HEADER CHAPERONE 31-MAR-11 2YEY
TITLE CRYSTAL STRUCTURE OF THE ALLOSTERIC-DEFECTIVE CHAPERONIN
TITLE 2 GROEL E434K MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 60 KDA CHAPERONIN;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N;
COMPND 4 SYNONYM: GROEL PROTEIN, PROTEIN CPN60;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: POF39
KEYWDS CHAPERONE, CHAPERONIN, COOPERATIVITY, TWINNING, LOW-RESOLUTION
KEYWDS 2 REFINEMENT
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CABO-BILBAO,A.E.MECHALY,J.AGIRRE,S.SPINELLI,B.SOT,A.MUGA,
AUTHOR 2 D.M.A.GUERIN
REVDAT 1 18-MAY-11 2YEY 0
SPRSDE 18-MAY-11 2YEY 3FBH
JRNL AUTH A.CABO-BILBAO,A.E.MECHALY,J.AGIRRE,S.SPINELLI,B.SOT,A.MUGA,
JRNL AUTH 2 D.M.A.GUERIN
JRNL TITL CRYSTAL STRUCTURE OF THE ALLOSTERIC-DEFECTIVE CHAPERONIN
JRNL TITL 2 GROELE434K MUTANT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 4.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 4.500
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.992
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.93
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.44
REMARK 3 NUMBER OF REFLECTIONS : 87551
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1653
REMARK 3 R VALUE (WORKING SET) : 0.1669
REMARK 3 FREE R VALUE : 0.2397
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.4
REMARK 3 FREE R VALUE TEST SET COUNT : 4012
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 19.9919 - 11.4462 0.92 8025 195 0.1708 0.3505
REMARK 3 2 11.4462 - 9.3882 0.93 8241 187 0.0906 0.1782
REMARK 3 3 9.3882 - 8.2979 0.93 8195 221 0.0859 0.1392
REMARK 3 4 8.2979 - 7.5846 0.94 8269 177 0.1121 0.1927
REMARK 3 5 7.5846 - 7.0668 0.94 8210 207 0.1343 0.1710
REMARK 3 6 7.0668 - 6.6665 0.94 8299 198 0.1514 0.2080
REMARK 3 7 6.6665 - 6.3438 0.94 8260 199 0.1737 0.2635
REMARK 3 8 6.3438 - 6.0757 0.94 8309 191 0.1905 0.2779
REMARK 3 9 6.0757 - 5.8479 0.95 8298 180 0.1962 0.3191
REMARK 3 10 5.8479 - 5.6508 0.95 8393 176 0.1981 0.2867
REMARK 3 11 5.6508 - 5.4779 0.95 8331 186 0.2086 0.2887
REMARK 3 12 5.4779 - 5.3243 0.95 8318 192 0.2077 0.3093
REMARK 3 13 5.3243 - 5.1866 0.95 8345 197 0.2101 0.2875
REMARK 3 14 5.1866 - 5.0622 0.95 8202 207 0.2145 0.2759
REMARK 3 15 5.0622 - 4.9489 0.95 8527 197 0.2069 0.2494
REMARK 3 16 4.9489 - 4.8451 0.95 8343 210 0.2144 0.2618
REMARK 3 17 4.8451 - 4.7495 0.95 8298 191 0.2146 0.3098
REMARK 3 18 4.7495 - 4.6610 0.95 8232 199 0.2198 0.2892
REMARK 3 19 4.6610 - 4.5788 0.95 8412 198 0.2308 0.2790
REMARK 3 20 4.5788 - 4.5021 0.95 8259 192 0.2362 0.2802
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 : 0.83
REMARK 3 K_SOL : 0.316
REMARK 3 B_SOL : 99
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.75
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.2812
REMARK 3 B22 (A**2) : -8.2812
REMARK 3 B33 (A**2) : 16.5623
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : 0.0000
REMARK 3 B23 (A**2) : 0.0000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: 0.5
REMARK 3 OPERATOR: H,-H-K,-L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.029 57208
REMARK 3 ANGLE : 2.298 73416
REMARK 3 CHIRALITY : 0.111 8932
REMARK 3 PLANARITY : 0.013 9618
REMARK 3 DIHEDRAL : 15.014 20524
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 75
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 2:133)
REMARK 3 ORIGIN FOR THE GROUP (A): -17.4320 -33.1811 -35.0454
REMARK 3 T TENSOR
REMARK 3 T11: 0.9744 T22: 0.8018
REMARK 3 T33: 1.0112 T12: -0.1431
REMARK 3 T13: 0.0413 T23: -0.0421
REMARK 3 L TENSOR
REMARK 3 L11: 0.3455 L22: 0.0572
REMARK 3 L33: 0.8417 L12: -0.1599
REMARK 3 L13: -0.1202 L23: 0.2847
REMARK 3 S TENSOR
REMARK 3 S11: -0.0152 S12: -0.0368 S13: -0.0970
REMARK 3 S21: -0.0616 S22: -0.1391 S23: 0.1391
REMARK 3 S31: 0.2720 S32: 0.0089 S33: 0.0594
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 134:179)
REMARK 3 ORIGIN FOR THE GROUP (A): -21.9994 -62.1402 -22.2359
REMARK 3 T TENSOR
REMARK 3 T11: 1.2829 T22: 0.8308
REMARK 3 T33: 1.5941 T12: -0.0441
REMARK 3 T13: 0.3592 T23: 0.0583
REMARK 3 L TENSOR
REMARK 3 L11: 0.7964 L22: 0.4181
REMARK 3 L33: 0.5052 L12: -0.0696
REMARK 3 L13: 0.3841 L23: -0.3866
REMARK 3 S TENSOR
REMARK 3 S11: -0.4535 S12: -0.1636 S13: -0.5613
REMARK 3 S21: -0.5233 S22: 0.1483 S23: -0.2310
REMARK 3 S31: -0.2343 S32: 0.0606 S33: 0.1439
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 180:296)
REMARK 3 ORIGIN FOR THE GROUP (A): -18.5045 -63.0443 -51.3527
REMARK 3 T TENSOR
REMARK 3 T11: 1.0572 T22: 0.7585
REMARK 3 T33: 1.3325 T12: -0.0237
REMARK 3 T13: 0.4134 T23: -0.1167
REMARK 3 L TENSOR
REMARK 3 L11: 0.1955 L22: 0.6661
REMARK 3 L33: 0.1005 L12: 0.2255
REMARK 3 L13: -0.0266 L23: -0.1958
REMARK 3 S TENSOR
REMARK 3 S11: 0.2250 S12: 0.2104 S13: -0.0258
REMARK 3 S21: 0.0188 S22: -0.0712 S23: -0.2592
REMARK 3 S31: -0.2565 S32: -0.0482 S33: -0.0462
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 297:338)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.7202 -69.7859 -52.3384
REMARK 3 T TENSOR
REMARK 3 T11: 0.9921 T22: 0.8222
REMARK 3 T33: 1.1916 T12: 0.1465
REMARK 3 T13: 0.2349 T23: -0.2485
REMARK 3 L TENSOR
REMARK 3 L11: 0.0996 L22: 0.0143
REMARK 3 L33: 0.0081 L12: 0.0767
REMARK 3 L13: -0.1004 L23: 0.0068
REMARK 3 S TENSOR
REMARK 3 S11: 0.3070 S12: 0.0267 S13: -0.4174
REMARK 3 S21: -0.1691 S22: 0.2593 S23: 0.0609
REMARK 3 S31: 0.0875 S32: -0.0410 S33: -0.0278
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 339:458)
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7106 -54.1237 -28.1756
REMARK 3 T TENSOR
REMARK 3 T11: 1.2144 T22: 0.7505
REMARK 3 T33: 1.3979 T12: 0.0610
REMARK 3 T13: 0.0154 T23: -0.1766
REMARK 3 L TENSOR
REMARK 3 L11: 0.4340 L22: 0.0390
REMARK 3 L33: 0.0062 L12: 0.3130
REMARK 3 L13: -0.1614 L23: 0.0890
REMARK 3 S TENSOR
REMARK 3 S11: -0.1874 S12: -0.1601 S13: -0.5966
REMARK 3 S21: 0.1794 S22: -0.3303 S23: 0.3358
REMARK 3 S31: -0.0045 S32: 0.0748 S33: 0.3281
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 459:493)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.6027 -38.5063 -10.4247
REMARK 3 T TENSOR
REMARK 3 T11: 1.1247 T22: 0.6782
REMARK 3 T33: 0.4529 T12: -0.1911
REMARK 3 T13: 0.0901 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 0.1401 L22: 0.6303
REMARK 3 L33: 0.2267 L12: 0.0391
REMARK 3 L13: 0.1258 L23: 0.3213
REMARK 3 S TENSOR
REMARK 3 S11: -0.1825 S12: -0.1360 S13: 0.0057
REMARK 3 S21: 0.4876 S22: -0.1817 S23: 0.0261
REMARK 3 S31: -0.3313 S32: 0.0058 S33: 0.1006
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 494:525)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.9359 -35.9420 -35.4276
REMARK 3 T TENSOR
REMARK 3 T11: 1.3475 T22: 0.7930
REMARK 3 T33: 1.3343 T12: 0.0575
REMARK 3 T13: -0.0598 T23: 0.1530
REMARK 3 L TENSOR
REMARK 3 L11: 0.0311 L22: 0.4661
REMARK 3 L33: 0.3703 L12: -0.1247
REMARK 3 L13: -0.0525 L23: 0.2286
REMARK 3 S TENSOR
REMARK 3 S11: -0.0869 S12: 0.1637 S13: -0.3985
REMARK 3 S21: 0.0979 S22: -0.0975 S23: 0.2921
REMARK 3 S31: -0.1186 S32: -0.0093 S33: -0.0046
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 2:30)
REMARK 3 ORIGIN FOR THE GROUP (A): -44.4137 -27.0361 -37.4320
REMARK 3 T TENSOR
REMARK 3 T11: 0.6764 T22: 0.4850
REMARK 3 T33: 1.3266 T12: -0.1149
REMARK 3 T13: -0.0327 T23: 0.0502
REMARK 3 L TENSOR
REMARK 3 L11: 0.7635 L22: 0.0146
REMARK 3 L33: 0.0872 L12: 0.0969
REMARK 3 L13: 0.2106 L23: 0.0390
REMARK 3 S TENSOR
REMARK 3 S11: -0.4384 S12: 0.0767 S13: 0.4805
REMARK 3 S21: 0.1111 S22: -0.0327 S23: 0.1523
REMARK 3 S31: -0.3056 S32: -0.1060 S33: 0.2841
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 31:88)
REMARK 3 ORIGIN FOR THE GROUP (A): -56.2630 -34.2071 -43.8393
REMARK 3 T TENSOR
REMARK 3 T11: 1.1251 T22: 0.7060
REMARK 3 T33: 1.2381 T12: -0.1928
REMARK 3 T13: 0.0368 T23: -0.1152
REMARK 3 L TENSOR
REMARK 3 L11: 0.2113 L22: 0.2794
REMARK 3 L33: 0.3594 L12: -0.2059
REMARK 3 L13: -0.0330 L23: -0.0319
REMARK 3 S TENSOR
REMARK 3 S11: -0.0174 S12: 0.0228 S13: -0.0606
REMARK 3 S21: 0.3236 S22: -0.5066 S23: -0.1197
REMARK 3 S31: 0.4045 S32: -0.1027 S33: 0.2103
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 89:133)
REMARK 3 ORIGIN FOR THE GROUP (A): -49.8848 -34.7589 -22.5565
REMARK 3 T TENSOR
REMARK 3 T11: 1.2568 T22: 0.8404
REMARK 3 T33: 1.2728 T12: 0.0097
REMARK 3 T13: -0.0288 T23: 0.1424
REMARK 3 L TENSOR
REMARK 3 L11: 0.7724 L22: 1.1092
REMARK 3 L33: 0.1246 L12: 0.4200
REMARK 3 L13: -0.3296 L23: -0.1393
REMARK 3 S TENSOR
REMARK 3 S11: -0.0237 S12: -0.1284 S13: -0.5392
REMARK 3 S21: -0.6706 S22: -0.0416 S23: -0.9049
REMARK 3 S31: -0.1535 S32: -0.1341 S33: 0.2109
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 134:352)
REMARK 3 ORIGIN FOR THE GROUP (A): -57.2871 -63.4357 -47.9460
REMARK 3 T TENSOR
REMARK 3 T11: 1.0465 T22: 0.9366
REMARK 3 T33: 1.0513 T12: -0.1771
REMARK 3 T13: -0.0462 T23: -0.0522
REMARK 3 L TENSOR
REMARK 3 L11: 0.8886 L22: 0.0140
REMARK 3 L33: 0.6232 L12: 0.0405
REMARK 3 L13: 0.0496 L23: -0.0629
REMARK 3 S TENSOR
REMARK 3 S11: 0.1992 S12: 0.0931 S13: 0.2239
REMARK 3 S21: 0.0321 S22: -0.0387 S23: -0.0285
REMARK 3 S31: 0.3034 S32: -0.1286 S33: -0.0976
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 353:433)
REMARK 3 ORIGIN FOR THE GROUP (A): -63.2031 -54.9084 -32.0451
REMARK 3 T TENSOR
REMARK 3 T11: 0.9805 T22: 0.8593
REMARK 3 T33: 0.7843 T12: -0.2318
REMARK 3 T13: 0.0062 T23: -0.0802
REMARK 3 L TENSOR
REMARK 3 L11: 0.1811 L22: 0.4248
REMARK 3 L33: 0.0628 L12: -0.1989
REMARK 3 L13: -0.0522 L23: 0.2641
REMARK 3 S TENSOR
REMARK 3 S11: -0.1474 S12: -0.0012 S13: 0.1272
REMARK 3 S21: 0.0698 S22: 0.1312 S23: -0.2571
REMARK 3 S31: 0.1102 S32: -0.0372 S33: 0.0504
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 434:458)
REMARK 3 ORIGIN FOR THE GROUP (A): -57.2589 -29.6075 -21.8995
REMARK 3 T TENSOR
REMARK 3 T11: 1.2163 T22: 1.1353
REMARK 3 T33: 0.9500 T12: -0.0882
REMARK 3 T13: 0.0867 T23: -0.1615
REMARK 3 L TENSOR
REMARK 3 L11: 0.9803 L22: 2.5370
REMARK 3 L33: 3.5038 L12: 0.2938
REMARK 3 L13: 0.7731 L23: -0.5124
REMARK 3 S TENSOR
REMARK 3 S11: -0.0263 S12: -0.2822 S13: 0.1585
REMARK 3 S21: -0.5075 S22: -0.5368 S23: -0.0363
REMARK 3 S31: 0.2614 S32: 0.5128 S33: 0.2070
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 459:525)
REMARK 3 ORIGIN FOR THE GROUP (A): -61.4470 -34.7034 -26.7801
REMARK 3 T TENSOR
REMARK 3 T11: 0.7583 T22: 0.8928
REMARK 3 T33: 0.8905 T12: -0.2657
REMARK 3 T13: 0.1541 T23: -0.1624
REMARK 3 L TENSOR
REMARK 3 L11: 0.7755 L22: 0.5488
REMARK 3 L33: 0.8440 L12: -0.3534
REMARK 3 L13: 0.0393 L23: 0.4434
REMARK 3 S TENSOR
REMARK 3 S11: -0.2133 S12: 0.0608 S13: -0.0712
REMARK 3 S21: 0.0310 S22: -0.1951 S23: 0.5550
REMARK 3 S31: 0.1173 S32: -0.1762 S33: 0.2291
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 2:27)
REMARK 3 ORIGIN FOR THE GROUP (A): -63.5319 -17.7009 -53.0177
REMARK 3 T TENSOR
REMARK 3 T11: 0.8860 T22: 0.9796
REMARK 3 T33: 0.7356 T12: -0.2851
REMARK 3 T13: 0.0772 T23: -0.1782
REMARK 3 L TENSOR
REMARK 3 L11: 3.3512 L22: 2.1563
REMARK 3 L33: 2.0616 L12: -1.6024
REMARK 3 L13: 1.6499 L23: -0.8283
REMARK 3 S TENSOR
REMARK 3 S11: -0.4752 S12: 0.1838 S13: 0.5269
REMARK 3 S21: 0.1609 S22: -0.2812 S23: -0.1825
REMARK 3 S31: 0.1133 S32: -0.2696 S33: 0.4985
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 28:64)
REMARK 3 ORIGIN FOR THE GROUP (A): -70.2272 -16.7398 -73.0727
REMARK 3 T TENSOR
REMARK 3 T11: 1.4741 T22: 1.1837
REMARK 3 T33: 1.0347 T12: -0.1783
REMARK 3 T13: -0.2375 T23: -0.1420
REMARK 3 L TENSOR
REMARK 3 L11: 0.4505 L22: 0.4575
REMARK 3 L33: 0.1416 L12: 0.0139
REMARK 3 L13: -0.2290 L23: -0.0436
REMARK 3 S TENSOR
REMARK 3 S11: 0.2535 S12: 0.1757 S13: -0.3639
REMARK 3 S21: -0.2785 S22: -0.1988 S23: 0.0987
REMARK 3 S31: -0.0006 S32: -0.2732 S33: -0.0244
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 65:156)
REMARK 3 ORIGIN FOR THE GROUP (A): -82.9594 -22.9312 -58.5946
REMARK 3 T TENSOR
REMARK 3 T11: 0.6699 T22: 1.0655
REMARK 3 T33: 1.0909 T12: -0.2121
REMARK 3 T13: 0.0151 T23: -0.3259
REMARK 3 L TENSOR
REMARK 3 L11: 0.2000 L22: 1.1361
REMARK 3 L33: 0.6118 L12: 0.5378
REMARK 3 L13: -0.1636 L23: -0.2360
REMARK 3 S TENSOR
REMARK 3 S11: -0.1365 S12: 0.3178 S13: -0.0197
REMARK 3 S21: -0.0525 S22: -0.0318 S23: 0.2275
REMARK 3 S31: 0.0778 S32: -0.6442 S33: 0.0771
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 157:246)
REMARK 3 ORIGIN FOR THE GROUP (A): -78.1379 -44.8445 -79.1740
REMARK 3 T TENSOR
REMARK 3 T11: 1.4517 T22: 1.4082
REMARK 3 T33: 1.7114 T12: -0.1798
REMARK 3 T13: 0.0080 T23: 0.0997
REMARK 3 L TENSOR
REMARK 3 L11: 0.5293 L22: 0.1348
REMARK 3 L33: 0.7704 L12: 0.2112
REMARK 3 L13: 0.2505 L23: 0.2520
REMARK 3 S TENSOR
REMARK 3 S11: -0.4461 S12: 0.0710 S13: 0.3234
REMARK 3 S21: -0.1491 S22: -0.3065 S23: -0.2041
REMARK 3 S31: -0.0583 S32: 0.1506 S33: 0.3423
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 247:281)
REMARK 3 ORIGIN FOR THE GROUP (A): -65.8400 -48.3876 -73.1993
REMARK 3 T TENSOR
REMARK 3 T11: 1.5048 T22: 1.6216
REMARK 3 T33: 1.7220 T12: -0.2181
REMARK 3 T13: 0.2863 T23: 0.4742
REMARK 3 L TENSOR
REMARK 3 L11: 0.7409 L22: 0.5192
REMARK 3 L33: 1.3679 L12: 0.0340
REMARK 3 L13: -0.6667 L23: 0.3405
REMARK 3 S TENSOR
REMARK 3 S11: -0.5292 S12: 0.0877 S13: -0.0772
REMARK 3 S21: -0.0665 S22: -0.3269 S23: -0.1446
REMARK 3 S31: 0.5255 S32: 0.2006 S33: 0.6205
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 282:312)
REMARK 3 ORIGIN FOR THE GROUP (A): -75.3309 -61.3501 -70.9264
REMARK 3 T TENSOR
REMARK 3 T11: 1.6013 T22: 1.0425
REMARK 3 T33: 1.0135 T12: -0.1171
REMARK 3 T13: 0.2919 T23: 0.1801
REMARK 3 L TENSOR
REMARK 3 L11: 0.9867 L22: 0.5026
REMARK 3 L33: 1.2122 L12: 0.4092
REMARK 3 L13: -0.5514 L23: -0.0348
REMARK 3 S TENSOR
REMARK 3 S11: -0.0082 S12: -0.2291 S13: -0.1552
REMARK 3 S21: 0.4334 S22: -0.3432 S23: -0.2838
REMARK 3 S31: -0.1541 S32: 0.1390 S33: 0.2926
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 313:354)
