 3 S TENSOR
REMARK 3 S11: -0.1921 S12: -0.6988 S13: -1.0574
REMARK 3 S21: 0.8673 S22: -0.0065 S23: 0.7592
REMARK 3 S31: 0.5880 S32: -0.1811 S33: 0.2579
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 109:181)
REMARK 3 ORIGIN FOR THE GROUP (A): 66.7209 -11.6825 -15.1914
REMARK 3 T TENSOR
REMARK 3 T11: 0.7268 T22: 0.3633
REMARK 3 T33: 0.6614 T12: 0.0681
REMARK 3 T13: 0.1469 T23: 0.0679
REMARK 3 L TENSOR
REMARK 3 L11: 4.9005 L22: 3.4108
REMARK 3 L33: 2.4635 L12: -1.1680
REMARK 3 L13: -0.0214 L23: -1.1020
REMARK 3 S TENSOR
REMARK 3 S11: -0.1474 S12: -0.0420 S13: -0.8680
REMARK 3 S21: 0.0681 S22: 0.1739 S23: 0.8060
REMARK 3 S31: -0.2951 S32: -0.1187 S33: -0.0878
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 182:301)
REMARK 3 ORIGIN FOR THE GROUP (A): 95.6997 -9.5851 6.3708
REMARK 3 T TENSOR
REMARK 3 T11: 1.0491 T22: 2.1241
REMARK 3 T33: 1.3471 T12: 0.4187
REMARK 3 T13: -0.2859 T23: 0.2706
REMARK 3 L TENSOR
REMARK 3 L11: 2.2111 L22: 3.1731
REMARK 3 L33: 3.2018 L12: -0.0393
REMARK 3 L13: 2.2394 L23: -1.6257
REMARK 3 S TENSOR
REMARK 3 S11: -0.2055 S12: -1.8605 S13: -1.1056
REMARK 3 S21: 0.7327 S22: 0.1197 S23: -1.0043
REMARK 3 S31: 0.8771 S32: 1.5837 S33: 0.0583
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 302:373)
REMARK 3 ORIGIN FOR THE GROUP (A): 82.4167 -2.8989 -3.3368
REMARK 3 T TENSOR
REMARK 3 T11: 0.7401 T22: 0.6840
REMARK 3 T33: 0.5877 T12: 0.0867
REMARK 3 T13: 0.0090 T23: 0.0321
REMARK 3 L TENSOR
REMARK 3 L11: 2.5063 L22: 5.8795
REMARK 3 L33: 2.6323 L12: 2.0991
REMARK 3 L13: -0.6369 L23: 1.9100
REMARK 3 S TENSOR
REMARK 3 S11: -0.0263 S12: -0.3901 S13: 0.6008
REMARK 3 S21: 0.3874 S22: 0.0579 S23: 0.0918
REMARK 3 S31: 0.2099 S32: 0.6859 S33: 0.0333
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 0:190)
REMARK 3 ORIGIN FOR THE GROUP (A): 87.7245 -11.3380 -37.6586
REMARK 3 T TENSOR
REMARK 3 T11: 0.7707 T22: 0.7889
REMARK 3 T33: 0.5157 T12: 0.2447
REMARK 3 T13: 0.0431 T23: 0.1370
REMARK 3 L TENSOR
REMARK 3 L11: 6.8262 L22: 2.2650
REMARK 3 L33: 5.0157 L12: 1.2065
REMARK 3 L13: -4.5888 L23: -0.6218
REMARK 3 S TENSOR
REMARK 3 S11: 0.2462 S12: 1.6021 S13: 0.5640
REMARK 3 S21: -0.4753 S22: 0.0532 S23: -0.0397
REMARK 3 S31: -0.2784 S32: -0.8562 S33: -0.3222
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 191:295)
REMARK 3 ORIGIN FOR THE GROUP (A): 108.9717 10.1863 -36.2414
REMARK 3 T TENSOR
REMARK 3 T11: 1.1989 T22: 0.6245
REMARK 3 T33: 1.5123 T12: 0.0453
REMARK 3 T13: 0.1213 T23: 0.0717
REMARK 3 L TENSOR
REMARK 3 L11: 2.6170 L22: 7.6152
REMARK 3 L33: 5.0913 L12: -1.4900
REMARK 3 L13: 0.5924 L23: 1.3294
REMARK 3 S TENSOR
REMARK 3 S11: 0.0766 S12: 0.3066 S13: 1.8215
REMARK 3 S21: -0.4088 S22: -0.2292 S23: -0.6414
REMARK 3 S31: -1.3834 S32: -0.1229 S33: 0.2282
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 296:373)
REMARK 3 ORIGIN FOR THE GROUP (A): 106.2013 -8.1396 -30.7996
REMARK 3 T TENSOR
REMARK 3 T11: 0.9121 T22: 0.7564
REMARK 3 T33: 0.9119 T12: 0.0775
REMARK 3 T13: 0.1410 T23: 0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 5.5199 L22: 1.9528
REMARK 3 L33: 1.8796 L12: 1.7336
REMARK 3 L13: 1.5520 L23: 0.8174
REMARK 3 S TENSOR
REMARK 3 S11: 0.1109 S12: -0.4141 S13: 0.0248
REMARK 3 S21: -0.0733 S22: -0.1603 S23: -0.5002
REMARK 3 S31: -0.0737 S32: -0.2156 S33: 0.0287
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ -1:56 OR RESSEQ
REMARK 3 69:131 OR RESSEQ 133:272 OR RESSEQ 274:
REMARK 3 373 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ -1:56 OR RESSEQ
REMARK 3 69:131 OR RESSEQ 133:272 OR RESSEQ 274:
REMARK 3 373 )
REMARK 3 ATOM PAIRS NUMBER : 4958
REMARK 3 RMSD : 0.954
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 1:59 OR RESSEQ 69:131
REMARK 3 OR RESSEQ 159:171)
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 1:59 OR RESSEQ 69:131
