HEADER HYDROLASE 03-APR-12 3VR4
TITLE CRYSTAL STRUCTURE OF ENTEROCOCCUS HIRAE V1-ATPASE [EV1]
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: V-TYPE SODIUM ATPASE CATALYTIC SUBUNIT A;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: NA(+)-TRANSLOCATING ATPASE SUBUNIT A, V-TYPE SODIUM PUMP
COMPND 5 CATALYTIC SUBUNIT A;
COMPND 6 EC: 3.6.3.15;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: V-TYPE SODIUM ATPASE SUBUNIT B;
COMPND 10 CHAIN: D, E, F;
COMPND 11 SYNONYM: NA(+)-TRANSLOCATING ATPASE SUBUNIT B, V-TYPE SODIUM PUMP
COMPND 12 SUBUNIT B;
COMPND 13 EC: 3.6.3.15;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: V-TYPE SODIUM ATPASE SUBUNIT D;
COMPND 17 CHAIN: G;
COMPND 18 SYNONYM: NA(+)-TRANSLOCATING ATPASE SUBUNIT D, V-TYPE SODIUM PUMP
COMPND 19 SUBUNIT D;
COMPND 20 EC: 3.6.3.15;
COMPND 21 ENGINEERED: YES;
COMPND 22 MOL_ID: 4;
COMPND 23 MOLECULE: V-TYPE SODIUM ATPASE SUBUNIT G;
COMPND 24 CHAIN: H;
COMPND 25 SYNONYM: NA(+)-TRANSLOCATING ATPASE SUBUNIT G, V-TYPE SODIUM PUMP
COMPND 26 SUBUNIT G;
COMPND 27 EC: 3.6.3.15;
COMPND 28 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROCOCCUS HIRAE;
SOURCE 3 ORGANISM_TAXID: 1354;
SOURCE 4 GENE: NTPA;
SOURCE 5 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: ENTEROCOCCUS HIRAE;
SOURCE 8 ORGANISM_TAXID: 1354;
SOURCE 9 GENE: NTPB;
SOURCE 10 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: ENTEROCOCCUS HIRAE;
SOURCE 13 ORGANISM_TAXID: 1354;
SOURCE 14 GENE: NTPD;
SOURCE 15 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 16 MOL_ID: 4;
SOURCE 17 ORGANISM_SCIENTIFIC: ENTEROCOCCUS HIRAE;
SOURCE 18 ORGANISM_TAXID: 1354;
SOURCE 19 GENE: NTPG;
SOURCE 20 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS
KEYWDS V-ATPASE, ENTEROCOCCUS HIRAE, ROTARY MOTOR, P-LOOP, HYDROLASE, NA(+)-
KEYWDS 2 ATPASE, ATP BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SAIJO,S.ARAI,K.SUZUKI,K.MIZUTANI,Y.KAKINUMA,Y.ISHIZUKA-KATSURA,
AUTHOR 2 N.OHSAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,S.IWATA,I.YAMATO,T.MURATA
REVDAT 4 06-DEC-23 3VR4 1 REMARK
REVDAT 3 08-NOV-23 3VR4 1 REMARK SEQADV LINK
REVDAT 2 06-FEB-13 3VR4 1 JRNL
REVDAT 1 16-JAN-13 3VR4 0
JRNL AUTH S.ARAI,S.SAIJO,K.SUZUKI,K.MIZUTANI,Y.KAKINUMA,
JRNL AUTH 2 Y.ISHIZUKA-KATSURA,N.OHSAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,
JRNL AUTH 3 S.IWATA,I.YAMATO,T.MURATA
JRNL TITL ROTATION MECHANISM OF ENTEROCOCCUS HIRAE V(1)-ATPASE BASED
JRNL TITL 2 ON ASYMMETRIC CRYSTAL STRUCTURES
JRNL REF NATURE V. 493 703 2013
JRNL REFN ISSN 0028-0836
JRNL PMID 23334411
JRNL DOI 10.1038/NATURE11778
REMARK 2
REMARK 2 RESOLUTION. 2.17 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_934)
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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.17
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.04
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.320
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 194627
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 9799
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 28.0517 - 5.8814 0.90 16955 835 0.1731 0.2014
REMARK 3 2 5.8814 - 4.6752 0.92 17482 905 0.1440 0.1697
REMARK 3 3 4.6752 - 4.0863 0.93 17635 928 0.1164 0.1535
REMARK 3 4 4.0863 - 3.7136 0.94 17722 989 0.1287 0.1717
REMARK 3 5 3.7136 - 3.4479 0.94 17838 1004 0.1397 0.1867
REMARK 3 6 3.4479 - 3.2450 0.95 18005 941 0.1543 0.2174
REMARK 3 7 3.2450 - 3.0827 0.95 17949 959 0.1625 0.2210
REMARK 3 8 3.0827 - 2.9486 0.95 17963 941 0.1699 0.2269
REMARK 3 9 2.9486 - 2.8352 0.95 17998 876 0.1774 0.2262
REMARK 3 10 2.8352 - 2.7375 0.94 17894 1041 0.1819 0.2382
REMARK 3 11 2.7375 - 2.6520 0.95 17957 1008 0.1891 0.2422
REMARK 3 12 2.6520 - 2.5762 0.95 17938 973 0.1916 0.2361
REMARK 3 13 2.5762 - 2.5084 0.95 18006 878 0.2011 0.2475
REMARK 3 14 2.5084 - 2.4473 0.95 17943 962 0.2039 0.2530
REMARK 3 15 2.4473 - 2.3917 0.95 18057 910 0.2066 0.2511
REMARK 3 16 2.3917 - 2.3408 0.95 17861 986 0.2078 0.2546
REMARK 3 17 2.3408 - 2.2940 0.95 17847 981 0.2117 0.2573
REMARK 3 18 2.2940 - 2.2507 0.95 18031 943 0.2226 0.2548
REMARK 3 19 2.2507 - 2.2105 0.95 17895 946 0.2263 0.2756
REMARK 3 20 2.2105 - 2.1731 0.92 17502 943 0.2303 0.2669
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 : 0.86
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 41.00
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.35
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.55250
REMARK 3 B22 (A**2) : -0.27840
REMARK 3 B33 (A**2) : 0.83090
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: 0.0360
REMARK 3 OPERATOR: K,H,-L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 26903
REMARK 3 ANGLE : 0.738 36359
REMARK 3 CHIRALITY : 0.051 4168
REMARK 3 PLANARITY : 0.003 4728
REMARK 3 DIHEDRAL : 12.970 10089
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 39
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 0:63)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.2916 26.3255 56.8945
REMARK 3 T TENSOR
REMARK 3 T11: 0.2314 T22: 0.1441
REMARK 3 T33: 0.2090 T12: -0.0221
REMARK 3 T13: 0.0410 T23: 0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 2.8912 L22: 3.9807
REMARK 3 L33: 3.2319 L12: 0.4251
REMARK 3 L13: 1.3553 L23: 2.4049
REMARK 3 S TENSOR
REMARK 3 S11: -0.0855 S12: 0.1391 S13: 0.1111
REMARK 3 S21: -0.2517 S22: 0.1706 S23: -0.0261
REMARK 3 S31: -0.2094 S32: 0.0848 S33: -0.0934
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 64:390)
REMARK 3 ORIGIN FOR THE GROUP (A): 60.8939 2.3693 57.6053
REMARK 3 T TENSOR
REMARK 3 T11: 0.1398 T22: 0.1784
REMARK 3 T33: 0.2108 T12: -0.0132
REMARK 3 T13: 0.0100 T23: -0.0463
REMARK 3 L TENSOR
REMARK 3 L11: 0.3896 L22: 1.4051
REMARK 3 L33: 0.7310 L12: 0.0546
REMARK 3 L13: -0.0976 L23: 0.1820
REMARK 3 S TENSOR
REMARK 3 S11: -0.0279 S12: 0.0080 S13: 0.0710
REMARK 3 S21: -0.1709 S22: 0.0508 S23: -0.1671
REMARK 3 S31: -0.0469 S32: 0.1608 S33: -0.0174
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 391:426)
REMARK 3 ORIGIN FOR THE GROUP (A): 51.5823 -8.4865 78.0030
REMARK 3 T TENSOR
REMARK 3 T11: 0.2805 T22: 0.2484
REMARK 3 T33: 0.2556 T12: 0.0264
REMARK 3 T13: 0.0143 T23: -0.0613
REMARK 3 L TENSOR
REMARK 3 L11: 1.7876 L22: 2.6541
REMARK 3 L33: 1.6947 L12: -1.3233
REMARK 3 L13: 1.4325 L23: -1.3781
REMARK 3 S TENSOR
REMARK 3 S11: -0.2891 S12: -0.3774 S13: 0.1363
REMARK 3 S21: 0.6339 S22: 0.1901 S23: 0.0902
REMARK 3 S31: -0.0877 S32: -0.2832 S33: 0.0309
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 427:587)
REMARK 3 ORIGIN FOR THE GROUP (A): 63.8019 -30.2972 80.5299
REMARK 3 T TENSOR
REMARK 3 T11: 0.3366 T22: 0.1334
REMARK 3 T33: 0.2170 T12: 0.1162
REMARK 3 T13: -0.0526 T23: -0.0534
REMARK 3 L TENSOR
REMARK 3 L11: 0.9957 L22: 1.9694
REMARK 3 L33: 1.0108 L12: -0.5194
REMARK 3 L13: 0.4285 L23: -0.7058
REMARK 3 S TENSOR
REMARK 3 S11: 0.0519 S12: -0.0734 S13: -0.1627
REMARK 3 S21: 0.2884 S22: 0.0384 S23: -0.1228
REMARK 3 S31: 0.4122 S32: 0.1323 S33: -0.0390
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND (RESSEQ -6:90)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6228 11.2315 53.4007
REMARK 3 T TENSOR
REMARK 3 T11: 0.2196 T22: 0.1871
REMARK 3 T33: 0.1503 T12: 0.0238
REMARK 3 T13: -0.0338 T23: 0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 0.7011 L22: 0.7409
REMARK 3 L33: 0.4648 L12: 0.4893
REMARK 3 L13: -0.5172 L23: -0.1858
REMARK 3 S TENSOR
REMARK 3 S11: 0.0506 S12: 0.0511 S13: 0.0607
REMARK 3 S21: -0.1427 S22: -0.0295 S23: 0.0516
REMARK 3 S31: -0.0837 S32: -0.1109 S33: -0.0308
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 91:226)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.9775 -2.7973 63.7099
REMARK 3 T TENSOR
REMARK 3 T11: 0.1333 T22: 0.2194
REMARK 3 T33: 0.2455 T12: -0.0226
REMARK 3 T13: -0.0527 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0.9144 L22: 0.5837
REMARK 3 L33: 1.1915 L12: -0.0636
REMARK 3 L13: 0.0745 L23: -0.0171
REMARK 3 S TENSOR
REMARK 3 S11: 0.0646 S12: 0.2348 S13: -0.0322
REMARK 3 S21: -0.1555 S22: 0.0255 S23: 0.2291
REMARK 3 S31: -0.0225 S32: -0.3415 S33: -0.0821
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 227:344)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.7048 -9.2054 68.4242
REMARK 3 T TENSOR
REMARK 3 T11: 0.1641 T22: 0.1528
REMARK 3 T33: 0.1660 T12: -0.0107
REMARK 3 T13: -0.0275 T23: -0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 0.7821 L22: 0.4475
REMARK 3 L33: 0.7147 L12: -0.2497
REMARK 3 L13: -0.3279 L23: -0.2267
REMARK 3 S TENSOR
REMARK 3 S11: 0.0029 S12: 0.0236 S13: -0.1481
REMARK 3 S21: -0.0902 S22: -0.0060 S23: 0.1385
REMARK 3 S31: 0.1602 S32: -0.0533 S33: 0.0105
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 345:586)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9854 -19.0402 90.6489
REMARK 3 T TENSOR
REMARK 3 T11: 0.1002 T22: 0.0164
REMARK 3 T33: 0.1147 T12: -0.0369
REMARK 3 T13: -0.0143 T23: 0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 1.1287 L22: 1.3946
REMARK 3 L33: 1.1033 L12: -0.3710
REMARK 3 L13: 0.1006 L23: -0.3860
REMARK 3 S TENSOR
REMARK 3 S11: 0.0329 S12: -0.1616 S13: -0.3194
REMARK 3 S21: 0.0675 S22: -0.0217 S23: 0.1001
REMARK 3 S31: 0.2494 S32: -0.0425 S33: 0.0177
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 1:90)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.0176 45.8758 86.0002
REMARK 3 T TENSOR
REMARK 3 T11: 0.2416 T22: 0.1158
REMARK 3 T33: 0.2509 T12: 0.0508
REMARK 3 T13: 0.0028 T23: 0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 0.7306 L22: 0.0721
REMARK 3 L33: 2.9392 L12: 0.1612
REMARK 3 L13: 0.5982 L23: 0.4179
REMARK 3 S TENSOR
REMARK 3 S11: -0.0396 S12: 0.0543 S13: 0.2300
REMARK 3 S21: -0.0771 S22: -0.0074 S23: -0.0813
REMARK 3 S31: -0.0470 S32: 0.0690 S33: 0.0557
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 91:185)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.5457 56.5803 108.9934
REMARK 3 T TENSOR
REMARK 3 T11: 0.2406 T22: 0.1320
REMARK 3 T33: 0.3756 T12: 0.0241
REMARK 3 T13: -0.0316 T23: -0.0712
REMARK 3 L TENSOR
REMARK 3 L11: 2.1010 L22: 1.5721
REMARK 3 L33: 0.4913 L12: 1.0358
REMARK 3 L13: 0.2671 L23: 0.2203
REMARK 3 S TENSOR
REMARK 3 S11: -0.0715 S12: -0.1346 S13: 0.6110
REMARK 3 S21: -0.0175 S22: 0.0192 S23: 0.0903
REMARK 3 S31: -0.1299 S32: 0.0363 S33: 0.0385
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 186:344)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.9112 33.6796 107.2243
REMARK 3 T TENSOR
REMARK 3 T11: 0.1442 T22: 0.1205
REMARK 3 T33: 0.1766 T12: 0.0042
REMARK 3 T13: 0.0030 T23: -0.0570
REMARK 3 L TENSOR
REMARK 3 L11: 1.4310 L22: 0.4751
REMARK 3 L33: 0.6131 L12: 0.0085
REMARK 3 L13: 0.4847 L23: -0.3351
REMARK 3 S TENSOR
REMARK 3 S11: 0.0224 S12: -0.0277 S13: 0.0216
REMARK 3 S21: 0.0832 S22: 0.0044 S23: 0.0364
REMARK 3 S31: -0.0580 S32: -0.0290 S33: -0.0314
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 345:452)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.4927 24.6114 103.4307
REMARK 3 T TENSOR
REMARK 3 T11: 0.0922 T22: 0.1061
REMARK 3 T33: 0.1826 T12: -0.0009
REMARK 3 T13: 0.0073 T23: -0.0661
REMARK 3 L TENSOR
REMARK 3 L11: 1.0783 L22: 0.9197
REMARK 3 L33: 0.7842 L12: 0.0435
REMARK 3 L13: 0.2896 L23: -0.6031
REMARK 3 S TENSOR
REMARK 3 S11: 0.0133 S12: 0.0820 S13: -0.1008
REMARK 3 S21: -0.0508 S22: 0.0402 S23: -0.0480
REMARK 3 S31: 0.1086 S32: -0.0353 S33: -0.0514
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 453:586)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.7423 5.1405 124.9289
REMARK 3 T TENSOR
REMARK 3 T11: 0.3245 T22: 0.1599
REMARK 3 T33: 0.2131 T12: -0.0426
REMARK 3 T13: -0.0533 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 2.6545 L22: 2.8902
REMARK 3 L33: 2.2376 L12: -0.4648
REMARK 3 L13: -0.1514 L23: -0.9972
REMARK 3 S TENSOR
REMARK 3 S11: 0.1711 S12: -0.3120 S13: -0.2377
REMARK 3 S21: 0.5135 S22: -0.0301 S23: 0.1600
REMARK 3 S31: 0.2835 S32: 0.0643 S33: -0.0877
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN D AND (RESSEQ 4:77)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.2359 44.3491 73.9856
REMARK 3 T TENSOR
REMARK 3 T11: 0.2969 T22: 0.1748
REMARK 3 T33: 0.2676 T12: 0.0020
REMARK 3 T13: 0.0304 T23: 0.0451
REMARK 3 L TENSOR
REMARK 3 L11: 4.3710 L22: 2.6227
REMARK 3 L33: 1.1283 L12: -3.2967
REMARK 3 L13: -1.6658 L23: 1.5031
REMARK 3 S TENSOR
REMARK 3 S11: -0.1977 S12: -0.1343 S13: 0.0629
REMARK 3 S21: 0.1259 S22: 0.1271 S23: -0.0062
REMARK 3 S31: -0.1122 S32: 0.0294 S33: 0.0704
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN D AND (RESSEQ 78:147)
REMARK 3 ORIGIN FOR THE GROUP (A): 63.8691 26.0168 86.5190
REMARK 3 T TENSOR
REMARK 3 T11: 0.1473 T22: 0.2543
REMARK 3 T33: 0.2726 T12: -0.0585