REMARK 3 ORIGIN FOR THE GROUP (A): -84.0797 -54.6936 -76.6858
REMARK 3 T TENSOR
REMARK 3 T11: 1.1791 T22: 0.8524
REMARK 3 T33: 0.7919 T12: -0.2224
REMARK 3 T13: 0.1027 T23: -0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 1.7764 L22: 1.2152
REMARK 3 L33: 1.2018 L12: -0.6889
REMARK 3 L13: -0.3614 L23: -0.1996
REMARK 3 S TENSOR
REMARK 3 S11: 0.1358 S12: -0.1344 S13: 0.1925
REMARK 3 S21: -0.3606 S22: -0.3434 S23: -0.2364
REMARK 3 S31: 0.2363 S32: -0.3630 S33: 0.0212
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 355:525)
REMARK 3 ORIGIN FOR THE GROUP (A): -87.5983 -24.0297 -62.8025
REMARK 3 T TENSOR
REMARK 3 T11: 0.4985 T22: 0.6651
REMARK 3 T33: 0.7581 T12: -0.0938
REMARK 3 T13: 0.0424 T23: -0.2891
REMARK 3 L TENSOR
REMARK 3 L11: -0.2467 L22: 0.3421
REMARK 3 L33: 1.0571 L12: 0.1688
REMARK 3 L13: 0.2408 L23: -0.1056
REMARK 3 S TENSOR
REMARK 3 S11: 0.0343 S12: -0.1657 S13: 0.3061
REMARK 3 S21: 0.0095 S22: -0.1924 S23: 0.3137
REMARK 3 S31: 0.0729 S32: -0.1632 S33: 0.1559
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN D AND (RESSEQ 2:216)
REMARK 3 ORIGIN FOR THE GROUP (A): -65.2553 -9.3453 -98.9377
REMARK 3 T TENSOR
REMARK 3 T11: 0.8601 T22: 1.0403
REMARK 3 T33: 0.7796 T12: -0.0166
REMARK 3 T13: -0.0979 T23: -0.2036
REMARK 3 L TENSOR
REMARK 3 L11: 0.0220 L22: 0.3612
REMARK 3 L33: 0.2380 L12: 0.1328
REMARK 3 L13: -0.3296 L23: -0.0855
REMARK 3 S TENSOR
REMARK 3 S11: -0.0518 S12: -0.0591 S13: -0.1217
REMARK 3 S21: -0.1898 S22: -0.1289 S23: 0.0590
REMARK 3 S31: -0.1283 S32: -0.3805 S33: 0.1234
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN D AND (RESSEQ 217:338)
REMARK 3 ORIGIN FOR THE GROUP (A): -64.4669 -39.2559-103.4548
REMARK 3 T TENSOR
REMARK 3 T11: 1.5533 T22: 1.5729
REMARK 3 T33: 1.4847 T12: -0.1625
REMARK 3 T13: 0.1890 T23: 0.0325
REMARK 3 L TENSOR
REMARK 3 L11: 2.2882 L22: 0.8653
REMARK 3 L33: 0.1341 L12: 0.3231
REMARK 3 L13: -0.0768 L23: -0.2408
REMARK 3 S TENSOR
REMARK 3 S11: 0.1684 S12: -0.6640 S13: -0.5759
REMARK 3 S21: -0.4133 S22: -0.2538 S23: -0.3347
REMARK 3 S31: 0.0680 S32: -0.0622 S33: -0.0054
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN D AND (RESSEQ 339:525)
REMARK 3 ORIGIN FOR THE GROUP (A): -73.5878 -6.8516-103.6387
REMARK 3 T TENSOR
REMARK 3 T11: 0.2033 T22: -0.2353
REMARK 3 T33: -1.2166 T12: 0.3939
REMARK 3 T13: 0.1416 T23: -1.2728
REMARK 3 L TENSOR
REMARK 3 L11: 0.1175 L22: 0.0424
REMARK 3 L33: 0.3958 L12: 0.2591
REMARK 3 L13: -0.4071 L23: 0.1391
REMARK 3 S TENSOR
REMARK 3 S11: -0.1590 S12: -0.0689 S13: -0.2586
REMARK 3 S21: 0.0386 S22: -0.1419 S23: 0.2836
REMARK 3 S31: -0.0866 S32: -0.2394 S33: 0.1041
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN E AND (RESSEQ 2:179)
REMARK 3 ORIGIN FOR THE GROUP (A): -29.7363 -0.1064-108.0854
REMARK 3 T TENSOR
REMARK 3 T11: 0.6960 T22: 0.7335
REMARK 3 T33: 0.8694 T12: 0.0686
REMARK 3 T13: 0.1134 T23: -0.0592
REMARK 3 L TENSOR
REMARK 3 L11: 1.1968 L22: 0.0917
REMARK 3 L33: 0.6469 L12: 0.5686
REMARK 3 L13: -0.8717 L23: -0.1564
REMARK 3 S TENSOR
REMARK 3 S11: -0.1318 S12: 0.0492 S13: -0.0804
REMARK 3 S21: -0.1480 S22: -0.0887 S23: -0.0181
REMARK 3 S31: 0.1498 S32: -0.1612 S33: 0.1147
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN E AND (RESSEQ 180:267)
REMARK 3 ORIGIN FOR THE GROUP (A): -31.6139 -28.9563-115.1601
REMARK 3 T TENSOR
REMARK 3 T11: 1.5562 T22: 1.3039
REMARK 3 T33: 1.4815 T12: -0.1614
REMARK 3 T13: 0.1205 T23: -0.0625
REMARK 3 L TENSOR
REMARK 3 L11: 0.5887 L22: 0.5122
REMARK 3 L33: 0.5671 L12: -0.0745
REMARK 3 L13: 0.3942 L23: -0.3730
REMARK 3 S TENSOR
REMARK 3 S11: 0.3396 S12: 0.0621 S13: 0.0343
REMARK 3 S21: -0.0145 S22: -0.0357 S23: -0.0137
REMARK 3 S31: 0.1364 S32: 0.2134 S33: -0.0474
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN E AND (RESSEQ 268:354)
REMARK 3 ORIGIN FOR THE GROUP (A): -36.6392 -29.7133-125.9262
REMARK 3 T TENSOR
REMARK 3 T11: 1.8069 T22: 1.3919
REMARK 3 T33: 1.7512 T12: -0.0889
REMARK 3 T13: -0.0184 T23: -0.0787
REMARK 3 L TENSOR
REMARK 3 L11: 0.3350 L22: 0.1897
REMARK 3 L33: 0.3856 L12: -0.0137
REMARK 3 L13: 0.0929 L23: 0.1946
REMARK 3 S TENSOR
REMARK 3 S11: -0.1500 S12: 0.0252 S13: -0.3163
REMARK 3 S21: -0.3466 S22: -0.0176 S23: -0.3075
REMARK 3 S31: 0.0837 S32: -0.2474 S33: 0.0322
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN E AND (RESSEQ 355:493)
REMARK 3 ORIGIN FOR THE GROUP (A): -26.7856 3.8771-118.8208
REMARK 3 T TENSOR
REMARK 3 T11: 1.3819 T22: 1.1554
REMARK 3 T33: 1.3623 T12: -0.0521
REMARK 3 T13: 0.1870 T23: -0.1052
REMARK 3 L TENSOR
REMARK 3 L11: 0.5708 L22: 1.1828
REMARK 3 L33: 0.2943 L12: -0.4962
REMARK 3 L13: -0.1935 L23: 0.3675
REMARK 3 S TENSOR
REMARK 3 S11: 0.1176 S12: -0.1087 S13: -0.2175
REMARK 3 S21: -0.1876 S22: -0.1807 S23: 0.4550
REMARK 3 S31: -0.3197 S32: 0.0515 S33: -0.0039
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN E AND (RESSEQ 494:525)
REMARK 3 ORIGIN FOR THE GROUP (A): -38.8956 1.4494-105.8256
REMARK 3 T TENSOR
REMARK 3 T11: 1.0435 T22: 0.8572
REMARK 3 T33: 0.8507 T12: 0.0002
REMARK 3 T13: 0.1346 T23: 0.0435
REMARK 3 L TENSOR
REMARK 3 L11: 0.8535 L22: 0.4525
REMARK 3 L33: 0.1340 L12: -0.0963
REMARK 3 L13: 0.1439 L23: 0.2091
REMARK 3 S TENSOR
REMARK 3 S11: 0.1255 S12: -0.0614 S13: 0.3357
REMARK 3 S21: -0.2413 S22: 0.0882 S23: -0.0670
REMARK 3 S31: 0.3320 S32: -0.3674 S33: -0.1702
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN F AND (RESSEQ 2:88)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.6859 -8.8176 -82.9936
REMARK 3 T TENSOR
REMARK 3 T11: 0.4805 T22: -0.8536
REMARK 3 T33: 0.5386 T12: -0.2860
REMARK 3 T13: -0.1611 T23: -0.9602
REMARK 3 L TENSOR
REMARK 3 L11: 0.0671 L22: 0.2174
REMARK 3 L33: 0.0160 L12: 0.0908
REMARK 3 L13: 0.1273 L23: -0.0137
REMARK 3 S TENSOR
REMARK 3 S11: -0.0749 S12: 0.2467 S13: -0.3170
REMARK 3 S21: -0.3230 S22: -0.0874 S23: -0.0883
REMARK 3 S31: 0.4878 S32: -0.0497 S33: -0.0187
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN F AND (RESSEQ 89:179)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.6762 -9.0556 -96.5569
REMARK 3 T TENSOR
REMARK 3 T11: 0.8012 T22: 0.9115
REMARK 3 T33: 0.7935 T12: 0.0694
REMARK 3 T13: 0.0423 T23: -0.0979
REMARK 3 L TENSOR
REMARK 3 L11: 0.7595 L22: 1.0032
REMARK 3 L33: 0.7905 L12: -0.2514
REMARK 3 L13: -0.3429 L23: -0.2263
REMARK 3 S TENSOR
REMARK 3 S11: 0.0251 S12: -0.1957 S13: 0.2195
REMARK 3 S21: -0.2214 S22: -0.0469 S23: -0.0580
REMARK 3 S31: 0.2137 S32: 0.2731 S33: -0.0267
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN F AND (RESSEQ 180:338)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7337 -36.7180-102.4047
REMARK 3 T TENSOR
REMARK 3 T11: 0.3416 T22: 1.5104
REMARK 3 T33: -1.6596 T12: -0.1491
REMARK 3 T13: 1.4651 T23: 0.1427
REMARK 3 L TENSOR
REMARK 3 L11: 0.4858 L22: 0.3959
REMARK 3 L33: 0.8890 L12: 0.0333
REMARK 3 L13: -0.1532 L23: 0.2386
REMARK 3 S TENSOR
REMARK 3 S11: -0.2991 S12: -0.1671 S13: 0.3186
REMARK 3 S21: 0.4171 S22: 0.1008 S23: -0.1525
REMARK 3 S31: -0.2638 S32: -0.4351 S33: 0.0036
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN F AND (RESSEQ 339:433)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2345 -20.9790-104.7365
REMARK 3 T TENSOR
REMARK 3 T11: 1.0276 T22: 0.7152
REMARK 3 T33: 0.0921 T12: -0.0580
REMARK 3 T13: 0.3390 T23: -0.0777
REMARK 3 L TENSOR
REMARK 3 L11: 0.1329 L22: 0.3317
REMARK 3 L33: -0.0804 L12: 0.3375
REMARK 3 L13: 0.0037 L23: 0.0720
REMARK 3 S TENSOR
REMARK 3 S11: -0.1867 S12: 0.1605 S13: 0.2180
REMARK 3 S21: 0.1010 S22: 0.0628 S23: -0.0640
REMARK 3 S31: 0.4698 S32: 0.0675 S33: -0.0724
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN F AND (RESSEQ 434:525)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2880 0.9192 -89.6301
REMARK 3 T TENSOR
REMARK 3 T11: 0.7496 T22: 0.7270
REMARK 3 T33: 0.9660 T12: -0.0440
REMARK 3 T13: 0.0461 T23: -0.0586
REMARK 3 L TENSOR
REMARK 3 L11: 0.1981 L22: 0.4478
REMARK 3 L33: 0.4089 L12: 0.1592
REMARK 3 L13: 0.0548 L23: 0.2476
REMARK 3 S TENSOR
REMARK 3 S11: 0.2062 S12: 0.1361 S13: -0.1688
REMARK 3 S21: -0.1216 S22: -0.0302 S23: -0.4247
REMARK 3 S31: 0.1597 S32: 0.0304 S33: -0.0812
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN G AND (RESSEQ 2:64)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4360 -22.6183 -55.3120
REMARK 3 T TENSOR
REMARK 3 T11: 0.9595 T22: 0.6802
REMARK 3 T33: 0.7432 T12: -0.0658
REMARK 3 T13: 0.0120 T23: -0.0501
REMARK 3 L TENSOR
REMARK 3 L11: 0.8671 L22: 0.2458
REMARK 3 L33: 0.8394 L12: 0.0511
REMARK 3 L13: 0.0177 L23: -0.1635
REMARK 3 S TENSOR
REMARK 3 S11: 0.0487 S12: 0.0539 S13: -0.2679
REMARK 3 S21: 0.2935 S22: -0.4052 S23: 0.0432
REMARK 3 S31: 0.3215 S32: -0.1579 S33: 0.1768
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN G AND (RESSEQ 65:216)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6972 -35.0242 -57.8955
REMARK 3 T TENSOR
REMARK 3 T11: 0.4844 T22: 0.2603
REMARK 3 T33: 0.6301 T12: 0.1262
REMARK 3 T13: -0.1030 T23: -0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 0.2579 L22: 0.0895
REMARK 3 L33: 0.3213 L12: 0.1154
REMARK 3 L13: -0.1090 L23: -0.0845
REMARK 3 S TENSOR
REMARK 3 S11: -0.0306 S12: -0.2438 S13: -0.2584
REMARK 3 S21: 0.0384 S22: -0.0545 S23: -0.1136
REMARK 3 S31: -0.1146 S32: -0.1967 S33: 0.0491
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: CHAIN G AND (RESSEQ 217:352)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.4357 -53.6988 -77.6014
REMARK 3 T TENSOR
REMARK 3 T11: 0.6974 T22: 0.5771
REMARK 3 T33: 0.7219 T12: 0.0403
REMARK 3 T13: 0.0814 T23: -0.0279
REMARK 3 L TENSOR
REMARK 3 L11: 0.9066 L22: 0.4229
REMARK 3 L33: 0.5239 L12: 0.2965
REMARK 3 L13: -0.1707 L23: 0.2744
REMARK 3 S TENSOR
REMARK 3 S11: -0.0100 S12: 0.0659 S13: -0.0379
REMARK 3 S21: 0.2356 S22: 0.1469 S23: -0.3733
REMARK 3 S31: 0.2787 S32: 0.0477 S33: -0.0348
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: CHAIN G AND (RESSEQ 353:433)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7520 -40.2652 -59.1421
REMARK 3 T TENSOR
REMARK 3 T11: 0.8869 T22: 0.8691
REMARK 3 T33: 0.9093 T12: 0.1206
REMARK 3 T13: -0.0010 T23: -0.0258
REMARK 3 L TENSOR
REMARK 3 L11: 0.6937 L22: 0.8928
REMARK 3 L33: 0.7928 L12: -0.7984
REMARK 3 L13: -0.2622 L23: 0.1963
REMARK 3 S TENSOR
REMARK 3 S11: -0.2899 S12: 0.0211 S13: -0.2214
REMARK 3 S21: 0.2194 S22: 0.0629 S23: 0.2563
REMARK 3 S31: 0.2459 S32: 0.0624 S33: 0.1811
REMARK 3 TLS GROUP : 40
REMARK 3 SELECTION: CHAIN G AND (RESSEQ 434:525)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.9692 -19.7137 -50.2954
REMARK 3 T TENSOR
REMARK 3 T11: 0.6979 T22: 0.3942
REMARK 3 T33: 0.7996 T12: 0.0401
REMARK 3 T13: -0.1609 T23: 0.0935
REMARK 3 L TENSOR
REMARK 3 L11: 0.7554 L22: 0.0527
REMARK 3 L33: 1.1642 L12: -0.1197
REMARK 3 L13: 0.0960 L23: 0.2447
REMARK 3 S TENSOR
REMARK 3 S11: 0.3767 S12: -0.0382 S13: -0.2521
REMARK 3 S21: -0.1176 S22: -0.3938 S23: -0.2486
REMARK 3 S31: 0.3136 S32: -0.1197 S33: -0.0524
REMARK 3 TLS GROUP : 41
REMARK 3 SELECTION: CHAIN H AND (RESSEQ 2:134)
REMARK 3 ORIGIN FOR THE GROUP (A): -33.5624 -2.5331 -14.2589
REMARK 3 T TENSOR
REMARK 3 T11: 0.7680 T22: 0.5503
REMARK 3 T33: 0.3510 T12: -0.0076
REMARK 3 T13: 0.0094 T23: -0.0489
REMARK 3 L TENSOR
REMARK 3 L11: 0.5982 L22: 0.4632
REMARK 3 L33: 0.1928 L12: 0.0701
REMARK 3 L13: -0.2977 L23: -0.3355
REMARK 3 S TENSOR
REMARK 3 S11: 0.0374 S12: 0.0734 S13: -0.1434
REMARK 3 S21: 0.3315 S22: 0.1404 S23: -0.1087
REMARK 3 S31: -0.0613 S32: -0.1050 S33: -0.0910
REMARK 3 TLS GROUP : 42
REMARK 3 SELECTION: CHAIN H AND (RESSEQ 135:338)
REMARK 3 ORIGIN FOR THE GROUP (A): -29.7342 24.4391 4.2511
REMARK 3 T TENSOR
REMARK 3 T11: 0.4162 T22: 0.9268
REMARK 3 T33: -0.2513 T12: -0.1230
REMARK 3 T13: -0.1432 T23: -0.1243
REMARK 3 L TENSOR
REMARK 3 L11: 0.7009 L22: 0.5244
REMARK 3 L33: 0.9119 L12: 0.0697
REMARK 3 L13: 0.5772 L23: -0.1293
REMARK 3 S TENSOR
REMARK 3 S11: 0.1380 S12: -0.0180 S13: 1.1875
REMARK 3 S21: -0.5858 S22: 0.3918 S23: 0.3941
REMARK 3 S31: 0.2970 S32: 0.0627 S33: -0.0883
REMARK 3 TLS GROUP : 43
REMARK 3 SELECTION: CHAIN H AND (RESSEQ 339:493)
REMARK 3 ORIGIN FOR THE GROUP (A): -28.0005 -1.0122 5.5267
REMARK 3 T TENSOR
REMARK 3 T11: 0.6645 T22: 0.6263
REMARK 3 T33: 0.3601 T12: 0.0221
REMARK 3 T13: -0.0043 T23: 0.0397
REMARK 3 L TENSOR
REMARK 3 L11: 0.9626 L22: 0.3674
REMARK 3 L33: 0.4646 L12: 0.5868
REMARK 3 L13: -0.0887 L23: 0.1326
REMARK 3 S TENSOR
REMARK 3 S11: -0.3723 S12: -0.5518 S13: -0.3460
REMARK 3 S21: -0.5054 S22: 0.2400 S23: -0.1161
REMARK 3 S31: -0.1326 S32: 0.0398 S33: 0.0636
REMARK 3 TLS GROUP : 44
REMARK 3 SELECTION: CHAIN H AND (RESSEQ 494:525)
REMARK 3 ORIGIN FOR THE GROUP (A): -39.0021 -1.7702 -9.9008
REMARK 3 T TENSOR
REMARK 3 T11: 1.2627 T22: 1.0695
REMARK 3 T33: 0.6503 T12: 0.0072
REMARK 3 T13: -0.0370 T23: 0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 0.3305 L22: 0.1194
REMARK 3 L33: 1.1037 L12: 0.0539
REMARK 3 L13: 0.1292 L23: 0.1042
REMARK 3 S TENSOR
REMARK 3 S11: 0.1296 S12: -0.3376 S13: 0.2994
REMARK 3 S21: 0.5818 S22: -0.2531 S23: 0.0862
REMARK 3 S31: 0.3847 S32: 0.6072 S33: 0.1029
REMARK 3 TLS GROUP : 45
REMARK 3 SELECTION: CHAIN I AND (RESSEQ 2:179)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.1725 9.6723 -25.1114
REMARK 3 T TENSOR
REMARK 3 T11: 0.6344 T22: 0.4946
REMARK 3 T33: 0.6881 T12: 0.0114
REMARK 3 T13: -0.0180 T23: 0.0490
REMARK 3 L TENSOR
REMARK 3 L11: 0.2935 L22: 0.5231
REMARK 3 L33: 0.9006 L12: 0.3411
REMARK 3 L13: 0.3023 L23: 0.4709
REMARK 3 S TENSOR
REMARK 3 S11: 0.0931 S12: -0.0383 S13: 0.0102
REMARK 3 S21: -0.1522 S22: -0.0855 S23: -0.3098
REMARK 3 S31: 0.0279 S32: 0.0258 S33: -0.0048
REMARK 3 TLS GROUP : 46
REMARK 3 SELECTION: CHAIN I AND (RESSEQ 180:458)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.1806 27.7029 -12.1522
REMARK 3 T TENSOR
REMARK 3 T11: 0.9945 T22: 1.0526
REMARK 3 T33: 1.1695 T12: -0.0185
REMARK 3 T13: -0.2149 T23: -0.1017
REMARK 3 L TENSOR
REMARK 3 L11: 0.2549 L22: 0.4736