REMARK 3 OR RESSEQ 159:171)
REMARK 3 ATOM PAIRS NUMBER : 1914
REMARK 3 RMSD : 0.704
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4NC9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1000083020.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0668
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31022
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.190
REMARK 200 RESOLUTION RANGE LOW (A) : 43.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.51200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 2GEK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4000, 200 MM MGCL2, 100 MM
REMARK 280 TRIS-HCL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K, PH 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 112.42733
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 56.21367
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 56.21367
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 112.42733
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: 1810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 GLY A -3
REMARK 465 SER A -2
REMARK 465 PRO A 59
REMARK 465 ILE A 60
REMARK 465 PRO A 61
REMARK 465 TYR A 62
REMARK 465 ASN A 63
REMARK 465 GLY A 64
REMARK 465 SER A 65
REMARK 465 VAL A 66
REMARK 465 ALA A 376
REMARK 465 ASN A 377
REMARK 465 ARG A 378
REMARK 465 ASP A 379
REMARK 465 GLU A 380
REMARK 465 THR A 381
REMARK 465 ALA A 382
REMARK 465 GLY A 383
REMARK 465 GLU A 384
REMARK 465 SER A 385
REMARK 465 VAL A 386
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 ILE B 60
REMARK 465 PRO B 61
REMARK 465 TYR B 62
REMARK 465 ASN B 63
REMARK 465 GLY B 64
REMARK 465 SER B 65
REMARK 465 GLU B 139
REMARK 465 LYS B 140
REMARK 465 ILE B 141
REMARK 465 ILE B 142
REMARK 465 GLY B 143
REMARK 465 ARG B 144
REMARK 465 GLY B 272
REMARK 465 GLY B 273
REMARK 465 GLY B 374
REMARK 465 ALA B 375
REMARK 465 ALA B 376
REMARK 465 ASN B 377
REMARK 465 ARG B 378
REMARK 465 ASP B 379
REMARK 465 GLU B 380
REMARK 465 THR B 381
REMARK 465 ALA B 382
REMARK 465 GLY B 383
REMARK 465 GLU B 384
REMARK 465 SER B 385
REMARK 465 VAL B 386
REMARK 465 GLY C -3
REMARK 465 PRO C 61
REMARK 465 TYR C 62
REMARK 465 ASN C 63
REMARK 465 GLY C 64
REMARK 465 SER C 65
REMARK 465 VAL C 66
REMARK 465 ALA C 67
REMARK 465 LYS C 140
REMARK 465 ILE C 141
REMARK 465 ILE C 142
REMARK 465 GLY C 143
REMARK 465 ARG C 144
REMARK 465 ILE C 145
REMARK 465 GLU C 187
REMARK 465 GLY C 188
REMARK 465 ARG C 189
REMARK 465 GLY C 195
REMARK 465 ARG C 196
REMARK 465 PRO C 219
REMARK 465 ASP C 220
REMARK 465 VAL C 221
REMARK 465 GLU C 222
REMARK 465 GLY C 227
REMARK 465 ARG C 228
REMARK 465 GLY C 229
REMARK 465 ASP C 230
REMARK 465 ASP C 240
REMARK 465 LEU C 241
REMARK 465 ALA C 242
REMARK 465 GLY C 243
REMARK 465 GLY C 374
REMARK 465 ALA C 375
REMARK 465 ALA C 376
REMARK 465 ASN C 377
REMARK 465 ARG C 378
REMARK 465 ASP C 379
REMARK 465 GLU C 380
REMARK 465 THR C 381
REMARK 465 ALA C 382
REMARK 465 GLY C 383
REMARK 465 GLU C 384
REMARK 465 SER C 385
REMARK 465 VAL C 386
REMARK 465 GLY D -3
REMARK 465 SER D -2
REMARK 465 GLY D -1
REMARK 465 ALA D 57
REMARK 465 VAL D 58
REMARK 465 PRO D 59
REMARK 465 ILE D 60
REMARK 465 PRO D 61
REMARK 465 TYR D 62
REMARK 465 ASN D 63
REMARK 465 GLY D 64
REMARK 465 SER D 65
REMARK 465 VAL D 66
REMARK 465 ALA D 67
REMARK 465 ARG D 68
REMARK 465 LEU D 69
REMARK 465 ARG D 70
REMARK 465 PHE D 71
REMARK 465 GLY D 374
REMARK 465 ALA D 375
REMARK 465 ALA D 376
REMARK 465 ASN D 377
REMARK 465 ARG D 378
REMARK 465 ASP D 379
REMARK 465 GLU D 380
REMARK 465 THR D 381
REMARK 465 ALA D 382
REMARK 465 GLY D 383
REMARK 465 GLU D 384
REMARK 465 SER D 385
REMARK 465 VAL D 386
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 ARG A 29 CZ NH1 NH2