REMARK 3 T13: -0.0584 T23: -0.0717
REMARK 3 L TENSOR
REMARK 3 L11: 0.6168 L22: 0.9356
REMARK 3 L33: 1.3595 L12: 0.0105
REMARK 3 L13: -0.6219 L23: -0.8028
REMARK 3 S TENSOR
REMARK 3 S11: 0.0639 S12: 0.0442 S13: 0.0130
REMARK 3 S21: 0.0343 S22: -0.0420 S23: -0.2242
REMARK 3 S31: -0.1583 S32: 0.2608 S33: -0.0104
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN D AND (RESSEQ 148:217)
REMARK 3 ORIGIN FOR THE GROUP (A): 57.4271 26.4081 97.4599
REMARK 3 T TENSOR
REMARK 3 T11: 0.2038 T22: 0.2111
REMARK 3 T33: 0.2520 T12: -0.0165
REMARK 3 T13: -0.0555 T23: -0.0739
REMARK 3 L TENSOR
REMARK 3 L11: 0.7814 L22: 1.9001
REMARK 3 L33: 1.7546 L12: -0.3535
REMARK 3 L13: 0.0588 L23: -0.6668
REMARK 3 S TENSOR
REMARK 3 S11: 0.0310 S12: -0.0393 S13: 0.0666
REMARK 3 S21: 0.3054 S22: 0.0215 S23: -0.2793
REMARK 3 S31: -0.2398 S32: 0.3420 S33: -0.0570
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN D AND (RESSEQ 218:389)
REMARK 3 ORIGIN FOR THE GROUP (A): 54.4703 14.3680 88.8359
REMARK 3 T TENSOR
REMARK 3 T11: 0.1163 T22: 0.1636
REMARK 3 T33: 0.2419 T12: -0.0029
REMARK 3 T13: -0.0331 T23: -0.0759
REMARK 3 L TENSOR
REMARK 3 L11: 0.3096 L22: 0.6764
REMARK 3 L33: 1.1760 L12: -0.1075
REMARK 3 L13: 0.0360 L23: -0.3313
REMARK 3 S TENSOR
REMARK 3 S11: 0.0188 S12: 0.0322 S13: -0.0562
REMARK 3 S21: -0.0213 S22: 0.0508 S23: -0.1389
REMARK 3 S31: 0.1027 S32: 0.1539 S33: -0.0629
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN D AND (RESSEQ 390:455)
REMARK 3 ORIGIN FOR THE GROUP (A): 63.9146 -2.4053 107.9464
REMARK 3 T TENSOR
REMARK 3 T11: 0.3047 T22: 0.2601
REMARK 3 T33: 0.4960 T12: 0.0868
REMARK 3 T13: -0.1701 T23: -0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 1.9629 L22: 0.4755
REMARK 3 L33: 1.6865 L12: 0.0123
REMARK 3 L13: 0.0685 L23: -0.7713
REMARK 3 S TENSOR
REMARK 3 S11: 0.1066 S12: -0.0810 S13: -0.5731
REMARK 3 S21: 0.1746 S22: -0.0882 S23: -0.5117
REMARK 3 S31: 0.3402 S32: 0.2783 S33: 0.0348
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN E AND (RESSEQ 4:77)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.4882 12.4180 45.8493
REMARK 3 T TENSOR
REMARK 3 T11: 0.2742 T22: 0.1746
REMARK 3 T33: 0.1511 T12: 0.0294
REMARK 3 T13: 0.0378 T23: 0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 4.6794 L22: 2.3586
REMARK 3 L33: 0.3022 L12: 2.7663
REMARK 3 L13: 0.8099 L23: 0.1701
REMARK 3 S TENSOR
REMARK 3 S11: -0.0651 S12: 0.1616 S13: 0.0466
REMARK 3 S21: -0.2404 S22: 0.1113 S23: 0.0166
REMARK 3 S31: 0.0205 S32: 0.0156 S33: -0.0481
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN E AND (RESSEQ 78:187)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.8038 -20.1390 53.2266
REMARK 3 T TENSOR
REMARK 3 T11: 0.1710 T22: 0.1285
REMARK 3 T33: 0.1526 T12: 0.0244
REMARK 3 T13: 0.0036 T23: -0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 1.6299 L22: 1.4720
REMARK 3 L33: 1.6933 L12: 0.4724
REMARK 3 L13: 0.5588 L23: -0.2184
REMARK 3 S TENSOR
REMARK 3 S11: -0.0051 S12: 0.1830 S13: -0.1233
REMARK 3 S21: -0.2479 S22: -0.0335 S23: -0.1066
REMARK 3 S31: 0.1512 S32: 0.0472 S33: 0.0484
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN E AND (RESSEQ 188:330)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.8734 -12.2511 58.8326
REMARK 3 T TENSOR
REMARK 3 T11: 0.0926 T22: 0.0938
REMARK 3 T33: 0.0979 T12: -0.0105
REMARK 3 T13: -0.0078 T23: -0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 1.7032 L22: 1.0209
REMARK 3 L33: 0.6442 L12: 0.0500
REMARK 3 L13: 0.1446 L23: -0.3372
REMARK 3 S TENSOR
REMARK 3 S11: -0.0310 S12: 0.0889 S13: 0.0535
REMARK 3 S21: -0.0653 S22: 0.0210 S23: -0.0864
REMARK 3 S31: 0.0131 S32: 0.0522 S33: 0.0080
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN E AND (RESSEQ 331:455)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0926 -37.1271 75.9523
REMARK 3 T TENSOR
REMARK 3 T11: 0.3510 T22: 0.1892
REMARK 3 T33: 0.2861 T12: -0.1214
REMARK 3 T13: -0.1951 T23: 0.1664
REMARK 3 L TENSOR
REMARK 3 L11: 0.9001 L22: 0.7929
REMARK 3 L33: 0.4484 L12: 0.3441
REMARK 3 L13: 0.1771 L23: -0.1429
REMARK 3 S TENSOR
REMARK 3 S11: 0.2662 S12: -0.5848 S13: -0.4677
REMARK 3 S21: 0.3186 S22: -0.1748 S23: -0.3586
REMARK 3 S31: 0.5216 S32: 0.0013 S33: -0.0378
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN F AND (RESSEQ 1:77)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.9469 31.0229 70.6091
REMARK 3 T TENSOR
REMARK 3 T11: 0.2133 T22: 0.1353
REMARK 3 T33: 0.1982 T12: 0.0506
REMARK 3 T13: 0.0465 T23: 0.0546
REMARK 3 L TENSOR
REMARK 3 L11: 1.7627 L22: 2.7199
REMARK 3 L33: 3.9304 L12: 0.6027
REMARK 3 L13: 1.4376 L23: 2.0347
REMARK 3 S TENSOR
REMARK 3 S11: -0.0328 S12: 0.0160 S13: -0.0134
REMARK 3 S21: 0.0549 S22: 0.0256 S23: 0.1580
REMARK 3 S31: 0.0130 S32: -0.0801 S33: 0.0069
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN F AND (RESSEQ 78:106)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.8851 24.6926 90.1758
REMARK 3 T TENSOR
REMARK 3 T11: 0.1757 T22: 0.2484
REMARK 3 T33: 0.2491 T12: 0.0577
REMARK 3 T13: -0.0525 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 1.2281 L22: 5.8706
REMARK 3 L33: 1.9329 L12: 0.1585
REMARK 3 L13: -1.3572 L23: 0.7700
REMARK 3 S TENSOR
REMARK 3 S11: 0.0435 S12: 0.2724 S13: -0.0573
REMARK 3 S21: -0.4102 S22: 0.0090 S23: 0.6206
REMARK 3 S31: -0.0419 S32: -0.4124 S33: -0.0643
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN F AND (RESSEQ 107:263)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.2386 17.1394 98.5215
REMARK 3 T TENSOR
REMARK 3 T11: 0.1234 T22: 0.1444
REMARK 3 T33: 0.1499 T12: 0.0060
REMARK 3 T13: 0.0169 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.2024 L22: 0.7007
REMARK 3 L33: 0.6992 L12: -0.0828
REMARK 3 L13: 0.1056 L23: 0.0976
REMARK 3 S TENSOR
REMARK 3 S11: -0.0101 S12: -0.0632 S13: 0.0265
REMARK 3 S21: 0.0135 S22: 0.0213 S23: 0.0493
REMARK 3 S31: 0.0024 S32: -0.1276 S33: -0.0121
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN F AND (RESSEQ 264:296)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1461 24.0331 92.1370
REMARK 3 T TENSOR
REMARK 3 T11: 0.1219 T22: 0.1049
REMARK 3 T33: 0.2081 T12: -0.0208
REMARK 3 T13: -0.0155 T23: -0.0383
REMARK 3 L TENSOR
REMARK 3 L11: 2.0002 L22: 2.0875
REMARK 3 L33: 3.8759 L12: 0.2057
REMARK 3 L13: -1.4087 L23: 0.0508
REMARK 3 S TENSOR
REMARK 3 S11: -0.1635 S12: 0.0073 S13: -0.1309
REMARK 3 S21: -0.1973 S22: 0.0816 S23: -0.2040
REMARK 3 S31: 0.0328 S32: 0.2179 S33: 0.0152
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN F AND (RESSEQ 297:364)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7933 9.9829 104.4706
REMARK 3 T TENSOR
REMARK 3 T11: 0.1169 T22: 0.1299
REMARK 3 T33: 0.1786 T12: -0.0171
REMARK 3 T13: -0.0191 T23: -0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 1.1923 L22: 0.8289
REMARK 3 L33: 1.9126 L12: -0.3432
REMARK 3 L13: -0.4259 L23: -0.9238
REMARK 3 S TENSOR
REMARK 3 S11: 0.0071 S12: -0.0209 S13: -0.0524
REMARK 3 S21: 0.0591 S22: -0.0039 S23: -0.0636
REMARK 3 S31: 0.0504 S32: 0.0278 S33: -0.0043
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN F AND (RESSEQ 365:455)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2535 -0.7931 119.7914
REMARK 3 T TENSOR
REMARK 3 T11: 0.2849 T22: 0.1897
REMARK 3 T33: 0.1833 T12: 0.0343
REMARK 3 T13: 0.0004 T23: 0.0879
REMARK 3 L TENSOR
REMARK 3 L11: 2.1538 L22: 1.3296
REMARK 3 L33: 2.5084 L12: -0.1922
REMARK 3 L13: 0.9058 L23: 0.3086
REMARK 3 S TENSOR
REMARK 3 S11: 0.0197 S12: -0.2233 S13: -0.3443
REMARK 3 S21: 0.3356 S22: 0.0522 S23: -0.1054
REMARK 3 S31: 0.4656 S32: 0.2085 S33: -0.0468
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN G AND (RESSEQ 6:89)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.2215 -32.2940 115.7607
REMARK 3 T TENSOR
REMARK 3 T11: 0.1623 T22: 0.2145
REMARK 3 T33: 0.1496 T12: 0.0001
REMARK 3 T13: -0.0265 T23: -0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 0.8786 L22: 3.4083
REMARK 3 L33: 2.6306 L12: -0.1889
REMARK 3 L13: 0.2120 L23: -2.1215
REMARK 3 S TENSOR
REMARK 3 S11: 0.0555 S12: -0.2206 S13: -0.0684
REMARK 3 S21: 0.1524 S22: -0.0691 S23: 0.0990
REMARK 3 S31: 0.0546 S32: 0.1673 S33: 0.0231
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN G AND (RESSEQ 90:206)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.5912 -20.0024 107.3950
REMARK 3 T TENSOR
REMARK 3 T11: 0.0350 T22: -0.0406
REMARK 3 T33: 0.0529 T12: -0.0573
REMARK 3 T13: -0.0844 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 0.3401 L22: 4.0791
REMARK 3 L33: 2.9932 L12: -0.5500
REMARK 3 L13: 0.2623 L23: -3.3091
REMARK 3 S TENSOR
REMARK 3 S11: 0.0182 S12: -0.3017 S13: 0.0834
REMARK 3 S21: -0.0166 S22: 0.1399 S23: 0.2266
REMARK 3 S31: 0.0451 S32: 0.0614 S33: -0.0535
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN H AND (RESSEQ 2:10)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.1621 -38.4723 134.6169
REMARK 3 T TENSOR
REMARK 3 T11: 0.4321 T22: 0.4750
REMARK 3 T33: 0.3993 T12: 0.1133
REMARK 3 T13: 0.1627 T23: 0.1397
REMARK 3 L TENSOR
REMARK 3 L11: 4.8843 L22: 4.6376
REMARK 3 L33: 5.2990 L12: 0.3869
REMARK 3 L13: 1.0491 L23: 1.3312
REMARK 3 S TENSOR
REMARK 3 S11: 0.3353 S12: -0.9256 S13: -0.0816
REMARK 3 S21: 0.1620 S22: -0.0924 S23: 0.1094
REMARK 3 S31: -0.7435 S32: -0.4260 S33: -0.2150
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN H AND (RESSEQ 11:20)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4375 -49.3926 137.1967
REMARK 3 T TENSOR
REMARK 3 T11: 0.3875 T22: 0.7288
REMARK 3 T33: 0.5382 T12: -0.0766
REMARK 3 T13: 0.0468 T23: 0.3131
REMARK 3 L TENSOR
REMARK 3 L11: 2.6412 L22: 2.1798
REMARK 3 L33: 2.4270 L12: 1.7091
REMARK 3 L13: 2.3308 L23: 2.1385
REMARK 3 S TENSOR
REMARK 3 S11: 0.5391 S12: -0.8740 S13: -0.4956
REMARK 3 S21: 0.7118 S22: -0.1407 S23: 0.7414
REMARK 3 S31: 0.6499 S32: -1.2864 S33: -0.6336
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN H AND (RESSEQ 21:29)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.1806 -43.0874 135.2277
REMARK 3 T TENSOR
REMARK 3 T11: 0.5246 T22: 0.7364
REMARK 3 T33: 0.6688 T12: -0.0194
REMARK 3 T13: 0.0952 T23: 0.1808
REMARK 3 L TENSOR
REMARK 3 L11: 5.6162 L22: 2.6332
REMARK 3 L33: 2.4962 L12: 0.5236
REMARK 3 L13: 0.8955 L23: 0.1084
REMARK 3 S TENSOR
REMARK 3 S11: 0.6214 S12: -0.2820 S13: 0.2504
REMARK 3 S21: 0.4303 S22: -0.3562 S23: 0.6411
REMARK 3 S31: 0.3295 S32: -0.9137 S33: -0.2983
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN H AND (RESSEQ 30:42)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6732 -35.1955 130.6311
REMARK 3 T TENSOR
REMARK 3 T11: 0.3819 T22: 0.7470
REMARK 3 T33: 0.8097 T12: 0.1947
REMARK 3 T13: 0.2725 T23: 0.1978
REMARK 3 L TENSOR
REMARK 3 L11: 1.8634 L22: 3.8030
REMARK 3 L33: 1.5488 L12: 2.6104
REMARK 3 L13: 1.1215 L23: 1.7058
REMARK 3 S TENSOR
REMARK 3 S11: 0.1620 S12: 0.1761 S13: 0.3158
REMARK 3 S21: 0.1146 S22: -0.1934 S23: 0.7385
REMARK 3 S31: -0.1911 S32: -0.7796 S33: 0.0794
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN H AND (RESSEQ 43:64)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2729 -38.4179 126.1476
REMARK 3 T TENSOR
REMARK 3 T11: 0.2414 T22: 0.4486
REMARK 3 T33: 0.4711 T12: 0.1059
REMARK 3 T13: 0.0680 T23: 0.1585
REMARK 3 L TENSOR
REMARK 3 L11: 4.3974 L22: 4.0974
REMARK 3 L33: 2.8368 L12: 0.2792
REMARK 3 L13: 0.9482 L23: -0.6267
REMARK 3 S TENSOR
REMARK 3 S11: 0.1399 S12: -0.1531 S13: 0.2288
REMARK 3 S21: -0.0121 S22: 0.0722 S23: 1.0823
REMARK 3 S31: -0.3461 S32: -0.9612 S33: -0.1183
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN H AND (RESSEQ 65:71)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.6524 -29.5410 124.4173
REMARK 3 T TENSOR
REMARK 3 T11: 0.4570 T22: 0.4119
REMARK 3 T33: 0.4378 T12: 0.1750
REMARK 3 T13: -0.0118 T23: 0.0705
REMARK 3 L TENSOR
REMARK 3 L11: 2.2758 L22: 0.3590
REMARK 3 L33: 0.8554 L12: 0.3090
REMARK 3 L13: -1.0910 L23: 0.1760
REMARK 3 S TENSOR
REMARK 3 S11: 0.1199 S12: -0.0399 S13: 0.6688
REMARK 3 S21: -0.3807 S22: 0.1544 S23: 0.0391
REMARK 3 S31: -0.2868 S32: 0.3189 S33: -0.0045
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN H AND (RESSEQ 72:84)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.1365 -48.0935 123.7805
REMARK 3 T TENSOR
REMARK 3 T11: 0.3422 T22: 0.4924
REMARK 3 T33: 0.5128 T12: -0.1101
REMARK 3 T13: -0.1345 T23: 0.2044
REMARK 3 L TENSOR
REMARK 3 L11: 2.5411 L22: 1.2384
REMARK 3 L33: 4.7155 L12: -1.3481
REMARK 3 L13: -0.0802 L23: -0.7536
REMARK 3 S TENSOR
REMARK 3 S11: 0.1760 S12: -0.3008 S13: -0.4825
REMARK 3 S21: 0.0093 S22: 0.1260 S23: 0.8975
REMARK 3 S31: 0.8182 S32: -1.0434 S33: -0.2629
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: CHAIN H AND (RESSEQ 85:97)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2013 -40.2619 110.6510