REMARK 3 L33: 0.1790 L12: -0.1660
REMARK 3 L13: -0.1009 L23: 0.0023
REMARK 3 S TENSOR
REMARK 3 S11: -0.1678 S12: -0.2663 S13: -0.0172
REMARK 3 S21: -0.1395 S22: 0.0615 S23: 0.2189
REMARK 3 S31: -0.1264 S32: 0.1589 S33: -0.0180
REMARK 3 TLS GROUP : 47
REMARK 3 SELECTION: CHAIN I AND (RESSEQ 459:525)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3648 1.7926 -25.8400
REMARK 3 T TENSOR
REMARK 3 T11: 0.7516 T22: 0.6171
REMARK 3 T33: 0.8596 T12: -0.0759
REMARK 3 T13: -0.2506 T23: -0.0497
REMARK 3 L TENSOR
REMARK 3 L11: 0.0052 L22: 0.4298
REMARK 3 L33: 0.2832 L12: 0.0583
REMARK 3 L13: -0.0234 L23: 0.2551
REMARK 3 S TENSOR
REMARK 3 S11: 0.1563 S12: 0.0168 S13: -0.0216
REMARK 3 S21: 0.1296 S22: -0.0980 S23: -0.4231
REMARK 3 S31: 0.1169 S32: 0.0226 S33: -0.0132
REMARK 3 TLS GROUP : 48
REMARK 3 SELECTION: CHAIN J AND (RESSEQ 2:88)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.4174 22.9415 -58.6246
REMARK 3 T TENSOR
REMARK 3 T11: 0.5247 T22: 0.3416
REMARK 3 T33: 0.6246 T12: -0.0404
REMARK 3 T13: -0.0190 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 0.5921 L22: 0.0909
REMARK 3 L33: 0.5001 L12: -0.1756
REMARK 3 L13: -0.2268 L23: -0.1845
REMARK 3 S TENSOR
REMARK 3 S11: 0.1502 S12: 0.0349 S13: 0.5642
REMARK 3 S21: 0.0756 S22: -0.2013 S23: -0.0255
REMARK 3 S31: -0.0953 S32: 0.0471 S33: -0.0051
REMARK 3 TLS GROUP : 49
REMARK 3 SELECTION: CHAIN J AND (RESSEQ 89:133)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0598 14.8450 -55.8578
REMARK 3 T TENSOR
REMARK 3 T11: 0.8857 T22: 0.9626
REMARK 3 T33: 1.2614 T12: 0.0077
REMARK 3 T13: -0.0716 T23: 0.0786
REMARK 3 L TENSOR
REMARK 3 L11: 2.2861 L22: 0.6272
REMARK 3 L33: 0.6294 L12: 0.9277
REMARK 3 L13: -0.3828 L23: -0.2266
REMARK 3 S TENSOR
REMARK 3 S11: -0.1705 S12: -0.6926 S13: -0.8044
REMARK 3 S21: 0.3859 S22: -0.3416 S23: -0.4332
REMARK 3 S31: -0.1207 S32: 0.0779 S33: 0.2557
REMARK 3 TLS GROUP : 50
REMARK 3 SELECTION: CHAIN J AND (RESSEQ 134:316)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.2131 50.4205 -46.2034
REMARK 3 T TENSOR
REMARK 3 T11: 0.8607 T22: 0.7268
REMARK 3 T33: 0.9302 T12: -0.2167
REMARK 3 T13: 0.0381 T23: -0.0741
REMARK 3 L TENSOR
REMARK 3 L11: 1.0453 L22: 1.0313
REMARK 3 L33: 0.4265 L12: 0.2752
REMARK 3 L13: 0.4622 L23: -0.1960
REMARK 3 S TENSOR
REMARK 3 S11: 0.1364 S12: -0.3611 S13: 0.3414
REMARK 3 S21: -0.3630 S22: -0.0461 S23: -0.0638
REMARK 3 S31: 0.1522 S32: -0.0833 S33: 0.0277
REMARK 3 TLS GROUP : 51
REMARK 3 SELECTION: CHAIN J AND (RESSEQ 317:385)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.5411 53.9296 -43.9796
REMARK 3 T TENSOR
REMARK 3 T11: 1.2169 T22: 0.9318
REMARK 3 T33: 1.4292 T12: -0.1890
REMARK 3 T13: 0.1340 T23: -0.1051
REMARK 3 L TENSOR
REMARK 3 L11: 0.1725 L22: 0.6092
REMARK 3 L33: 0.3946 L12: -0.2471
REMARK 3 L13: 0.2291 L23: -0.4173
REMARK 3 S TENSOR
REMARK 3 S11: -0.4944 S12: -0.0986 S13: 0.1345
REMARK 3 S21: 0.2240 S22: 0.0216 S23: -0.5123
REMARK 3 S31: 0.2416 S32: -0.0385 S33: 0.2511
REMARK 3 TLS GROUP : 52
REMARK 3 SELECTION: CHAIN J AND (RESSEQ 386:433)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2314 33.4047 -63.8421
REMARK 3 T TENSOR
REMARK 3 T11: 0.9470 T22: 0.8582
REMARK 3 T33: 1.0769 T12: -0.0325
REMARK 3 T13: -0.1535 T23: -0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.0502 L22: 1.0328
REMARK 3 L33: 0.0203 L12: -0.0972
REMARK 3 L13: 0.0796 L23: -0.2794
REMARK 3 S TENSOR
REMARK 3 S11: 0.0509 S12: -0.3747 S13: -0.2180
REMARK 3 S21: -0.1478 S22: 0.2865 S23: -0.0903
REMARK 3 S31: 0.1235 S32: -0.0127 S33: -0.1673
REMARK 3 TLS GROUP : 53
REMARK 3 SELECTION: CHAIN J AND (RESSEQ 434:525)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.3056 20.1851 -65.2753
REMARK 3 T TENSOR
REMARK 3 T11: 0.8259 T22: 0.5789
REMARK 3 T33: 0.7267 T12: -0.0619
REMARK 3 T13: -0.0531 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 1.1062 L22: 0.8140
REMARK 3 L33: 0.3715 L12: 0.0789
REMARK 3 L13: -0.2831 L23: 0.3491
REMARK 3 S TENSOR
REMARK 3 S11: -0.2467 S12: -0.0192 S13: -0.1950
REMARK 3 S21: -0.2763 S22: 0.0609 S23: -0.4651
REMARK 3 S31: -0.2753 S32: 0.1765 S33: 0.1004
REMARK 3 TLS GROUP : 54
REMARK 3 SELECTION: CHAIN K AND (RESSEQ 2:64)
REMARK 3 ORIGIN FOR THE GROUP (A): -24.9149 31.0665 -77.6192
REMARK 3 T TENSOR
REMARK 3 T11: 0.6618 T22: 0.3641
REMARK 3 T33: 0.6340 T12: -0.0128
REMARK 3 T13: -0.0974 T23: -0.0979
REMARK 3 L TENSOR
REMARK 3 L11: 0.3327 L22: 0.1087
REMARK 3 L33: 0.1670 L12: -0.1130
REMARK 3 L13: 0.0331 L23: -0.0352
REMARK 3 S TENSOR
REMARK 3 S11: -0.1025 S12: 0.0557 S13: 0.3264
REMARK 3 S21: -0.4025 S22: -0.0648 S23: 0.3347
REMARK 3 S31: -0.4061 S32: -0.0003 S33: 0.0803
REMARK 3 TLS GROUP : 55
REMARK 3 SELECTION: CHAIN K AND (RESSEQ 65:112)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.2810 32.3870 -81.5142
REMARK 3 T TENSOR
REMARK 3 T11: 0.9356 T22: 0.4506
REMARK 3 T33: 0.6134 T12: -0.1340
REMARK 3 T13: 0.0179 T23: -0.0769
REMARK 3 L TENSOR
REMARK 3 L11: 0.3046 L22: 0.2261
REMARK 3 L33: 0.4727 L12: -0.2636
REMARK 3 L13: -0.2143 L23: -0.0513
REMARK 3 S TENSOR
REMARK 3 S11: -0.0446 S12: 0.1508 S13: -0.0290
REMARK 3 S21: -0.1097 S22: 0.3273 S23: -0.3433
REMARK 3 S31: -0.2208 S32: -0.0496 S33: -0.1547
REMARK 3 TLS GROUP : 56
REMARK 3 SELECTION: CHAIN K AND (RESSEQ 113:338)
REMARK 3 ORIGIN FOR THE GROUP (A): -18.1494 60.6525 -72.3943
REMARK 3 T TENSOR
REMARK 3 T11: -0.1673 T22: -1.2270
REMARK 3 T33: 1.0193 T12: -1.0423
REMARK 3 T13: -0.0932 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 0.1965 L22: 1.0831
REMARK 3 L33: -0.0903 L12: -0.0832
REMARK 3 L13: -0.2157 L23: 0.2584
REMARK 3 S TENSOR
REMARK 3 S11: 0.3406 S12: 0.1746 S13: 0.3701
REMARK 3 S21: -0.7196 S22: -0.9658 S23: -0.0662
REMARK 3 S31: 0.3019 S32: 0.1561 S33: 0.1076
REMARK 3 TLS GROUP : 57
REMARK 3 SELECTION: CHAIN K AND (RESSEQ 339:433)
REMARK 3 ORIGIN FOR THE GROUP (A): -13.5345 60.1641 -85.6160
REMARK 3 T TENSOR
REMARK 3 T11: 0.4047 T22: 0.3622
REMARK 3 T33: 0.9549 T12: -0.3812
REMARK 3 T13: -0.0373 T23: 0.3630
REMARK 3 L TENSOR
REMARK 3 L11: 0.0764 L22: 0.0692
REMARK 3 L33: 0.4054 L12: -0.0052
REMARK 3 L13: 0.2214 L23: -0.0157
REMARK 3 S TENSOR
REMARK 3 S11: -0.0810 S12: 0.5892 S13: 0.8086
REMARK 3 S21: -0.0388 S22: 0.2004 S23: -0.2048
REMARK 3 S31: 0.5085 S32: 0.4047 S33: 0.0340
REMARK 3 TLS GROUP : 58
REMARK 3 SELECTION: CHAIN K AND (RESSEQ 434:493)
REMARK 3 ORIGIN FOR THE GROUP (A): -18.5510 34.6259-101.3540
REMARK 3 T TENSOR
REMARK 3 T11: 1.3094 T22: 0.8696
REMARK 3 T33: 1.1329 T12: 0.0665
REMARK 3 T13: -0.0218 T23: 0.1077
REMARK 3 L TENSOR
REMARK 3 L11: 1.3418 L22: 0.4367
REMARK 3 L33: 0.7374 L12: -0.6971
REMARK 3 L13: 0.1968 L23: 0.0412
REMARK 3 S TENSOR
REMARK 3 S11: 0.0604 S12: 0.2451 S13: 0.3058
REMARK 3 S21: -0.1208 S22: -0.3591 S23: -0.4255
REMARK 3 S31: -0.2355 S32: 0.0411 S33: 0.2091
REMARK 3 TLS GROUP : 59
REMARK 3 SELECTION: CHAIN K AND (RESSEQ 494:525)
REMARK 3 ORIGIN FOR THE GROUP (A): -11.0687 35.4168 -80.7838
REMARK 3 T TENSOR
REMARK 3 T11: 0.4286 T22: 0.4117
REMARK 3 T33: -0.1483 T12: 0.0202
REMARK 3 T13: 0.0661 T23: 0.1793
REMARK 3 L TENSOR
REMARK 3 L11: 0.2273 L22: 1.0206
REMARK 3 L33: 0.1044 L12: -0.3219
REMARK 3 L13: -0.1080 L23: 0.2348
REMARK 3 S TENSOR
REMARK 3 S11: 0.3967 S12: -0.0212 S13: 0.1147
REMARK 3 S21: -0.6342 S22: -0.2981 S23: 0.0321
REMARK 3 S31: -0.2503 S32: -0.1205 S33: -0.0175
REMARK 3 TLS GROUP : 60
REMARK 3 SELECTION: CHAIN L AND (RESSEQ 2:88)
REMARK 3 ORIGIN FOR THE GROUP (A): -52.5310 31.7118 -74.1113
REMARK 3 T TENSOR
REMARK 3 T11: 0.4360 T22: 0.5783
REMARK 3 T33: 0.5780 T12: 0.0617
REMARK 3 T13: -0.1132 T23: -0.1347
REMARK 3 L TENSOR
REMARK 3 L11: 0.8076 L22: 0.2442
REMARK 3 L33: 0.7793 L12: -0.3359
REMARK 3 L13: -0.0365 L23: 0.1028
REMARK 3 S TENSOR
REMARK 3 S11: -0.1011 S12: 0.1794 S13: 0.2174
REMARK 3 S21: -0.0118 S22: -0.2570 S23: 0.2134
REMARK 3 S31: -0.2336 S32: -0.1385 S33: 0.2217
REMARK 3 TLS GROUP : 61
REMARK 3 SELECTION: CHAIN L AND (RESSEQ 89:133)
REMARK 3 ORIGIN FOR THE GROUP (A): -50.4548 34.4774 -93.2421
REMARK 3 T TENSOR
REMARK 3 T11: 0.9181 T22: 1.0120
REMARK 3 T33: 1.1847 T12: 0.1513
REMARK 3 T13: -0.2529 T23: -0.1837
REMARK 3 L TENSOR
REMARK 3 L11: 1.0137 L22: 0.8764
REMARK 3 L33: 0.8950 L12: -0.4812
REMARK 3 L13: -0.9415 L23: 0.4162
REMARK 3 S TENSOR
REMARK 3 S11: 0.2026 S12: 0.4894 S13: 0.0696
REMARK 3 S21: -0.1741 S22: -0.3196 S23: -0.3086
REMARK 3 S31: 0.1935 S32: -0.2149 S33: 0.0302
REMARK 3 TLS GROUP : 62
REMARK 3 SELECTION: CHAIN L AND (RESSEQ 134:216)
REMARK 3 ORIGIN FOR THE GROUP (A): -67.9582 56.8504 -74.5285
REMARK 3 T TENSOR
REMARK 3 T11: 1.3050 T22: 1.0288
REMARK 3 T33: 1.6494 T12: 0.3370
REMARK 3 T13: -0.2988 T23: -0.1871
REMARK 3 L TENSOR
REMARK 3 L11: 0.2660 L22: 0.6126
REMARK 3 L33: 0.2802 L12: -0.0087
REMARK 3 L13: -0.1576 L23: -0.2366
REMARK 3 S TENSOR
REMARK 3 S11: 0.1284 S12: 0.1256 S13: -0.1210
REMARK 3 S21: 0.2934 S22: -0.3111 S23: -0.4748
REMARK 3 S31: -0.2035 S32: -0.1943 S33: 0.0548
REMARK 3 TLS GROUP : 63
REMARK 3 SELECTION: CHAIN L AND (RESSEQ 217:246)
REMARK 3 ORIGIN FOR THE GROUP (A): -46.0846 66.2646 -56.6001
REMARK 3 T TENSOR
REMARK 3 T11: 1.3423 T22: 1.2135
REMARK 3 T33: 1.2984 T12: 0.2463
REMARK 3 T13: -0.3368 T23: -0.0766
REMARK 3 L TENSOR
REMARK 3 L11: 2.5607 L22: 1.4308
REMARK 3 L33: 1.5098 L12: -0.3076
REMARK 3 L13: 0.0894 L23: -0.7249
REMARK 3 S TENSOR
REMARK 3 S11: -0.0699 S12: -0.2412 S13: 0.0827
REMARK 3 S21: 0.1034 S22: -0.4603 S23: -0.2641
REMARK 3 S31: -0.0416 S32: 0.1360 S33: 0.2096
REMARK 3 TLS GROUP : 64
REMARK 3 SELECTION: CHAIN L AND (RESSEQ 247:282)
REMARK 3 ORIGIN FOR THE GROUP (A): -45.7200 58.8879 -61.5097
REMARK 3 T TENSOR
REMARK 3 T11: 1.3732 T22: 1.2297
REMARK 3 T33: 1.7707 T12: 0.0510
REMARK 3 T13: -0.0222 T23: 0.2302
REMARK 3 L TENSOR
REMARK 3 L11: 1.0677 L22: 0.7075
REMARK 3 L33: 1.9959 L12: 0.2183
REMARK 3 L13: -1.3779 L23: -0.3521
REMARK 3 S TENSOR
REMARK 3 S11: 0.1209 S12: -0.2500 S13: 0.5556
REMARK 3 S21: -0.0940 S22: 0.3724 S23: 0.2946
REMARK 3 S31: -0.1016 S32: 0.0249 S33: -0.4263
REMARK 3 TLS GROUP : 65
REMARK 3 SELECTION: CHAIN L AND (RESSEQ 283:313)
REMARK 3 ORIGIN FOR THE GROUP (A): -45.1472 73.7656 -66.9796
REMARK 3 T TENSOR
REMARK 3 T11: 1.8059 T22: 1.1461
REMARK 3 T33: 1.4275 T12: 0.1689
REMARK 3 T13: 0.1197 T23: -0.0990
REMARK 3 L TENSOR
REMARK 3 L11: 1.5688 L22: 0.8348
REMARK 3 L33: 0.6150 L12: -0.9126
REMARK 3 L13: 0.2176 L23: -0.5665
REMARK 3 S TENSOR
REMARK 3 S11: 0.1275 S12: -0.1410 S13: 0.7257
REMARK 3 S21: 0.2380 S22: -0.1984 S23: -0.5823
REMARK 3 S31: -0.2635 S32: 0.0060 S33: 0.0060
REMARK 3 TLS GROUP : 66
REMARK 3 SELECTION: CHAIN L AND (RESSEQ 314:352)
REMARK 3 ORIGIN FOR THE GROUP (A): -57.3438 71.3855 -69.7275
REMARK 3 T TENSOR
REMARK 3 T11: 1.3277 T22: 0.7088
REMARK 3 T33: 1.2251 T12: 0.4351
REMARK 3 T13: -0.4664 T23: -0.2158
REMARK 3 L TENSOR
REMARK 3 L11: 0.1103 L22: 0.8795
REMARK 3 L33: 0.2070 L12: 0.3224
REMARK 3 L13: -0.1810 L23: -0.4562
REMARK 3 S TENSOR
REMARK 3 S11: 0.4493 S12: 0.0135 S13: -0.1923
REMARK 3 S21: 0.3721 S22: -0.2226 S23: 0.3180
REMARK 3 S31: 0.0019 S32: -0.2189 S33: -0.1903
REMARK 3 TLS GROUP : 67
REMARK 3 SELECTION: CHAIN L AND (RESSEQ 353:385)
REMARK 3 ORIGIN FOR THE GROUP (A): -58.3664 70.0026 -80.9374
REMARK 3 T TENSOR
REMARK 3 T11: 1.3618 T22: 1.2769
REMARK 3 T33: 1.5831 T12: 0.4862
REMARK 3 T13: -0.2555 T23: -0.5244
REMARK 3 L TENSOR
REMARK 3 L11: 2.4003 L22: 1.8888
REMARK 3 L33: 1.2809 L12: 1.5929
REMARK 3 L13: -1.1946 L23: -1.0567
REMARK 3 S TENSOR
REMARK 3 S11: 0.5079 S12: 0.4661 S13: -0.6345
REMARK 3 S21: 0.1801 S22: 0.0496 S23: -0.2696
REMARK 3 S31: 0.1395 S32: -0.0187 S33: -0.1846
REMARK 3 TLS GROUP : 68
REMARK 3 SELECTION: CHAIN L AND (RESSEQ 386:433)
REMARK 3 ORIGIN FOR THE GROUP (A): -65.8809 44.8963 -85.6419
REMARK 3 T TENSOR
REMARK 3 T11: 1.1618 T22: 1.1059
REMARK 3 T33: 1.0939 T12: 0.2318
REMARK 3 T13: -0.0849 T23: -0.1607
REMARK 3 L TENSOR
REMARK 3 L11: 0.2736 L22: 1.0759
REMARK 3 L33: 0.3002 L12: 0.0156
REMARK 3 L13: 0.2323 L23: 0.2595
REMARK 3 S TENSOR
REMARK 3 S11: -0.1635 S12: 0.2270 S13: 0.2276
REMARK 3 S21: -0.0287 S22: 0.0186 S23: 0.3726
REMARK 3 S31: -0.2478 S32: -0.0189 S33: 0.2087
REMARK 3 TLS GROUP : 69
REMARK 3 SELECTION: CHAIN L AND (RESSEQ 434:525)
REMARK 3 ORIGIN FOR THE GROUP (A): -60.7709 33.3321 -90.2251
REMARK 3 T TENSOR
REMARK 3 T11: 0.7510 T22: 0.7860
REMARK 3 T33: 0.8439 T12: 0.1861
REMARK 3 T13: -0.2137 T23: -0.1297
REMARK 3 L TENSOR
REMARK 3 L11: 0.3057 L22: 0.3482
REMARK 3 L33: 0.4009 L12: -0.0359
REMARK 3 L13: 0.1310 L23: -0.1309
REMARK 3 S TENSOR
REMARK 3 S11: 0.1266 S12: 0.0232 S13: -0.1853
REMARK 3 S21: 0.0501 S22: -0.0875 S23: -0.4404
REMARK 3 S31: -0.4541 S32: -0.2250 S33: 0.0635
REMARK 3 TLS GROUP : 70
REMARK 3 SELECTION: CHAIN M AND (RESSEQ 2:179)
REMARK 3 ORIGIN FOR THE GROUP (A): -78.2282 23.2846 -51.7875
REMARK 3 T TENSOR
REMARK 3 T11: 0.9235 T22: 0.9232
REMARK 3 T33: 1.0607 T12: 0.0065
REMARK 3 T13: -0.1165 T23: -0.2003
REMARK 3 L TENSOR
REMARK 3 L11: 0.0868 L22: 0.6060
REMARK 3 L33: 0.3678 L12: -0.1967
REMARK 3 L13: -0.2783 L23: 0.1941
REMARK 3 S TENSOR
REMARK 3 S11: 0.1413 S12: 0.0212 S13: 0.1611
REMARK 3 S21: -0.1420 S22: -0.0837 S23: 0.0863
REMARK 3 S31: -0.2971 S32: 0.0180 S33: 0.0005
REMARK 3 TLS GROUP : 71
REMARK 3 SELECTION: CHAIN M AND (RESSEQ 180:338)
REMARK 3 ORIGIN FOR THE GROUP (A): -71.1603 50.8986 -38.7338
REMARK 3 T TENSOR
REMARK 3 T11: 1.6712 T22: 1.2637
REMARK 3 T33: 1.5396 T12: 0.0433
REMARK 3 T13: -0.3148 T23: -0.1096
REMARK 3 L TENSOR
REMARK 3 L11: 0.7560 L22: 0.0477
REMARK 3 L33: 1.6246 L12: 0.0761
REMARK 3 L13: -0.5650 L23: 0.0668
REMARK 3 S TENSOR
REMARK 3 S11: 0.5585 S12: -0.1190 S13: -0.3899
REMARK 3 S21: 0.4211 S22: -0.2827 S23: -0.2116
REMARK 3 S31: -1.1741 S32: 0.0106 S33: -0.0187
REMARK 3 TLS GROUP : 72
REMARK 3 SELECTION: CHAIN M AND (RESSEQ 339:525)
REMARK 3 ORIGIN FOR THE GROUP (A): -87.3772 28.3872 -51.7712