REMARK 470 LYS A 46 CG CD CE NZ
REMARK 470 VAL A 58 CG1 CG2
REMARK 470 ARG A 68 NE CZ NH1 NH2
REMARK 470 LEU A 69 CG CD1 CD2
REMARK 470 ARG A 70 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 77 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 78 CG CD CE NZ
REMARK 470 LYS A 80 CG CD CE NZ
REMARK 470 GLU A 157 OE1 OE2
REMARK 470 ASP A 162 CG OD1 OD2
REMARK 470 GLU A 187 CG CD OE1 OE2
REMARK 470 ARG A 196 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 214 CG CD1 CD2
REMARK 470 ARG A 217 CZ NH1 NH2
REMARK 470 ARG A 228 CZ NH1 NH2
REMARK 470 GLU A 274 CG CD OE1 OE2
REMARK 470 ARG A 309 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 331 CG CD OE1 NE2
REMARK 470 ARG A 339 CZ NH1 NH2
REMARK 470 GLN B 18 OE1 NE2
REMARK 470 HIS B 44 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 46 CG CD CE NZ
REMARK 470 LEU B 47 CG CD1 CD2
REMARK 470 ASP B 49 CG OD1 OD2
REMARK 470 LYS B 56 CG CD CE NZ
REMARK 470 VAL B 58 CG1 CG2
REMARK 470 ARG B 68 CZ NH1 NH2
REMARK 470 ARG B 77 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 78 CG CD CE NZ
REMARK 470 LYS B 81 CG CD CE NZ
REMARK 470 ARG B 135 CZ NH1 NH2
REMARK 470 ILE B 145 CG1 CG2 CD1
REMARK 470 ARG B 186 CZ NH1 NH2
REMARK 470 GLU B 187 CG CD OE1 OE2
REMARK 470 ARG B 196 NE CZ NH1 NH2
REMARK 470 ARG B 201 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 202 CG CD CE NZ
REMARK 470 LEU B 208 CG CD1 CD2
REMARK 470 ARG B 228 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 234 CG CD1 CD2
REMARK 470 ARG B 235 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 236 CG CD OE1 OE2
REMARK 470 ASP B 240 CG OD1 OD2
REMARK 470 ARG B 246 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 274 CG CD OE1 OE2
REMARK 470 PHE B 276 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 328 CG CD OE1 OE2
REMARK 470 GLN B 331 CG CD OE1 NE2
REMARK 470 ARG B 346 NE CZ NH1 NH2
REMARK 470 ILE B 368 CG1 CG2 CD1
REMARK 470 LYS B 369 CD CE NZ
REMARK 470 SER C -2 OG
REMARK 470 HIS C 44 CG ND1 CD2 CE1 NE2
REMARK 470 LYS C 46 CG CD CE NZ
REMARK 470 LYS C 56 CG CD CE NZ
REMARK 470 ARG C 68 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 135 CZ NH1 NH2
REMARK 470 GLU C 139 CG CD OE1 OE2
REMARK 470 ARG C 152 CZ NH1 NH2
REMARK 470 LEU C 180 CG CD1 CD2
REMARK 470 LEU C 181 CG CD1 CD2
REMARK 470 ASP C 182 CG OD1 OD2
REMARK 470 TYR C 184 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG C 186 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 194 CG CD1 CD2
REMARK 470 TYR C 197 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP C 198 CG OD1 OD2
REMARK 470 ARG C 201 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 202 CG CD CE NZ
REMARK 470 MET C 204 SD CE
REMARK 470 LEU C 207 CG CD1 CD2
REMARK 470 LEU C 208 CG CD1 CD2
REMARK 470 LEU C 211 CG CD1 CD2
REMARK 470 LYS C 213 CG CD CE NZ
REMARK 470 LEU C 214 CG CD1 CD2
REMARK 470 ARG C 217 CG CD NE CZ NH1 NH2
REMARK 470 PHE C 218 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE C 223 CG1 CG2 CD1
REMARK 470 LEU C 224 CG CD1 CD2
REMARK 470 ILE C 225 CG1 CG2 CD1
REMARK 470 VAL C 226 CG1 CG2
REMARK 470 GLU C 231 CG CD OE1 OE2
REMARK 470 ASP C 232 CG OD1 OD2
REMARK 470 GLU C 233 CG CD OE1 OE2
REMARK 470 LEU C 234 CG CD1 CD2
REMARK 470 ARG C 235 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 236 CG CD OE1 OE2
REMARK 470 GLN C 237 CG CD OE1 NE2
REMARK 470 HIS C 244 CG ND1 CD2 CE1 NE2
REMARK 470 ARG C 246 CG CD NE CZ NH1 NH2
REMARK 470 PHE C 247 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS C 256 CG CD CE NZ
REMARK 470 MET C 260 CG SD CE
REMARK 470 HIS C 270 CG ND1 CD2 CE1 NE2
REMARK 470 LEU C 271 CG CD1 CD2
REMARK 470 GLU C 274 CG CD OE1 OE2
REMARK 470 PHE C 276 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG C 309 CG CD NE CZ NH1 NH2