REMARK 3 T TENSOR
REMARK 3 T11: 0.4129 T22: 0.3635
REMARK 3 T33: 0.4056 T12: -0.0600
REMARK 3 T13: -0.2049 T23: 0.0807
REMARK 3 L TENSOR
REMARK 3 L11: 3.8176 L22: 6.6798
REMARK 3 L33: 5.3975 L12: 5.0495
REMARK 3 L13: -4.5397 L23: -6.0049
REMARK 3 S TENSOR
REMARK 3 S11: -0.1161 S12: 0.8855 S13: -0.0352
REMARK 3 S21: -1.0393 S22: 0.9257 S23: 0.9493
REMARK 3 S31: 0.9599 S32: -1.2692 S33: -0.6275
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: CHAIN H AND (RESSEQ 98:103)
REMARK 3 ORIGIN FOR THE GROUP (A): 37.1992 -40.4914 104.5676
REMARK 3 T TENSOR
REMARK 3 T11: 0.7302 T22: 0.4299
REMARK 3 T33: 0.5407 T12: -0.0315
REMARK 3 T13: -0.0177 T23: 0.1925
REMARK 3 L TENSOR
REMARK 3 L11: 1.1079 L22: 2.4767
REMARK 3 L33: 2.3640 L12: -0.6022
REMARK 3 L13: 0.7699 L23: 1.5641
REMARK 3 S TENSOR
REMARK 3 S11: 0.0692 S12: 0.9782 S13: 0.1412
REMARK 3 S21: -2.5407 S22: 0.1432 S23: 0.4243
REMARK 3 S31: 0.9049 S32: -0.0717 S33: -0.2498
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 3VR4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1000095396.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-DEC-09; 16-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY; PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A; AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97919; 1.0000
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111); DOUBLE
REMARK 200 CRYSTAL SI(111)
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R; ADSC QUANTUM
REMARK 200 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 195452
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.170
REMARK 200 RESOLUTION RANGE LOW (A) : 37.120
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.53500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT AND
REMARK 200 SAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3VR2, 3AON, 3A5C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 29.2% PEG3350, 0.1M NAF, 0.1M BIS-TRIS
REMARK 280 PROPANE, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 296K
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 63.99000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 112.96500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 64.24000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 112.96500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 63.99000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 64.24000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 37740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 117040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -148.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
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 -6
REMARK 465 SER A -5
REMARK 465 SER A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 SER A -1
REMARK 465 GLY A 588
REMARK 465 GLY A 589
REMARK 465 MSE A 590
REMARK 465 THR A 591
REMARK 465 ASP A 592
REMARK 465 ASP A 593
REMARK 465 GLU B 587
REMARK 465 GLY B 588
REMARK 465 GLY B 589
REMARK 465 MSE B 590
REMARK 465 THR B 591
REMARK 465 ASP B 592
REMARK 465 ASP B 593
REMARK 465 GLY C -6
REMARK 465 SER C -5
REMARK 465 SER C -4
REMARK 465 GLY C -3
REMARK 465 SER C -2
REMARK 465 SER C -1
REMARK 465 GLY C 0
REMARK 465 GLU C 587
REMARK 465 GLY C 588
REMARK 465 GLY C 589
REMARK 465 MSE C 590
REMARK 465 THR C 591
REMARK 465 ASP C 592
REMARK 465 ASP C 593
REMARK 465 GLY D -6
REMARK 465 SER D -5
REMARK 465 SER D -4
REMARK 465 GLY D -3
REMARK 465 SER D -2
REMARK 465 SER D -1
REMARK 465 GLY D 0
REMARK 465 MSE D 1
REMARK 465 ILE D 2
REMARK 465 LYS D 3
REMARK 465 GLU D 456
REMARK 465 GLY D 457
REMARK 465 LYS D 458
REMARK 465 GLY E -6
REMARK 465 SER E -5
REMARK 465 SER E -4
REMARK 465 GLY E -3
REMARK 465 SER E -2
REMARK 465 SER E -1
REMARK 465 GLY E 0
REMARK 465 MSE E 1
REMARK 465 ILE E 2
REMARK 465 LYS E 3
REMARK 465 GLU E 456
REMARK 465 GLY E 457
REMARK 465 LYS E 458
REMARK 465 GLY F -6
REMARK 465 SER F -5
REMARK 465 SER F -4
REMARK 465 GLY F -3
REMARK 465 SER F -2
REMARK 465 SER F -1
REMARK 465 GLY F 0
REMARK 465 GLU F 456
REMARK 465 GLY F 457
REMARK 465 LYS F 458
REMARK 465 GLY G -6
REMARK 465 SER G -5
REMARK 465 SER G -4
REMARK 465 GLY G -3
REMARK 465 SER G -2
REMARK 465 SER G -1
REMARK 465 GLY G 0
REMARK 465 MSE G 1
REMARK 465 ARG G 2
REMARK 465 LEU G 3
REMARK 465 ASN G 4
REMARK 465 VAL G 5
REMARK 465 THR G 71
REMARK 465 PRO G 84
REMARK 465 ALA G 85
REMARK 465 TYR G 109
REMARK 465 ASP G 110
REMARK 465 GLU G 111
REMARK 465 THR G 112
REMARK 465 LEU G 113
REMARK 465 ASN G 114
REMARK 465 GLU G 115
REMARK 465 THR G 116
REMARK 465 PRO G 117
REMARK 465 LEU G 118
REMARK 465 GLU G 119
REMARK 465 TYR G 120
REMARK 465 GLY G 121
REMARK 465 TYR G 122
REMARK 465 LEU G 123
REMARK 465 HIS G 124
REMARK 465 SER G 125
REMARK 465 GLY G 207
REMARK 465 THR G 208
REMARK 465 GLU G 209
REMARK 465 GLU G 210
REMARK 465 MSE H 1
REMARK 465 SER H 104
REMARK 465 GLY H 105
REMARK 465 PRO H 106
REMARK 465 SER H 107
REMARK 465 SER H 108
REMARK 465 GLY H 109
REMARK 465 GLU H 110
REMARK 465 ASN H 111
REMARK 465 LEU H 112
REMARK 465 TYR H 113
REMARK 465 PHE H 114
REMARK 465 GLN H 115
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 LYS A 5 CE NZ
REMARK 470 GLU A 96 CD OE1 OE2
REMARK 470 GLN A 108 CD OE1 NE2
REMARK 470 GLU A 125 CD OE1 OE2
REMARK 470 LYS A 156 CE NZ
REMARK 470 GLN A 160 CG CD OE1 NE2
REMARK 470 LYS A 161 CG CD CE NZ
REMARK 470 GLU A 179 CG CD OE1 OE2
REMARK 470 GLN A 180 CD OE1 NE2
REMARK 470 LYS A 200 CE NZ
REMARK 470 GLU A 275 CD OE1 OE2
REMARK 470 ARG A 423 NE CZ NH1 NH2
REMARK 470 ASP A 480 CG OD1 OD2
REMARK 470 ASP A 508 OD1 OD2
REMARK 470 GLU A 516 CD OE1 OE2
REMARK 470 LYS A 523 CE NZ
REMARK 470 LYS A 530 CD CE NZ
REMARK 470 LYS A 534 CD CE NZ
REMARK 470 ARG A 558 CD NE CZ NH1 NH2
REMARK 470 GLU A 575 CG CD OE1 OE2
REMARK 470 LYS A 578 CE NZ
REMARK 470 GLU A 579 CD OE1 OE2
REMARK 470 GLU A 587 CG CD OE1 OE2
REMARK 470 LYS B 5 NZ
REMARK 470 GLU B 96 CD OE1 OE2
REMARK 470 GLU B 129 CG CD OE1 OE2
REMARK 470 LYS B 143 CD CE NZ
REMARK 470 ILE B 144 CG1 CG2 CD1
REMARK 470 LYS B 156 CD CE NZ
REMARK 470 GLN B 160 CG CD OE1 NE2
REMARK 470 LYS B 161 CG CD CE NZ
REMARK 470 GLU B 163 CD OE1 OE2
REMARK 470 GLU B 179 CG CD OE1 OE2
REMARK 470 GLN B 180 CG CD OE1 NE2
REMARK 470 LYS B 183 CD CE NZ
REMARK 470 LYS B 247 NZ
REMARK 470 ASN B 280 CG OD1 ND2
REMARK 470 GLU B 472 CG CD OE1 OE2
REMARK 470 ARG B 475 CZ NH1 NH2
REMARK 470 LYS B 534 CG CD CE NZ
REMARK 470 TYR B 541 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN B 543 CG OD1 ND2
REMARK 470 GLU B 544 CD OE1 OE2
REMARK 470 GLU B 566 CD OE1 OE2
REMARK 470 LYS B 569 CE NZ
REMARK 470 GLU B 575 CG CD OE1 OE2
REMARK 470 LYS B 578 CE NZ
REMARK 470 GLN B 582 CG CD OE1 NE2
REMARK 470 LEU B 583 CG CD1 CD2
REMARK 470 GLU C 69 CD OE1 OE2
REMARK 470 GLU C 125 OE1 OE2
REMARK 470 LYS C 143 CE NZ
REMARK 470 LYS C 161 CD CE NZ
REMARK 470 GLU C 177 CD OE1 OE2
REMARK 470 GLU C 179 CG CD OE1 OE2
REMARK 470 GLN C 180 CG CD OE1 NE2
REMARK 470 LYS C 183 CD CE NZ
REMARK 470 ASN C 280 CG OD1 ND2
REMARK 470 LYS C 530 CD CE NZ
REMARK 470 LYS C 534 CD CE NZ
REMARK 470 GLU C 544 CG CD OE1 OE2
REMARK 470 LYS C 578 CE NZ
REMARK 470 GLU C 579 CG CD OE1 OE2
REMARK 470 GLN C 582 CD OE1 NE2
REMARK 470 LEU C 583 CG CD1 CD2
REMARK 470 ARG D 6 CD NE CZ NH1 NH2
REMARK 470 LYS D 9 CE NZ
REMARK 470 LYS D 20 CG CD CE NZ
REMARK 470 ARG D 33 CD NE CZ NH1 NH2
REMARK 470 ASN D 99 CG OD1 ND2
REMARK 470 GLU D 102 CG CD OE1 OE2
REMARK 470 LEU D 104 CG CD1 CD2
REMARK 470 ASP D 172 CG OD1 OD2
REMARK 470 ASP D 175 CG OD1 OD2
REMARK 470 ASP D 176 CG OD1 OD2
REMARK 470 GLN D 200 CG CD OE1 NE2
REMARK 470 ASP D 353 CG OD1 OD2
REMARK 470 LYS D 354 CG CD CE NZ
REMARK 470 LYS D 380 CE NZ
REMARK 470 GLN D 381 CD OE1 NE2
REMARK 470 LYS D 383 CD CE NZ
REMARK 470 GLU D 391 CG CD OE1 OE2
REMARK 470 LYS D 403 CD CE NZ
REMARK 470 LYS D 443 CG CD CE NZ
REMARK 470 LYS D 446 CG CD CE NZ
REMARK 470 ASP D 447 CG OD1 OD2
REMARK 470 LEU D 450 CG CD1 CD2
REMARK 470 ASP D 451 CG OD1 OD2
REMARK 470 LEU D 454 CG CD1 CD2
REMARK 470 LYS E 20 CD CE NZ
REMARK 470 GLU E 102 CG CD OE1 OE2
REMARK 470 LEU E 104 CG CD1 CD2
REMARK 470 ASP E 175 CG OD1 OD2
REMARK 470 GLN E 200 CD OE1 NE2
REMARK 470 LYS E 335 CG CD CE NZ
REMARK 470 GLU E 384 CD OE1 OE2
REMARK 470 LEU E 385 CG CD1 CD2
REMARK 470 GLU E 391 CG CD OE1 OE2
REMARK 470 ASP E 396 CG OD1 OD2
REMARK 470 ILE E 397 CG1 CG2 CD1
REMARK 470 LYS E 403 CD CE NZ
REMARK 470 LYS E 443 CE NZ
REMARK 470 ILE F 2 CG1 CG2 CD1
REMARK 470 LYS F 9 CD CE NZ
REMARK 470 LYS F 20 CE NZ
REMARK 470 LYS F 295 CD CE NZ
REMARK 470 LYS F 335 CD CE NZ
REMARK 470 LYS F 383 CE NZ
REMARK 470 VAL F 388 CG1 CG2
REMARK 470 GLU F 391 CG CD OE1 OE2
REMARK 470 ASP F 396 CG OD1 OD2
REMARK 470 LYS F 399 CD CE NZ
REMARK 470 LYS F 403 CD CE NZ
REMARK 470 LYS F 443 CE NZ
REMARK 470 LYS G 17 CG CD CE NZ
REMARK 470 LYS G 27 CG CD CE NZ
REMARK 470 LYS G 56 CG CD CE NZ
REMARK 470 LYS G 63 CG CD CE NZ
REMARK 470 LEU G 67 CG CD1 CD2
REMARK 470 LYS G 69 CD CE NZ
REMARK 470 GLU G 73 CG CD OE1 OE2
REMARK 470 GLU G 74 CG CD OE1 OE2
REMARK 470 PHE G 76 CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE G 77 CG1 CG2 CD1
REMARK 470 ASP G 78 CG OD1 OD2
REMARK 470 GLU G 79 CG CD OE1 OE2
REMARK 470 LEU G 80 CG CD1 CD2
REMARK 470 LEU G 83 CG CD1 CD2
REMARK 470 LYS G 101 CG CD CE NZ
REMARK 470 GLN G 108 CG CD OE1 NE2
REMARK 470 ASN G 126 CG OD1 ND2
REMARK 470 GLU G 128 CG CD OE1 OE2
REMARK 470 LEU G 129 CG CD1 CD2
REMARK 470 ARG G 131 CG CD NE CZ NH1 NH2
REMARK 470 ASP G 134 CG OD1 OD2
REMARK 470 GLU G 158 CD OE1 OE2
REMARK 470 GLU G 180 CG CD OE1 OE2
REMARK 470 LYS G 188 CG CD CE NZ
REMARK 470 GLU G 190 CG CD OE1 OE2
REMARK 470 GLU G 196 CD OE1 OE2
REMARK 470 LYS H 11 CD CE NZ
REMARK 470 ARG H 18 CG CD NE CZ NH1 NH2
REMARK 470 ARG H 34 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 35 CE NZ
REMARK 470 LYS H 42 CG CD CE NZ
REMARK 470 GLU H 60 CG CD OE1 OE2
REMARK 470 GLU H 63 CD OE1 OE2
REMARK 470 ARG H 64 CG CD NE CZ NH1 NH2
REMARK 470 GLN H 100 CG CD OE1 NE2
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 OH TYR D 253 OD1 ASN D 280 2.09
REMARK 500 OH TYR F 253 OD1 ASN F 280 2.12
REMARK 500 ND1 HIS B 243 O HOH B 738 2.14
REMARK 500 OE1 GLU C 336 O HOH C 1030 2.16
REMARK 500 OE2 GLU B 340 O HOH B 1023 2.16
REMARK 500 O SER A 398 O HOH A 983 2.17
REMARK 500 O GLY A 133 NH2 ARG A 380 2.19
REMARK 500 O HOH B 1019 O HOH B 1050 2.19
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 GLN A 44 -118.37 56.14
REMARK 500 ARG A 288 36.50 -140.92
REMARK 500 SER A 427 43.04 -77.69
REMARK 500 TYR A 500 -60.39 -122.71
REMARK 500 GLN B 25 1.21 81.23
REMARK 500 GLN B 44 -112.57 53.35
REMARK 500 GLU B 261 -163.34 -118.22
REMARK 500 ARG B 288 27.43 -141.29
REMARK 500 SER B 427 40.62 -84.78
REMARK 500 TYR B 500 -56.86 -128.36
REMARK 500 GLN C 44 -114.64 56.04
REMARK 500 GLU C 261 -162.41 -112.29
REMARK 500 SER C 427 47.01 -81.24
REMARK 500 VAL C 477 -37.31 -160.60
REMARK 500 TYR C 500 -56.08 -122.03
REMARK 500 ARG D 6 63.45 -103.94
REMARK 500 GLU D 46 142.25 -172.10
REMARK 500 ILE D 135 -64.09 -98.62
REMARK 500 SER D 151 -153.38 -123.13
REMARK 500 ASP D 172 -132.67 63.11
REMARK 500 SER D 173 -36.36 68.44
REMARK 500 SER D 174 -55.60 67.55
REMARK 500 GLU D 308 28.60 48.32
REMARK 500 LYS D 360 -60.37 -102.62
REMARK 500 THR D 361 -90.38 -119.88
REMARK 500 TYR D 412 -61.00 -91.45
REMARK 500 ARG E 6 46.56 -109.46
REMARK 500 GLU E 49 -103.72 53.30
REMARK 500 GLU E 126 158.01 80.00
REMARK 500 SER E 151 -153.03 -126.50
REMARK 500 PRO E 156 49.76 -83.73
REMARK 500 SER E 173 102.10 -165.71
REMARK 500 ASP E 176 26.82 -142.60
REMARK 500 GLU E 324 55.96 -110.49
REMARK 500 THR E 361 -92.09 -121.36
REMARK 500 TYR E 412 -65.07 -90.44
REMARK 500 ARG F 6 41.39 -107.59
REMARK 500 GLU F 49 -116.88 52.52
REMARK 500 SER F 151 -149.14 -136.24
REMARK 500 PRO F 156 49.56 -84.15
REMARK 500 GLU F 324 56.71 -99.70
REMARK 500 LYS F 360 -57.52 -126.71
REMARK 500 THR F 361 -92.91 -118.95
REMARK 500 TYR F 412 -61.26 -94.43
REMARK 500 ALA G 82 -68.83 -104.40
REMARK 500 MSE G 98 -103.35 56.81
REMARK 500 ALA G 127 -57.22 -126.90
REMARK 500 MSE G 173 -67.30 -125.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B3P F 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B3P F 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VR2 RELATED DB: PDB
REMARK 900 RELATED ID: 3VR3 RELATED DB: PDB
REMARK 900 RELATED ID: 3VR5 RELATED DB: PDB
REMARK 900 RELATED ID: 3VR6 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CURRENTLY THE SEQUENCE OF CHAIN G HAS NOT BEEN SUBMITTED TO THE
REMARK 999 SEQUENCE DATABASE. RESIDUES (-6)-0 IN CHAIN G ARE EXPRESSION TAGS.