REMARK 3 T TENSOR
REMARK 3 T11: 0.4500 T22: 0.7076
REMARK 3 T33: 1.0809 T12: 0.3814
REMARK 3 T13: -0.3242 T23: -0.4286
REMARK 3 L TENSOR
REMARK 3 L11: -0.1907 L22: 0.7778
REMARK 3 L33: 0.3300 L12: -0.0896
REMARK 3 L13: 0.0860 L23: 0.0429
REMARK 3 S TENSOR
REMARK 3 S11: -0.8207 S12: 0.2543 S13: 0.5522
REMARK 3 S21: -0.0405 S22: 0.2853 S23: 0.1459
REMARK 3 S31: 0.1816 S32: -0.2614 S33: 0.1112
REMARK 3 TLS GROUP : 73
REMARK 3 SELECTION: CHAIN N AND (RESSEQ 2:88)
REMARK 3 ORIGIN FOR THE GROUP (A): -58.5772 6.5198 -26.6070
REMARK 3 T TENSOR
REMARK 3 T11: 0.8996 T22: 0.8626
REMARK 3 T33: 0.9296 T12: -0.0031
REMARK 3 T13: -0.0802 T23: -0.2311
REMARK 3 L TENSOR
REMARK 3 L11: 0.4937 L22: 0.7036
REMARK 3 L33: 0.2919 L12: -0.3916
REMARK 3 L13: 0.2018 L23: -0.1982
REMARK 3 S TENSOR
REMARK 3 S11: 0.2303 S12: -0.0950 S13: 0.2218
REMARK 3 S21: -0.0924 S22: 0.0013 S23: -0.0518
REMARK 3 S31: 0.3148 S32: 0.0122 S33: -0.0571
REMARK 3 TLS GROUP : 74
REMARK 3 SELECTION: CHAIN N AND (RESSEQ 89:408)
REMARK 3 ORIGIN FOR THE GROUP (A): -69.0382 24.9495 -8.2628
REMARK 3 T TENSOR
REMARK 3 T11: 1.2766 T22: 1.1722
REMARK 3 T33: 1.1741 T12: 0.1167
REMARK 3 T13: -0.1392 T23: -0.1316
REMARK 3 L TENSOR
REMARK 3 L11: 0.9610 L22: 0.1929
REMARK 3 L33: 0.8845 L12: -0.3245
REMARK 3 L13: 0.0456 L23: 0.2753
REMARK 3 S TENSOR
REMARK 3 S11: -0.3817 S12: -0.1198 S13: -0.1257
REMARK 3 S21: -0.1302 S22: 0.2283 S23: -0.0059
REMARK 3 S31: -0.3946 S32: 0.0729 S33: 0.0858
REMARK 3 TLS GROUP : 75
REMARK 3 SELECTION: CHAIN N AND (RESSEQ 409:525)
REMARK 3 ORIGIN FOR THE GROUP (A): -73.6437 -4.1673 -19.4453
REMARK 3 T TENSOR
REMARK 3 T11: 0.7800 T22: 0.8722
REMARK 3 T33: 0.7486 T12: -0.0418
REMARK 3 T13: 0.1053 T23: -0.1908
REMARK 3 L TENSOR
REMARK 3 L11: 0.7675 L22: 0.5215
REMARK 3 L33: 0.4617 L12: -0.1122
REMARK 3 L13: 0.2499 L23: 0.0093
REMARK 3 S TENSOR
REMARK 3 S11: 0.2396 S12: -0.1838 S13: 0.2561
REMARK 3 S21: 0.1345 S22: -0.0820 S23: 0.0191
REMARK 3 S31: 0.0188 S32: -0.3019 S33: 0.0026
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 2YEY COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAR-11.
REMARK 100 THE PDBE ID CODE IS EBI-47885.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 210)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 87597
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.50
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 2.9
REMARK 200 R MERGE (I) : 0.15
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.9
REMARK 200 R MERGE FOR SHELL (I) : 0.47
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1XCK
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.5
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.0
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 303.06133
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 151.53067
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: TETRADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRADECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 49960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 285030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -221.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, G, F, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLU 434 TO LYS
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLU 434 TO LYS
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, GLU 434 TO LYS
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, GLU 434 TO LYS
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, GLU 434 TO LYS
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, GLU 434 TO LYS
REMARK 400 ENGINEERED RESIDUE IN CHAIN G, GLU 434 TO LYS
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, GLU 434 TO LYS
REMARK 400 ENGINEERED RESIDUE IN CHAIN I, GLU 434 TO LYS
REMARK 400 ENGINEERED RESIDUE IN CHAIN J, GLU 434 TO LYS
REMARK 400 ENGINEERED RESIDUE IN CHAIN K, GLU 434 TO LYS
REMARK 400 ENGINEERED RESIDUE IN CHAIN L, GLU 434 TO LYS
REMARK 400 ENGINEERED RESIDUE IN CHAIN M, GLU 434 TO LYS
REMARK 400 ENGINEERED RESIDUE IN CHAIN N, GLU 434 TO LYS
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 OG1 THR A 516 OD1 ASN G 37 2.04
REMARK 500 O GLY I 269 ND2 ASN J 229 2.06
REMARK 500 O ALA C 356 NH2 ARG C 362 2.08
REMARK 500 O LYS K 171 NH1 ARG K 404 2.09
REMARK 500 O LYS L 171 NH1 ARG L 404 2.11
REMARK 500 NZ LYS C 122 O ARG C 430 2.14
REMARK 500 N VAL H 39 O CYS I 519 2.17
REMARK 500 O LYS G 171 NH1 ARG G 404 2.17
REMARK 500 OD1 ASN H 37 OG1 THR I 516 2.19
REMARK 500 N THR C 299 O ASP C 316 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CB SER F 358 OD1 ASP H 167 2554 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS B 519 CB CYS B 519 SG -0.097
REMARK 500 CYS F 458 CB CYS F 458 SG -0.103
REMARK 500 THR I 90 CA THR I 90 CB 0.175
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 47 C - N - CA ANGL. DEV. = 10.4 DEGREES
REMARK 500 LEU A 187 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 LEU A 295 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 PRO B 208 C - N - CA ANGL. DEV. = 12.7 DEGREES
REMARK 500 LEU B 314 CA - CB - CG ANGL. DEV. = -14.0 DEGREES
REMARK 500 LEU B 494 CB - CG - CD1 ANGL. DEV. = -10.2 DEGREES
REMARK 500 LEU B 513 CB - CG - CD2 ANGL. DEV. = -11.7 DEGREES
REMARK 500 CYS B 519 N - CA - C ANGL. DEV. = 16.4 DEGREES
REMARK 500 PRO C 113 C - N - CA ANGL. DEV. = 10.9 DEGREES
REMARK 500 VAL C 136 N - CA - C ANGL. DEV. = -16.6 DEGREES
REMARK 500 PRO C 208 C - N - CA ANGL. DEV. = 10.3 DEGREES
REMARK 500 PRO C 218 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 LEU C 513 CA - CB - CG ANGL. DEV. = -21.9 DEGREES
REMARK 500 LYS D 7 CD - CE - NZ ANGL. DEV. = 16.6 DEGREES
REMARK 500 LEU D 187 CA - CB - CG ANGL. DEV. = 19.8 DEGREES
REMARK 500 PRO D 218 C - N - CA ANGL. DEV. = 12.4 DEGREES
REMARK 500 LYS E 7 CD - CE - NZ ANGL. DEV. = 14.4 DEGREES
REMARK 500 PHE E 44 N - CA - CB ANGL. DEV. = 11.1 DEGREES
REMARK 500 THR E 385 C - N - CA ANGL. DEV. = 16.5 DEGREES
REMARK 500 LEU E 513 CA - CB - CG ANGL. DEV. = -16.6 DEGREES
REMARK 500 PRO F 47 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 PRO F 208 C - N - CA ANGL. DEV. = 11.0 DEGREES
REMARK 500 LEU F 221 CB - CG - CD1 ANGL. DEV. = -11.0 DEGREES
REMARK 500 ASP F 398 CB - CG - OD1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 ASP F 398 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 LEU F 504 CB - CG - CD1 ANGL. DEV. = -14.7 DEGREES
REMARK 500 LEU G 295 CA - CB - CG ANGL. DEV. = 17.2 DEGREES
REMARK 500 LEU G 513 CA - CB - CG ANGL. DEV. = -18.2 DEGREES
REMARK 500 PRO H 33 C - N - CD ANGL. DEV. = -12.9 DEGREES
REMARK 500 LEU H 161 CA - CB - CG ANGL. DEV. = -14.5 DEGREES
REMARK 500 PRO H 218 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500 MET H 233 CB - CG - SD ANGL. DEV. = -18.7 DEGREES
REMARK 500 LEU H 295 CA - CB - CG ANGL. DEV. = 16.4 DEGREES
REMARK 500 LYS H 425 CD - CE - NZ ANGL. DEV. = 14.9 DEGREES
REMARK 500 CYS H 458 CA - CB - SG ANGL. DEV. = 7.7 DEGREES
REMARK 500 PRO H 462 C - N - CA ANGL. DEV. = 10.2 DEGREES
REMARK 500 PRO H 525 C - N - CD ANGL. DEV. = -14.9 DEGREES
REMARK 500 PRO I 208 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 PRO I 218 C - N - CA ANGL. DEV. = 9.8 DEGREES
REMARK 500 LEU I 221 CA - CB - CG ANGL. DEV. = -22.0 DEGREES
REMARK 500 LEU I 504 CB - CG - CD1 ANGL. DEV. = -23.5 DEGREES
REMARK 500 CYS I 519 CA - CB - SG ANGL. DEV. = -12.7 DEGREES
REMARK 500 LEU J 104 CA - CB - CG ANGL. DEV. = -16.3 DEGREES
REMARK 500 PRO J 113 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 PRO J 137 C - N - CA ANGL. DEV. = 9.6 DEGREES
REMARK 500 PRO J 202 C - N - CA ANGL. DEV. = -9.0 DEGREES
REMARK 500 PRO J 208 C - N - CA ANGL. DEV. = 12.2 DEGREES
REMARK 500 LEU J 456 CB - CG - CD1 ANGL. DEV. = -13.8 DEGREES
REMARK 500 LEU J 494 CB - CG - CD1 ANGL. DEV. = -13.4 DEGREES
REMARK 500 LEU J 504 CB - CG - CD1 ANGL. DEV. = -13.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 69 ANGLE DEVIATIONS.
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 ALA A 85 -50.77 -121.39
REMARK 500 GLN A 184 127.72 157.91
REMARK 500 PRO A 202 -150.10 -66.15
REMARK 500 TYR A 203 -44.18 68.26
REMARK 500 LYS A 225 173.54 178.90
REMARK 500 ALA A 243 -14.12 68.20
REMARK 500 VAL A 264 -72.93 -73.46
REMARK 500 VAL A 271 119.08 72.32
REMARK 500 ASP A 328 25.59 -149.72
REMARK 500 ASP A 334 77.10 48.28
REMARK 500 ALA A 383 -28.02 -161.14
REMARK 500 ALA A 384 91.04 72.19
REMARK 500 THR A 385 115.44 101.01
REMARK 500 ASN A 475 31.34 -94.49
REMARK 500 LEU B 183 104.70 -54.74
REMARK 500 GLN B 184 160.20 157.72
REMARK 500 SER B 201 136.54 173.49
REMARK 500 PRO B 202 -169.72 -64.98
REMARK 500 TYR B 203 -42.14 85.30
REMARK 500 LYS B 225 178.02 169.61
REMARK 500 ALA B 243 -20.84 69.81
REMARK 500 ASP B 253 161.08 178.59
REMARK 500 VAL B 271 117.18 38.12
REMARK 500 THR B 313 -163.28 -122.01
REMARK 500 ASP B 328 16.32 -140.70
REMARK 500 ASP B 334 78.57 65.73
REMARK 500 ALA B 383 4.69 -161.15
REMARK 500 ALA B 384 91.49 71.44
REMARK 500 THR B 385 116.65 82.77
REMARK 500 ASN B 475 30.70 -93.26
REMARK 500 ALA C 85 -55.43 -121.70
REMARK 500 LEU C 183 107.50 -59.81
REMARK 500 GLN C 184 127.69 156.93
REMARK 500 PRO C 202 -147.19 -68.34
REMARK 500 TYR C 203 -29.61 68.26
REMARK 500 ILE C 230 0.89 -64.78
REMARK 500 LEU C 234 -55.97 -22.64
REMARK 500 ALA C 243 -24.61 89.66
REMARK 500 VAL C 271 111.76 42.24
REMARK 500 ASP C 328 23.53 -140.69
REMARK 500 ASP C 334 78.47 64.71
REMARK 500 ALA C 383 -3.60 -160.31
REMARK 500 ALA C 384 102.49 73.04
REMARK 500 THR C 385 118.87 78.38
REMARK 500 LEU D 31 143.99 -39.02
REMARK 500 ALA D 85 -53.78 -120.52
REMARK 500 GLN D 184 127.84 158.45
REMARK 500 ASP D 196 41.17 -82.63
REMARK 500 SER D 201 136.87 -177.61
REMARK 500 PRO D 202 -150.69 -64.71
REMARK 500
REMARK 500 THIS ENTRY HAS 210 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR H 385 GLU H 386 -137.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG J 345 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLN A 432 -14.95
REMARK 500 GLY D 256 10.28
REMARK 500 ALA H 163 12.36
REMARK 500 ASP I 359 12.71
REMARK 500 GLY M 431 11.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 PRO A 202 45.2 L L OUTSIDE RANGE
REMARK 500 VAL L 381 24.5 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GR5 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF APO GROEL BY CRYO-ELECTRON
REMARK 900 MICROSCOPY
REMARK 900 RELATED ID: 1SX4 RELATED DB: PDB
REMARK 900 GROEL-GROES-ADP7
REMARK 900 RELATED ID: 1SS8 RELATED DB: PDB
REMARK 900 GROEL
REMARK 900 RELATED ID: 1AON RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ASYMMETRIC CHAPERONIN COMPLEX
REMARK 900 GROEL/GROES/(ADP)7
REMARK 900 RELATED ID: 1GRL RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: GROEL (HSP60 CLASS); CHAIN: NULL;
REMARK 900 ENGINEERED: YES; MUTATION: R13G, A126V
REMARK 900 RELATED ID: 1OEL RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: GROEL (HSP60 CLASS); CHAIN: A, B,
REMARK 900 C, D, E, F, G; ENGINEERED: YES; MUTATION: R13G, A126V
REMARK 900 RELATED ID: 1PCQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GROEL-GROES
REMARK 900 RELATED ID: 1DKD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A
REMARK 900 DODECAMERIC PEPTIDE COMPLEX
REMARK 900 RELATED ID: 2C7C RELATED DB: PDB
REMARK 900 FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM
REMARK 900 COMPLEX (EMD-1180)
REMARK 900 RELATED ID: 1SVT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GROEL14-GROES7-(ADP-ALFX)7
REMARK 900 RELATED ID: 1PF9 RELATED DB: PDB
REMARK 900 GROEL-GROES-ADP
REMARK 900 RELATED ID: 1FY9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HEXA-SUBSTITUTED MUTANT OF
REMARK 900 THEMOLECULAR CHAPERONIN GROEL APICAL DOMAIN
REMARK 900 RELATED ID: 1KID RELATED DB: PDB
REMARK 900 GROEL (HSP60 CLASS) FRAGMENT (APICAL DOMAIN) COMPRISING
REMARK 900 RESIDUES 191-376, MUTANT WITH ALA 262 REPLACED WITH
REMARK 900 LEU AND ILE 267 REPLACED WITH MET
REMARK 900 RELATED ID: 1J4Z RELATED DB: PDB
REMARK 900 STRUCTURAL AND MECHANISTIC BASIS FOR ALLOSTERY IN
REMARK 900 THEBACTERIAL CHAPERONIN GROEL; SEE REMARK 400
REMARK 900 RELATED ID: 1FYA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HEXA-SUBSTITUTED MUTANT OF
REMARK 900 THEMOLECULAR CHAPERONIN GROEL APICAL DOMAIN
REMARK 900 RELATED ID: 1DK7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AN ISOLATED APICAL DOMAIN OF GROEL
REMARK 900 RELATED ID: 2C7D RELATED DB: PDB
REMARK 900 FITTED COORDINATES FOR GROEL-ADP7-GROES CRYO-EM
REMARK 900 COMPLEX (EMD-1181)
REMARK 900 RELATED ID: 1GRU RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF GROES-ADP7-GROEL-ATP7 COMPLEX BY
REMARK 900 CRYO-EM
REMARK 900 RELATED ID: 1JON RELATED DB: PDB
REMARK 900 GROEL (HSP60 CLASS) FRAGMENT COMPRISING RESIDUES 191 - 345
REMARK 900 RELATED ID: 1KP8 RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR GROEL-ASSISTED PROTEIN FOLDING
REMARK 900 FROMTHE CRYSTAL STRUCTURE OF (GROEL-KMGATP)14 AT 2.0 A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1LA1 RELATED DB: PDB
REMARK 900 GRO-EL FRAGMENT (APICAL DOMAIN) COMPRISING RESIDUES 188-379
REMARK 900 RELATED ID: 1MNF RELATED DB: PDB
REMARK 900 DOMAIN MOTIONS IN GROEL UPON BINDING OF AN
REMARK 900 OLIGOPEPTIDE
REMARK 900 RELATED ID: 2CGT RELATED DB: PDB
REMARK 900 GROEL-ADP-GP31 COMPLEX
REMARK 900 RELATED ID: 1KPO RELATED DB: PDB
REMARK 900 STRUCTURAL AND MECHANISTIC BASIS FOR ALLOSTERY IN
REMARK 900 THEBACTERIAL CHAPERONIN GROEL; SEE REMARK 400
REMARK 900 RELATED ID: 1SX3 RELATED DB: PDB
REMARK 900 GROEL14-(ATPGAMMAS)14
REMARK 900 RELATED ID: 1XCK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APO GROEL
REMARK 900 RELATED ID: 2C7E RELATED DB: PDB
REMARK 900 REVISED ATOMIC STRUCTURE FITTING INTO A GROEL(D398A)-
REMARK 900 ATP7 CRYO-EM MAP (EMD 1047)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE 1 IS AN INITIATOR METHIONINE AND IS REMOVED.