REMARK 470 VAL C 311 CG1 CG2
REMARK 470 VAL C 313 CG1 CG2
REMARK 470 ASP C 314 CG OD1 OD2
REMARK 470 ASP C 317 CG OD1 OD2
REMARK 470 MET C 319 CG SD CE
REMARK 470 ILE C 324 CG1 CG2 CD1
REMARK 470 ILE C 326 CG1 CG2 CD1
REMARK 470 GLU C 328 CG CD OE1 OE2
REMARK 470 GLN C 331 CG CD OE1 NE2
REMARK 470 LEU C 332 CG CD1 CD2
REMARK 470 ARG C 333 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 339 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 2 NE CZ NH1 NH2
REMARK 470 HIS D 44 CG ND1 CD2 CE1 NE2
REMARK 470 LYS D 46 CG CD CE NZ
REMARK 470 LEU D 47 CG CD1 CD2
REMARK 470 ASP D 49 CG OD1 OD2
REMARK 470 LYS D 56 CG CD CE NZ
REMARK 470 HIS D 76 CG ND1 CD2 CE1 NE2
REMARK 470 ARG D 77 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 80 CG CD CE NZ
REMARK 470 LYS D 81 CG CD CE NZ
REMARK 470 GLU D 85 CG CD OE1 OE2
REMARK 470 GLU D 110 CG CD OE1 OE2
REMARK 470 ARG D 186 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 187 CG CD OE1 OE2
REMARK 470 TYR D 197 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS D 202 CG CD CE NZ
REMARK 470 LEU D 208 CG CD1 CD2
REMARK 470 LYS D 213 CE NZ
REMARK 470 ARG D 217 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 228 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 233 CG CD OE1 OE2
REMARK 470 LEU D 234 CG CD1 CD2
REMARK 470 ARG D 235 CZ NH1 NH2
REMARK 470 GLU D 236 CG CD OE1 OE2
REMARK 470 GLN D 237 CD OE1 NE2
REMARK 470 LYS D 256 CG CD CE NZ
REMARK 470 GLU D 274 CG CD OE1 OE2
REMARK 470 ARG D 309 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 331 CG CD OE1 NE2
REMARK 470 ARG D 333 CG CD NE CZ NH1 NH2
REMARK 470 ILE D 368 CG1 CG2 CD1
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 96 59.40 -68.95
REMARK 500 PRO A 112 81.31 -69.39
REMARK 500 ARG A 189 79.83 64.65
REMARK 500 PRO A 269 48.11 -89.64
REMARK 500 GLU A 274 18.23 54.05
REMARK 500 SER A 275 -56.39 -135.40
REMARK 500 PHE A 276 -12.72 -47.37
REMARK 500 ALA A 303 65.97 60.12
REMARK 500 PRO B 136 67.02 -63.63
REMARK 500 TYR B 137 -58.36 -127.70
REMARK 500 ALA B 163 65.68 37.26
REMARK 500 ARG B 189 -152.79 56.13
REMARK 500 ARG B 246 -60.78 -124.19
REMARK 500 PHE B 247 71.18 60.95
REMARK 500 PRO B 269 47.97 -88.81
REMARK 500 ASP B 314 -3.53 68.32
REMARK 500 LEU B 332 -60.48 -90.68
REMARK 500 VAL B 363 -56.97 -127.27
REMARK 500 ARG C 135 -36.69 -39.64
REMARK 500 PRO C 136 51.38 -66.25
REMARK 500 HIS C 270 156.17 178.10
REMARK 500 GLU C 274 22.23 48.54
REMARK 500 ASP C 314 -3.24 72.15
REMARK 500 VAL C 363 -56.52 -127.52
REMARK 500 PRO D 8 43.45 -93.82
REMARK 500 SER D 100 160.61 177.39
REMARK 500 PHE D 175 -61.66 -100.83
REMARK 500 ARG D 189 -153.27 56.89
REMARK 500 GLN D 250 66.71 36.15
REMARK 500 PRO D 269 48.09 -89.34
REMARK 500 SER D 275 -5.55 90.25
REMARK 500 ASP D 314 -2.11 75.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4N9W RELATED DB: PDB
DBREF 4NC9 A 1 386 UNP A0QWG6 PIMA_MYCS2 1 386
DBREF 4NC9 B 1 386 UNP A0QWG6 PIMA_MYCS2 1 386
DBREF 4NC9 C 1 386 UNP A0QWG6 PIMA_MYCS2 1 386
DBREF 4NC9 D 1 386 UNP A0QWG6 PIMA_MYCS2 1 386
SEQADV 4NC9 GLY A -3 UNP A0QWG6 EXPRESSION TAG
SEQADV 4NC9 SER A -2 UNP A0QWG6 EXPRESSION TAG
SEQADV 4NC9 GLY A -1 UNP A0QWG6 EXPRESSION TAG
SEQADV 4NC9 ALA A 0 UNP A0QWG6 EXPRESSION TAG
SEQADV 4NC9 GLY B -3 UNP A0QWG6 EXPRESSION TAG
SEQADV 4NC9 SER B -2 UNP A0QWG6 EXPRESSION TAG
SEQADV 4NC9 GLY B -1 UNP A0QWG6 EXPRESSION TAG
SEQADV 4NC9 ALA B 0 UNP A0QWG6 EXPRESSION TAG
SEQADV 4NC9 GLY C -3 UNP A0QWG6 EXPRESSION TAG
SEQADV 4NC9 SER C -2 UNP A0QWG6 EXPRESSION TAG
SEQADV 4NC9 GLY C -1 UNP A0QWG6 EXPRESSION TAG
SEQADV 4NC9 ALA C 0 UNP A0QWG6 EXPRESSION TAG
SEQADV 4NC9 GLY D -3 UNP A0QWG6 EXPRESSION TAG
SEQADV 4NC9 SER D -2 UNP A0QWG6 EXPRESSION TAG
SEQADV 4NC9 GLY D -1 UNP A0QWG6 EXPRESSION TAG