DBREF 3VR4 A 1 593 UNP Q08636 NTPA_ENTHR 1 593
DBREF 3VR4 B 1 593 UNP Q08636 NTPA_ENTHR 1 593
DBREF 3VR4 C 1 593 UNP Q08636 NTPA_ENTHR 1 593
DBREF 3VR4 D 1 458 UNP Q08637 NTPB_ENTHR 1 458
DBREF 3VR4 E 1 458 UNP Q08637 NTPB_ENTHR 1 458
DBREF 3VR4 F 1 458 UNP Q08637 NTPB_ENTHR 1 458
DBREF 3VR4 G -6 210 PDB 3VR4 3VR4 -6 210
DBREF 3VR4 H 1 103 UNP P43455 NTPG_ENTHR 1 103
SEQADV 3VR4 GLY A -6 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 SER A -5 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 SER A -4 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 GLY A -3 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 SER A -2 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 SER A -1 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 GLY A 0 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 GLY B -6 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 SER B -5 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 SER B -4 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 GLY B -3 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 SER B -2 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 SER B -1 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 GLY B 0 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 GLY C -6 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 SER C -5 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 SER C -4 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 GLY C -3 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 SER C -2 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 SER C -1 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 GLY C 0 UNP Q08636 EXPRESSION TAG
SEQADV 3VR4 GLY D -6 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 SER D -5 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 SER D -4 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 GLY D -3 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 SER D -2 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 SER D -1 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 GLY D 0 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 GLY E -6 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 SER E -5 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 SER E -4 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 GLY E -3 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 SER E -2 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 SER E -1 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 GLY E 0 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 GLY F -6 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 SER F -5 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 SER F -4 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 GLY F -3 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 SER F -2 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 SER F -1 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 GLY F 0 UNP Q08637 EXPRESSION TAG
SEQADV 3VR4 SER H 104 UNP P43455 EXPRESSION TAG
SEQADV 3VR4 GLY H 105 UNP P43455 EXPRESSION TAG
SEQADV 3VR4 PRO H 106 UNP P43455 EXPRESSION TAG
SEQADV 3VR4 SER H 107 UNP P43455 EXPRESSION TAG
SEQADV 3VR4 SER H 108 UNP P43455 EXPRESSION TAG
SEQADV 3VR4 GLY H 109 UNP P43455 EXPRESSION TAG
SEQADV 3VR4 GLU H 110 UNP P43455 EXPRESSION TAG
SEQADV 3VR4 ASN H 111 UNP P43455 EXPRESSION TAG
SEQADV 3VR4 LEU H 112 UNP P43455 EXPRESSION TAG
SEQADV 3VR4 TYR H 113 UNP P43455 EXPRESSION TAG
SEQADV 3VR4 PHE H 114 UNP P43455 EXPRESSION TAG
SEQADV 3VR4 GLN H 115 UNP P43455 EXPRESSION TAG
SEQRES 1 A 600 GLY SER SER GLY SER SER GLY MSE GLN ILE GLY LYS ILE
SEQRES 2 A 600 ILE LYS VAL SER GLY PRO LEU VAL MSE ALA GLU ASN MSE
SEQRES 3 A 600 SER GLU ALA SER ILE GLN ASP MSE CYS LEU VAL GLY ASP
SEQRES 4 A 600 LEU GLY VAL ILE GLY GLU ILE ILE GLU MSE ARG GLN ASP
SEQRES 5 A 600 VAL ALA SER ILE GLN VAL TYR GLU GLU THR SER GLY ILE
SEQRES 6 A 600 GLY PRO GLY GLU PRO VAL ARG SER THR GLY GLU ALA LEU
SEQRES 7 A 600 SER VAL GLU LEU GLY PRO GLY ILE ILE SER GLN MSE PHE
SEQRES 8 A 600 ASP GLY ILE GLN ARG PRO LEU ASP THR PHE MSE GLU VAL
SEQRES 9 A 600 THR GLN SER ASN PHE LEU GLY ARG GLY VAL GLN LEU PRO
SEQRES 10 A 600 ALA LEU ASP HIS GLU LYS GLN TRP TRP PHE GLU ALA THR
SEQRES 11 A 600 ILE GLU GLU GLY THR GLU VAL SER ALA GLY ASP ILE ILE
SEQRES 12 A 600 GLY TYR VAL ASP GLU THR LYS ILE ILE GLN HIS LYS ILE
SEQRES 13 A 600 MSE VAL PRO ASN GLY ILE LYS GLY THR VAL GLN LYS ILE
SEQRES 14 A 600 GLU SER GLY SER PHE THR ILE ASP ASP PRO ILE CYS VAL
SEQRES 15 A 600 ILE GLU THR GLU GLN GLY LEU LYS GLU LEU THR MSE MSE
SEQRES 16 A 600 GLN LYS TRP PRO VAL ARG ARG GLY ARG PRO ILE LYS GLN
SEQRES 17 A 600 LYS LEU ASN PRO ASP VAL PRO MSE ILE THR GLY GLN ARG
SEQRES 18 A 600 VAL ILE ASP THR PHE PHE PRO VAL THR LYS GLY GLY ALA
SEQRES 19 A 600 ALA ALA VAL PRO GLY PRO PHE GLY ALA GLY LYS THR VAL
SEQRES 20 A 600 VAL GLN HIS GLN ILE ALA LYS TRP SER ASP VAL ASP LEU
SEQRES 21 A 600 VAL VAL TYR VAL GLY CYS GLY GLU ARG GLY ASN GLU MSE
SEQRES 22 A 600 THR ASP VAL VAL ASN GLU PHE PRO GLU LEU ILE ASP PRO
SEQRES 23 A 600 ASN THR GLY GLU SER LEU MSE GLU ARG THR VAL LEU ILE
SEQRES 24 A 600 ALA ASN THR SER ASN MSE PRO VAL ALA ALA ARG GLU ALA
SEQRES 25 A 600 SER ILE TYR THR GLY ILE THR ILE ALA GLU TYR PHE ARG
SEQRES 26 A 600 ASP MSE GLY TYR ASP VAL ALA ILE MSE ALA ASP SER THR
SEQRES 27 A 600 SER ARG TRP ALA GLU ALA LEU ARG GLU MSE SER GLY ARG
SEQRES 28 A 600 LEU GLU GLU MSE PRO GLY ASP GLU GLY TYR PRO ALA TYR
SEQRES 29 A 600 LEU GLY SER ARG LEU ALA GLU TYR TYR GLU ARG SER GLY
SEQRES 30 A 600 ARG VAL ILE ALA LEU GLY SER ASP GLN ARG GLU GLY SER
SEQRES 31 A 600 ILE THR ALA ILE SER ALA VAL SER PRO SER GLY GLY ASP
SEQRES 32 A 600 ILE SER GLU PRO VAL THR GLN ASN THR LEU ARG VAL VAL
SEQRES 33 A 600 LYS VAL PHE TRP GLY LEU ASP SER SER LEU ALA GLN LYS
SEQRES 34 A 600 ARG HIS PHE PRO SER ILE ASN TRP ILE GLN SER TYR SER
SEQRES 35 A 600 LEU TYR SER THR GLU VAL GLY ARG TYR MSE ASP GLN ILE
SEQRES 36 A 600 LEU GLN GLN ASP TRP SER ASP MSE VAL THR GLU GLY MSE
SEQRES 37 A 600 ARG ILE LEU GLN GLU GLU GLU GLN LEU ASN GLU ILE VAL
SEQRES 38 A 600 ARG LEU VAL GLY ILE ASP SER LEU SER ASP ASN ASP ARG
SEQRES 39 A 600 LEU THR LEU GLU VAL ALA LYS SER ILE ARG GLU ASP TYR
SEQRES 40 A 600 LEU GLN GLN ASN ALA PHE ASP ASP VAL ASP THR PHE THR
SEQRES 41 A 600 SER ARG GLU LYS GLN PHE ASN MSE LEU LYS VAL ILE LEU
SEQRES 42 A 600 THR PHE GLY LYS GLU ALA ARG LYS ALA LEU SER LEU GLY
SEQRES 43 A 600 ALA TYR PHE ASN GLU ILE MSE GLU GLY THR VAL ALA VAL
SEQRES 44 A 600 ARG GLU ARG ILE SER ARG SER LYS TYR ILE PRO GLU GLU
SEQRES 45 A 600 GLU LEU ALA LYS ILE SER SER ILE ASN GLU GLU ILE LYS
SEQRES 46 A 600 GLU THR ILE GLN LEU ILE VAL SER GLU GLY GLY MSE THR
SEQRES 47 A 600 ASP ASP
SEQRES 1 B 600 GLY SER SER GLY SER SER GLY MSE GLN ILE GLY LYS ILE
SEQRES 2 B 600 ILE LYS VAL SER GLY PRO LEU VAL MSE ALA GLU ASN MSE
SEQRES 3 B 600 SER GLU ALA SER ILE GLN ASP MSE CYS LEU VAL GLY ASP
SEQRES 4 B 600 LEU GLY VAL ILE GLY GLU ILE ILE GLU MSE ARG GLN ASP
SEQRES 5 B 600 VAL ALA SER ILE GLN VAL TYR GLU GLU THR SER GLY ILE
SEQRES 6 B 600 GLY PRO GLY GLU PRO VAL ARG SER THR GLY GLU ALA LEU
SEQRES 7 B 600 SER VAL GLU LEU GLY PRO GLY ILE ILE SER GLN MSE PHE
SEQRES 8 B 600 ASP GLY ILE GLN ARG PRO LEU ASP THR PHE MSE GLU VAL
SEQRES 9 B 600 THR GLN SER ASN PHE LEU GLY ARG GLY VAL GLN LEU PRO
SEQRES 10 B 600 ALA LEU ASP HIS GLU LYS GLN TRP TRP PHE GLU ALA THR
SEQRES 11 B 600 ILE GLU GLU GLY THR GLU VAL SER ALA GLY ASP ILE ILE
SEQRES 12 B 600 GLY TYR VAL ASP GLU THR LYS ILE ILE GLN HIS LYS ILE
SEQRES 13 B 600 MSE VAL PRO ASN GLY ILE LYS GLY THR VAL GLN LYS ILE
SEQRES 14 B 600 GLU SER GLY SER PHE THR ILE ASP ASP PRO ILE CYS VAL
SEQRES 15 B 600 ILE GLU THR GLU GLN GLY LEU LYS GLU LEU THR MSE MSE
SEQRES 16 B 600 GLN LYS TRP PRO VAL ARG ARG GLY ARG PRO ILE LYS GLN
SEQRES 17 B 600 LYS LEU ASN PRO ASP VAL PRO MSE ILE THR GLY GLN ARG
SEQRES 18 B 600 VAL ILE ASP THR PHE PHE PRO VAL THR LYS GLY GLY ALA
SEQRES 19 B 600 ALA ALA VAL PRO GLY PRO PHE GLY ALA GLY LYS THR VAL
SEQRES 20 B 600 VAL GLN HIS GLN ILE ALA LYS TRP SER ASP VAL ASP LEU
SEQRES 21 B 600 VAL VAL TYR VAL GLY CYS GLY GLU ARG GLY ASN GLU MSE
SEQRES 22 B 600 THR ASP VAL VAL ASN GLU PHE PRO GLU LEU ILE ASP PRO
SEQRES 23 B 600 ASN THR GLY GLU SER LEU MSE GLU ARG THR VAL LEU ILE
SEQRES 24 B 600 ALA ASN THR SER ASN MSE PRO VAL ALA ALA ARG GLU ALA
SEQRES 25 B 600 SER ILE TYR THR GLY ILE THR ILE ALA GLU TYR PHE ARG
SEQRES 26 B 600 ASP MSE GLY TYR ASP VAL ALA ILE MSE ALA ASP SER THR
SEQRES 27 B 600 SER ARG TRP ALA GLU ALA LEU ARG GLU MSE SER GLY ARG
SEQRES 28 B 600 LEU GLU GLU MSE PRO GLY ASP GLU GLY TYR PRO ALA TYR
SEQRES 29 B 600 LEU GLY SER ARG LEU ALA GLU TYR TYR GLU ARG SER GLY
SEQRES 30 B 600 ARG VAL ILE ALA LEU GLY SER ASP GLN ARG GLU GLY SER
SEQRES 31 B 600 ILE THR ALA ILE SER ALA VAL SER PRO SER GLY GLY ASP
SEQRES 32 B 600 ILE SER GLU PRO VAL THR GLN ASN THR LEU ARG VAL VAL
SEQRES 33 B 600 LYS VAL PHE TRP GLY LEU ASP SER SER LEU ALA GLN LYS
SEQRES 34 B 600 ARG HIS PHE PRO SER ILE ASN TRP ILE GLN SER TYR SER
SEQRES 35 B 600 LEU TYR SER THR GLU VAL GLY ARG TYR MSE ASP GLN ILE
SEQRES 36 B 600 LEU GLN GLN ASP TRP SER ASP MSE VAL THR GLU GLY MSE
SEQRES 37 B 600 ARG ILE LEU GLN GLU GLU GLU GLN LEU ASN GLU ILE VAL
SEQRES 38 B 600 ARG LEU VAL GLY ILE ASP SER LEU SER ASP ASN ASP ARG
SEQRES 39 B 600 LEU THR LEU GLU VAL ALA LYS SER ILE ARG GLU ASP TYR
SEQRES 40 B 600 LEU GLN GLN ASN ALA PHE ASP ASP VAL ASP THR PHE THR
SEQRES 41 B 600 SER ARG GLU LYS GLN PHE ASN MSE LEU LYS VAL ILE LEU
SEQRES 42 B 600 THR PHE GLY LYS GLU ALA ARG LYS ALA LEU SER LEU GLY
SEQRES 43 B 600 ALA TYR PHE ASN GLU ILE MSE GLU GLY THR VAL ALA VAL
SEQRES 44 B 600 ARG GLU ARG ILE SER ARG SER LYS TYR ILE PRO GLU GLU
SEQRES 45 B 600 GLU LEU ALA LYS ILE SER SER ILE ASN GLU GLU ILE LYS
SEQRES 46 B 600 GLU THR ILE GLN LEU ILE VAL SER GLU GLY GLY MSE THR
SEQRES 47 B 600 ASP ASP
SEQRES 1 C 600 GLY SER SER GLY SER SER GLY MSE GLN ILE GLY LYS ILE
SEQRES 2 C 600 ILE LYS VAL SER GLY PRO LEU VAL MSE ALA GLU ASN MSE
SEQRES 3 C 600 SER GLU ALA SER ILE GLN ASP MSE CYS LEU VAL GLY ASP
SEQRES 4 C 600 LEU GLY VAL ILE GLY GLU ILE ILE GLU MSE ARG GLN ASP
SEQRES 5 C 600 VAL ALA SER ILE GLN VAL TYR GLU GLU THR SER GLY ILE
SEQRES 6 C 600 GLY PRO GLY GLU PRO VAL ARG SER THR GLY GLU ALA LEU
SEQRES 7 C 600 SER VAL GLU LEU GLY PRO GLY ILE ILE SER GLN MSE PHE
SEQRES 8 C 600 ASP GLY ILE GLN ARG PRO LEU ASP THR PHE MSE GLU VAL
SEQRES 9 C 600 THR GLN SER ASN PHE LEU GLY ARG GLY VAL GLN LEU PRO
SEQRES 10 C 600 ALA LEU ASP HIS GLU LYS GLN TRP TRP PHE GLU ALA THR
SEQRES 11 C 600 ILE GLU GLU GLY THR GLU VAL SER ALA GLY ASP ILE ILE
SEQRES 12 C 600 GLY TYR VAL ASP GLU THR LYS ILE ILE GLN HIS LYS ILE
SEQRES 13 C 600 MSE VAL PRO ASN GLY ILE LYS GLY THR VAL GLN LYS ILE
SEQRES 14 C 600 GLU SER GLY SER PHE THR ILE ASP ASP PRO ILE CYS VAL
SEQRES 15 C 600 ILE GLU THR GLU GLN GLY LEU LYS GLU LEU THR MSE MSE
SEQRES 16 C 600 GLN LYS TRP PRO VAL ARG ARG GLY ARG PRO ILE LYS GLN
SEQRES 17 C 600 LYS LEU ASN PRO ASP VAL PRO MSE ILE THR GLY GLN ARG
SEQRES 18 C 600 VAL ILE ASP THR PHE PHE PRO VAL THR LYS GLY GLY ALA
SEQRES 19 C 600 ALA ALA VAL PRO GLY PRO PHE GLY ALA GLY LYS THR VAL
SEQRES 20 C 600 VAL GLN HIS GLN ILE ALA LYS TRP SER ASP VAL ASP LEU
SEQRES 21 C 600 VAL VAL TYR VAL GLY CYS GLY GLU ARG GLY ASN GLU MSE
SEQRES 22 C 600 THR ASP VAL VAL ASN GLU PHE PRO GLU LEU ILE ASP PRO
SEQRES 23 C 600 ASN THR GLY GLU SER LEU MSE GLU ARG THR VAL LEU ILE
SEQRES 24 C 600 ALA ASN THR SER ASN MSE PRO VAL ALA ALA ARG GLU ALA
SEQRES 25 C 600 SER ILE TYR THR GLY ILE THR ILE ALA GLU TYR PHE ARG
SEQRES 26 C 600 ASP MSE GLY TYR ASP VAL ALA ILE MSE ALA ASP SER THR