DBREF 2YEY A 2 525 UNP P0A6F5 CH60_ECOLI 2 525
DBREF 2YEY B 2 525 UNP P0A6F5 CH60_ECOLI 2 525
DBREF 2YEY C 2 525 UNP P0A6F5 CH60_ECOLI 2 525
DBREF 2YEY D 2 525 UNP P0A6F5 CH60_ECOLI 2 525
DBREF 2YEY E 2 525 UNP P0A6F5 CH60_ECOLI 2 525
DBREF 2YEY F 2 525 UNP P0A6F5 CH60_ECOLI 2 525
DBREF 2YEY G 2 525 UNP P0A6F5 CH60_ECOLI 2 525
DBREF 2YEY H 2 525 UNP P0A6F5 CH60_ECOLI 2 525
DBREF 2YEY I 2 525 UNP P0A6F5 CH60_ECOLI 2 525
DBREF 2YEY J 2 525 UNP P0A6F5 CH60_ECOLI 2 525
DBREF 2YEY K 2 525 UNP P0A6F5 CH60_ECOLI 2 525
DBREF 2YEY L 2 525 UNP P0A6F5 CH60_ECOLI 2 525
DBREF 2YEY M 2 525 UNP P0A6F5 CH60_ECOLI 2 525
DBREF 2YEY N 2 525 UNP P0A6F5 CH60_ECOLI 2 525
SEQADV 2YEY LYS A 434 UNP P0A6F5 GLU 434 ENGINEERED MUTATION
SEQADV 2YEY LYS B 434 UNP P0A6F5 GLU 434 ENGINEERED MUTATION
SEQADV 2YEY LYS C 434 UNP P0A6F5 GLU 434 ENGINEERED MUTATION
SEQADV 2YEY LYS D 434 UNP P0A6F5 GLU 434 ENGINEERED MUTATION
SEQADV 2YEY LYS E 434 UNP P0A6F5 GLU 434 ENGINEERED MUTATION
SEQADV 2YEY LYS F 434 UNP P0A6F5 GLU 434 ENGINEERED MUTATION
SEQADV 2YEY LYS G 434 UNP P0A6F5 GLU 434 ENGINEERED MUTATION
SEQADV 2YEY LYS H 434 UNP P0A6F5 GLU 434 ENGINEERED MUTATION
SEQADV 2YEY LYS I 434 UNP P0A6F5 GLU 434 ENGINEERED MUTATION
SEQADV 2YEY LYS J 434 UNP P0A6F5 GLU 434 ENGINEERED MUTATION
SEQADV 2YEY LYS K 434 UNP P0A6F5 GLU 434 ENGINEERED MUTATION
SEQADV 2YEY LYS L 434 UNP P0A6F5 GLU 434 ENGINEERED MUTATION
SEQADV 2YEY LYS M 434 UNP P0A6F5 GLU 434 ENGINEERED MUTATION
SEQADV 2YEY LYS N 434 UNP P0A6F5 GLU 434 ENGINEERED MUTATION
SEQRES 1 A 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 A 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 A 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 A 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 A 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 A 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 A 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 A 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 A 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 A 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 A 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 A 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 A 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 A 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 A 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 A 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 A 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 A 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 A 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 A 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 A 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 A 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 A 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 A 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 A 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 A 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 A 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 A 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 A 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 A 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 A 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 A 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 A 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 A 524 GLY GLN ASN LYS ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 A 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 A 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 A 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 A 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 A 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 A 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 A 524 THR ASP LEU PRO
SEQRES 1 B 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 B 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 B 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 B 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 B 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 B 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 B 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 B 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 B 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 B 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 B 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 B 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 B 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 B 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 B 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 B 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 B 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 B 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 B 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 B 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 B 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 B 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 B 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 B 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 B 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 B 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 B 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 B 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 B 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 B 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 B 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 B 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 B 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 B 524 GLY GLN ASN LYS ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 B 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 B 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 B 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 B 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 B 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 B 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 B 524 THR ASP LEU PRO
SEQRES 1 C 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 C 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 C 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 C 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 C 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 C 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 C 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 C 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 C 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 C 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 C 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 C 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 C 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 C 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 C 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 C 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 C 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 C 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 C 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 C 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 C 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 C 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 C 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 C 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 C 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 C 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 C 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 C 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 C 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 C 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 C 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 C 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 C 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 C 524 GLY GLN ASN LYS ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 C 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 C 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 C 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 C 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 C 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 C 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 C 524 THR ASP LEU PRO
SEQRES 1 D 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 D 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 D 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 D 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 D 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 D 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 D 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 D 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 D 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 D 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 D 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 D 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 D 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 D 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 D 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 D 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 D 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 D 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 D 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 D 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 D 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 D 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 D 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 D 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 D 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 D 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 D 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 D 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 D 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 D 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 D 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 D 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 D 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 D 524 GLY GLN ASN LYS ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 D 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 D 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 D 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 D 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 D 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 D 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 D 524 THR ASP LEU PRO
SEQRES 1 E 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 E 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 E 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 E 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 E 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 E 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 E 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 E 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 E 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 E 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 E 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 E 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 E 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 E 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 E 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 E 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 E 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 E 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 E 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 E 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 E 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 E 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 E 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 E 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 E 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 E 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 E 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 E 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 E 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 E 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 E 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 E 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 E 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 E 524 GLY GLN ASN LYS ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 E 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 E 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 E 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 E 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 E 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 E 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 E 524 THR ASP LEU PRO
SEQRES 1 F 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 F 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 F 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 F 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 F 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 F 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 F 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 F 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 F 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 F 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 F 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 F 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 F 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 F 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 F 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 F 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 F 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 F 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 F 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 F 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 F 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 F 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 F 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 F 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 F 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 F 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 F 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 F 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 F 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 F 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 F 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 F 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 F 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 F 524 GLY GLN ASN LYS ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 F 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 F 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 F 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 F 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 F 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 F 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 F 524 THR ASP LEU PRO
SEQRES 1 G 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 G 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 G 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 G 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 G 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 G 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 G 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 G 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 G 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 G 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 G 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 G 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 G 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 G 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 G 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 G 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 G 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 G 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 G 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 G 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 G 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 G 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 G 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 G 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 G 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 G 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 G 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 G 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 G 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 G 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 G 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 G 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 G 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 G 524 GLY GLN ASN LYS ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 G 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 G 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 G 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 G 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 G 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 G 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 G 524 THR ASP LEU PRO
