HEADER STRUCTURAL PROTEIN 13-JUL-16 5LHY
TITLE PB3 DOMAIN OF HUMAN PLK4 (APO)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK4;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U,
COMPND 4 V, W, X, Y, Z, 1, 2, 3, 4, 5, 6, 7, 8, 9, a, b, c, d, e, f, g, h, i,
COMPND 5 j, k, l, m, n, o, p, q, r, s, t, u, v, w, x, y;
COMPND 6 FRAGMENT: UNP RESIDUES 884-970;
COMPND 7 SYNONYM: POLO-LIKE KINASE 4,PLK-4,SERINE/THREONINE-PROTEIN KINASE 18,
COMPND 8 SERINE/THREONINE-PROTEIN KINASE SAK;
COMPND 9 EC: 2.7.11.21;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PLK4, SAK, STK18;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 37762;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834
KEYWDS POLO BOX DOMAIN, CENTRIOLE, TRANSFERASE, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.COTTEE,S.JOHNSON,S.M.LEA
REVDAT 5 10-JAN-24 5LHY 1 REMARK
REVDAT 4 10-MAY-17 5LHY 1 JRNL
REVDAT 3 29-MAR-17 5LHY 1 JRNL
REVDAT 2 08-MAR-17 5LHY 1 JRNL
REVDAT 1 01-MAR-17 5LHY 0
JRNL AUTH M.A.COTTEE,S.JOHNSON,J.W.RAFF,S.M.LEA
JRNL TITL A KEY CENTRIOLE ASSEMBLY INTERACTION INTERFACE BETWEEN HUMAN
JRNL TITL 2 PLK4 AND STIL APPEARS TO NOT BE CONSERVED IN FLIES.
JRNL REF BIOL OPEN V. 6 381 2017
JRNL REFN ESSN 2046-6390
JRNL PMID 28202467
JRNL DOI 10.1242/BIO.024661
REMARK 2
REMARK 2 RESOLUTION. 3.31 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 104.37
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 119305
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.271
REMARK 3 R VALUE (WORKING SET) : 0.269
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 5936
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.500
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.410
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 36300
REMARK 3 ANGLE : 0.528 49380
REMARK 3 CHIRALITY : 0.044 5700
REMARK 3 PLANARITY : 0.005 6240
REMARK 3 DIHEDRAL : 15.865 21360
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 60
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'A' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -50.7535 -73.0113 15.3301
REMARK 3 T TENSOR
REMARK 3 T11: 0.7676 T22: 0.6984
REMARK 3 T33: 1.4530 T12: 0.0951
REMARK 3 T13: -0.1309 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 5.7226 L22: 7.3540
REMARK 3 L33: 5.8034 L12: -0.4374
REMARK 3 L13: 1.1913 L23: -0.0625
REMARK 3 S TENSOR
REMARK 3 S11: 0.1213 S12: -0.2573 S13: 0.7802
REMARK 3 S21: 0.5203 S22: 0.2204 S23: 1.1297
REMARK 3 S31: 0.0028 S32: -0.5307 S33: -0.4976
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'B' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -51.7381 -75.2579 8.9668
REMARK 3 T TENSOR
REMARK 3 T11: 0.7728 T22: 0.7566
REMARK 3 T33: 1.3501 T12: 0.0340
REMARK 3 T13: -0.1819 T23: 0.0745
REMARK 3 L TENSOR
REMARK 3 L11: 5.9580 L22: 4.4033
REMARK 3 L33: 6.1205 L12: 0.4499
REMARK 3 L13: -0.4403 L23: -0.1502
REMARK 3 S TENSOR
REMARK 3 S11: 0.3647 S12: 0.2798 S13: -0.2570
REMARK 3 S21: -0.0210 S22: 0.1614 S23: 0.5578
REMARK 3 S31: -0.1623 S32: -0.3892 S33: -0.4876
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN 'C' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -34.1618 -89.0798 16.2839
REMARK 3 T TENSOR
REMARK 3 T11: 0.8928 T22: 0.8968
REMARK 3 T33: 1.4603 T12: 0.0923
REMARK 3 T13: -0.2684 T23: -0.0503
REMARK 3 L TENSOR
REMARK 3 L11: 6.8310 L22: 4.7153
REMARK 3 L33: 5.2769 L12: -0.7062
REMARK 3 L13: 0.7936 L23: -1.8096
REMARK 3 S TENSOR
REMARK 3 S11: 0.3708 S12: 0.2595 S13: -1.2233
REMARK 3 S21: 0.5487 S22: 0.1498 S23: -0.4647
REMARK 3 S31: 1.0957 S32: 0.8501 S33: -0.4483
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN 'D' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -31.3121 -85.7894 11.2293
REMARK 3 T TENSOR
REMARK 3 T11: 0.8350 T22: 0.9590
REMARK 3 T33: 1.5726 T12: 0.1021
REMARK 3 T13: -0.2266 T23: -0.0813
REMARK 3 L TENSOR