SEQADV 4NC9 ALA D 0 UNP A0QWG6 EXPRESSION TAG
SEQRES 1 A 390 GLY SER GLY ALA MET ARG ILE GLY MET VAL CYS PRO TYR
SEQRES 2 A 390 SER PHE ASP VAL PRO GLY GLY VAL GLN SER HIS VAL LEU
SEQRES 3 A 390 GLN LEU ALA GLU VAL LEU ARG ASP ALA GLY HIS GLU VAL
SEQRES 4 A 390 SER VAL LEU ALA PRO ALA SER PRO HIS VAL LYS LEU PRO
SEQRES 5 A 390 ASP TYR VAL VAL SER GLY GLY LYS ALA VAL PRO ILE PRO
SEQRES 6 A 390 TYR ASN GLY SER VAL ALA ARG LEU ARG PHE GLY PRO ALA
SEQRES 7 A 390 THR HIS ARG LYS VAL LYS LYS TRP ILE ALA GLU GLY ASP
SEQRES 8 A 390 PHE ASP VAL LEU HIS ILE HIS GLU PRO ASN ALA PRO SER
SEQRES 9 A 390 LEU SER MET LEU ALA LEU GLN ALA ALA GLU GLY PRO ILE
SEQRES 10 A 390 VAL ALA THR PHE HIS THR SER THR THR LYS SER LEU THR
SEQRES 11 A 390 LEU SER VAL PHE GLN GLY ILE LEU ARG PRO TYR HIS GLU
SEQRES 12 A 390 LYS ILE ILE GLY ARG ILE ALA VAL SER ASP LEU ALA ARG
SEQRES 13 A 390 ARG TRP GLN MET GLU ALA LEU GLY SER ASP ALA VAL GLU
SEQRES 14 A 390 ILE PRO ASN GLY VAL ASP VAL ALA SER PHE ALA ASP ALA
SEQRES 15 A 390 PRO LEU LEU ASP GLY TYR PRO ARG GLU GLY ARG THR VAL
SEQRES 16 A 390 LEU PHE LEU GLY ARG TYR ASP GLU PRO ARG LYS GLY MET
SEQRES 17 A 390 ALA VAL LEU LEU ALA ALA LEU PRO LYS LEU VAL ALA ARG
SEQRES 18 A 390 PHE PRO ASP VAL GLU ILE LEU ILE VAL GLY ARG GLY ASP
SEQRES 19 A 390 GLU ASP GLU LEU ARG GLU GLN ALA GLY ASP LEU ALA GLY
SEQRES 20 A 390 HIS LEU ARG PHE LEU GLY GLN VAL ASP ASP ALA THR LYS
SEQRES 21 A 390 ALA SER ALA MET ARG SER ALA ASP VAL TYR CYS ALA PRO
SEQRES 22 A 390 HIS LEU GLY GLY GLU SER PHE GLY ILE VAL LEU VAL GLU
SEQRES 23 A 390 ALA MET ALA ALA GLY THR ALA VAL VAL ALA SER ASP LEU
SEQRES 24 A 390 ASP ALA PHE ARG ARG VAL LEU ALA ASP GLY ASP ALA GLY
SEQRES 25 A 390 ARG LEU VAL PRO VAL ASP ASP ALA ASP GLY MET ALA ALA
SEQRES 26 A 390 ALA LEU ILE GLY ILE LEU GLU ASP ASP GLN LEU ARG ALA
SEQRES 27 A 390 GLY TYR VAL ALA ARG ALA SER GLU ARG VAL HIS ARG TYR
SEQRES 28 A 390 ASP TRP SER VAL VAL SER ALA GLN ILE MET ARG VAL TYR
SEQRES 29 A 390 GLU THR VAL SER GLY ALA GLY ILE LYS VAL GLN VAL SER
SEQRES 30 A 390 GLY ALA ALA ASN ARG ASP GLU THR ALA GLY GLU SER VAL
SEQRES 1 B 390 GLY SER GLY ALA MET ARG ILE GLY MET VAL CYS PRO TYR
SEQRES 2 B 390 SER PHE ASP VAL PRO GLY GLY VAL GLN SER HIS VAL LEU
SEQRES 3 B 390 GLN LEU ALA GLU VAL LEU ARG ASP ALA GLY HIS GLU VAL
SEQRES 4 B 390 SER VAL LEU ALA PRO ALA SER PRO HIS VAL LYS LEU PRO
SEQRES 5 B 390 ASP TYR VAL VAL SER GLY GLY LYS ALA VAL PRO ILE PRO
SEQRES 6 B 390 TYR ASN GLY SER VAL ALA ARG LEU ARG PHE GLY PRO ALA
SEQRES 7 B 390 THR HIS ARG LYS VAL LYS LYS TRP ILE ALA GLU GLY ASP
SEQRES 8 B 390 PHE ASP VAL LEU HIS ILE HIS GLU PRO ASN ALA PRO SER
SEQRES 9 B 390 LEU SER MET LEU ALA LEU GLN ALA ALA GLU GLY PRO ILE
SEQRES 10 B 390 VAL ALA THR PHE HIS THR SER THR THR LYS SER LEU THR
SEQRES 11 B 390 LEU SER VAL PHE GLN GLY ILE LEU ARG PRO TYR HIS GLU
SEQRES 12 B 390 LYS ILE ILE GLY ARG ILE ALA VAL SER ASP LEU ALA ARG
SEQRES 13 B 390 ARG TRP GLN MET GLU ALA LEU GLY SER ASP ALA VAL GLU
SEQRES 14 B 390 ILE PRO ASN GLY VAL ASP VAL ALA SER PHE ALA ASP ALA
SEQRES 15 B 390 PRO LEU LEU ASP GLY TYR PRO ARG GLU GLY ARG THR VAL
SEQRES 16 B 390 LEU PHE LEU GLY ARG TYR ASP GLU PRO ARG LYS GLY MET
SEQRES 17 B 390 ALA VAL LEU LEU ALA ALA LEU PRO LYS LEU VAL ALA ARG
SEQRES 18 B 390 PHE PRO ASP VAL GLU ILE LEU ILE VAL GLY ARG GLY ASP
SEQRES 19 B 390 GLU ASP GLU LEU ARG GLU GLN ALA GLY ASP LEU ALA GLY
SEQRES 20 B 390 HIS LEU ARG PHE LEU GLY GLN VAL ASP ASP ALA THR LYS
SEQRES 21 B 390 ALA SER ALA MET ARG SER ALA ASP VAL TYR CYS ALA PRO
SEQRES 22 B 390 HIS LEU GLY GLY GLU SER PHE GLY ILE VAL LEU VAL GLU
SEQRES 23 B 390 ALA MET ALA ALA GLY THR ALA VAL VAL ALA SER ASP LEU
SEQRES 24 B 390 ASP ALA PHE ARG ARG VAL LEU ALA ASP GLY ASP ALA GLY