SEQRES 27 C 600 SER ARG TRP ALA GLU ALA LEU ARG GLU MSE SER GLY ARG
SEQRES 28 C 600 LEU GLU GLU MSE PRO GLY ASP GLU GLY TYR PRO ALA TYR
SEQRES 29 C 600 LEU GLY SER ARG LEU ALA GLU TYR TYR GLU ARG SER GLY
SEQRES 30 C 600 ARG VAL ILE ALA LEU GLY SER ASP GLN ARG GLU GLY SER
SEQRES 31 C 600 ILE THR ALA ILE SER ALA VAL SER PRO SER GLY GLY ASP
SEQRES 32 C 600 ILE SER GLU PRO VAL THR GLN ASN THR LEU ARG VAL VAL
SEQRES 33 C 600 LYS VAL PHE TRP GLY LEU ASP SER SER LEU ALA GLN LYS
SEQRES 34 C 600 ARG HIS PHE PRO SER ILE ASN TRP ILE GLN SER TYR SER
SEQRES 35 C 600 LEU TYR SER THR GLU VAL GLY ARG TYR MSE ASP GLN ILE
SEQRES 36 C 600 LEU GLN GLN ASP TRP SER ASP MSE VAL THR GLU GLY MSE
SEQRES 37 C 600 ARG ILE LEU GLN GLU GLU GLU GLN LEU ASN GLU ILE VAL
SEQRES 38 C 600 ARG LEU VAL GLY ILE ASP SER LEU SER ASP ASN ASP ARG
SEQRES 39 C 600 LEU THR LEU GLU VAL ALA LYS SER ILE ARG GLU ASP TYR
SEQRES 40 C 600 LEU GLN GLN ASN ALA PHE ASP ASP VAL ASP THR PHE THR
SEQRES 41 C 600 SER ARG GLU LYS GLN PHE ASN MSE LEU LYS VAL ILE LEU
SEQRES 42 C 600 THR PHE GLY LYS GLU ALA ARG LYS ALA LEU SER LEU GLY
SEQRES 43 C 600 ALA TYR PHE ASN GLU ILE MSE GLU GLY THR VAL ALA VAL
SEQRES 44 C 600 ARG GLU ARG ILE SER ARG SER LYS TYR ILE PRO GLU GLU
SEQRES 45 C 600 GLU LEU ALA LYS ILE SER SER ILE ASN GLU GLU ILE LYS
SEQRES 46 C 600 GLU THR ILE GLN LEU ILE VAL SER GLU GLY GLY MSE THR
SEQRES 47 C 600 ASP ASP
SEQRES 1 D 465 GLY SER SER GLY SER SER GLY MSE ILE LYS GLU TYR ARG
SEQRES 2 D 465 THR ILE LYS GLU VAL VAL GLY PRO LEU MSE ALA VAL GLU
SEQRES 3 D 465 LYS VAL SER GLY VAL LYS TYR GLU GLU LEU ILE GLU VAL
SEQRES 4 D 465 ARG MSE GLN ASN GLY GLU ILE ARG ARG GLY GLN VAL LEU
SEQRES 5 D 465 GLU VAL GLN GLU ASP LYS ALA MSE VAL GLN ILE PHE GLU
SEQRES 6 D 465 GLY THR SER GLY ILE ASN LEU LYS ASN SER SER VAL ARG
SEQRES 7 D 465 PHE LEU GLY HIS PRO LEU GLN LEU GLY VAL SER GLU ASP
SEQRES 8 D 465 MSE ILE GLY ARG VAL PHE ASP GLY LEU GLY ARG PRO LYS
SEQRES 9 D 465 ASP ASN GLY PRO GLU ILE LEU PRO GLU LYS TYR LEU ASP
SEQRES 10 D 465 ILE ASN GLY GLU VAL ILE ASN PRO ILE ALA ARG ASP TYR
SEQRES 11 D 465 PRO ASP GLU PHE ILE GLN THR GLY ILE SER ALA ILE ASP
SEQRES 12 D 465 HIS LEU ASN THR LEU VAL ARG GLY GLN LYS LEU PRO VAL
SEQRES 13 D 465 PHE SER GLY SER GLY LEU PRO HIS LYS GLU LEU ALA ALA
SEQRES 14 D 465 GLN ILE ALA ARG GLN ALA THR VAL LEU ASP SER SER ASP
SEQRES 15 D 465 ASP PHE ALA VAL VAL PHE ALA ALA ILE GLY ILE THR PHE
SEQRES 16 D 465 GLU GLU ALA GLU PHE PHE MSE GLU ASP PHE ARG GLN THR
SEQRES 17 D 465 GLY ALA ILE ASP ARG SER VAL MSE PHE MSE ASN LEU ALA
SEQRES 18 D 465 ASN ASP PRO ALA ILE GLU ARG ILE ALA THR PRO ARG MSE
SEQRES 19 D 465 ALA LEU THR ALA ALA GLU TYR LEU ALA TYR GLU LYS GLY
SEQRES 20 D 465 MSE HIS VAL LEU VAL ILE MSE THR ASP MSE THR ASN TYR
SEQRES 21 D 465 ALA GLU ALA LEU ARG GLU ILE SER ALA ALA ARG ARG GLU
SEQRES 22 D 465 VAL PRO GLY ARG ARG GLY TYR PRO GLY TYR LEU TYR THR
SEQRES 23 D 465 ASN LEU ALA THR LEU PHE GLU ARG ALA GLY ARG ILE ARG
SEQRES 24 D 465 GLY LEU LYS GLY SER VAL THR GLN ILE PRO ILE LEU THR
SEQRES 25 D 465 MSE PRO GLU ASP ASP LYS THR HIS PRO ILE PRO ASP LEU
SEQRES 26 D 465 THR GLY TYR ILE THR GLU GLY GLN ILE ILE LEU THR ARG
SEQRES 27 D 465 GLU LEU TYR LYS SER GLY ILE GLN PRO PRO ILE ASP VAL
SEQRES 28 D 465 LEU PRO SER LEU SER ARG LEU LYS ASP LYS GLY THR GLY
SEQRES 29 D 465 ALA GLY LYS THR ARG GLU ASP HIS ALA ALA THR MSE ASN
SEQRES 30 D 465 GLN LEU PHE ALA ALA TYR ALA GLN GLY LYS GLN ALA LYS
SEQRES 31 D 465 GLU LEU ALA VAL VAL LEU GLY GLU SER ALA LEU SER ASP
SEQRES 32 D 465 ILE ASP LYS ILE TYR ALA LYS PHE ALA GLU ARG PHE GLU
SEQRES 33 D 465 ASN GLU TYR VAL ASN GLN GLY PHE TYR THR ASN ARG THR
SEQRES 34 D 465 ILE THR GLU THR LEU ASP LEU GLY TRP GLU LEU LEU ALA
SEQRES 35 D 465 MSE LEU PRO ARG THR GLU LEU LYS ARG ILE LYS ASP ASP
SEQRES 36 D 465 LEU LEU ASP LYS TYR LEU PRO GLU GLY LYS
SEQRES 1 E 465 GLY SER SER GLY SER SER GLY MSE ILE LYS GLU TYR ARG
SEQRES 2 E 465 THR ILE LYS GLU VAL VAL GLY PRO LEU MSE ALA VAL GLU
SEQRES 3 E 465 LYS VAL SER GLY VAL LYS TYR GLU GLU LEU ILE GLU VAL
SEQRES 4 E 465 ARG MSE GLN ASN GLY GLU ILE ARG ARG GLY GLN VAL LEU
SEQRES 5 E 465 GLU VAL GLN GLU ASP LYS ALA MSE VAL GLN ILE PHE GLU
SEQRES 6 E 465 GLY THR SER GLY ILE ASN LEU LYS ASN SER SER VAL ARG
SEQRES 7 E 465 PHE LEU GLY HIS PRO LEU GLN LEU GLY VAL SER GLU ASP
SEQRES 8 E 465 MSE ILE GLY ARG VAL PHE ASP GLY LEU GLY ARG PRO LYS
SEQRES 9 E 465 ASP ASN GLY PRO GLU ILE LEU PRO GLU LYS TYR LEU ASP
SEQRES 10 E 465 ILE ASN GLY GLU VAL ILE ASN PRO ILE ALA ARG ASP TYR
SEQRES 11 E 465 PRO ASP GLU PHE ILE GLN THR GLY ILE SER ALA ILE ASP
SEQRES 12 E 465 HIS LEU ASN THR LEU VAL ARG GLY GLN LYS LEU PRO VAL
SEQRES 13 E 465 PHE SER GLY SER GLY LEU PRO HIS LYS GLU LEU ALA ALA
SEQRES 14 E 465 GLN ILE ALA ARG GLN ALA THR VAL LEU ASP SER SER ASP
SEQRES 15 E 465 ASP PHE ALA VAL VAL PHE ALA ALA ILE GLY ILE THR PHE
SEQRES 16 E 465 GLU GLU ALA GLU PHE PHE MSE GLU ASP PHE ARG GLN THR
SEQRES 17 E 465 GLY ALA ILE ASP ARG SER VAL MSE PHE MSE ASN LEU ALA
SEQRES 18 E 465 ASN ASP PRO ALA ILE GLU ARG ILE ALA THR PRO ARG MSE
SEQRES 19 E 465 ALA LEU THR ALA ALA GLU TYR LEU ALA TYR GLU LYS GLY
SEQRES 20 E 465 MSE HIS VAL LEU VAL ILE MSE THR ASP MSE THR ASN TYR
SEQRES 21 E 465 ALA GLU ALA LEU ARG GLU ILE SER ALA ALA ARG ARG GLU
SEQRES 22 E 465 VAL PRO GLY ARG ARG GLY TYR PRO GLY TYR LEU TYR THR
SEQRES 23 E 465 ASN LEU ALA THR LEU PHE GLU ARG ALA GLY ARG ILE ARG
SEQRES 24 E 465 GLY LEU LYS GLY SER VAL THR GLN ILE PRO ILE LEU THR
SEQRES 25 E 465 MSE PRO GLU ASP ASP LYS THR HIS PRO ILE PRO ASP LEU
SEQRES 26 E 465 THR GLY TYR ILE THR GLU GLY GLN ILE ILE LEU THR ARG
SEQRES 27 E 465 GLU LEU TYR LYS SER GLY ILE GLN PRO PRO ILE ASP VAL
SEQRES 28 E 465 LEU PRO SER LEU SER ARG LEU LYS ASP LYS GLY THR GLY
SEQRES 29 E 465 ALA GLY LYS THR ARG GLU ASP HIS ALA ALA THR MSE ASN
SEQRES 30 E 465 GLN LEU PHE ALA ALA TYR ALA GLN GLY LYS GLN ALA LYS
SEQRES 31 E 465 GLU LEU ALA VAL VAL LEU GLY GLU SER ALA LEU SER ASP
SEQRES 32 E 465 ILE ASP LYS ILE TYR ALA LYS PHE ALA GLU ARG PHE GLU
SEQRES 33 E 465 ASN GLU TYR VAL ASN GLN GLY PHE TYR THR ASN ARG THR
SEQRES 34 E 465 ILE THR GLU THR LEU ASP LEU GLY TRP GLU LEU LEU ALA
SEQRES 35 E 465 MSE LEU PRO ARG THR GLU LEU LYS ARG ILE LYS ASP ASP
SEQRES 36 E 465 LEU LEU ASP LYS TYR LEU PRO GLU GLY LYS
SEQRES 1 F 465 GLY SER SER GLY SER SER GLY MSE ILE LYS GLU TYR ARG
SEQRES 2 F 465 THR ILE LYS GLU VAL VAL GLY PRO LEU MSE ALA VAL GLU
SEQRES 3 F 465 LYS VAL SER GLY VAL LYS TYR GLU GLU LEU ILE GLU VAL
SEQRES 4 F 465 ARG MSE GLN ASN GLY GLU ILE ARG ARG GLY GLN VAL LEU
SEQRES 5 F 465 GLU VAL GLN GLU ASP LYS ALA MSE VAL GLN ILE PHE GLU
SEQRES 6 F 465 GLY THR SER GLY ILE ASN LEU LYS ASN SER SER VAL ARG
SEQRES 7 F 465 PHE LEU GLY HIS PRO LEU GLN LEU GLY VAL SER GLU ASP
SEQRES 8 F 465 MSE ILE GLY ARG VAL PHE ASP GLY LEU GLY ARG PRO LYS
SEQRES 9 F 465 ASP ASN GLY PRO GLU ILE LEU PRO GLU LYS TYR LEU ASP
SEQRES 10 F 465 ILE ASN GLY GLU VAL ILE ASN PRO ILE ALA ARG ASP TYR
SEQRES 11 F 465 PRO ASP GLU PHE ILE GLN THR GLY ILE SER ALA ILE ASP
SEQRES 12 F 465 HIS LEU ASN THR LEU VAL ARG GLY GLN LYS LEU PRO VAL
SEQRES 13 F 465 PHE SER GLY SER GLY LEU PRO HIS LYS GLU LEU ALA ALA
SEQRES 14 F 465 GLN ILE ALA ARG GLN ALA THR VAL LEU ASP SER SER ASP
SEQRES 15 F 465 ASP PHE ALA VAL VAL PHE ALA ALA ILE GLY ILE THR PHE
SEQRES 16 F 465 GLU GLU ALA GLU PHE PHE MSE GLU ASP PHE ARG GLN THR
SEQRES 17 F 465 GLY ALA ILE ASP ARG SER VAL MSE PHE MSE ASN LEU ALA
SEQRES 18 F 465 ASN ASP PRO ALA ILE GLU ARG ILE ALA THR PRO ARG MSE
SEQRES 19 F 465 ALA LEU THR ALA ALA GLU TYR LEU ALA TYR GLU LYS GLY
SEQRES 20 F 465 MSE HIS VAL LEU VAL ILE MSE THR ASP MSE THR ASN TYR
SEQRES 21 F 465 ALA GLU ALA LEU ARG GLU ILE SER ALA ALA ARG ARG GLU
SEQRES 22 F 465 VAL PRO GLY ARG ARG GLY TYR PRO GLY TYR LEU TYR THR
SEQRES 23 F 465 ASN LEU ALA THR LEU PHE GLU ARG ALA GLY ARG ILE ARG
SEQRES 24 F 465 GLY LEU LYS GLY SER VAL THR GLN ILE PRO ILE LEU THR
SEQRES 25 F 465 MSE PRO GLU ASP ASP LYS THR HIS PRO ILE PRO ASP LEU
SEQRES 26 F 465 THR GLY TYR ILE THR GLU GLY GLN ILE ILE LEU THR ARG
SEQRES 27 F 465 GLU LEU TYR LYS SER GLY ILE GLN PRO PRO ILE ASP VAL
SEQRES 28 F 465 LEU PRO SER LEU SER ARG LEU LYS ASP LYS GLY THR GLY
SEQRES 29 F 465 ALA GLY LYS THR ARG GLU ASP HIS ALA ALA THR MSE ASN
SEQRES 30 F 465 GLN LEU PHE ALA ALA TYR ALA GLN GLY LYS GLN ALA LYS
SEQRES 31 F 465 GLU LEU ALA VAL VAL LEU GLY GLU SER ALA LEU SER ASP
SEQRES 32 F 465 ILE ASP LYS ILE TYR ALA LYS PHE ALA GLU ARG PHE GLU
SEQRES 33 F 465 ASN GLU TYR VAL ASN GLN GLY PHE TYR THR ASN ARG THR
SEQRES 34 F 465 ILE THR GLU THR LEU ASP LEU GLY TRP GLU LEU LEU ALA
SEQRES 35 F 465 MSE LEU PRO ARG THR GLU LEU LYS ARG ILE LYS ASP ASP
SEQRES 36 F 465 LEU LEU ASP LYS TYR LEU PRO GLU GLY LYS
SEQRES 1 G 217 GLY SER SER GLY SER SER GLY MSE ARG LEU ASN VAL ASN
SEQRES 2 G 217 PRO THR ARG MSE GLU LEU THR ARG LEU LYS LYS GLN LEU
SEQRES 3 G 217 THR THR ALA THR ARG GLY HIS LYS LEU LEU LYS ASP LYS
SEQRES 4 G 217 GLN ASP GLU LEU MSE ARG GLN PHE ILE LEU LEU ILE ARG
SEQRES 5 G 217 LYS ASN ASN GLU LEU ARG GLN ALA ILE GLU LYS GLU THR
SEQRES 6 G 217 GLN THR ALA MSE LYS ASP PHE VAL LEU ALA LYS SER THR
SEQRES 7 G 217 VAL GLU GLU ALA PHE ILE ASP GLU LEU LEU ALA LEU PRO
SEQRES 8 G 217 ALA GLU ASN VAL SER ILE SER VAL VAL GLU LYS ASN ILE
SEQRES 9 G 217 MSE SER VAL LYS VAL PRO LEU MSE ASN PHE GLN TYR ASP
SEQRES 10 G 217 GLU THR LEU ASN GLU THR PRO LEU GLU TYR GLY TYR LEU
SEQRES 11 G 217 HIS SER ASN ALA GLU LEU ASP ARG SER ILE ASP GLY PHE
SEQRES 12 G 217 THR GLN LEU LEU PRO LYS LEU LEU LYS LEU ALA GLU VAL
SEQRES 13 G 217 GLU LYS THR CYS GLN LEU MSE ALA GLU GLU ILE GLU LYS
SEQRES 14 G 217 THR ARG ARG ARG VAL ASN ALA LEU GLU TYR MSE THR ILE
SEQRES 15 G 217 PRO GLN LEU GLU GLU THR ILE TYR TYR ILE LYS MSE LYS
SEQRES 16 G 217 LEU GLU GLU ASN GLU ARG ALA GLU VAL THR ARG LEU ILE
SEQRES 17 G 217 LYS VAL LYS ASN MSE GLY THR GLU GLU
SEQRES 1 H 115 MSE THR TYR LYS ILE GLY VAL VAL GLY ASP LYS ASP SER
SEQRES 2 H 115 VAL SER PRO PHE ARG LEU PHE GLY PHE ASP VAL GLN HIS
SEQRES 3 H 115 GLY THR THR LYS THR GLU ILE ARG LYS THR ILE ASP GLU
SEQRES 4 H 115 MSE ALA LYS ASN GLU TYR GLY VAL ILE TYR ILE THR GLU
SEQRES 5 H 115 GLN CYS ALA ASN LEU VAL PRO GLU THR ILE GLU ARG TYR
SEQRES 6 H 115 LYS GLY GLN LEU THR PRO ALA ILE ILE LEU ILE PRO SER
SEQRES 7 H 115 HIS GLN GLY THR LEU GLY ILE GLY LEU GLU GLU ILE GLN
SEQRES 8 H 115 ASN SER VAL GLU LYS ALA VAL GLY GLN ASN ILE LEU SER
SEQRES 9 H 115 GLY PRO SER SER GLY GLU ASN LEU TYR PHE GLN
MODRES 3VR4 MSE A 1 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 15 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 19 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 27 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 42 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 83 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 95 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 150 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 187 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 188 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 209 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 266 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 286 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 298 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 320 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 327 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 341 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 348 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 445 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 456 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 461 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 521 MET SELENOMETHIONINE