SEQRES 1 H 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 H 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 H 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 H 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 H 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 H 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 H 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 H 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 H 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 H 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 H 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 H 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 H 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 H 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 H 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 H 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 H 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 H 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 H 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 H 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 H 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 H 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 H 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 H 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 H 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 H 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 H 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 H 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 H 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 H 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 H 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 H 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 H 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 H 524 GLY GLN ASN LYS ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 H 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 H 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 H 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 H 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 H 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 H 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 H 524 THR ASP LEU PRO
SEQRES 1 I 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 I 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 I 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 I 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 I 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 I 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 I 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 I 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 I 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 I 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 I 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 I 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 I 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 I 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 I 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 I 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 I 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 I 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 I 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 I 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 I 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 I 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 I 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 I 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 I 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 I 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 I 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 I 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 I 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 I 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 I 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 I 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 I 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 I 524 GLY GLN ASN LYS ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 I 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 I 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 I 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 I 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 I 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 I 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 I 524 THR ASP LEU PRO
SEQRES 1 J 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 J 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 J 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 J 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 J 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 J 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 J 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 J 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 J 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 J 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 J 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 J 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 J 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 J 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 J 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 J 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 J 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 J 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 J 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 J 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 J 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 J 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 J 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 J 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 J 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 J 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 J 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 J 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 J 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 J 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 J 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 J 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 J 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 J 524 GLY GLN ASN LYS ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 J 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 J 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 J 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 J 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 J 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 J 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 J 524 THR ASP LEU PRO
SEQRES 1 K 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 K 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 K 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 K 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 K 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 K 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 K 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 K 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 K 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 K 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 K 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 K 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 K 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 K 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 K 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 K 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 K 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 K 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 K 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 K 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 K 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 K 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 K 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 K 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 K 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 K 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 K 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 K 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 K 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 K 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 K 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 K 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 K 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 K 524 GLY GLN ASN LYS ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 K 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 K 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 K 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 K 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 K 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 K 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 K 524 THR ASP LEU PRO
SEQRES 1 L 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 L 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 L 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 L 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 L 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 L 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 L 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 L 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 L 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 L 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 L 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 L 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 L 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 L 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 L 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 L 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 L 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 L 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 L 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 L 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 L 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 L 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 L 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 L 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 L 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 L 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 L 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 L 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 L 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 L 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 L 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 L 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 L 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 L 524 GLY GLN ASN LYS ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 L 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 L 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 L 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 L 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 L 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 L 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 L 524 THR ASP LEU PRO
SEQRES 1 M 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 M 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 M 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 M 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 M 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 M 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 M 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 M 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 M 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 M 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 M 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 M 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 M 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 M 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 M 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 M 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 M 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 M 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 M 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 M 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 M 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 M 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 M 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 M 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 M 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 M 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 M 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 M 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 M 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 M 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 M 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 M 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 M 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 M 524 GLY GLN ASN LYS ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 M 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 M 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 M 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 M 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 M 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 M 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 M 524 THR ASP LEU PRO
SEQRES 1 N 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 N 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 N 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 N 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 N 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 N 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 N 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 N 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 N 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 N 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 N 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 N 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 N 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 N 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 N 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 N 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 N 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 N 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 N 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 N 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 N 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 N 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 N 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 N 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 N 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 N 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 N 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 N 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 N 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 N 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 N 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 N 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 N 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 N 524 GLY GLN ASN LYS ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 N 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 N 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 N 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 N 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 N 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 N 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 N 524 THR ASP LEU PRO
HELIX 1 1 GLY A 9 VAL A 29 1 21
HELIX 2 2 ASP A 52 GLU A 59 1 8
HELIX 3 3 ASP A 64 GLY A 86 1 23
HELIX 4 4 GLY A 88 ALA A 109 1 22
HELIX 5 5 ASN A 112 SER A 135 1 24
HELIX 6 6 ASP A 140 ALA A 152 1 13
HELIX 7 7 ASP A 155 GLY A 170 1 16
HELIX 8 8 MET A 233 LYS A 242 1 10
HELIX 9 9 ALA A 243 LYS A 245 5 3
HELIX 10 10 GLY A 256 THR A 266 1 11
HELIX 11 11 MET A 267 GLY A 269 5 3
HELIX 12 12 PHE A 281 GLY A 297 1 17
HELIX 13 13 GLU A 338 ILE A 353 1 16
HELIX 14 14 SER A 358 GLY A 375 1 18
HELIX 15 15 THR A 385 GLY A 410 1 26
HELIX 16 16 GLY A 416 LEU A 426 1 11
HELIX 17 17 ASN A 433 MET A 447 1 15
HELIX 18 18 GLU A 448 CYS A 458 1 11
HELIX 19 19 GLU A 461 GLY A 471 1 11
HELIX 20 20 THR A 497 THR A 516 1 20
HELIX 21 21 GLY B 9 VAL B 29 1 21
HELIX 22 22 ASP B 52 ILE B 60 1 9
HELIX 23 23 ASP B 64 ALA B 85 1 22
HELIX 24 24 GLY B 88 ALA B 109 1 22
HELIX 25 25 ASN B 112 SER B 135 1 24
HELIX 26 26 ASP B 140 ALA B 152 1 13
HELIX 27 27 ASP B 155 GLY B 170 1 16
HELIX 28 28 MET B 233 LYS B 242 1 10
HELIX 29 29 ALA B 243 LYS B 245 5 3
HELIX 30 30 GLU B 255 THR B 266 1 12
HELIX 31 31 PHE B 281 GLY B 297 1 17
HELIX 32 32 GLU B 338 ALA B 356 1 19
HELIX 33 33 SER B 358 GLY B 375 1 18
HELIX 34 34 THR B 385 GLY B 410 1 26
HELIX 35 35 GLY B 416 LEU B 426 1 11
HELIX 36 36 ASN B 433 MET B 447 1 15
HELIX 37 37 GLU B 448 GLY B 459 1 12
HELIX 38 38 GLU B 461 GLY B 471 1 11
HELIX 39 39 MET B 488 GLY B 492 1 5
HELIX 40 40 THR B 497 THR B 516 1 20
HELIX 41 41 GLY C 9 VAL C 29 1 21
HELIX 42 42 ASP C 52 ILE C 60 1 9
HELIX 43 43 ASP C 64 ALA C 85 1 22
HELIX 44 44 GLY C 88 ALA C 109 1 22
HELIX 45 45 ASN C 112 SER C 135 1 24
HELIX 46 46 ASP C 140 ALA C 152 1 13
HELIX 47 47 ASP C 155 GLY C 170 1 16
HELIX 48 48 ASN C 229 LYS C 242 1 14
HELIX 49 49 GLU C 255 THR C 266 1 12
HELIX 50 50 PHE C 281 THR C 296 1 16
HELIX 51 51 GLU C 338 ALA C 356 1 19
HELIX 52 52 SER C 358 GLY C 375 1 18
HELIX 53 53 THR C 385 GLY C 410 1 26
HELIX 54 54 GLY C 416 LYS C 425 1 10
HELIX 55 55 ASN C 433 MET C 447 1 15
HELIX 56 56 GLU C 448 CYS C 458 1 11