SEQRES 25 B 390 ARG LEU VAL PRO VAL ASP ASP ALA ASP GLY MET ALA ALA
SEQRES 26 B 390 ALA LEU ILE GLY ILE LEU GLU ASP ASP GLN LEU ARG ALA
SEQRES 27 B 390 GLY TYR VAL ALA ARG ALA SER GLU ARG VAL HIS ARG TYR
SEQRES 28 B 390 ASP TRP SER VAL VAL SER ALA GLN ILE MET ARG VAL TYR
SEQRES 29 B 390 GLU THR VAL SER GLY ALA GLY ILE LYS VAL GLN VAL SER
SEQRES 30 B 390 GLY ALA ALA ASN ARG ASP GLU THR ALA GLY GLU SER VAL
SEQRES 1 C 390 GLY SER GLY ALA MET ARG ILE GLY MET VAL CYS PRO TYR
SEQRES 2 C 390 SER PHE ASP VAL PRO GLY GLY VAL GLN SER HIS VAL LEU
SEQRES 3 C 390 GLN LEU ALA GLU VAL LEU ARG ASP ALA GLY HIS GLU VAL
SEQRES 4 C 390 SER VAL LEU ALA PRO ALA SER PRO HIS VAL LYS LEU PRO
SEQRES 5 C 390 ASP TYR VAL VAL SER GLY GLY LYS ALA VAL PRO ILE PRO
SEQRES 6 C 390 TYR ASN GLY SER VAL ALA ARG LEU ARG PHE GLY PRO ALA
SEQRES 7 C 390 THR HIS ARG LYS VAL LYS LYS TRP ILE ALA GLU GLY ASP
SEQRES 8 C 390 PHE ASP VAL LEU HIS ILE HIS GLU PRO ASN ALA PRO SER
SEQRES 9 C 390 LEU SER MET LEU ALA LEU GLN ALA ALA GLU GLY PRO ILE
SEQRES 10 C 390 VAL ALA THR PHE HIS THR SER THR THR LYS SER LEU THR
SEQRES 11 C 390 LEU SER VAL PHE GLN GLY ILE LEU ARG PRO TYR HIS GLU
SEQRES 12 C 390 LYS ILE ILE GLY ARG ILE ALA VAL SER ASP LEU ALA ARG
SEQRES 13 C 390 ARG TRP GLN MET GLU ALA LEU GLY SER ASP ALA VAL GLU
SEQRES 14 C 390 ILE PRO ASN GLY VAL ASP VAL ALA SER PHE ALA ASP ALA
SEQRES 15 C 390 PRO LEU LEU ASP GLY TYR PRO ARG GLU GLY ARG THR VAL
SEQRES 16 C 390 LEU PHE LEU GLY ARG TYR ASP GLU PRO ARG LYS GLY MET
SEQRES 17 C 390 ALA VAL LEU LEU ALA ALA LEU PRO LYS LEU VAL ALA ARG
SEQRES 18 C 390 PHE PRO ASP VAL GLU ILE LEU ILE VAL GLY ARG GLY ASP
SEQRES 19 C 390 GLU ASP GLU LEU ARG GLU GLN ALA GLY ASP LEU ALA GLY
SEQRES 20 C 390 HIS LEU ARG PHE LEU GLY GLN VAL ASP ASP ALA THR LYS
SEQRES 21 C 390 ALA SER ALA MET ARG SER ALA ASP VAL TYR CYS ALA PRO
SEQRES 22 C 390 HIS LEU GLY GLY GLU SER PHE GLY ILE VAL LEU VAL GLU
SEQRES 23 C 390 ALA MET ALA ALA GLY THR ALA VAL VAL ALA SER ASP LEU
SEQRES 24 C 390 ASP ALA PHE ARG ARG VAL LEU ALA ASP GLY ASP ALA GLY
SEQRES 25 C 390 ARG LEU VAL PRO VAL ASP ASP ALA ASP GLY MET ALA ALA
SEQRES 26 C 390 ALA LEU ILE GLY ILE LEU GLU ASP ASP GLN LEU ARG ALA
SEQRES 27 C 390 GLY TYR VAL ALA ARG ALA SER GLU ARG VAL HIS ARG TYR
SEQRES 28 C 390 ASP TRP SER VAL VAL SER ALA GLN ILE MET ARG VAL TYR
SEQRES 29 C 390 GLU THR VAL SER GLY ALA GLY ILE LYS VAL GLN VAL SER
SEQRES 30 C 390 GLY ALA ALA ASN ARG ASP GLU THR ALA GLY GLU SER VAL
SEQRES 1 D 390 GLY SER GLY ALA MET ARG ILE GLY MET VAL CYS PRO TYR
SEQRES 2 D 390 SER PHE ASP VAL PRO GLY GLY VAL GLN SER HIS VAL LEU
SEQRES 3 D 390 GLN LEU ALA GLU VAL LEU ARG ASP ALA GLY HIS GLU VAL
SEQRES 4 D 390 SER VAL LEU ALA PRO ALA SER PRO HIS VAL LYS LEU PRO
SEQRES 5 D 390 ASP TYR VAL VAL SER GLY GLY LYS ALA VAL PRO ILE PRO
SEQRES 6 D 390 TYR ASN GLY SER VAL ALA ARG LEU ARG PHE GLY PRO ALA
SEQRES 7 D 390 THR HIS ARG LYS VAL LYS LYS TRP ILE ALA GLU GLY ASP
SEQRES 8 D 390 PHE ASP VAL LEU HIS ILE HIS GLU PRO ASN ALA PRO SER
SEQRES 9 D 390 LEU SER MET LEU ALA LEU GLN ALA ALA GLU GLY PRO ILE
SEQRES 10 D 390 VAL ALA THR PHE HIS THR SER THR THR LYS SER LEU THR
SEQRES 11 D 390 LEU SER VAL PHE GLN GLY ILE LEU ARG PRO TYR HIS GLU
SEQRES 12 D 390 LYS ILE ILE GLY ARG ILE ALA VAL SER ASP LEU ALA ARG
SEQRES 13 D 390 ARG TRP GLN MET GLU ALA LEU GLY SER ASP ALA VAL GLU
SEQRES 14 D 390 ILE PRO ASN GLY VAL ASP VAL ALA SER PHE ALA ASP ALA
SEQRES 15 D 390 PRO LEU LEU ASP GLY TYR PRO ARG GLU GLY ARG THR VAL
SEQRES 16 D 390 LEU PHE LEU GLY ARG TYR ASP GLU PRO ARG LYS GLY MET
SEQRES 17 D 390 ALA VAL LEU LEU ALA ALA LEU PRO LYS LEU VAL ALA ARG
SEQRES 18 D 390 PHE PRO ASP VAL GLU ILE LEU ILE VAL GLY ARG GLY ASP
SEQRES 19 D 390 GLU ASP GLU LEU ARG GLU GLN ALA GLY ASP LEU ALA GLY