MODRES 3VR4 MSE A 546 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 1 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 15 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 19 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 27 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 42 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 83 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 95 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 150 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 187 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 188 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 209 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 266 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 286 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 298 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 320 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 327 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 341 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 348 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 445 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 456 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 461 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 521 MET SELENOMETHIONINE
MODRES 3VR4 MSE B 546 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 1 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 15 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 19 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 27 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 42 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 83 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 95 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 150 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 187 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 188 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 209 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 266 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 286 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 298 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 320 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 327 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 341 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 348 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 445 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 456 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 461 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 521 MET SELENOMETHIONINE
MODRES 3VR4 MSE C 546 MET SELENOMETHIONINE
MODRES 3VR4 MSE D 16 MET SELENOMETHIONINE
MODRES 3VR4 MSE D 34 MET SELENOMETHIONINE
MODRES 3VR4 MSE D 53 MET SELENOMETHIONINE
MODRES 3VR4 MSE D 85 MET SELENOMETHIONINE
MODRES 3VR4 MSE D 195 MET SELENOMETHIONINE
MODRES 3VR4 MSE D 209 MET SELENOMETHIONINE
MODRES 3VR4 MSE D 211 MET SELENOMETHIONINE
MODRES 3VR4 MSE D 227 MET SELENOMETHIONINE
MODRES 3VR4 MSE D 241 MET SELENOMETHIONINE
MODRES 3VR4 MSE D 247 MET SELENOMETHIONINE
MODRES 3VR4 MSE D 250 MET SELENOMETHIONINE
MODRES 3VR4 MSE D 306 MET SELENOMETHIONINE
MODRES 3VR4 MSE D 369 MET SELENOMETHIONINE
MODRES 3VR4 MSE D 436 MET SELENOMETHIONINE
MODRES 3VR4 MSE E 16 MET SELENOMETHIONINE
MODRES 3VR4 MSE E 34 MET SELENOMETHIONINE
MODRES 3VR4 MSE E 53 MET SELENOMETHIONINE
MODRES 3VR4 MSE E 85 MET SELENOMETHIONINE
MODRES 3VR4 MSE E 195 MET SELENOMETHIONINE
MODRES 3VR4 MSE E 209 MET SELENOMETHIONINE
MODRES 3VR4 MSE E 211 MET SELENOMETHIONINE
MODRES 3VR4 MSE E 227 MET SELENOMETHIONINE
MODRES 3VR4 MSE E 241 MET SELENOMETHIONINE
MODRES 3VR4 MSE E 247 MET SELENOMETHIONINE
MODRES 3VR4 MSE E 250 MET SELENOMETHIONINE
MODRES 3VR4 MSE E 306 MET SELENOMETHIONINE
MODRES 3VR4 MSE E 369 MET SELENOMETHIONINE
MODRES 3VR4 MSE E 436 MET SELENOMETHIONINE
MODRES 3VR4 MSE F 1 MET SELENOMETHIONINE
MODRES 3VR4 MSE F 16 MET SELENOMETHIONINE
MODRES 3VR4 MSE F 34 MET SELENOMETHIONINE
MODRES 3VR4 MSE F 53 MET SELENOMETHIONINE
MODRES 3VR4 MSE F 85 MET SELENOMETHIONINE
MODRES 3VR4 MSE F 195 MET SELENOMETHIONINE
MODRES 3VR4 MSE F 209 MET SELENOMETHIONINE
MODRES 3VR4 MSE F 211 MET SELENOMETHIONINE
MODRES 3VR4 MSE F 227 MET SELENOMETHIONINE
MODRES 3VR4 MSE F 241 MET SELENOMETHIONINE
MODRES 3VR4 MSE F 247 MET SELENOMETHIONINE
MODRES 3VR4 MSE F 250 MET SELENOMETHIONINE
MODRES 3VR4 MSE F 306 MET SELENOMETHIONINE
MODRES 3VR4 MSE F 369 MET SELENOMETHIONINE
MODRES 3VR4 MSE F 436 MET SELENOMETHIONINE
MODRES 3VR4 MSE G 10 MET SELENOMETHIONINE
MODRES 3VR4 MSE G 37 MET SELENOMETHIONINE
MODRES 3VR4 MSE G 62 MET SELENOMETHIONINE
MODRES 3VR4 MSE G 98 MET SELENOMETHIONINE
MODRES 3VR4 MSE G 105 MET SELENOMETHIONINE
MODRES 3VR4 MSE G 156 MET SELENOMETHIONINE
MODRES 3VR4 MSE G 173 MET SELENOMETHIONINE
MODRES 3VR4 MSE G 187 MET SELENOMETHIONINE
MODRES 3VR4 MSE G 206 MET SELENOMETHIONINE
MODRES 3VR4 MSE H 40 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 15 8
HET MSE A 19 8
HET MSE A 27 8
HET MSE A 42 8
HET MSE A 83 8
HET MSE A 95 8
HET MSE A 150 8
HET MSE A 187 8
HET MSE A 188 8
HET MSE A 209 12
HET MSE A 266 8
HET MSE A 286 8
HET MSE A 298 8
HET MSE A 320 8
HET MSE A 327 12
HET MSE A 341 8
HET MSE A 348 8
HET MSE A 445 8
HET MSE A 456 8
HET MSE A 461 8
HET MSE A 521 8
HET MSE A 546 8
HET MSE B 1 8
HET MSE B 15 12
HET MSE B 19 8
HET MSE B 27 12
HET MSE B 42 8
HET MSE B 83 8
HET MSE B 95 8
HET MSE B 150 8
HET MSE B 187 8
HET MSE B 188 12
HET MSE B 209 12
HET MSE B 266 8
HET MSE B 286 8
HET MSE B 298 8
HET MSE B 320 8
HET MSE B 327 8
HET MSE B 341 12
HET MSE B 348 8
HET MSE B 445 8
HET MSE B 456 8
HET MSE B 461 8
HET MSE B 521 8
HET MSE B 546 8
HET MSE C 1 8
HET MSE C 15 12
HET MSE C 19 8
HET MSE C 27 12
HET MSE C 42 8
HET MSE C 83 8
HET MSE C 95 8
HET MSE C 150 8
HET MSE C 187 8
HET MSE C 188 8
HET MSE C 209 12
HET MSE C 266 8
HET MSE C 286 8
HET MSE C 298 8
HET MSE C 320 8
HET MSE C 327 12
HET MSE C 341 8
HET MSE C 348 8
HET MSE C 445 8
HET MSE C 456 8
HET MSE C 461 8
HET MSE C 521 8
HET MSE C 546 8
HET MSE D 16 12
HET MSE D 34 8
HET MSE D 53 8
HET MSE D 85 8
HET MSE D 195 8
HET MSE D 209 8
HET MSE D 211 8
HET MSE D 227 8
HET MSE D 241 8
HET MSE D 247 8
HET MSE D 250 8
HET MSE D 306 8
HET MSE D 369 8
HET MSE D 436 8
HET MSE E 16 12
HET MSE E 34 8
HET MSE E 53 12
HET MSE E 85 8
HET MSE E 195 12
HET MSE E 209 8
HET MSE E 211 8
HET MSE E 227 8
HET MSE E 241 8
HET MSE E 247 8
HET MSE E 250 8
HET MSE E 306 8
HET MSE E 369 8
HET MSE E 436 8
HET MSE F 1 8
HET MSE F 16 12
HET MSE F 34 8
HET MSE F 53 12
HET MSE F 85 8
HET MSE F 195 8
HET MSE F 209 8
HET MSE F 211 8
HET MSE F 227 8
HET MSE F 241 8
HET MSE F 247 8
HET MSE F 250 8
HET MSE F 306 8
HET MSE F 369 12
HET MSE F 436 8
HET MSE G 10 8
HET MSE G 37 8
HET MSE G 62 8
HET MSE G 98 8
HET MSE G 105 8
HET MSE G 156 8
HET MSE G 173 8
HET MSE G 187 12
HET MSE G 206 8
HET MSE H 40 8
HET GOL A 601 6
HET CL B 601 1
HET GOL B 602 6
HET GOL D 501 6
HET GOL D 502 6
HET B3P F 501 19
HET B3P F 502 19
HET GOL F 503 6
HET GOL F 504 6
HET GOL F 505 6
HET GOL G 301 6
HETNAM MSE SELENOMETHIONINE
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM B3P 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-
HETNAM 2 B3P PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 122(C5 H11 N O2 SE)
FORMUL 9 GOL 8(C3 H8 O3)
FORMUL 10 CL CL 1-
FORMUL 14 B3P 2(C11 H26 N2 O6)
FORMUL 20 HOH *1795(H2 O)
HELIX 1 1 PRO A 90 GLN A 99 1 10
HELIX 2 2 GLN A 213 PHE A 220 1 8
HELIX 3 3 GLY A 237 SER A 249 1 13
HELIX 4 4 ARG A 262 PHE A 273 1 12
HELIX 5 5 SER A 284 GLU A 287 5 4
HELIX 6 6 PRO A 299 ASP A 319 1 21
HELIX 7 7 SER A 330 LEU A 345 1 16
HELIX 8 8 GLY A 350 TYR A 354 5 5
HELIX 9 9 TYR A 357 GLU A 367 1 11
HELIX 10 10 GLU A 399 ARG A 407 1 9
HELIX 11 11 ASP A 416 GLN A 421 1 6
HELIX 12 12 TYR A 437 GLN A 450 1 14
HELIX 13 13 ASP A 452 VAL A 477 1 26
HELIX 14 14 GLY A 478 LEU A 482 5 5
HELIX 15 15 SER A 483 TYR A 500 1 18
HELIX 16 16 SER A 514 SER A 537 1 24
HELIX 17 17 TYR A 541 THR A 549 1 9
HELIX 18 18 THR A 549 ARG A 558 1 10
HELIX 19 19 SER A 559 ILE A 562 5 4
HELIX 20 20 PRO A 563 GLU A 566 5 4
HELIX 21 21 LEU A 567 SER A 572 1 6
HELIX 22 22 SER A 572 GLU A 587 1 16
HELIX 23 23 PRO B 90 GLN B 99 1 10
HELIX 24 24 GLN B 213 PHE B 220 1 8
HELIX 25 25 GLY B 237 SER B 249 1 13
HELIX 26 26 ARG B 262 PHE B 273 1 12
HELIX 27 27 SER B 284 GLU B 287 5 4
HELIX 28 28 VAL B 300 MSE B 320 1 21
HELIX 29 29 SER B 330 LEU B 345 1 16
HELIX 30 30 GLY B 350 TYR B 354 5 5
HELIX 31 31 TYR B 357 GLU B 367 1 11
HELIX 32 32 PRO B 392 ASP B 396 5 5
HELIX 33 33 GLU B 399 ARG B 407 1 9
HELIX 34 34 ASP B 416 LYS B 422 1 7
HELIX 35 35 TYR B 437 GLN B 450 1 14
HELIX 36 36 ASP B 452 GLY B 478 1 27
HELIX 37 37 ILE B 479 LEU B 482 5 4
HELIX 38 38 SER B 483 TYR B 500 1 18
HELIX 39 39 SER B 514 LEU B 538 1 25
HELIX 40 40 TYR B 541 GLY B 548 1 8
HELIX 41 41 THR B 549 SER B 557 1 9
HELIX 42 42 ARG B 558 ILE B 562 5 5
HELIX 43 43 PRO B 563 GLU B 566 5 4
HELIX 44 44 LEU B 567 SER B 572 1 6
HELIX 45 45 SER B 572 SER B 586 1 15
HELIX 46 46 PRO C 90 GLN C 99 1 10
HELIX 47 47 GLN C 213 PHE C 220 1 8
HELIX 48 48 GLY C 237 SER C 249 1 13
HELIX 49 49 ARG C 262 PHE C 273 1 12
HELIX 50 50 PRO C 274 LEU C 276 5 3
HELIX 51 51 SER C 284 GLU C 287 5 4
HELIX 52 52 ALA C 301 ASP C 319 1 19
HELIX 53 53 SER C 330 LEU C 345 1 16
HELIX 54 54 GLY C 350 TYR C 354 5 5
HELIX 55 55 TYR C 357 GLU C 367 1 11
HELIX 56 56 PRO C 392 ASP C 396 5 5
HELIX 57 57 GLU C 399 ARG C 407 1 9
HELIX 58 58 ASP C 416 LYS C 422 1 7
HELIX 59 59 TYR C 437 GLN C 450 1 14
HELIX 60 60 ASP C 452 LEU C 476 1 25
HELIX 61 61 SER C 483 TYR C 500 1 18
HELIX 62 62 SER C 514 LEU C 538 1 25
HELIX 63 63 TYR C 541 GLY C 548 1 8
HELIX 64 64 THR C 549 ARG C 558 1 10
HELIX 65 65 SER C 559 ILE C 562 5 4
HELIX 66 66 PRO C 563 GLU C 566 5 4
HELIX 67 67 LEU C 567 SER C 572 1 6
HELIX 68 68 SER C 572 SER C 586 1 15
HELIX 69 69 SER D 82 ILE D 86 5 5
HELIX 70 70 ILE D 132 HIS D 137 1 6
HELIX 71 71 PRO D 156 ALA D 168 1 13
HELIX 72 72 THR D 187 GLY D 202 1 16
HELIX 73 73 ALA D 203 ASP D 205 5 3
HELIX 74 74 PRO D 217 GLU D 238 1 22
HELIX 75 75 ASP D 249 ARG D 264 1 16
HELIX 76 76 GLY D 269 TYR D 273 5 5
HELIX 77 77 PRO D 274 GLY D 275 5 2
HELIX 78 78 TYR D 276 GLU D 286 1 11
HELIX 79 79 PRO D 307 ASP D 310 5 4
HELIX 80 80 HIS D 313 THR D 323 1 11
HELIX 81 81 THR D 330 SER D 336 1 7
HELIX 82 82 LEU D 351 GLY D 355 5 5
HELIX 83 83 ASP D 364 GLY D 390 1 27
HELIX 84 84 SER D 395 TYR D 412 1 18
HELIX 85 85 THR D 422 ALA D 435 1 14
HELIX 86 86 LYS D 446 LEU D 454 1 9
HELIX 87 87 SER E 82 ILE E 86 5 5
HELIX 88 88 ILE E 132 HIS E 137 1 6
HELIX 89 89 PRO E 156 ALA E 168 1 13
HELIX 90 90 THR E 187 GLY E 202 1 16
HELIX 91 91 ALA E 203 ASP E 205 5 3
HELIX 92 92 PRO E 217 GLU E 238 1 22
HELIX 93 93 ASP E 249 ARG E 264 1 16
HELIX 94 94 GLY E 269 TYR E 273 5 5
HELIX 95 95 TYR E 276 GLU E 286 1 11
HELIX 96 96 PRO E 307 ASP E 310 5 4
HELIX 97 97 HIS E 313 TYR E 321 1 9
HELIX 98 98 THR E 330 LYS E 335 1 6
HELIX 99 99 LEU E 351 THR E 356 5 6
HELIX 100 100 ASP E 364 GLY E 390 1 27
HELIX 101 101 GLU E 391 LEU E 394 5 4
HELIX 102 102 SER E 395 TYR E 412 1 18
HELIX 103 103 THR E 422 ALA E 435 1 14
HELIX 104 104 MSE E 436 LEU E 437 5 2
HELIX 105 105 PRO E 438 LEU E 442 5 5
HELIX 106 106 LYS E 446 LEU E 454 1 9
HELIX 107 107 SER F 82 ILE F 86 5 5
HELIX 108 108 ILE F 132 HIS F 137 1 6
HELIX 109 109 PRO F 156 ALA F 168 1 13
HELIX 110 110 THR F 187 GLY F 202 1 16
HELIX 111 111 ALA F 203 ASP F 205 5 3
HELIX 112 112 ALA F 218 ILE F 222 5 5
HELIX 113 113 ALA F 223 GLU F 238 1 16
HELIX 114 114 ASP F 249 ARG F 264 1 16
HELIX 115 115 GLY F 269 TYR F 273 5 5