HELIX 57 57 GLU C 461 GLY C 472 1 12
HELIX 58 58 MET C 488 GLY C 492 1 5
HELIX 59 59 THR C 497 THR C 516 1 20
HELIX 60 60 GLY D 9 VAL D 29 1 21
HELIX 61 61 ASP D 52 ARG D 58 1 7
HELIX 62 62 ASP D 64 GLY D 86 1 23
HELIX 63 63 GLY D 88 ALA D 109 1 22
HELIX 64 64 ASN D 112 LEU D 134 1 23
HELIX 65 65 ASP D 140 ALA D 152 1 13
HELIX 66 66 ASP D 155 GLY D 170 1 16
HELIX 67 67 MET D 233 LYS D 242 1 10
HELIX 68 68 GLU D 255 THR D 266 1 12
HELIX 69 69 PHE D 281 GLY D 297 1 17
HELIX 70 70 GLU D 304 GLY D 306 5 3
HELIX 71 71 GLU D 338 ILE D 353 1 16
HELIX 72 72 SER D 358 GLY D 375 1 18
HELIX 73 73 THR D 385 GLY D 410 1 26
HELIX 74 74 GLY D 416 LYS D 425 1 10
HELIX 75 75 ASN D 433 MET D 447 1 15
HELIX 76 76 GLU D 448 CYS D 458 1 11
HELIX 77 77 GLU D 461 GLY D 472 1 12
HELIX 78 78 THR D 497 THR D 516 1 20
HELIX 79 79 GLY E 9 LYS E 28 1 20
HELIX 80 80 VAL E 29 LEU E 31 5 3
HELIX 81 81 ASP E 52 ILE E 60 1 9
HELIX 82 82 ASP E 64 ALA E 85 1 22
HELIX 83 83 GLY E 88 ALA E 109 1 22
HELIX 84 84 ASN E 112 SER E 135 1 24
HELIX 85 85 ASP E 140 ALA E 152 1 13
HELIX 86 86 ASP E 155 GLY E 170 1 16
HELIX 87 87 MET E 233 LYS E 242 1 10
HELIX 88 88 ALA E 243 LYS E 245 5 3
HELIX 89 89 GLU E 255 THR E 266 1 12
HELIX 90 90 PHE E 281 GLY E 297 1 17
HELIX 91 91 GLU E 338 ALA E 356 1 19
HELIX 92 92 SER E 358 GLY E 375 1 18
HELIX 93 93 THR E 385 GLY E 410 1 26
HELIX 94 94 GLY E 416 LYS E 425 1 10
HELIX 95 95 ASN E 433 MET E 447 1 15
HELIX 96 96 GLU E 448 CYS E 458 1 11
HELIX 97 97 GLU E 461 GLY E 471 1 11
HELIX 98 98 THR E 497 THR E 516 1 20
HELIX 99 99 GLY F 9 VAL F 29 1 21
HELIX 100 100 ASP F 52 ILE F 60 1 9
HELIX 101 101 ASP F 64 ALA F 84 1 21
HELIX 102 102 GLY F 88 ALA F 109 1 22
HELIX 103 103 ASN F 112 SER F 135 1 24
HELIX 104 104 ASP F 140 ALA F 152 1 13
HELIX 105 105 ASP F 155 GLY F 170 1 16
HELIX 106 106 ASN F 229 LYS F 242 1 14
HELIX 107 107 ALA F 243 LYS F 245 5 3
HELIX 108 108 GLU F 255 THR F 266 1 12
HELIX 109 109 PHE F 281 GLY F 297 1 17
HELIX 110 110 GLU F 304 GLY F 306 5 3
HELIX 111 111 GLU F 308 ALA F 312 5 5
HELIX 112 112 THR F 313 LEU F 317 5 5
HELIX 113 113 GLU F 338 ALA F 356 1 19
HELIX 114 114 SER F 358 GLY F 375 1 18
HELIX 115 115 THR F 385 GLY F 410 1 26
HELIX 116 116 GLY F 416 LYS F 425 1 10
HELIX 117 117 ASN F 433 MET F 447 1 15
HELIX 118 118 GLU F 448 CYS F 458 1 11
HELIX 119 119 GLU F 461 GLY F 471 1 11
HELIX 120 120 THR F 497 THR F 516 1 20
HELIX 121 121 GLY G 9 VAL G 29 1 21
HELIX 122 122 ASP G 52 ILE G 60 1 9
HELIX 123 123 ASP G 64 GLY G 86 1 23
HELIX 124 124 GLY G 88 ALA G 109 1 22
HELIX 125 125 ASN G 112 SER G 135 1 24
HELIX 126 126 ASP G 140 ALA G 152 1 13
HELIX 127 127 ASP G 155 GLY G 170 1 16
HELIX 128 128 MET G 233 LYS G 242 1 10
HELIX 129 129 GLY G 256 THR G 266 1 11
HELIX 130 130 MET G 267 GLY G 269 5 3
HELIX 131 131 PHE G 281 THR G 296 1 16
HELIX 132 132 GLU G 308 ALA G 312 5 5
HELIX 133 133 GLU G 338 ALA G 356 1 19
HELIX 134 134 SER G 358 GLY G 375 1 18
HELIX 135 135 THR G 385 GLY G 410 1 26
HELIX 136 136 GLY G 416 LYS G 425 1 10
HELIX 137 137 ASN G 433 MET G 447 1 15
HELIX 138 138 GLU G 448 GLY G 459 1 12
HELIX 139 139 GLU G 461 GLY G 472 1 12
HELIX 140 140 THR G 497 THR G 516 1 20
HELIX 141 141 GLY H 9 VAL H 29 1 21
HELIX 142 142 ASP H 52 ILE H 60 1 9
HELIX 143 143 ASP H 64 GLY H 86 1 23
HELIX 144 144 GLY H 88 ALA H 109 1 22
HELIX 145 145 ASN H 112 SER H 135 1 24
HELIX 146 146 ASP H 140 ALA H 152 1 13
HELIX 147 147 ASP H 155 VAL H 169 1 15
HELIX 148 148 MET H 233 LYS H 242 1 10
HELIX 149 149 ALA H 243 LYS H 245 5 3
HELIX 150 150 GLU H 255 THR H 266 1 12
HELIX 151 151 MET H 267 GLY H 269 5 3
HELIX 152 152 PHE H 281 GLY H 297 1 17
HELIX 153 153 GLU H 304 GLY H 306 5 3
HELIX 154 154 GLU H 308 ALA H 312 5 5
HELIX 155 155 THR H 313 LEU H 317 5 5
HELIX 156 156 GLU H 338 ILE H 353 1 16
HELIX 157 157 SER H 358 GLY H 375 1 18
HELIX 158 158 THR H 385 GLY H 410 1 26
HELIX 159 159 GLY H 416 LEU H 426 1 11
HELIX 160 160 ASN H 433 MET H 447 1 15
HELIX 161 161 GLU H 448 CYS H 458 1 11
HELIX 162 162 GLU H 461 GLY H 472 1 12
HELIX 163 163 THR H 497 THR H 517 1 21
HELIX 164 164 GLY I 9 VAL I 29 1 21
HELIX 165 165 ASP I 52 ILE I 60 1 9
HELIX 166 166 ASP I 64 GLY I 86 1 23
HELIX 167 167 GLY I 88 ALA I 109 1 22
HELIX 168 168 ASN I 112 SER I 135 1 24
HELIX 169 169 ASP I 140 ALA I 152 1 13
HELIX 170 170 ASP I 155 GLY I 170 1 16
HELIX 171 171 MET I 233 LYS I 242 1 10
HELIX 172 172 ALA I 243 LYS I 245 5 3
HELIX 173 173 GLU I 255 THR I 266 1 12
HELIX 174 174 MET I 267 GLY I 269 5 3
HELIX 175 175 GLY I 282 GLY I 297 1 16
HELIX 176 176 GLU I 308 ALA I 312 5 5
HELIX 177 177 GLU I 338 GLN I 351 1 14
HELIX 178 178 GLN I 352 ALA I 356 5 5
HELIX 179 179 SER I 358 GLY I 375 1 18
HELIX 180 180 THR I 385 GLY I 410 1 26
HELIX 181 181 GLY I 416 LEU I 426 1 11
HELIX 182 182 ASN I 433 MET I 447 1 15
HELIX 183 183 GLU I 448 GLY I 459 1 12
HELIX 184 184 GLU I 461 GLY I 472 1 12
HELIX 185 185 THR I 497 THR I 516 1 20
HELIX 186 186 GLY J 9 VAL J 29 1 21
HELIX 187 187 ASP J 52 ILE J 60 1 9
HELIX 188 188 ASP J 64 ALA J 85 1 22
HELIX 189 189 GLY J 88 ALA J 109 1 22
HELIX 190 190 ASN J 112 LEU J 134 1 23
HELIX 191 191 ASP J 140 ALA J 152 1 13
HELIX 192 192 ASP J 155 GLY J 170 1 16
HELIX 193 193 MET J 233 LYS J 242 1 10
HELIX 194 194 ALA J 243 LYS J 245 5 3
HELIX 195 195 GLU J 255 THR J 266 1 12
HELIX 196 196 PHE J 281 GLY J 297 1 17
HELIX 197 197 GLU J 304 GLY J 306 5 3
HELIX 198 198 GLU J 308 ALA J 312 5 5
HELIX 199 199 GLU J 338 ILE J 353 1 16
HELIX 200 200 SER J 358 GLY J 375 1 18
HELIX 201 201 THR J 385 GLY J 410 1 26
HELIX 202 202 GLY J 416 LEU J 426 1 11
HELIX 203 203 ASN J 433 MET J 447 1 15
HELIX 204 204 GLU J 448 CYS J 458 1 11
HELIX 205 205 GLU J 461 GLY J 472 1 12
HELIX 206 206 MET J 488 GLY J 492 1 5
HELIX 207 207 THR J 497 THR J 516 1 20
HELIX 208 208 GLY K 9 VAL K 29 1 21
HELIX 209 209 ASP K 52 ILE K 60 1 9
HELIX 210 210 ASP K 64 ALA K 84 1 21
HELIX 211 211 GLY K 88 ALA K 109 1 22
HELIX 212 212 ASN K 112 SER K 135 1 24
HELIX 213 213 ASP K 140 ALA K 152 1 13
HELIX 214 214 ASP K 155 GLY K 170 1 16
HELIX 215 215 MET K 233 LYS K 242 1 10
HELIX 216 216 ALA K 243 LYS K 245 5 3
HELIX 217 217 GLU K 255 THR K 266 1 12
HELIX 218 218 PHE K 281 GLY K 297 1 17
HELIX 219 219 GLU K 338 ILE K 353 1 16
HELIX 220 220 SER K 358 GLY K 375 1 18
HELIX 221 221 THR K 385 GLY K 410 1 26
HELIX 222 222 GLY K 416 LEU K 426 1 11
HELIX 223 223 ASN K 433 MET K 447 1 15
HELIX 224 224 GLU K 448 GLY K 459 1 12
HELIX 225 225 GLU K 461 GLY K 472 1 12
HELIX 226 226 THR K 497 THR K 517 1 21
HELIX 227 227 GLY L 9 VAL L 29 1 21
HELIX 228 228 ASP L 52 GLU L 59 1 8
HELIX 229 229 ASP L 64 ALA L 85 1 22
HELIX 230 230 GLY L 88 ALA L 109 1 22
HELIX 231 231 ASN L 112 LEU L 134 1 23
HELIX 232 232 ASP L 140 ALA L 152 1 13
HELIX 233 233 ASP L 155 GLY L 170 1 16
HELIX 234 234 ASN L 229 VAL L 240 1 12
HELIX 235 235 ALA L 241 LYS L 245 5 5
HELIX 236 236 GLU L 255 THR L 266 1 12
HELIX 237 237 MET L 267 GLY L 269 5 3
HELIX 238 238 PHE L 281 GLY L 297 1 17
HELIX 239 239 GLU L 308 ALA L 312 5 5
HELIX 240 240 THR L 313 LEU L 317 5 5
HELIX 241 241 GLU L 338 GLN L 352 1 15
HELIX 242 242 SER L 358 GLY L 375 1 18
HELIX 243 243 THR L 385 GLY L 410 1 26
HELIX 244 244 GLY L 416 LEU L 426 1 11
HELIX 245 245 ASN L 433 MET L 447 1 15
HELIX 246 246 GLU L 448 GLY L 459 1 12
HELIX 247 247 GLU L 461 GLY L 472 1 12
HELIX 248 248 THR L 497 THR L 516 1 20
HELIX 249 249 GLY M 9 VAL M 29 1 21
HELIX 250 250 ASP M 52 ILE M 60 1 9
HELIX 251 251 ASP M 64 ALA M 85 1 22
HELIX 252 252 GLY M 88 ALA M 109 1 22
HELIX 253 253 ASN M 112 SER M 135 1 24
HELIX 254 254 ASP M 140 ALA M 152 1 13
HELIX 255 255 ASP M 155 GLY M 170 1 16
HELIX 256 256 MET M 233 LYS M 242 1 10
HELIX 257 257 ALA M 243 LYS M 245 5 3
HELIX 258 258 GLY M 256 ARG M 268 1 13
HELIX 259 259 PHE M 281 GLY M 297 1 17
HELIX 260 260 GLU M 338 ILE M 353 1 16
HELIX 261 261 SER M 358 GLY M 375 1 18
HELIX 262 262 THR M 385 GLY M 410 1 26
HELIX 263 263 GLY M 416 LEU M 426 1 11
HELIX 264 264 ASN M 433 MET M 447 1 15
HELIX 265 265 GLU M 448 CYS M 458 1 11
HELIX 266 266 GLU M 461 GLY M 472 1 12
HELIX 267 267 MET M 488 GLY M 492 1 5
HELIX 268 268 THR M 497 THR M 516 1 20
HELIX 269 269 GLY N 9 LYS N 28 1 20
HELIX 270 270 ASP N 52 ILE N 60 1 9
HELIX 271 271 ASP N 64 ALA N 84 1 21
HELIX 272 272 GLY N 88 ALA N 109 1 22
HELIX 273 273 ASN N 112 SER N 135 1 24
HELIX 274 274 ASP N 140 ALA N 152 1 13
HELIX 275 275 ASP N 155 GLY N 170 1 16
HELIX 276 276 MET N 233 LYS N 242 1 10
HELIX 277 277 ALA N 243 LYS N 245 5 3
HELIX 278 278 GLU N 255 THR N 266 1 12
HELIX 279 279 PHE N 281 GLY N 297 1 17
HELIX 280 280 GLU N 304 GLY N 306 5 3
HELIX 281 281 GLU N 338 GLN N 352 1 15
HELIX 282 282 SER N 358 GLY N 375 1 18
HELIX 283 283 THR N 385 GLY N 410 1 26
HELIX 284 284 GLY N 416 LEU N 426 1 11
HELIX 285 285 ASN N 433 MET N 447 1 15
HELIX 286 286 GLU N 448 CYS N 458 1 11
HELIX 287 287 GLU N 461 GLY N 472 1 12
HELIX 288 288 MET N 488 GLY N 492 1 5
HELIX 289 289 THR N 497 THR N 516 1 20
SHEET 1 AA 4 LYS A 4 PHE A 8 0
SHEET 2 AA 4 THR A 517 ASP A 523 -1 O MET A 520 N LYS A 7
SHEET 3 AA 4 ASN G 37 LEU G 40 1 O ASN G 37 N GLU A 518
SHEET 4 AA 4 THR G 48 THR G 50 -1 O THR G 48 N LEU G 40
SHEET 1 AB 4 THR A 48 THR A 50 0
SHEET 2 AB 4 ASN A 37 LEU A 40 -1 O VAL A 38 N THR A 50
SHEET 3 AB 4 THR B 517 ASP B 523 1 N GLU B 518 O ASN A 37
SHEET 4 AB 4 LYS B 4 PHE B 8 -1 O ASP B 5 N THR B 522
SHEET 1 AC 3 VAL A 174 ASP A 179 0
SHEET 2 AC 3 VAL A 376 VAL A 381 1 O ALA A 377 N THR A 176
SHEET 3 AC 3 GLU A 186 LEU A 187 -1 O GLU A 186 N LYS A 380
SHEET 1 AD 6 GLY A 192 PHE A 195 0
SHEET 2 AD 6 THR A 330 GLY A 335 -1 O THR A 330 N PHE A 195
SHEET 3 AD 6 GLY A 318 ILE A 325 -1 N LYS A 321 O ASP A 334
SHEET 4 AD 6 PHE A 219 ILE A 227 -1 O ILE A 220 N GLY A 318
SHEET 5 AD 6 LEU A 247 VAL A 254 1 O LEU A 248 N LEU A 221
SHEET 6 AD 6 VAL A 273 LYS A 277 1 O ALA A 274 N ILE A 249
SHEET 1 AE 4 GLY A 192 PHE A 195 0
SHEET 2 AE 4 THR A 330 GLY A 335 -1 O THR A 330 N PHE A 195
SHEET 3 AE 4 GLY A 318 ILE A 325 -1 N LYS A 321 O ASP A 334
SHEET 4 AE 4 VAL A 213 GLU A 216 1 O VAL A 213 N ILE A 325
SHEET 1 AF 2 VAL A 411 ALA A 413 0
SHEET 2 AF 2 LEU A 494 PRO A 496 -1 O ASP A 495 N VAL A 412
SHEET 1 AG 2 TYR A 476 ASN A 479 0
SHEET 2 AG 2 GLU A 484 ASN A 487 -1 O GLU A 484 N ASN A 479
SHEET 1 BA 4 THR B 48 THR B 50 0
SHEET 2 BA 4 ASN B 37 LEU B 40 -1 O VAL B 38 N THR B 50
SHEET 3 BA 4 THR C 517 ASP C 523 1 N GLU C 518 O ASN B 37
SHEET 4 BA 4 LYS C 4 PHE C 8 -1 O ASP C 5 N THR C 522
SHEET 1 BB 3 VAL B 174 ASP B 179 0
SHEET 2 BB 3 VAL B 376 VAL B 381 1 O ALA B 377 N THR B 176
SHEET 3 BB 3 GLU B 186 LEU B 187 -1 O GLU B 186 N LYS B 380
SHEET 1 BC 6 MET B 193 PHE B 195 0
SHEET 2 BC 6 THR B 330 GLY B 335 -1 O THR B 330 N PHE B 195
SHEET 3 BC 6 GLY B 318 ILE B 325 -1 N LYS B 321 O ILE B 333
SHEET 4 BC 6 PHE B 219 LYS B 226 -1 O ILE B 220 N GLY B 318
SHEET 5 BC 6 LEU B 247 ASP B 253 1 O LEU B 248 N LEU B 221
SHEET 6 BC 6 VAL B 273 LYS B 277 1 O ALA B 274 N ILE B 249
SHEET 1 BD 4 MET B 193 PHE B 195 0
SHEET 2 BD 4 THR B 330 GLY B 335 -1 O THR B 330 N PHE B 195
SHEET 3 BD 4 GLY B 318 ILE B 325 -1 N LYS B 321 O ILE B 333
SHEET 4 BD 4 VAL B 213 GLU B 216 1 O VAL B 213 N ILE B 325
SHEET 1 BE 2 VAL B 411 ALA B 413 0
SHEET 2 BE 2 LEU B 494 PRO B 496 -1 O ASP B 495 N VAL B 412
SHEET 1 BF 2 TYR B 476 ASN B 479 0
SHEET 2 BF 2 GLU B 484 ASN B 487 -1 O GLU B 484 N ASN B 479
SHEET 1 CA 4 THR C 48 THR C 50 0
SHEET 2 CA 4 ASN C 37 LEU C 40 -1 O VAL C 38 N THR C 50
SHEET 3 CA 4 THR D 517 ASP D 523 1 N GLU D 518 O ASN C 37
SHEET 4 CA 4 LYS D 4 PHE D 8 -1 O ASP D 5 N THR D 522
SHEET 1 CB 3 VAL C 174 ASP C 179 0
SHEET 2 CB 3 VAL C 376 VAL C 381 1 O ALA C 377 N THR C 176
SHEET 3 CB 3 GLU C 186 VAL C 190 -1 O GLU C 186 N LYS C 380
SHEET 1 CC 6 MET C 193 PHE C 195 0
SHEET 2 CC 6 THR C 330 GLY C 335 -1 O THR C 330 N PHE C 195
SHEET 3 CC 6 GLY C 318 ILE C 325 -1 N LYS C 321 O ASP C 334
SHEET 4 CC 6 PHE C 219 LEU C 222 -1 O ILE C 220 N GLY C 318
SHEET 5 CC 6 LEU C 247 ALA C 251 1 O LEU C 248 N LEU C 221
SHEET 6 CC 6 VAL C 273 LYS C 277 1 O ALA C 274 N ILE C 249
SHEET 1 CD 4 MET C 193 PHE C 195 0
SHEET 2 CD 4 THR C 330 GLY C 335 -1 O THR C 330 N PHE C 195
SHEET 3 CD 4 GLY C 318 ILE C 325 -1 N LYS C 321 O ASP C 334
SHEET 4 CD 4 VAL C 213 GLU C 216 1 O VAL C 213 N ILE C 325
SHEET 1 CE 2 LYS C 226 ILE C 227 0
SHEET 2 CE 2 ASP C 253 VAL C 254 1 O ASP C 253 N ILE C 227
SHEET 1 CF 2 VAL C 411 ALA C 413 0
SHEET 2 CF 2 LEU C 494 PRO C 496 -1 O ASP C 495 N VAL C 412
SHEET 1 CG 2 TYR C 476 TYR C 478 0
SHEET 2 CG 2 TYR C 485 ASN C 487 -1 O GLY C 486 N GLY C 477
SHEET 1 DA 4 THR D 48 THR D 50 0
SHEET 2 DA 4 ASN D 37 LEU D 40 -1 O VAL D 38 N THR D 50
SHEET 3 DA 4 THR E 517 ASP E 523 1 N GLU E 518 O ASN D 37
SHEET 4 DA 4 LYS E 4 PHE E 8 -1 O ASP E 5 N THR E 522
SHEET 1 DB 3 ILE D 175 ASP D 179 0
SHEET 2 DB 3 ALA D 377 VAL D 381 1 O ALA D 377 N THR D 176
SHEET 3 DB 3 GLU D 186 LEU D 187 -1 O GLU D 186 N LYS D 380
SHEET 1 DC 5 GLY D 192 PHE D 195 0
SHEET 2 DC 5 THR D 330 GLY D 335 -1 O THR D 330 N PHE D 195
SHEET 3 DC 5 GLY D 318 ILE D 325 -1 N LYS D 321 O ASP D 334
SHEET 4 DC 5 PHE D 219 ASP D 224 -1 O ILE D 220 N GLY D 318
SHEET 5 DC 5 ILE D 301 SER D 302 -1 O ILE D 301 N ASP D 224
SHEET 1 DD 4 GLY D 192 PHE D 195 0
SHEET 2 DD 4 THR D 330 GLY D 335 -1 O THR D 330 N PHE D 195
SHEET 3 DD 4 GLY D 318 ILE D 325 -1 N LYS D 321 O ASP D 334
SHEET 4 DD 4 VAL D 213 GLU D 216 1 O VAL D 213 N ILE D 325
SHEET 1 DE 4 VAL D 273 LYS D 277 0
SHEET 2 DE 4 LEU D 247 ALA D 251 1 O LEU D 247 N ALA D 274
SHEET 3 DE 4 PHE D 219 ASP D 224 1 O PHE D 219 N LEU D 248
SHEET 4 DE 4 ILE D 301 SER D 302 -1 O ILE D 301 N ASP D 224
SHEET 1 DF 6 GLY D 192 PHE D 195 0
SHEET 2 DF 6 THR D 330 GLY D 335 -1 O THR D 330 N PHE D 195
SHEET 3 DF 6 GLY D 318 ILE D 325 -1 N LYS D 321 O ASP D 334
SHEET 4 DF 6 PHE D 219 ASP D 224 -1 O ILE D 220 N GLY D 318
SHEET 5 DF 6 LEU D 247 ALA D 251 1 O LEU D 248 N LEU D 221
SHEET 6 DF 6 VAL D 273 LYS D 277 1 O ALA D 274 N ILE D 249
SHEET 1 DG 6 VAL D 273 LYS D 277 0
SHEET 2 DG 6 LEU D 247 ALA D 251 1 O LEU D 247 N ALA D 274
SHEET 3 DG 6 PHE D 219 ASP D 224 1 O PHE D 219 N LEU D 248
SHEET 4 DG 6 GLY D 318 ILE D 325 -1 O GLY D 318 N ILE D 220
SHEET 5 DG 6 THR D 330 GLY D 335 -1 O THR D 331 N VAL D 324
SHEET 6 DG 6 GLY D 192 PHE D 195 -1 O MET D 193 N ILE D 332
SHEET 1 DH 5 VAL D 273 LYS D 277 0
SHEET 2 DH 5 LEU D 247 ALA D 251 1 O LEU D 247 N ALA D 274
SHEET 3 DH 5 PHE D 219 ASP D 224 1 O PHE D 219 N LEU D 248
SHEET 4 DH 5 GLY D 318 ILE D 325 -1 O GLY D 318 N ILE D 220
SHEET 5 DH 5 VAL D 213 GLU D 216 1 O VAL D 213 N ILE D 325
SHEET 1 DI 2 ILE D 301 SER D 302 0
SHEET 2 DI 2 PHE D 219 ASP D 224 -1 O LEU D 222 N ILE D 301
SHEET 1 DJ 2 LYS D 226 ILE D 227 0
SHEET 2 DJ 2 ASP D 253 VAL D 254 1 O ASP D 253 N ILE D 227
SHEET 1 DK 2 VAL D 411 ALA D 413 0
SHEET 2 DK 2 LEU D 494 PRO D 496 -1 O ASP D 495 N VAL D 412
SHEET 1 DL 2 TYR D 476 ASN D 479 0
SHEET 2 DL 2 GLU D 484 ASN D 487 -1 O GLU D 484 N ASN D 479
SHEET 1 EA 4 THR E 48 THR E 50 0
SHEET 2 EA 4 ASN E 37 LEU E 40 -1 O VAL E 38 N THR E 50
SHEET 3 EA 4 THR F 517 ASP F 523 1 N GLU F 518 O ASN E 37
SHEET 4 EA 4 LYS F 4 PHE F 8 -1 O ASP F 5 N THR F 522
SHEET 1 EB 3 ILE E 175 ASP E 179 0
SHEET 2 EB 3 VAL E 376 VAL E 381 1 O ALA E 377 N THR E 176
SHEET 3 EB 3 GLU E 186 VAL E 190 -1 O GLU E 186 N LYS E 380
SHEET 1 EC 5 MET E 193 PHE E 195 0
SHEET 2 EC 5 THR E 330 GLY E 335 -1 O THR E 330 N PHE E 195
SHEET 3 EC 5 GLY E 318 ILE E 325 -1 N LYS E 321 O ASP E 334
SHEET 4 EC 5 PHE E 219 ASP E 224 -1 O ILE E 220 N GLY E 318
SHEET 5 EC 5 ILE E 301 SER E 302 -1 O ILE E 301 N ASP E 224
SHEET 1 ED 4 MET E 193 PHE E 195 0
SHEET 2 ED 4 THR E 330 GLY E 335 -1 O THR E 330 N PHE E 195
SHEET 3 ED 4 GLY E 318 ILE E 325 -1 N LYS E 321 O ASP E 334
SHEET 4 ED 4 VAL E 213 GLU E 216 1 O VAL E 213 N ILE E 325
SHEET 1 EE 4 VAL E 273 LYS E 277 0
SHEET 2 EE 4 LEU E 247 ALA E 251 1 O LEU E 247 N ALA E 274
SHEET 3 EE 4 PHE E 219 ASP E 224 1 O PHE E 219 N LEU E 248
SHEET 4 EE 4 ILE E 301 SER E 302 -1 O ILE E 301 N ASP E 224
SHEET 1 EF 6 MET E 193 PHE E 195 0
SHEET 2 EF 6 THR E 330 GLY E 335 -1 O THR E 330 N PHE E 195
SHEET 3 EF 6 GLY E 318 ILE E 325 -1 N LYS E 321 O ASP E 334
SHEET 4 EF 6 PHE E 219 ASP E 224 -1 O ILE E 220 N GLY E 318
SHEET 5 EF 6 LEU E 247 ALA E 251 1 O LEU E 248 N LEU E 221
SHEET 6 EF 6 VAL E 273 LYS E 277 1 O ALA E 274 N ILE E 249
SHEET 1 EG 6 VAL E 273 LYS E 277 0
SHEET 2 EG 6 LEU E 247 ALA E 251 1 O LEU E 247 N ALA E 274
SHEET 3 EG 6 PHE E 219 ASP E 224 1 O PHE E 219 N LEU E 248
SHEET 4 EG 6 GLY E 318 ILE E 325 -1 O GLY E 318 N ILE E 220
SHEET 5 EG 6 THR E 330 GLY E 335 -1 O THR E 331 N VAL E 324
SHEET 6 EG 6 MET E 193 PHE E 195 -1 O MET E 193 N ILE E 332
SHEET 1 EH 5 VAL E 273 LYS E 277 0
SHEET 2 EH 5 LEU E 247 ALA E 251 1 O LEU E 247 N ALA E 274
SHEET 3 EH 5 PHE E 219 ASP E 224 1 O PHE E 219 N LEU E 248
SHEET 4 EH 5 GLY E 318 ILE E 325 -1 O GLY E 318 N ILE E 220
SHEET 5 EH 5 VAL E 213 GLU E 216 1 O VAL E 213 N ILE E 325
SHEET 1 EI 2 ILE E 301 SER E 302 0
SHEET 2 EI 2 PHE E 219 ASP E 224 -1 O LEU E 222 N ILE E 301
SHEET 1 EJ 2 VAL E 411 ALA E 413 0
SHEET 2 EJ 2 LEU E 494 PRO E 496 -1 O ASP E 495 N VAL E 412
SHEET 1 EK 2 TYR E 476 ASN E 479 0
SHEET 2 EK 2 GLU E 484 ASN E 487 -1 O GLU E 484 N ASN E 479
SHEET 1 FA 4 THR F 48 THR F 50 0
SHEET 2 FA 4 VAL F 38 LEU F 40 -1 O VAL F 38 N THR F 50
SHEET 3 FA 4 CYS G 519 ASP G 523 1 O CYS G 519 N VAL F 39
SHEET 4 FA 4 LYS G 4 PHE G 8 -1 O ASP G 5 N THR G 522
SHEET 1 FB 3 VAL F 174 ASP F 179 0
SHEET 2 FB 3 VAL F 376 VAL F 381 1 O ALA F 377 N THR F 176
SHEET 3 FB 3 GLU F 186 VAL F 190 -1 O GLU F 186 N LYS F 380
SHEET 1 FC 5 GLY F 192 PHE F 195 0
SHEET 2 FC 5 THR F 330 GLY F 335 -1 O THR F 330 N PHE F 195
SHEET 3 FC 5 GLY F 318 ILE F 325 -1 N LYS F 321 O ASP F 334
SHEET 4 FC 5 PHE F 219 ILE F 227 -1 O ILE F 220 N GLY F 318
SHEET 5 FC 5 ILE F 301 SER F 302 -1 O ILE F 301 N ASP F 224
SHEET 1 FD 4 GLY F 192 PHE F 195 0
SHEET 2 FD 4 THR F 330 GLY F 335 -1 O THR F 330 N PHE F 195