SEQRES 20 D 390 HIS LEU ARG PHE LEU GLY GLN VAL ASP ASP ALA THR LYS
SEQRES 21 D 390 ALA SER ALA MET ARG SER ALA ASP VAL TYR CYS ALA PRO
SEQRES 22 D 390 HIS LEU GLY GLY GLU SER PHE GLY ILE VAL LEU VAL GLU
SEQRES 23 D 390 ALA MET ALA ALA GLY THR ALA VAL VAL ALA SER ASP LEU
SEQRES 24 D 390 ASP ALA PHE ARG ARG VAL LEU ALA ASP GLY ASP ALA GLY
SEQRES 25 D 390 ARG LEU VAL PRO VAL ASP ASP ALA ASP GLY MET ALA ALA
SEQRES 26 D 390 ALA LEU ILE GLY ILE LEU GLU ASP ASP GLN LEU ARG ALA
SEQRES 27 D 390 GLY TYR VAL ALA ARG ALA SER GLU ARG VAL HIS ARG TYR
SEQRES 28 D 390 ASP TRP SER VAL VAL SER ALA GLN ILE MET ARG VAL TYR
SEQRES 29 D 390 GLU THR VAL SER GLY ALA GLY ILE LYS VAL GLN VAL SER
SEQRES 30 D 390 GLY ALA ALA ASN ARG ASP GLU THR ALA GLY GLU SER VAL
FORMUL 5 HOH *66(H2 O)
HELIX 1 1 GLY A 15 ALA A 31 1 17
HELIX 2 2 GLY A 72 ASP A 87 1 16
HELIX 3 3 SER A 100 ALA A 108 1 9
HELIX 4 4 LEU A 134 ALA A 146 1 13
HELIX 5 5 SER A 148 ALA A 158 1 11
HELIX 6 6 VAL A 172 ASP A 177 1 6
HELIX 7 7 GLU A 199 LYS A 202 5 4
HELIX 8 8 GLY A 203 ALA A 210 1 8
HELIX 9 9 ALA A 210 PHE A 218 1 9
HELIX 10 10 ASP A 230 GLY A 239 1 10
HELIX 11 11 ASP A 240 GLY A 243 5 4
HELIX 12 12 ASP A 252 ALA A 263 1 12
HELIX 13 13 GLY A 277 ALA A 286 1 10
HELIX 14 14 LEU A 295 LEU A 302 1 8
HELIX 15 15 ASP A 315 ASP A 329 1 15
HELIX 16 16 ASP A 329 VAL A 344 1 16
HELIX 17 17 HIS A 345 TYR A 347 5 3
HELIX 18 18 ASP A 348 SER A 364 1 17
HELIX 19 19 GLY B 15 ALA B 31 1 17
HELIX 20 20 GLY B 72 ASP B 87 1 16
HELIX 21 21 SER B 100 ALA B 108 1 9
HELIX 22 22 ASP B 149 ALA B 158 1 10
HELIX 23 23 ASP B 171 ASP B 177 1 7
HELIX 24 24 GLU B 199 LYS B 202 5 4
HELIX 25 25 GLY B 203 PHE B 218 1 16
HELIX 26 26 ASP B 230 GLY B 239 1 10
HELIX 27 27 ASP B 240 HIS B 244 5 5
HELIX 28 28 ASP B 252 ALA B 263 1 12
HELIX 29 29 PHE B 276 GLY B 287 1 12
HELIX 30 30 LEU B 295 LEU B 302 1 8
HELIX 31 31 ASP B 315 ASP B 329 1 15
HELIX 32 32 ASP B 329 HIS B 345 1 17
HELIX 33 33 ASP B 348 GLU B 361 1 14
HELIX 34 34 GLY C 15 ALA C 31 1 17
HELIX 35 35 GLY C 72 ASP C 87 1 16
HELIX 36 36 SER C 100 ALA C 108 1 9
HELIX 37 37 ASP C 149 ALA C 158 1 10
HELIX 38 38 ASP C 171 ASP C 177 1 7
HELIX 39 39 GLY C 203 PHE C 218 1 16
HELIX 40 40 ASP C 232 GLU C 236 1 5
HELIX 41 41 ASP C 252 ALA C 263 1 12
HELIX 42 42 PHE C 276 GLY C 287 1 12
HELIX 43 43 LEU C 295 LEU C 302 1 8
HELIX 44 44 ASP C 315 ASP C 329 1 15
HELIX 45 45 GLN C 331 GLU C 342 1 12
HELIX 46 46 ARG C 343 TYR C 347 5 5
HELIX 47 47 ASP C 348 GLU C 361 1 14
HELIX 48 48 GLY D 15 ASP D 30 1 16
HELIX 49 49 PRO D 73 ASP D 87 1 15
HELIX 50 50 SER D 100 ALA D 108 1 9
HELIX 51 51 LEU D 134 ALA D 146 1 13
HELIX 52 52 SER D 148 ALA D 158 1 11
HELIX 53 53 VAL D 172 ASP D 177 1 6
HELIX 54 54 GLU D 199 LYS D 202 5 4
HELIX 55 55 GLY D 203 PHE D 218 1 16
HELIX 56 56 ASP D 230 GLY D 239 1 10
HELIX 57 57 ASP D 240 GLY D 243 5 4
HELIX 58 58 ASP D 252 ALA D 263 1 12
HELIX 59 59 GLY D 277 GLY D 287 1 11
HELIX 60 60 LEU D 295 LEU D 302 1 8
HELIX 61 61 ASP D 315 ASP D 329 1 15
HELIX 62 62 ASP D 329 VAL D 344 1 16
HELIX 63 63 HIS D 345 TYR D 347 5 3
HELIX 64 64 ASP D 348 SER D 364 1 17
SHEET 1 A 7 VAL A 51 SER A 53 0
SHEET 2 A 7 GLU A 34 ALA A 39 1 N VAL A 37 O VAL A 52
SHEET 3 A 7 ARG A 2 VAL A 6 1 N MET A 5 O LEU A 38
SHEET 4 A 7 VAL A 90 HIS A 94 1 O HIS A 92 N GLY A 4
SHEET 5 A 7 ILE A 113 HIS A 118 1 O VAL A 114 N ILE A 93
SHEET 6 A 7 LYS A 123 SER A 128 -1 O LEU A 127 N ALA A 115
SHEET 7 A 7 VAL A 164 PRO A 167 -1 O VAL A 164 N THR A 126
SHEET 1 B 2 ALA A 109 GLU A 110 0
SHEET 2 B 2 GLN A 371 VAL A 372 -1 O GLN A 371 N GLU A 110
SHEET 1 C 6 LEU A 245 GLY A 249 0
SHEET 2 C 6 ILE A 223 VAL A 226 1 N ILE A 225 O ARG A 246
SHEET 3 C 6 VAL A 191 LEU A 194 1 N PHE A 193 O LEU A 224
SHEET 4 C 6 VAL A 265 ALA A 268 1 O VAL A 265 N LEU A 192