HELIX 116 116 TYR F 276 GLU F 286 1 11
HELIX 117 117 PRO F 307 ASP F 310 5 4
HELIX 118 118 HIS F 313 THR F 323 1 11
HELIX 119 119 THR F 330 SER F 336 1 7
HELIX 120 120 ASP F 364 GLY F 390 1 27
HELIX 121 121 GLU F 391 LEU F 394 5 4
HELIX 122 122 SER F 395 TYR F 412 1 18
HELIX 123 123 THR F 422 ALA F 435 1 14
HELIX 124 124 MSE F 436 LEU F 437 5 2
HELIX 125 125 PRO F 438 LEU F 442 5 5
HELIX 126 126 LYS F 446 LEU F 454 1 9
HELIX 127 127 THR G 8 SER G 70 1 63
HELIX 128 128 GLU G 73 LEU G 81 1 9
HELIX 129 129 ALA G 127 SER G 132 1 6
HELIX 130 130 SER G 132 MSE G 173 1 42
HELIX 131 131 MSE G 173 MSE G 206 1 34
HELIX 132 132 ASP H 10 SER H 15 1 6
HELIX 133 133 PRO H 16 GLY H 21 5 6
HELIX 134 134 THR H 29 ASN H 43 1 15
HELIX 135 135 GLU H 52 ASN H 56 1 5
HELIX 136 136 VAL H 58 TYR H 65 1 8
HELIX 137 137 GLY H 84 VAL H 98 1 15
SHEET 1 A27 SER D 69 PHE D 72 0
SHEET 2 A27 LEU D 29 ARG D 40 -1 N ARG D 40 O SER D 69
SHEET 3 A27 ILE D 39 GLN D 55 -1 O ARG D 40 N VAL D 32
SHEET 4 A27 LYS D 51 ILE D 63 -1 O LYS D 51 N GLN D 55
SHEET 5 A27 LEU D 15 GLU D 19 -1 N MSE D 16 O VAL D 54
SHEET 6 A27 ILE D 8 VAL D 12 -1 N LYS D 9 O ALA D 17
SHEET 7 A27 VAL C 35 ARG C 43 -1 N MSE C 42 O VAL D 18
SHEET 8 A27 ASP C 26 VAL C 30 -1 N VAL C 30 O VAL C 35
SHEET 9 A27 PRO C 63 ALA C 70 -1 O THR C 67 N MSE C 27
SHEET 10 A27 GLY C 11 SER C 10 -1 N GLY C 11 O VAL C 64
SHEET 11 A27 LEU C 13 GLU C 17 -1 O MSE C 15 N ILE C 7
SHEET 12 A27 VAL C 46 VAL C 51 -1 O ILE C 49 N VAL C 14
SHEET 13 A27 VAL C 35 ARG C 43 -1 N GLU C 38 O GLN C 50
SHEET 14 A27 ASP C 26 VAL C 30 -1 N VAL C 30 O VAL C 35
SHEET 15 A27 PRO C 63 ALA C 70 -1 O THR C 67 N MSE C 27
SHEET 16 A27 GLY C 11 SER C 10 -1 N GLY C 11 O VAL C 64
SHEET 17 A27 ILE F 39 GLN F 55 -1 O VAL F 54 N VAL C 9
SHEET 18 A27 LYS F 51 ILE F 63 -1 O MSE F 53 N LEU F 45
SHEET 19 A27 LEU F 15 VAL F 18 -1 N MSE F 16 O VAL F 54
SHEET 20 A27 ILE F 8 VAL F 12 -1 N VAL F 12 O LEU F 15
SHEET 21 A27 VAL B 35 ARG B 43 -1 N MSE B 42 O VAL F 18
SHEET 22 A27 ASP B 26 VAL B 30 -1 N CYS B 28 O GLY B 37
SHEET 23 A27 PRO B 63 ALA B 70 -1 O GLU B 69 N MSE B 27
SHEET 24 A27 GLY B 11 SER B 10 -1 N GLY B 11 O VAL B 64
SHEET 25 A27 ILE E 39 GLN E 55 -1 O VAL E 54 N VAL B 9
SHEET 26 A27 LEU E 29 ARG E 40 -1 N VAL E 32 O ARG E 40
SHEET 27 A27 SER E 69 PHE E 72 -1 O ARG E 71 N GLU E 38
SHEET 1 B14 LYS F 3 TYR F 5 0
SHEET 2 B14 SER F 69 PRO F 76 -1 O PHE F 72 N LYS F 3
SHEET 3 B14 GLU F 28 ARG F 40 -1 N GLU F 38 O ARG F 71
SHEET 4 B14 ILE F 39 GLN F 55 -1 O ARG F 40 N VAL F 32
SHEET 5 B14 LYS F 51 ILE F 63 -1 O MSE F 53 N LEU F 45
SHEET 6 B14 LEU F 15 VAL F 18 -1 N MSE F 16 O VAL F 54
SHEET 7 B14 ILE F 8 VAL F 12 -1 N VAL F 12 O LEU F 15
SHEET 8 B14 VAL B 35 ARG B 43 -1 N MSE B 42 O VAL F 18
SHEET 9 B14 VAL B 46 VAL B 51 -1 O GLN B 50 N GLU B 38
SHEET 10 B14 LEU B 13 GLU B 17 -1 N ALA B 16 O ALA B 47
SHEET 11 B14 GLY B 11 SER B 10 -1 N ILE B 7 O MSE B 15
SHEET 12 B14 ILE E 39 GLN E 55 -1 O VAL E 54 N VAL B 9
SHEET 13 B14 LEU E 29 ARG E 40 -1 N VAL E 32 O ARG E 40
SHEET 14 B14 SER E 69 PHE E 72 -1 O ARG E 71 N GLU E 38
SHEET 1 C13 SER E 69 PHE E 72 0
SHEET 2 C13 LEU E 29 ARG E 40 -1 N GLU E 38 O ARG E 71
SHEET 3 C13 ILE E 39 GLN E 55 -1 O ARG E 40 N VAL E 32
SHEET 4 C13 LYS E 51 ILE E 63 -1 O LYS E 51 N GLN E 55
SHEET 5 C13 LEU E 15 VAL E 18 -1 N MSE E 16 O VAL E 54
SHEET 6 C13 ILE E 8 VAL E 12 -1 N LYS E 9 O ALA E 17
SHEET 7 C13 VAL A 35 ARG A 43 -1 N MSE A 42 O VAL E 18
SHEET 8 C13 VAL A 46 VAL A 51 -1 O VAL A 46 N ARG A 43
SHEET 9 C13 LEU A 13 GLU A 17 -1 N VAL A 14 O ILE A 49
SHEET 10 C13 GLY A 11 SER A 10 -1 N SER A 10 O LEU A 13
SHEET 11 C13 ILE D 39 GLN D 55 -1 O VAL D 54 N VAL A 9
SHEET 12 C13 LEU D 29 ARG D 40 -1 N VAL D 32 O ARG D 40
SHEET 13 C13 SER D 69 PHE D 72 -1 O SER D 69 N ARG D 40
SHEET 1 D13 SER D 69 PHE D 72 0
SHEET 2 D13 LEU D 29 ARG D 40 -1 N ARG D 40 O SER D 69
SHEET 3 D13 ILE D 39 GLN D 55 -1 O ARG D 40 N VAL D 32
SHEET 4 D13 GLY A 11 SER A 10 -1 N VAL A 9 O VAL D 54
SHEET 5 D13 PRO A 63 SER A 66 -1 O VAL A 64 N GLY A 11
SHEET 6 D13 MSE A 27 VAL A 30 -1 N LEU A 29 O ARG A 65
SHEET 7 D13 VAL A 35 ARG A 43 -1 O VAL A 35 N VAL A 30
SHEET 8 D13 VAL A 46 VAL A 51 -1 O VAL A 46 N ARG A 43
SHEET 9 D13 LEU A 13 GLU A 17 -1 N VAL A 14 O ILE A 49
SHEET 10 D13 GLY A 11 SER A 10 -1 N SER A 10 O LEU A 13
SHEET 11 D13 ILE D 39 GLN D 55 -1 O VAL D 54 N VAL A 9
SHEET 12 D13 LEU D 29 ARG D 40 -1 N VAL D 32 O ARG D 40
SHEET 13 D13 SER D 69 PHE D 72 -1 O SER D 69 N ARG D 40
SHEET 1 E 2 SER A 72 LEU A 75 0
SHEET 2 E 2 GLN A 189 PRO A 192 -1 O GLN A 189 N LEU A 75
SHEET 1 F 7 MSE A 83 PHE A 84 0
SHEET 2 F 7 THR A 289 THR A 295 1 O ALA A 293 N PHE A 84
SHEET 3 F 7 LEU A 253 GLU A 261 1 N GLY A 258 O ILE A 292
SHEET 4 F 7 ASP A 323 ASP A 329 1 O MSE A 327 N VAL A 257
SHEET 5 F 7 GLU A 381 VAL A 390 1 O ALA A 389 N ALA A 335
SHEET 6 F 7 GLY A 370 ILE A 373 -1 N VAL A 372 O GLY A 382
SHEET 7 F 7 GLN A 201 LEU A 203 -1 N LEU A 203 O ARG A 371
SHEET 1 G 8 MSE A 83 PHE A 84 0
SHEET 2 G 8 THR A 289 THR A 295 1 O ALA A 293 N PHE A 84
SHEET 3 G 8 LEU A 253 GLU A 261 1 N GLY A 258 O ILE A 292
SHEET 4 G 8 ASP A 323 ASP A 329 1 O MSE A 327 N VAL A 257
SHEET 5 G 8 GLU A 381 VAL A 390 1 O ALA A 389 N ALA A 335
SHEET 6 G 8 ALA A 227 PRO A 231 1 N ALA A 228 O SER A 388
SHEET 7 G 8 VAL A 411 PHE A 412 1 O VAL A 411 N ALA A 236
SHEET 8 G 8 TYR A 434 SER A 435 -1 O TYR A 434 N PHE A 412
SHEET 1 H 4 HIS A 147 MSE A 150 0
SHEET 2 H 4 ILE A 135 VAL A 139 -1 N VAL A 139 O HIS A 147
SHEET 3 H 4 TRP A 118 ALA A 122 -1 N GLU A 121 O TYR A 138
SHEET 4 H 4 GLY A 165 PHE A 167 -1 O GLY A 165 N PHE A 120
SHEET 1 I 4 GLU A 129 VAL A 130 0
SHEET 2 I 4 GLY A 157 ILE A 169 -1 O GLY A 157 N VAL A 130
SHEET 3 I 4 CYS A 174 THR A 178 -1 O GLU A 184 N THR A 158
SHEET 4 I 4 GLY A 181 LEU A 185 -1 O LYS A 190 N ILE A 176
SHEET 1 J 2 SER B 72 LEU B 75 0
SHEET 2 J 2 GLN B 189 PRO B 192 -1 O GLN B 189 N LEU B 75
SHEET 1 K 7 MSE B 83 PHE B 84 0
SHEET 2 K 7 THR B 289 ASN B 294 1 O LEU B 291 N PHE B 84
SHEET 3 K 7 LEU B 253 CYS B 259 1 N GLY B 258 O ILE B 292
SHEET 4 K 7 ASP B 323 ASP B 329 1 O ALA B 325 N VAL B 255
SHEET 5 K 7 GLU B 381 VAL B 390 1 O THR B 385 N VAL B 324
SHEET 6 K 7 GLY B 370 ILE B 373 -1 N VAL B 372 O GLY B 382
SHEET 7 K 7 GLN B 201 LEU B 203 -1 N LEU B 203 O ARG B 371
SHEET 1 L 8 MSE B 83 PHE B 84 0
SHEET 2 L 8 THR B 289 ASN B 294 1 O LEU B 291 N PHE B 84
SHEET 3 L 8 LEU B 253 CYS B 259 1 N GLY B 258 O ILE B 292
SHEET 4 L 8 ASP B 323 ASP B 329 1 O ALA B 325 N VAL B 255
SHEET 5 L 8 GLU B 381 VAL B 390 1 O THR B 385 N VAL B 324
SHEET 6 L 8 ALA B 227 PRO B 231 1 N VAL B 230 O SER B 388
SHEET 7 L 8 VAL B 411 PHE B 412 1 O VAL B 411 N ALA B 236
SHEET 8 L 8 TYR B 434 SER B 435 -1 O TYR B 434 N PHE B 412
SHEET 1 M 4 HIS B 147 MSE B 150 0
SHEET 2 M 4 ILE B 135 VAL B 139 -1 N VAL B 139 O HIS B 147
SHEET 3 M 4 TRP B 118 ALA B 122 -1 N GLU B 121 O TYR B 138
SHEET 4 M 4 GLY B 165 PHE B 167 -1 O PHE B 167 N TRP B 118
SHEET 1 N 4 GLU B 129 VAL B 130 0
SHEET 2 N 4 GLY B 157 ILE B 169 -1 O GLY B 157 N VAL B 130
SHEET 3 N 4 CYS B 174 THR B 178 -1 O VAL B 175 N GLN B 160
SHEET 4 N 4 GLY B 181 LEU B 185 -1 O LYS B 190 N ILE B 176
SHEET 1 O 2 SER C 72 LEU C 75 0
SHEET 2 O 2 GLN C 189 PRO C 192 -1 O GLN C 189 N LEU C 75
SHEET 1 P 7 MSE C 83 PHE C 84 0
SHEET 2 P 7 THR C 289 ASN C 294 1 O ALA C 293 N PHE C 84
SHEET 3 P 7 LEU C 253 CYS C 259 1 N GLY C 258 O ILE C 292
SHEET 4 P 7 ASP C 323 ASP C 329 1 O MSE C 327 N VAL C 257
SHEET 5 P 7 GLU C 381 VAL C 390 1 O THR C 385 N VAL C 324
SHEET 6 P 7 GLY C 370 ILE C 373 -1 N VAL C 372 O GLY C 382
SHEET 7 P 7 GLN C 201 LEU C 203 -1 N LEU C 203 O ARG C 371
SHEET 1 Q 8 MSE C 83 PHE C 84 0
SHEET 2 Q 8 THR C 289 ASN C 294 1 O ALA C 293 N PHE C 84
SHEET 3 Q 8 LEU C 253 CYS C 259 1 N GLY C 258 O ILE C 292
SHEET 4 Q 8 ASP C 323 ASP C 329 1 O MSE C 327 N VAL C 257
SHEET 5 Q 8 GLU C 381 VAL C 390 1 O THR C 385 N VAL C 324
SHEET 6 Q 8 ALA C 227 PRO C 231 1 N ALA C 228 O ALA C 386
SHEET 7 Q 8 VAL C 411 PHE C 412 1 O VAL C 411 N ALA C 236
SHEET 8 Q 8 TYR C 434 SER C 435 -1 O TYR C 434 N PHE C 412
SHEET 1 R 4 GLN C 146 MSE C 150 0
SHEET 2 R 4 ILE C 135 ASP C 140 -1 N VAL C 139 O HIS C 147
SHEET 3 R 4 TRP C 118 ALA C 122 -1 N GLU C 121 O TYR C 138
SHEET 4 R 4 GLY C 165 PHE C 167 -1 O GLY C 165 N PHE C 120
SHEET 1 S 4 GLU C 129 VAL C 130 0
SHEET 2 S 4 GLY C 157 ILE C 169 -1 O GLY C 157 N VAL C 130
SHEET 3 S 4 CYS C 174 THR C 178 -1 O VAL C 175 N GLN C 160
SHEET 4 S 4 GLY C 181 LEU C 185 -1 O LEU C 185 N CYS C 174
SHEET 1 T 2 GLN D 78 VAL D 81 0
SHEET 2 T 2 LYS D 107 ASP D 110 -1 O LEU D 109 N LEU D 79
SHEET 1 U 7 ARG D 95 ASP D 98 0
SHEET 2 U 7 SER D 207 LEU D 213 1 O MSE D 209 N PHE D 90
SHEET 3 U 7 PHE D 177 ILE D 186 1 N PHE D 188 O PHE D 210
SHEET 4 U 7 HIS D 242 THR D 248 1 O THR D 248 N ILE D 184
SHEET 5 U 7 SER D 297 THR D 312 1 O THR D 299 N VAL D 245
SHEET 6 U 7 GLY D 296 ILE D 291 -1 N GLY D 296 O VAL D 298
SHEET 7 U 7 ARG D 121 ASP D 122 -1 N ASP D 122 O ARG D 290
SHEET 1 V 8 ARG D 95 ASP D 98 0
SHEET 2 V 8 SER D 207 LEU D 213 1 O MSE D 209 N PHE D 90
SHEET 3 V 8 PHE D 177 ILE D 186 1 N PHE D 188 O PHE D 210
SHEET 4 V 8 HIS D 242 THR D 248 1 O THR D 248 N ILE D 184
SHEET 5 V 8 SER D 297 THR D 312 1 O THR D 299 N VAL D 245
SHEET 6 V 8 VAL D 149 SER D 151 1 N SER D 151 O LEU D 304
SHEET 7 V 8 GLY D 325 ILE D 328 1 O ILE D 327 N PHE D 150
SHEET 8 V 8 LEU D 348 SER D 349 -1 O LEU D 348 N GLN D 326
SHEET 1 W 2 GLN E 78 VAL E 81 0
SHEET 2 W 2 LYS E 107 ASP E 110 -1 O LEU E 109 N LEU E 79
SHEET 1 X 7 VAL E 89 ASP E 98 0
SHEET 2 X 7 SER E 207 LEU E 213 1 O MSE E 209 N PHE E 90
SHEET 3 X 7 PHE E 177 ILE E 186 1 N PHE E 188 O PHE E 210
SHEET 4 X 7 HIS E 242 THR E 248 1 O THR E 248 N ILE E 184
SHEET 5 X 7 SER E 297 THR E 312 1 O THR E 299 N VAL E 245
SHEET 6 X 7 GLY E 296 ILE E 291 -1 N GLY E 296 O VAL E 298
SHEET 7 X 7 ARG E 121 ASP E 122 -1 N ASP E 122 O ARG E 290
SHEET 1 Y 8 VAL E 89 ASP E 98 0
SHEET 2 Y 8 SER E 207 LEU E 213 1 O MSE E 209 N PHE E 90
SHEET 3 Y 8 PHE E 177 ILE E 186 1 N PHE E 188 O PHE E 210
SHEET 4 Y 8 HIS E 242 THR E 248 1 O THR E 248 N ILE E 184
SHEET 5 Y 8 SER E 297 THR E 312 1 O THR E 299 N VAL E 245
SHEET 6 Y 8 VAL E 149 SER E 151 1 N SER E 151 O LEU E 304
SHEET 7 Y 8 GLY E 325 ILE E 328 1 O ILE E 327 N PHE E 150
SHEET 8 Y 8 LEU E 348 SER E 349 -1 O LEU E 348 N GLN E 326
SHEET 1 Z 2 GLN F 78 VAL F 81 0
SHEET 2 Z 2 LYS F 107 ASP F 110 -1 O LEU F 109 N LEU F 79
SHEET 1 AA 8 ARG F 95 ASP F 98 0
SHEET 2 AA 8 SER F 207 LEU F 213 1 O MSE F 209 N PHE F 90
SHEET 3 AA 8 ALA F 178 ILE F 186 1 N PHE F 188 O PHE F 210
SHEET 4 AA 8 HIS F 242 THR F 248 1 O LEU F 244 N ALA F 178
SHEET 5 AA 8 SER F 297 THR F 312 1 O THR F 299 N VAL F 245
SHEET 6 AA 8 VAL F 149 SER F 151 1 N SER F 151 O LEU F 304
SHEET 7 AA 8 GLY F 325 ILE F 328 1 O ILE F 327 N PHE F 150
SHEET 8 AA 8 LEU F 348 SER F 349 -1 O LEU F 348 N GLN F 326
SHEET 1 AB 2 ARG F 121 ASP F 122 0
SHEET 2 AB 2 ARG F 290 ILE F 291 -1 O ARG F 290 N ASP F 122
SHEET 1 AC 2 ILE F 135 GLN F 129 0
SHEET 2 AC 2 THR F 169 VAL F 170 -1 O THR F 169 N GLN F 129
SHEET 1 AD 2 ILE G 97 ILE G 97 0
SHEET 2 AD 2 VAL G 100 PHE G 107 -1 O VAL G 102 N LYS G 95
SHEET 1 AE 4 ASP H 23 GLN H 25 0
SHEET 2 AE 4 LYS H 4 VAL H 8 1 N VAL H 7 O GLN H 25
SHEET 3 AE 4 TYR H 45 THR H 51 1 O TYR H 49 N GLY H 6
SHEET 4 AE 4 ALA H 72 ILE H 76 1 O ILE H 76 N ILE H 50
LINK C GLY A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N GLN A 2 1555 1555 1.33
LINK C VAL A 14 N MSE A 15 1555 1555 1.33
LINK C MSE A 15 N ALA A 16 1555 1555 1.33
LINK C ASN A 18 N MSE A 19 1555 1555 1.33
LINK C MSE A 19 N SER A 20 1555 1555 1.33
LINK C ASP A 26 N MSE A 27 1555 1555 1.33
LINK C MSE A 27 N CYS A 28 1555 1555 1.33
LINK C GLU A 41 N MSE A 42 1555 1555 1.33