SHEET 3 FD 4 GLY F 318 ILE F 325 -1 N LYS F 321 O ASP F 334
SHEET 4 FD 4 VAL F 213 GLU F 216 1 O VAL F 213 N ILE F 325
SHEET 1 FE 4 VAL F 273 LYS F 277 0
SHEET 2 FE 4 LEU F 247 VAL F 254 1 O LEU F 247 N ALA F 274
SHEET 3 FE 4 PHE F 219 ILE F 227 1 O PHE F 219 N LEU F 248
SHEET 4 FE 4 ILE F 301 SER F 302 -1 O ILE F 301 N ASP F 224
SHEET 1 FF 6 GLY F 192 PHE F 195 0
SHEET 2 FF 6 THR F 330 GLY F 335 -1 O THR F 330 N PHE F 195
SHEET 3 FF 6 GLY F 318 ILE F 325 -1 N LYS F 321 O ASP F 334
SHEET 4 FF 6 PHE F 219 ILE F 227 -1 O ILE F 220 N GLY F 318
SHEET 5 FF 6 LEU F 247 VAL F 254 1 O LEU F 248 N LEU F 221
SHEET 6 FF 6 VAL F 273 LYS F 277 1 O ALA F 274 N ILE F 249
SHEET 1 FG 6 VAL F 273 LYS F 277 0
SHEET 2 FG 6 LEU F 247 VAL F 254 1 O LEU F 247 N ALA F 274
SHEET 3 FG 6 PHE F 219 ILE F 227 1 O PHE F 219 N LEU F 248
SHEET 4 FG 6 GLY F 318 ILE F 325 -1 O GLY F 318 N ILE F 220
SHEET 5 FG 6 THR F 330 GLY F 335 -1 O THR F 331 N VAL F 324
SHEET 6 FG 6 GLY F 192 PHE F 195 -1 O MET F 193 N ILE F 332
SHEET 1 FH 5 VAL F 273 LYS F 277 0
SHEET 2 FH 5 LEU F 247 VAL F 254 1 O LEU F 247 N ALA F 274
SHEET 3 FH 5 PHE F 219 ILE F 227 1 O PHE F 219 N LEU F 248
SHEET 4 FH 5 GLY F 318 ILE F 325 -1 O GLY F 318 N ILE F 220
SHEET 5 FH 5 VAL F 213 GLU F 216 1 O VAL F 213 N ILE F 325
SHEET 1 FI 2 ILE F 301 SER F 302 0
SHEET 2 FI 2 PHE F 219 ILE F 227 -1 O LEU F 222 N ILE F 301
SHEET 1 FJ 2 VAL F 411 ALA F 413 0
SHEET 2 FJ 2 LEU F 494 PRO F 496 -1 O ASP F 495 N VAL F 412
SHEET 1 FK 2 TYR F 476 ASN F 479 0
SHEET 2 FK 2 GLU F 484 ASN F 487 -1 O GLU F 484 N ASN F 479
SHEET 1 GA 3 ILE G 175 GLU G 178 0
SHEET 2 GA 3 VAL G 376 LYS G 380 1 O ALA G 377 N THR G 176
SHEET 3 GA 3 GLU G 186 VAL G 190 -1 O GLU G 186 N LYS G 380
SHEET 1 GB 5 GLY G 192 PHE G 195 0
SHEET 2 GB 5 THR G 330 GLY G 335 -1 O THR G 330 N PHE G 195
SHEET 3 GB 5 GLY G 318 ILE G 325 -1 N LYS G 321 O ASP G 334
SHEET 4 GB 5 PHE G 219 ASP G 224 -1 O ILE G 220 N GLY G 318
SHEET 5 GB 5 ILE G 301 SER G 302 -1 O ILE G 301 N ASP G 224
SHEET 1 GC 4 GLY G 192 PHE G 195 0
SHEET 2 GC 4 THR G 330 GLY G 335 -1 O THR G 330 N PHE G 195
SHEET 3 GC 4 GLY G 318 ILE G 325 -1 N LYS G 321 O ASP G 334
SHEET 4 GC 4 VAL G 213 GLU G 216 1 O VAL G 213 N ILE G 325
SHEET 1 GD 4 VAL G 273 LYS G 277 0
SHEET 2 GD 4 LEU G 247 ALA G 251 1 O LEU G 247 N ALA G 274
SHEET 3 GD 4 PHE G 219 ASP G 224 1 O PHE G 219 N LEU G 248
SHEET 4 GD 4 ILE G 301 SER G 302 -1 O ILE G 301 N ASP G 224
SHEET 1 GE 6 GLY G 192 PHE G 195 0
SHEET 2 GE 6 THR G 330 GLY G 335 -1 O THR G 330 N PHE G 195
SHEET 3 GE 6 GLY G 318 ILE G 325 -1 N LYS G 321 O ASP G 334
SHEET 4 GE 6 PHE G 219 ASP G 224 -1 O ILE G 220 N GLY G 318
SHEET 5 GE 6 LEU G 247 ALA G 251 1 O LEU G 248 N LEU G 221
SHEET 6 GE 6 VAL G 273 LYS G 277 1 O ALA G 274 N ILE G 249
SHEET 1 GF 6 VAL G 273 LYS G 277 0
SHEET 2 GF 6 LEU G 247 ALA G 251 1 O LEU G 247 N ALA G 274
SHEET 3 GF 6 PHE G 219 ASP G 224 1 O PHE G 219 N LEU G 248
SHEET 4 GF 6 GLY G 318 ILE G 325 -1 O GLY G 318 N ILE G 220
SHEET 5 GF 6 THR G 330 GLY G 335 -1 O THR G 331 N VAL G 324
SHEET 6 GF 6 GLY G 192 PHE G 195 -1 O MET G 193 N ILE G 332
SHEET 1 GG 5 VAL G 273 LYS G 277 0
SHEET 2 GG 5 LEU G 247 ALA G 251 1 O LEU G 247 N ALA G 274
SHEET 3 GG 5 PHE G 219 ASP G 224 1 O PHE G 219 N LEU G 248
SHEET 4 GG 5 GLY G 318 ILE G 325 -1 O GLY G 318 N ILE G 220
SHEET 5 GG 5 VAL G 213 GLU G 216 1 O VAL G 213 N ILE G 325
SHEET 1 GH 2 ILE G 301 SER G 302 0
SHEET 2 GH 2 PHE G 219 ASP G 224 -1 O LEU G 222 N ILE G 301
SHEET 1 GI 2 LYS G 226 ILE G 227 0
SHEET 2 GI 2 ASP G 253 VAL G 254 1 O ASP G 253 N ILE G 227
SHEET 1 GJ 2 VAL G 411 ALA G 413 0
SHEET 2 GJ 2 LEU G 494 PRO G 496 -1 O ASP G 495 N VAL G 412
SHEET 1 GK 2 TYR G 476 ASN G 479 0
SHEET 2 GK 2 GLU G 484 ASN G 487 -1 O GLU G 484 N ASN G 479
SHEET 1 HA 4 LYS H 4 PHE H 8 0
SHEET 2 HA 4 CYS H 519 ASP H 523 -1 O MET H 520 N LYS H 7
SHEET 3 HA 4 VAL N 38 LEU N 40 1 O VAL N 39 N VAL H 521
SHEET 4 HA 4 THR N 48 THR N 50 -1 O THR N 48 N LEU N 40
SHEET 1 HB 4 THR H 48 THR H 50 0
SHEET 2 HB 4 ASN H 37 LEU H 40 -1 O VAL H 38 N THR H 50
SHEET 3 HB 4 THR I 517 ASP I 523 1 N GLU I 518 O ASN H 37
SHEET 4 HB 4 LYS I 4 PHE I 8 -1 O ASP I 5 N THR I 522
SHEET 1 HC 3 ILE H 175 ASP H 179 0
SHEET 2 HC 3 VAL H 376 VAL H 381 1 O ALA H 377 N THR H 176
SHEET 3 HC 3 GLU H 186 VAL H 190 -1 O GLU H 186 N LYS H 380
SHEET 1 HD 5 GLY H 192 PHE H 195 0
SHEET 2 HD 5 THR H 330 GLY H 335 -1 O THR H 330 N PHE H 195
SHEET 3 HD 5 GLY H 318 ILE H 325 -1 N LYS H 321 O ASP H 334
SHEET 4 HD 5 PHE H 219 ASP H 224 -1 O ILE H 220 N GLY H 318
SHEET 5 HD 5 ILE H 301 SER H 302 -1 O ILE H 301 N ASP H 224
SHEET 1 HE 4 GLY H 192 PHE H 195 0
SHEET 2 HE 4 THR H 330 GLY H 335 -1 O THR H 330 N PHE H 195
SHEET 3 HE 4 GLY H 318 ILE H 325 -1 N LYS H 321 O ASP H 334
SHEET 4 HE 4 VAL H 213 GLU H 216 1 O VAL H 213 N ILE H 325
SHEET 1 HF 4 VAL H 273 LYS H 277 0
SHEET 2 HF 4 LEU H 247 ALA H 251 1 O LEU H 247 N ALA H 274
SHEET 3 HF 4 PHE H 219 ASP H 224 1 O PHE H 219 N LEU H 248
SHEET 4 HF 4 ILE H 301 SER H 302 -1 O ILE H 301 N ASP H 224
SHEET 1 HG 6 GLY H 192 PHE H 195 0
SHEET 2 HG 6 THR H 330 GLY H 335 -1 O THR H 330 N PHE H 195
SHEET 3 HG 6 GLY H 318 ILE H 325 -1 N LYS H 321 O ASP H 334
SHEET 4 HG 6 PHE H 219 ASP H 224 -1 O ILE H 220 N GLY H 318
SHEET 5 HG 6 LEU H 247 ALA H 251 1 O LEU H 248 N LEU H 221
SHEET 6 HG 6 VAL H 273 LYS H 277 1 O ALA H 274 N ILE H 249
SHEET 1 HH 6 VAL H 273 LYS H 277 0
SHEET 2 HH 6 LEU H 247 ALA H 251 1 O LEU H 247 N ALA H 274
SHEET 3 HH 6 PHE H 219 ASP H 224 1 O PHE H 219 N LEU H 248
SHEET 4 HH 6 GLY H 318 ILE H 325 -1 O GLY H 318 N ILE H 220
SHEET 5 HH 6 THR H 330 GLY H 335 -1 O THR H 331 N VAL H 324
SHEET 6 HH 6 GLY H 192 PHE H 195 -1 O MET H 193 N ILE H 332
SHEET 1 HI 5 VAL H 273 LYS H 277 0
SHEET 2 HI 5 LEU H 247 ALA H 251 1 O LEU H 247 N ALA H 274
SHEET 3 HI 5 PHE H 219 ASP H 224 1 O PHE H 219 N LEU H 248
SHEET 4 HI 5 GLY H 318 ILE H 325 -1 O GLY H 318 N ILE H 220
SHEET 5 HI 5 VAL H 213 GLU H 216 1 O VAL H 213 N ILE H 325
SHEET 1 HJ 2 ILE H 301 SER H 302 0
SHEET 2 HJ 2 PHE H 219 ASP H 224 -1 O LEU H 222 N ILE H 301
SHEET 1 HK 2 VAL H 411 ALA H 413 0
SHEET 2 HK 2 LEU H 494 PRO H 496 -1 O ASP H 495 N VAL H 412
SHEET 1 HL 2 TYR H 476 ASN H 479 0
SHEET 2 HL 2 GLU H 484 ASN H 487 -1 O GLU H 484 N ASN H 479
SHEET 1 IA 4 THR I 48 THR I 50 0
SHEET 2 IA 4 ASN I 37 LEU I 40 -1 O VAL I 38 N THR I 50
SHEET 3 IA 4 THR J 517 ASP J 523 1 N GLU J 518 O ASN I 37
SHEET 4 IA 4 LYS J 4 PHE J 8 -1 O ASP J 5 N THR J 522
SHEET 1 IB 3 ILE I 175 ASP I 179 0
SHEET 2 IB 3 VAL I 376 VAL I 381 1 O ALA I 377 N THR I 176
SHEET 3 IB 3 GLU I 186 VAL I 190 -1 O GLU I 186 N LYS I 380
SHEET 1 IC 5 GLY I 192 PHE I 195 0
SHEET 2 IC 5 THR I 330 GLY I 335 -1 O THR I 330 N PHE I 195
SHEET 3 IC 5 GLY I 318 ILE I 325 -1 N LYS I 321 O ASP I 334
SHEET 4 IC 5 PHE I 219 ILE I 227 -1 O ILE I 220 N GLY I 318
SHEET 5 IC 5 ILE I 301 SER I 302 -1 O ILE I 301 N ASP I 224
SHEET 1 ID 4 GLY I 192 PHE I 195 0
SHEET 2 ID 4 THR I 330 GLY I 335 -1 O THR I 330 N PHE I 195
SHEET 3 ID 4 GLY I 318 ILE I 325 -1 N LYS I 321 O ASP I 334
SHEET 4 ID 4 VAL I 213 GLU I 216 1 O VAL I 213 N ILE I 325
SHEET 1 IE 4 VAL I 273 LYS I 277 0
SHEET 2 IE 4 LEU I 247 VAL I 254 1 O LEU I 247 N ALA I 274
SHEET 3 IE 4 PHE I 219 ILE I 227 1 O PHE I 219 N LEU I 248
SHEET 4 IE 4 ILE I 301 SER I 302 -1 O ILE I 301 N ASP I 224
SHEET 1 IF 6 GLY I 192 PHE I 195 0
SHEET 2 IF 6 THR I 330 GLY I 335 -1 O THR I 330 N PHE I 195
SHEET 3 IF 6 GLY I 318 ILE I 325 -1 N LYS I 321 O ASP I 334
SHEET 4 IF 6 PHE I 219 ILE I 227 -1 O ILE I 220 N GLY I 318
SHEET 5 IF 6 LEU I 247 VAL I 254 1 O LEU I 248 N LEU I 221
SHEET 6 IF 6 VAL I 273 LYS I 277 1 O ALA I 274 N ILE I 249
SHEET 1 IG 6 VAL I 273 LYS I 277 0
SHEET 2 IG 6 LEU I 247 VAL I 254 1 O LEU I 247 N ALA I 274
SHEET 3 IG 6 PHE I 219 ILE I 227 1 O PHE I 219 N LEU I 248
SHEET 4 IG 6 GLY I 318 ILE I 325 -1 O GLY I 318 N ILE I 220
SHEET 5 IG 6 THR I 330 GLY I 335 -1 O THR I 331 N VAL I 324
SHEET 6 IG 6 GLY I 192 PHE I 195 -1 O MET I 193 N ILE I 332
SHEET 1 IH 5 VAL I 273 LYS I 277 0
SHEET 2 IH 5 LEU I 247 VAL I 254 1 O LEU I 247 N ALA I 274
SHEET 3 IH 5 PHE I 219 ILE I 227 1 O PHE I 219 N LEU I 248
SHEET 4 IH 5 GLY I 318 ILE I 325 -1 O GLY I 318 N ILE I 220
SHEET 5 IH 5 VAL I 213 GLU I 216 1 O VAL I 213 N ILE I 325
SHEET 1 II 2 ILE I 301 SER I 302 0
SHEET 2 II 2 PHE I 219 ILE I 227 -1 O LEU I 222 N ILE I 301
SHEET 1 IJ 2 VAL I 411 ALA I 413 0
SHEET 2 IJ 2 LEU I 494 PRO I 496 -1 O ASP I 495 N VAL I 412
SHEET 1 IK 2 TYR I 476 ASN I 479 0
SHEET 2 IK 2 GLU I 484 ASN I 487 -1 O GLU I 484 N ASN I 479
SHEET 1 JA 4 THR J 48 THR J 50 0
SHEET 2 JA 4 VAL J 38 LEU J 40 -1 O VAL J 38 N THR J 50
SHEET 3 JA 4 CYS K 519 ASP K 523 1 O CYS K 519 N VAL J 39
SHEET 4 JA 4 LYS K 4 PHE K 8 -1 O ASP K 5 N THR K 522
SHEET 1 JB 3 ILE J 175 ASP J 179 0
SHEET 2 JB 3 ALA J 377 VAL J 381 1 O ALA J 377 N THR J 176
SHEET 3 JB 3 GLU J 186 LEU J 187 -1 O GLU J 186 N LYS J 380
SHEET 1 JC 5 GLY J 192 PHE J 195 0
SHEET 2 JC 5 THR J 330 GLY J 335 -1 O THR J 330 N PHE J 195
SHEET 3 JC 5 GLY J 318 ILE J 325 -1 N LYS J 321 O ASP J 334
SHEET 4 JC 5 PHE J 219 ASP J 224 -1 O ILE J 220 N GLY J 318
SHEET 5 JC 5 ILE J 301 SER J 302 -1 O ILE J 301 N ASP J 224
SHEET 1 JD 4 GLY J 192 PHE J 195 0
SHEET 2 JD 4 THR J 330 GLY J 335 -1 O THR J 330 N PHE J 195
SHEET 3 JD 4 GLY J 318 ILE J 325 -1 N LYS J 321 O ASP J 334
SHEET 4 JD 4 VAL J 213 GLU J 216 1 O VAL J 213 N ILE J 325
SHEET 1 JE 4 VAL J 273 LYS J 277 0
SHEET 2 JE 4 LEU J 247 ALA J 251 1 O LEU J 247 N ALA J 274
SHEET 3 JE 4 PHE J 219 ASP J 224 1 O PHE J 219 N LEU J 248
SHEET 4 JE 4 ILE J 301 SER J 302 -1 O ILE J 301 N ASP J 224
SHEET 1 JF 6 GLY J 192 PHE J 195 0
SHEET 2 JF 6 THR J 330 GLY J 335 -1 O THR J 330 N PHE J 195
SHEET 3 JF 6 GLY J 318 ILE J 325 -1 N LYS J 321 O ASP J 334
SHEET 4 JF 6 PHE J 219 ASP J 224 -1 O ILE J 220 N GLY J 318
SHEET 5 JF 6 LEU J 247 ALA J 251 1 O LEU J 248 N LEU J 221
SHEET 6 JF 6 VAL J 273 LYS J 277 1 O ALA J 274 N ILE J 249
SHEET 1 JG 6 VAL J 273 LYS J 277 0
SHEET 2 JG 6 LEU J 247 ALA J 251 1 O LEU J 247 N ALA J 274
SHEET 3 JG 6 PHE J 219 ASP J 224 1 O PHE J 219 N LEU J 248
SHEET 4 JG 6 GLY J 318 ILE J 325 -1 O GLY J 318 N ILE J 220
SHEET 5 JG 6 THR J 330 GLY J 335 -1 O THR J 331 N VAL J 324
SHEET 6 JG 6 GLY J 192 PHE J 195 -1 O MET J 193 N ILE J 332
SHEET 1 JH 5 VAL J 273 LYS J 277 0
SHEET 2 JH 5 LEU J 247 ALA J 251 1 O LEU J 247 N ALA J 274
SHEET 3 JH 5 PHE J 219 ASP J 224 1 O PHE J 219 N LEU J 248
SHEET 4 JH 5 GLY J 318 ILE J 325 -1 O GLY J 318 N ILE J 220
SHEET 5 JH 5 VAL J 213 GLU J 216 1 O VAL J 213 N ILE J 325
SHEET 1 JI 2 ILE J 301 SER J 302 0
SHEET 2 JI 2 PHE J 219 ASP J 224 -1 O LEU J 222 N ILE J 301
SHEET 1 JJ 2 LYS J 226 ILE J 227 0
SHEET 2 JJ 2 ASP J 253 VAL J 254 1 O ASP J 253 N ILE J 227
SHEET 1 JK 2 VAL J 411 ALA J 413 0
SHEET 2 JK 2 LEU J 494 PRO J 496 -1 O ASP J 495 N VAL J 412
SHEET 1 JL 2 TYR J 476 ASN J 479 0
SHEET 2 JL 2 GLU J 484 ASN J 487 -1 O GLU J 484 N ASN J 479
SHEET 1 KA 4 THR K 48 THR K 50 0
SHEET 2 KA 4 ASN K 37 LEU K 40 -1 O VAL K 38 N THR K 50
SHEET 3 KA 4 THR L 517 ASP L 523 1 N GLU L 518 O ASN K 37
SHEET 4 KA 4 LYS L 4 PHE L 8 -1 O ASP L 5 N THR L 522
SHEET 1 KB 3 ILE K 175 ASP K 179 0
SHEET 2 KB 3 VAL K 376 VAL K 381 1 O ALA K 377 N THR K 176
SHEET 3 KB 3 GLU K 186 VAL K 190 -1 O GLU K 186 N LYS K 380
SHEET 1 KC 6 MET K 193 PHE K 195 0
SHEET 2 KC 6 THR K 330 GLY K 335 -1 O THR K 330 N PHE K 195
SHEET 3 KC 6 GLY K 318 ILE K 325 -1 N LYS K 321 O ASP K 334
SHEET 4 KC 6 PHE K 219 ILE K 227 -1 O ILE K 220 N GLY K 318
SHEET 5 KC 6 LEU K 247 VAL K 254 1 O LEU K 248 N LEU K 221
SHEET 6 KC 6 VAL K 273 LYS K 277 1 O ALA K 274 N ILE K 249
SHEET 1 KD 4 MET K 193 PHE K 195 0
SHEET 2 KD 4 THR K 330 GLY K 335 -1 O THR K 330 N PHE K 195
SHEET 3 KD 4 GLY K 318 ILE K 325 -1 N LYS K 321 O ASP K 334
SHEET 4 KD 4 VAL K 213 LEU K 215 1 O VAL K 213 N ILE K 325
SHEET 1 KE 2 VAL K 411 ALA K 413 0
SHEET 2 KE 2 LEU K 494 PRO K 496 -1 O ASP K 495 N VAL K 412
SHEET 1 KF 2 TYR K 476 TYR K 478 0
SHEET 2 KF 2 TYR K 485 ASN K 487 -1 O GLY K 486 N GLY K 477
SHEET 1 LA 4 THR L 48 THR L 50 0
SHEET 2 LA 4 ASN L 37 LEU L 40 -1 O VAL L 38 N THR L 50
SHEET 3 LA 4 THR M 517 ASP M 523 1 N GLU M 518 O ASN L 37
SHEET 4 LA 4 LYS M 4 PHE M 8 -1 O ASP M 5 N THR M 522
SHEET 1 LB 3 ILE L 175 ASP L 179 0
SHEET 2 LB 3 ALA L 377 VAL L 381 1 O ALA L 377 N THR L 176
SHEET 3 LB 3 GLU L 186 LEU L 187 -1 O GLU L 186 N LYS L 380
SHEET 1 LC 6 GLY L 192 PHE L 195 0
SHEET 2 LC 6 THR L 330 GLY L 335 -1 O THR L 330 N PHE L 195
SHEET 3 LC 6 GLY L 318 ILE L 325 -1 N LYS L 321 O ASP L 334
SHEET 4 LC 6 PHE L 219 ILE L 227 -1 O ILE L 220 N GLY L 318
SHEET 5 LC 6 LEU L 247 VAL L 254 1 O LEU L 248 N LEU L 221
SHEET 6 LC 6 VAL L 273 LYS L 277 1 O ALA L 274 N ILE L 249
SHEET 1 LD 4 GLY L 192 PHE L 195 0
SHEET 2 LD 4 THR L 330 GLY L 335 -1 O THR L 330 N PHE L 195
SHEET 3 LD 4 GLY L 318 ILE L 325 -1 N LYS L 321 O ASP L 334
SHEET 4 LD 4 VAL L 213 GLU L 216 1 O VAL L 213 N ILE L 325
SHEET 1 LE 2 VAL L 411 ALA L 413 0
SHEET 2 LE 2 LEU L 494 PRO L 496 -1 O ASP L 495 N VAL L 412
SHEET 1 LF 2 TYR L 476 ASN L 479 0
SHEET 2 LF 2 GLU L 484 ASN L 487 -1 O GLU L 484 N ASN L 479
SHEET 1 MA 4 THR M 48 THR M 50 0
SHEET 2 MA 4 ASN M 37 LEU M 40 -1 O VAL M 38 N THR M 50
SHEET 3 MA 4 THR N 517 ASP N 523 1 N GLU N 518 O ASN M 37
SHEET 4 MA 4 LYS N 4 PHE N 8 -1 O ASP N 5 N THR N 522
SHEET 1 MB 3 ILE M 175 ASP M 179 0
SHEET 2 MB 3 VAL M 376 VAL M 381 1 O ALA M 377 N THR M 176
SHEET 3 MB 3 GLU M 186 VAL M 190 -1 O GLU M 186 N LYS M 380
SHEET 1 MC 5 GLY M 192 PHE M 195 0
SHEET 2 MC 5 THR M 330 GLY M 335 -1 O THR M 330 N PHE M 195
SHEET 3 MC 5 GLY M 318 ILE M 325 -1 N LYS M 321 O ASP M 334
SHEET 4 MC 5 PHE M 219 ASP M 224 -1 O ILE M 220 N GLY M 318
SHEET 5 MC 5 ILE M 301 SER M 302 -1 O ILE M 301 N ASP M 224
SHEET 1 MD 4 GLY M 192 PHE M 195 0
SHEET 2 MD 4 THR M 330 GLY M 335 -1 O THR M 330 N PHE M 195
SHEET 3 MD 4 GLY M 318 ILE M 325 -1 N LYS M 321 O ASP M 334
SHEET 4 MD 4 VAL M 213 GLU M 216 1 O VAL M 213 N ILE M 325
SHEET 1 ME 4 VAL M 273 LYS M 277 0
SHEET 2 ME 4 LEU M 247 ALA M 251 1 O LEU M 247 N ALA M 274
SHEET 3 ME 4 PHE M 219 ASP M 224 1 O PHE M 219 N LEU M 248
SHEET 4 ME 4 ILE M 301 SER M 302 -1 O ILE M 301 N ASP M 224
SHEET 1 MF 6 GLY M 192 PHE M 195 0
SHEET 2 MF 6 THR M 330 GLY M 335 -1 O THR M 330 N PHE M 195
SHEET 3 MF 6 GLY M 318 ILE M 325 -1 N LYS M 321 O ASP M 334
SHEET 4 MF 6 PHE M 219 ASP M 224 -1 O ILE M 220 N GLY M 318
SHEET 5 MF 6 LEU M 247 ALA M 251 1 O LEU M 248 N LEU M 221
SHEET 6 MF 6 VAL M 273 LYS M 277 1 O ALA M 274 N ILE M 249
SHEET 1 MG 6 VAL M 273 LYS M 277 0
SHEET 2 MG 6 LEU M 247 ALA M 251 1 O LEU M 247 N ALA M 274
SHEET 3 MG 6 PHE M 219 ASP M 224 1 O PHE M 219 N LEU M 248
SHEET 4 MG 6 GLY M 318 ILE M 325 -1 O GLY M 318 N ILE M 220
SHEET 5 MG 6 THR M 330 GLY M 335 -1 O THR M 331 N VAL M 324
SHEET 6 MG 6 GLY M 192 PHE M 195 -1 O MET M 193 N ILE M 332
SHEET 1 MH 5 VAL M 273 LYS M 277 0
SHEET 2 MH 5 LEU M 247 ALA M 251 1 O LEU M 247 N ALA M 274
SHEET 3 MH 5 PHE M 219 ASP M 224 1 O PHE M 219 N LEU M 248
SHEET 4 MH 5 GLY M 318 ILE M 325 -1 O GLY M 318 N ILE M 220
SHEET 5 MH 5 VAL M 213 GLU M 216 1 O VAL M 213 N ILE M 325
SHEET 1 MI 2 ILE M 301 SER M 302 0
SHEET 2 MI 2 PHE M 219 ASP M 224 -1 O LEU M 222 N ILE M 301
SHEET 1 MJ 2 LYS M 226 ILE M 227 0
SHEET 2 MJ 2 ASP M 253 VAL M 254 1 O ASP M 253 N ILE M 227
SHEET 1 MK 2 VAL M 411 ALA M 413 0
SHEET 2 MK 2 LEU M 494 PRO M 496 -1 O ASP M 495 N VAL M 412
SHEET 1 ML 2 TYR M 476 TYR M 478 0
SHEET 2 ML 2 TYR M 485 ASN M 487 -1 O GLY M 486 N GLY M 477
SHEET 1 NA 3 ILE N 175 ASP N 179 0
SHEET 2 NA 3 VAL N 376 VAL N 381 1 O ALA N 377 N THR N 176
SHEET 3 NA 3 GLU N 186 VAL N 190 -1 O GLU N 186 N LYS N 380
SHEET 1 NB 5 GLY N 192 PHE N 195 0
SHEET 2 NB 5 THR N 330 GLY N 335 -1 O THR N 330 N PHE N 195
SHEET 3 NB 5 GLY N 318 ILE N 325 -1 N LYS N 321 O ASP N 334
SHEET 4 NB 5 PHE N 219 ILE N 227 -1 O ILE N 220 N GLY N 318
SHEET 5 NB 5 ILE N 301 SER N 302 -1 O ILE N 301 N ASP N 224
SHEET 1 NC 4 GLY N 192 PHE N 195 0
SHEET 2 NC 4 THR N 330 GLY N 335 -1 O THR N 330 N PHE N 195
SHEET 3 NC 4 GLY N 318 ILE N 325 -1 N LYS N 321 O ASP N 334
SHEET 4 NC 4 VAL N 213 GLU N 216 1 O VAL N 213 N ILE N 325
SHEET 1 ND 4 VAL N 273 LYS N 277 0
SHEET 2 ND 4 LEU N 247 VAL N 254 1 O LEU N 247 N ALA N 274
SHEET 3 ND 4 PHE N 219 ILE N 227 1 O PHE N 219 N LEU N 248
SHEET 4 ND 4 ILE N 301 SER N 302 -1 O ILE N 301 N ASP N 224
SHEET 1 NE 6 GLY N 192 PHE N 195 0
SHEET 2 NE 6 THR N 330 GLY N 335 -1 O THR N 330 N PHE N 195
SHEET 3 NE 6 GLY N 318 ILE N 325 -1 N LYS N 321 O ASP N 334
SHEET 4 NE 6 PHE N 219 ILE N 227 -1 O ILE N 220 N GLY N 318
SHEET 5 NE 6 LEU N 247 VAL N 254 1 O LEU N 248 N LEU N 221
SHEET 6 NE 6 VAL N 273 LYS N 277 1 O ALA N 274 N ILE N 249
SHEET 1 NF 6 VAL N 273 LYS N 277 0
SHEET 2 NF 6 LEU N 247 VAL N 254 1 O LEU N 247 N ALA N 274
SHEET 3 NF 6 PHE N 219 ILE N 227 1 O PHE N 219 N LEU N 248
SHEET 4 NF 6 GLY N 318 ILE N 325 -1 O GLY N 318 N ILE N 220
SHEET 5 NF 6 THR N 330 GLY N 335 -1 O THR N 331 N VAL N 324
SHEET 6 NF 6 GLY N 192 PHE N 195 -1 O MET N 193 N ILE N 332
SHEET 1 NG 5 VAL N 273 LYS N 277 0
SHEET 2 NG 5 LEU N 247 VAL N 254 1 O LEU N 247 N ALA N 274
SHEET 3 NG 5 PHE N 219 ILE N 227 1 O PHE N 219 N LEU N 248
SHEET 4 NG 5 GLY N 318 ILE N 325 -1 O GLY N 318 N ILE N 220
SHEET 5 NG 5 VAL N 213 GLU N 216 1 O VAL N 213 N ILE N 325
SHEET 1 NH 2 ILE N 301 SER N 302 0
SHEET 2 NH 2 PHE N 219 ILE N 227 -1 O LEU N 222 N ILE N 301
SHEET 1 NI 2 VAL N 411 ALA N 413 0
SHEET 2 NI 2 LEU N 494 PRO N 496 -1 O ASP N 495 N VAL N 412
SHEET 1 NJ 2 TYR N 476 ASN N 479 0
SHEET 2 NJ 2 GLU N 484 ASN N 487 -1 O GLU N 484 N ASN N 479
CRYST1 171.908 171.908 454.592 90.00 90.00 120.00 P 32 42
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 0.005817 0.003358 0.000000 0.00000
SCALE2 0.000000 0.006717 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002200 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