SHEET 5 C 6 ALA A 289 SER A 293 1 O VAL A 291 N TYR A 266
SHEET 6 C 6 ARG A 309 VAL A 311 1 O ARG A 309 N ALA A 292
SHEET 1 D 7 VAL B 51 SER B 53 0
SHEET 2 D 7 GLU B 34 ALA B 39 1 N VAL B 37 O VAL B 52
SHEET 3 D 7 ARG B 2 VAL B 6 1 N ILE B 3 O GLU B 34
SHEET 4 D 7 VAL B 90 HIS B 94 1 O HIS B 92 N GLY B 4
SHEET 5 D 7 ALA B 109 PHE B 117 1 O VAL B 114 N ILE B 93
SHEET 6 D 7 LYS B 123 GLN B 131 -1 O LEU B 125 N PHE B 117
SHEET 7 D 7 VAL B 164 PRO B 167 -1 O ILE B 166 N SER B 124
SHEET 1 E 6 VAL B 51 SER B 53 0
SHEET 2 E 6 GLU B 34 ALA B 39 1 N VAL B 37 O VAL B 52
SHEET 3 E 6 ARG B 2 VAL B 6 1 N ILE B 3 O GLU B 34
SHEET 4 E 6 VAL B 90 HIS B 94 1 O HIS B 92 N GLY B 4
SHEET 5 E 6 ALA B 109 PHE B 117 1 O VAL B 114 N ILE B 93
SHEET 6 E 6 GLN B 371 VAL B 372 -1 O GLN B 371 N GLU B 110
SHEET 1 F 2 ALA B 57 VAL B 58 0
SHEET 2 F 2 ARG B 70 PHE B 71 -1 O ARG B 70 N VAL B 58
SHEET 1 G 5 ILE B 223 VAL B 226 0
SHEET 2 G 5 VAL B 191 LEU B 194 1 N PHE B 193 O LEU B 224
SHEET 3 G 5 VAL B 265 ALA B 268 1 O CYS B 267 N LEU B 192
SHEET 4 G 5 ALA B 289 SER B 293 1 O VAL B 291 N TYR B 266
SHEET 5 G 5 ARG B 309 VAL B 311 1 O ARG B 309 N ALA B 292
SHEET 1 H 7 VAL C 51 SER C 53 0
SHEET 2 H 7 GLU C 34 ALA C 39 1 N VAL C 37 O VAL C 52
SHEET 3 H 7 ARG C 2 VAL C 6 1 N MET C 5 O LEU C 38
SHEET 4 H 7 VAL C 90 HIS C 94 1 O HIS C 92 N GLY C 4
SHEET 5 H 7 ALA C 109 PHE C 117 1 O VAL C 114 N ILE C 93
SHEET 6 H 7 LYS C 123 GLN C 131 -1 O LEU C 127 N ALA C 115
SHEET 7 H 7 VAL C 164 PRO C 167 -1 O VAL C 164 N THR C 126
SHEET 1 I 6 VAL C 51 SER C 53 0
SHEET 2 I 6 GLU C 34 ALA C 39 1 N VAL C 37 O VAL C 52
SHEET 3 I 6 ARG C 2 VAL C 6 1 N MET C 5 O LEU C 38
SHEET 4 I 6 VAL C 90 HIS C 94 1 O HIS C 92 N GLY C 4
SHEET 5 I 6 ALA C 109 PHE C 117 1 O VAL C 114 N ILE C 93
SHEET 6 I 6 GLN C 371 VAL C 372 -1 O GLN C 371 N GLU C 110
SHEET 1 J 2 ALA C 57 VAL C 58 0
SHEET 2 J 2 ARG C 70 PHE C 71 -1 O ARG C 70 N VAL C 58
SHEET 1 K 6 ARG C 246 PHE C 247 0
SHEET 2 K 6 LEU C 224 ILE C 225 1 N ILE C 225 O ARG C 246
SHEET 3 K 6 VAL C 191 PHE C 193 1 N VAL C 191 O LEU C 224
SHEET 4 K 6 VAL C 265 ALA C 268 1 O CYS C 267 N LEU C 192
SHEET 5 K 6 ALA C 289 SER C 293 1 O VAL C 291 N TYR C 266
SHEET 6 K 6 ARG C 309 VAL C 311 1 O ARG C 309 N ALA C 292
SHEET 1 L 7 VAL D 51 SER D 53 0
SHEET 2 L 7 GLU D 34 ALA D 39 1 N VAL D 37 O VAL D 52
SHEET 3 L 7 ARG D 2 VAL D 6 1 N ILE D 3 O SER D 36
SHEET 4 L 7 VAL D 90 HIS D 94 1 O HIS D 92 N VAL D 6
SHEET 5 L 7 VAL D 114 SER D 120 1 O VAL D 114 N LEU D 91
SHEET 6 L 7 LYS D 123 SER D 128 -1 O LEU D 127 N ALA D 115
SHEET 7 L 7 VAL D 164 PRO D 167 -1 O VAL D 164 N THR D 126
SHEET 1 M 2 ALA D 109 GLU D 110 0
SHEET 2 M 2 GLN D 371 VAL D 372 -1 O GLN D 371 N GLU D 110
SHEET 1 N 6 LEU D 245 LEU D 248 0
SHEET 2 N 6 ILE D 223 VAL D 226 1 N ILE D 225 O ARG D 246
SHEET 3 N 6 VAL D 191 LEU D 194 1 N VAL D 191 O LEU D 224
SHEET 4 N 6 VAL D 265 ALA D 268 1 O CYS D 267 N LEU D 192
SHEET 5 N 6 ALA D 289 SER D 293 1 O VAL D 291 N TYR D 266
SHEET 6 N 6 ARG D 309 VAL D 311 1 O ARG D 309 N ALA D 292
CISPEP 1 ALA A 98 PRO A 99 0 -3.03
CISPEP 2 TYR A 184 PRO A 185 0 1.70
CISPEP 3 SER A 373 GLY A 374 0 -0.61
CISPEP 4 TYR B 184 PRO B 185 0 -4.24
CISPEP 5 GLY B 365 ALA B 366 0 -15.10
CISPEP 6 ALA B 366 GLY B 367 0 -2.13
CISPEP 7 TYR C 184 PRO C 185 0 5.21
CISPEP 8 GLY C 365 ALA C 366 0 -12.61
CISPEP 9 ALA C 366 GLY C 367 0 -5.66
CISPEP 10 ALA D 98 PRO D 99 0 -5.84
CISPEP 11 GLN D 131 GLY D 132 0 -18.45
CISPEP 12 TYR D 184 PRO D 185 0 0.85
CRYST1 137.620 137.620 168.641 90.00 90.00 120.00 P 32 2 1 24
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 0.007266 0.004195 0.000000 0.00000
SCALE2 0.000000 0.008390 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005930 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