LINK C MSE A 42 N ARG A 43 1555 1555 1.33
LINK C GLN A 82 N MSE A 83 1555 1555 1.33
LINK C MSE A 83 N PHE A 84 1555 1555 1.33
LINK C PHE A 94 N MSE A 95 1555 1555 1.33
LINK C MSE A 95 N GLU A 96 1555 1555 1.33
LINK C ILE A 149 N MSE A 150 1555 1555 1.33
LINK C MSE A 150 N VAL A 151 1555 1555 1.33
LINK C THR A 186 N MSE A 187 1555 1555 1.33
LINK C MSE A 187 N MSE A 188 1555 1555 1.33
LINK C MSE A 188 N GLN A 189 1555 1555 1.33
LINK C PRO A 208 N MSE A 209 1555 1555 1.33
LINK C MSE A 209 N ILE A 210 1555 1555 1.33
LINK C GLU A 265 N MSE A 266 1555 1555 1.33
LINK C MSE A 266 N THR A 267 1555 1555 1.33
LINK C LEU A 285 N MSE A 286 1555 1555 1.33
LINK C MSE A 286 N GLU A 287 1555 1555 1.33
LINK C ASN A 297 N MSE A 298 1555 1555 1.33
LINK C MSE A 298 N PRO A 299 1555 1555 1.35
LINK C ASP A 319 N MSE A 320 1555 1555 1.33
LINK C MSE A 320 N GLY A 321 1555 1555 1.33
LINK C ILE A 326 N MSE A 327 1555 1555 1.33
LINK C MSE A 327 N ALA A 328 1555 1555 1.33
LINK C GLU A 340 N MSE A 341 1555 1555 1.33
LINK C MSE A 341 N SER A 342 1555 1555 1.33
LINK C GLU A 347 N MSE A 348 1555 1555 1.33
LINK C MSE A 348 N PRO A 349 1555 1555 1.34
LINK C TYR A 444 N MSE A 445 1555 1555 1.33
LINK C MSE A 445 N ASP A 446 1555 1555 1.33
LINK C ASP A 455 N MSE A 456 1555 1555 1.33
LINK C MSE A 456 N VAL A 457 1555 1555 1.33
LINK C GLY A 460 N MSE A 461 1555 1555 1.33
LINK C MSE A 461 N ARG A 462 1555 1555 1.33
LINK C ASN A 520 N MSE A 521 1555 1555 1.33
LINK C MSE A 521 N LEU A 522 1555 1555 1.33
LINK C ILE A 545 N MSE A 546 1555 1555 1.33
LINK C MSE A 546 N GLU A 547 1555 1555 1.33
LINK C GLY B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N GLN B 2 1555 1555 1.33
LINK C VAL B 14 N MSE B 15 1555 1555 1.33
LINK C MSE B 15 N ALA B 16 1555 1555 1.33
LINK C ASN B 18 N MSE B 19 1555 1555 1.33
LINK C MSE B 19 N SER B 20 1555 1555 1.33
LINK C ASP B 26 N MSE B 27 1555 1555 1.33
LINK C MSE B 27 N CYS B 28 1555 1555 1.33
LINK C GLU B 41 N MSE B 42 1555 1555 1.33
LINK C MSE B 42 N ARG B 43 1555 1555 1.33
LINK C GLN B 82 N MSE B 83 1555 1555 1.33
LINK C MSE B 83 N PHE B 84 1555 1555 1.33
LINK C PHE B 94 N MSE B 95 1555 1555 1.33
LINK C MSE B 95 N GLU B 96 1555 1555 1.33
LINK C ILE B 149 N MSE B 150 1555 1555 1.33
LINK C MSE B 150 N VAL B 151 1555 1555 1.33
LINK C THR B 186 N MSE B 187 1555 1555 1.33
LINK C MSE B 187 N MSE B 188 1555 1555 1.33
LINK C MSE B 188 N GLN B 189 1555 1555 1.33
LINK C PRO B 208 N MSE B 209 1555 1555 1.33
LINK C MSE B 209 N ILE B 210 1555 1555 1.33
LINK C GLU B 265 N MSE B 266 1555 1555 1.33
LINK C MSE B 266 N THR B 267 1555 1555 1.33
LINK C LEU B 285 N MSE B 286 1555 1555 1.33
LINK C MSE B 286 N GLU B 287 1555 1555 1.33
LINK C ASN B 297 N MSE B 298 1555 1555 1.33
LINK C MSE B 298 N PRO B 299 1555 1555 1.35
LINK C ASP B 319 N MSE B 320 1555 1555 1.33
LINK C MSE B 320 N GLY B 321 1555 1555 1.33
LINK C ILE B 326 N MSE B 327 1555 1555 1.33
LINK C MSE B 327 N ALA B 328 1555 1555 1.33
LINK C GLU B 340 N MSE B 341 1555 1555 1.33
LINK C MSE B 341 N SER B 342 1555 1555 1.33
LINK C GLU B 347 N MSE B 348 1555 1555 1.33
LINK C MSE B 348 N PRO B 349 1555 1555 1.34
LINK C TYR B 444 N MSE B 445 1555 1555 1.33
LINK C MSE B 445 N ASP B 446 1555 1555 1.33
LINK C ASP B 455 N MSE B 456 1555 1555 1.33
LINK C MSE B 456 N VAL B 457 1555 1555 1.33
LINK C GLY B 460 N MSE B 461 1555 1555 1.33
LINK C MSE B 461 N ARG B 462 1555 1555 1.33
LINK C ASN B 520 N MSE B 521 1555 1555 1.33
LINK C MSE B 521 N LEU B 522 1555 1555 1.33
LINK C ILE B 545 N MSE B 546 1555 1555 1.33
LINK C MSE B 546 N GLU B 547 1555 1555 1.33
LINK C MSE C 1 N GLN C 2 1555 1555 1.33
LINK C VAL C 14 N MSE C 15 1555 1555 1.33
LINK C MSE C 15 N ALA C 16 1555 1555 1.33
LINK C ASN C 18 N MSE C 19 1555 1555 1.33
LINK C MSE C 19 N SER C 20 1555 1555 1.33
LINK C ASP C 26 N MSE C 27 1555 1555 1.33
LINK C MSE C 27 N CYS C 28 1555 1555 1.33
LINK C GLU C 41 N MSE C 42 1555 1555 1.33
LINK C MSE C 42 N ARG C 43 1555 1555 1.33
LINK C GLN C 82 N MSE C 83 1555 1555 1.33
LINK C MSE C 83 N PHE C 84 1555 1555 1.33
LINK C PHE C 94 N MSE C 95 1555 1555 1.33
LINK C MSE C 95 N GLU C 96 1555 1555 1.33
LINK C ILE C 149 N MSE C 150 1555 1555 1.33
LINK C MSE C 150 N VAL C 151 1555 1555 1.33
LINK C THR C 186 N MSE C 187 1555 1555 1.33
LINK C MSE C 187 N MSE C 188 1555 1555 1.33
LINK C MSE C 188 N GLN C 189 1555 1555 1.33
LINK C PRO C 208 N MSE C 209 1555 1555 1.33
LINK C MSE C 209 N ILE C 210 1555 1555 1.33
LINK C GLU C 265 N MSE C 266 1555 1555 1.33
LINK C MSE C 266 N THR C 267 1555 1555 1.33
LINK C LEU C 285 N MSE C 286 1555 1555 1.33
LINK C MSE C 286 N GLU C 287 1555 1555 1.33
LINK C ASN C 297 N MSE C 298 1555 1555 1.33
LINK C MSE C 298 N PRO C 299 1555 1555 1.35
LINK C ASP C 319 N MSE C 320 1555 1555 1.33
LINK C MSE C 320 N GLY C 321 1555 1555 1.33
LINK C ILE C 326 N MSE C 327 1555 1555 1.33
LINK C MSE C 327 N ALA C 328 1555 1555 1.33
LINK C GLU C 340 N MSE C 341 1555 1555 1.33
LINK C MSE C 341 N SER C 342 1555 1555 1.33
LINK C GLU C 347 N MSE C 348 1555 1555 1.33
LINK C MSE C 348 N PRO C 349 1555 1555 1.34
LINK C TYR C 444 N MSE C 445 1555 1555 1.33
LINK C MSE C 445 N ASP C 446 1555 1555 1.33
LINK C ASP C 455 N MSE C 456 1555 1555 1.33
LINK C MSE C 456 N VAL C 457 1555 1555 1.33
LINK C GLY C 460 N MSE C 461 1555 1555 1.33
LINK C MSE C 461 N ARG C 462 1555 1555 1.33
LINK C ASN C 520 N MSE C 521 1555 1555 1.33
LINK C MSE C 521 N LEU C 522 1555 1555 1.33
LINK C ILE C 545 N MSE C 546 1555 1555 1.33
LINK C MSE C 546 N GLU C 547 1555 1555 1.33
LINK C LEU D 15 N MSE D 16 1555 1555 1.33
LINK C MSE D 16 N ALA D 17 1555 1555 1.33
LINK C ARG D 33 N MSE D 34 1555 1555 1.33
LINK C MSE D 34 N GLN D 35 1555 1555 1.33
LINK C ALA D 52 N MSE D 53 1555 1555 1.33
LINK C MSE D 53 N VAL D 54 1555 1555 1.33
LINK C ASP D 84 N MSE D 85 1555 1555 1.33
LINK C MSE D 85 N ILE D 86 1555 1555 1.33
LINK C PHE D 194 N MSE D 195 1555 1555 1.33
LINK C MSE D 195 N GLU D 196 1555 1555 1.33
LINK C VAL D 208 N MSE D 209 1555 1555 1.33
LINK C MSE D 209 N PHE D 210 1555 1555 1.33
LINK C PHE D 210 N MSE D 211 1555 1555 1.33
LINK C MSE D 211 N ASN D 212 1555 1555 1.33
LINK C ARG D 226 N MSE D 227 1555 1555 1.33
LINK C MSE D 227 N ALA D 228 1555 1555 1.33
LINK C GLY D 240 N MSE D 241 1555 1555 1.33
LINK C MSE D 241 N HIS D 242 1555 1555 1.33
LINK C ILE D 246 N MSE D 247 1555 1555 1.33
LINK C MSE D 247 N THR D 248 1555 1555 1.33
LINK C ASP D 249 N MSE D 250 1555 1555 1.33
LINK C MSE D 250 N THR D 251 1555 1555 1.33
LINK C THR D 305 N MSE D 306 1555 1555 1.33
LINK C MSE D 306 N PRO D 307 1555 1555 1.34
LINK C THR D 368 N MSE D 369 1555 1555 1.33
LINK C MSE D 369 N ASN D 370 1555 1555 1.33
LINK C ALA D 435 N MSE D 436 1555 1555 1.33
LINK C MSE D 436 N LEU D 437 1555 1555 1.33
LINK C LEU E 15 N MSE E 16 1555 1555 1.33
LINK C MSE E 16 N ALA E 17 1555 1555 1.33
LINK C ARG E 33 N MSE E 34 1555 1555 1.33
LINK C MSE E 34 N GLN E 35 1555 1555 1.33
LINK C ALA E 52 N MSE E 53 1555 1555 1.33
LINK C MSE E 53 N VAL E 54 1555 1555 1.33
LINK C ASP E 84 N MSE E 85 1555 1555 1.33
LINK C MSE E 85 N ILE E 86 1555 1555 1.33
LINK C PHE E 194 N MSE E 195 1555 1555 1.33
LINK C MSE E 195 N GLU E 196 1555 1555 1.33
LINK C VAL E 208 N MSE E 209 1555 1555 1.33
LINK C MSE E 209 N PHE E 210 1555 1555 1.33
LINK C PHE E 210 N MSE E 211 1555 1555 1.33
LINK C MSE E 211 N ASN E 212 1555 1555 1.33
LINK C ARG E 226 N MSE E 227 1555 1555 1.33
LINK C MSE E 227 N ALA E 228 1555 1555 1.33
LINK C GLY E 240 N MSE E 241 1555 1555 1.33
LINK C MSE E 241 N HIS E 242 1555 1555 1.33
LINK C ILE E 246 N MSE E 247 1555 1555 1.33
LINK C MSE E 247 N THR E 248 1555 1555 1.33
LINK C ASP E 249 N MSE E 250 1555 1555 1.33
LINK C MSE E 250 N THR E 251 1555 1555 1.33
LINK C THR E 305 N MSE E 306 1555 1555 1.33
LINK C MSE E 306 N PRO E 307 1555 1555 1.34
LINK C THR E 368 N MSE E 369 1555 1555 1.33
LINK C MSE E 369 N ASN E 370 1555 1555 1.33
LINK C ALA E 435 N MSE E 436 1555 1555 1.33
LINK C MSE E 436 N LEU E 437 1555 1555 1.33
LINK C MSE F 1 N ILE F 2 1555 1555 1.33
LINK C LEU F 15 N MSE F 16 1555 1555 1.33
LINK C MSE F 16 N ALA F 17 1555 1555 1.33
LINK C ARG F 33 N MSE F 34 1555 1555 1.33
LINK C MSE F 34 N GLN F 35 1555 1555 1.33
LINK C ALA F 52 N MSE F 53 1555 1555 1.33
LINK C MSE F 53 N VAL F 54 1555 1555 1.33
LINK C ASP F 84 N MSE F 85 1555 1555 1.33
LINK C MSE F 85 N ILE F 86 1555 1555 1.33
LINK C PHE F 194 N MSE F 195 1555 1555 1.33
LINK C MSE F 195 N GLU F 196 1555 1555 1.33
LINK C VAL F 208 N MSE F 209 1555 1555 1.33
LINK C MSE F 209 N PHE F 210 1555 1555 1.33
LINK C PHE F 210 N MSE F 211 1555 1555 1.33
LINK C MSE F 211 N ASN F 212 1555 1555 1.33
LINK C ARG F 226 N MSE F 227 1555 1555 1.33
LINK C MSE F 227 N ALA F 228 1555 1555 1.33
LINK C GLY F 240 N MSE F 241 1555 1555 1.33
LINK C MSE F 241 N HIS F 242 1555 1555 1.33
LINK C ILE F 246 N MSE F 247 1555 1555 1.33
LINK C MSE F 247 N THR F 248 1555 1555 1.33
LINK C ASP F 249 N MSE F 250 1555 1555 1.33
LINK C MSE F 250 N THR F 251 1555 1555 1.33
LINK C THR F 305 N MSE F 306 1555 1555 1.33
LINK C MSE F 306 N PRO F 307 1555 1555 1.34
LINK C THR F 368 N MSE F 369 1555 1555 1.33
LINK C MSE F 369 N ASN F 370 1555 1555 1.33
LINK C ALA F 435 N MSE F 436 1555 1555 1.33
LINK C MSE F 436 N LEU F 437 1555 1555 1.33
LINK C ARG G 9 N MSE G 10 1555 1555 1.33
LINK C MSE G 10 N GLU G 11 1555 1555 1.33
LINK C LEU G 36 N MSE G 37 1555 1555 1.33
LINK C MSE G 37 N ARG G 38 1555 1555 1.33
LINK C ALA G 61 N MSE G 62 1555 1555 1.33
LINK C MSE G 62 N LYS G 63 1555 1555 1.33
LINK C ILE G 97 N MSE G 98 1555 1555 1.33
LINK C MSE G 98 N SER G 99 1555 1555 1.33
LINK C LEU G 104 N MSE G 105 1555 1555 1.33
LINK C MSE G 105 N ASN G 106 1555 1555 1.33
LINK C LEU G 155 N MSE G 156 1555 1555 1.33
LINK C MSE G 156 N ALA G 157 1555 1555 1.33
LINK C TYR G 172 N MSE G 173 1555 1555 1.33
LINK C MSE G 173 N THR G 174 1555 1555 1.33
LINK C LYS G 186 N MSE G 187 1555 1555 1.33
LINK C MSE G 187 N LYS G 188 1555 1555 1.33
LINK C ASN G 205 N MSE G 206 1555 1555 1.33
LINK C GLU H 39 N MSE H 40 1555 1555 1.33
LINK C MSE H 40 N ALA H 41 1555 1555 1.33
CISPEP 1 ASP A 329 SER A 330 0 2.45
CISPEP 2 PHE A 425 PRO A 426 0 -2.54
CISPEP 3 ASP B 329 SER B 330 0 4.07
CISPEP 4 PHE B 425 PRO B 426 0 -5.54
CISPEP 5 ASP C 329 SER C 330 0 4.00
CISPEP 6 PHE C 425 PRO C 426 0 -4.57
CISPEP 7 THR D 248 ASP D 249 0 -0.42
CISPEP 8 GLN D 339 PRO D 340 0 -2.89
CISPEP 9 THR E 248 ASP E 249 0 -2.36
CISPEP 10 GLN E 339 PRO E 340 0 1.25
CISPEP 11 THR F 248 ASP F 249 0 -0.61
CISPEP 12 GLN F 339 PRO F 340 0 -1.13
CISPEP 13 THR H 70 PRO H 71 0 0.62
SITE 1 AC1 4 HIS A 243 GLN A 244 LYS A 247 PHE A 506
SITE 1 AC2 4 PHE B 234 GLY B 235 ARG B 262 ARG E 350
SITE 1 AC3 4 LEU B 419 ASN B 429 TRP B 430 ILE B 431
SITE 1 AC4 4 HIS D 75 GLN D 78 TYR D 108 HOH D 723
SITE 1 AC5 2 TYR D 418 GLY F 293
SITE 1 AC6 17 ASP C 206 TYR C 444 HOH C 809 HOH C 819
SITE 2 AC6 17 HOH C 894 GLU F 83 ASP F 176 ARG F 206
SITE 3 AC6 17 LYS F 239 GOL F 504 HOH F 619 HOH F 648
SITE 4 AC6 17 HOH F 661 HOH F 687 HOH F 710 HOH F 714
SITE 5 AC6 17 HOH F 721
SITE 1 AC7 8 ASN C 271 GLN D 200 ASP F 122 TYR F 123
SITE 2 AC7 8 ASP F 125 GLU F 126 ARG F 290 ARG F 292
SITE 1 AC8 6 LYS C 200 GLN C 379 THR F 169 ASP F 175
SITE 2 AC8 6 ASP F 176 HOH F 819
SITE 1 AC9 6 GLU C 440 GLU F 238 GLY F 240 B3P F 501
SITE 2 AC9 6 HOH F 634 HOH F 757
SITE 1 BC1 5 ASN D 99 ASP F 172 GLY F 359 LYS F 360
SITE 2 BC1 5 THR F 361
SITE 1 BC2 2 THR G 181 HOH G 436
CRYST1 127.980 128.480 225.930 90.00 90.00 90.00 P 21 21 21 12
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 0.007814 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007783 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004426 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