REMARK 3 L11: 6.5557 L22: 4.4505
REMARK 3 L33: 5.0893 L12: -0.1835
REMARK 3 L13: 3.1730 L23: -0.7458
REMARK 3 S TENSOR
REMARK 3 S11: 0.3006 S12: 1.1285 S13: -0.4156
REMARK 3 S21: -0.0533 S22: 0.2771 S23: -0.8946
REMARK 3 S31: 0.5876 S32: 1.2491 S33: -0.6818
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN 'E' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -93.3570-122.6001 41.2951
REMARK 3 T TENSOR
REMARK 3 T11: 0.7670 T22: 0.9373
REMARK 3 T33: 0.5377 T12: 0.1954
REMARK 3 T13: 0.0446 T23: 0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 4.6351 L22: 5.5191
REMARK 3 L33: 3.9217 L12: 0.5995
REMARK 3 L13: -0.0129 L23: 1.4735
REMARK 3 S TENSOR
REMARK 3 S11: -0.1064 S12: 0.0870 S13: -0.0938
REMARK 3 S21: -0.2604 S22: 0.2802 S23: -0.3719
REMARK 3 S31: 0.1345 S32: 0.1804 S33: -0.2076
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN 'F' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A):-100.0029-121.9385 39.1786
REMARK 3 T TENSOR
REMARK 3 T11: 0.7453 T22: 1.0416
REMARK 3 T33: 0.6625 T12: 0.0986
REMARK 3 T13: 0.0626 T23: 0.1216
REMARK 3 L TENSOR
REMARK 3 L11: 2.5262 L22: 6.9436
REMARK 3 L33: 4.1456 L12: 0.1383
REMARK 3 L13: 0.3697 L23: 3.6946
REMARK 3 S TENSOR
REMARK 3 S11: 0.0562 S12: 0.4451 S13: 0.0203
REMARK 3 S21: 0.3442 S22: -0.1104 S23: 0.4551
REMARK 3 S31: 0.2908 S32: -0.1474 S33: 0.0793
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN 'G' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A):-102.3447-121.2914 62.6839
REMARK 3 T TENSOR
REMARK 3 T11: 1.1341 T22: 1.2326
REMARK 3 T33: 0.6254 T12: 0.4218
REMARK 3 T13: 0.2820 T23: 0.2333
REMARK 3 L TENSOR
REMARK 3 L11: 4.2836 L22: 4.8127
REMARK 3 L33: 6.2373 L12: -0.8558
REMARK 3 L13: 0.7164 L23: 0.9004
REMARK 3 S TENSOR
REMARK 3 S11: -0.3215 S12: -0.6928 S13: 0.1615
REMARK 3 S21: 1.0159 S22: 0.6084 S23: 0.1954
REMARK 3 S31: -0.1166 S32: 0.1827 S33: -0.3421
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN 'H' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A):-105.5654-127.0603 61.1771
REMARK 3 T TENSOR
REMARK 3 T11: 1.3102 T22: 0.9386
REMARK 3 T33: 0.7392 T12: 0.3027
REMARK 3 T13: 0.3121 T23: 0.1761
REMARK 3 L TENSOR
REMARK 3 L11: 6.6419 L22: 6.9919
REMARK 3 L33: 4.8714 L12: 0.5621
REMARK 3 L13: -0.7464 L23: -0.8803
REMARK 3 S TENSOR
REMARK 3 S11: -0.1802 S12: -1.0294 S13: -0.1036
REMARK 3 S21: 1.0353 S22: 0.5215 S23: 0.9082
REMARK 3 S31: 0.5756 S32: -0.0212 S33: -0.2301
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN 'I' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.8581-103.8369 38.1743
REMARK 3 T TENSOR
REMARK 3 T11: 1.4063 T22: 0.9444
REMARK 3 T33: 1.1828 T12: 0.2439
REMARK 3 T13: 0.0408 T23: -0.1327
REMARK 3 L TENSOR
REMARK 3 L11: 5.5518 L22: 3.4257
REMARK 3 L33: 5.3302 L12: -1.2521
REMARK 3 L13: 0.7293 L23: -1.2925
REMARK 3 S TENSOR
REMARK 3 S11: 0.0588 S12: -0.2481 S13: 0.6398
REMARK 3 S21: 0.3002 S22: -0.1084 S23: 0.2106
REMARK 3 S31: -1.4227 S32: 0.1395 S33: 0.2347
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN 'J' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.2425-106.1532 41.5562
REMARK 3 T TENSOR
REMARK 3 T11: 1.2227 T22: 0.8775
REMARK 3 T33: 1.1650 T12: 0.2218
REMARK 3 T13: 0.0379 T23: -0.1006
REMARK 3 L TENSOR
REMARK 3 L11: 6.3988 L22: 6.1960
REMARK 3 L33: 6.6271 L12: -0.0853
REMARK 3 L13: 0.2559 L23: 1.1886
REMARK 3 S TENSOR
REMARK 3 S11: -0.6892 S12: -0.8868 S13: 0.9521
REMARK 3 S21: 0.4116 S22: 0.1903 S23: 0.3380
REMARK 3 S31: -0.9647 S32: -1.0864 S33: 0.5485
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN 'K' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.4278-125.3431 41.6436
REMARK 3 T TENSOR
REMARK 3 T11: 1.1684 T22: 0.8343
REMARK 3 T33: 0.9914 T12: 0.1169
REMARK 3 T13: 0.0460 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 6.6901 L22: 3.8096
REMARK 3 L33: 4.1215 L12: -1.8408
REMARK 3 L13: 1.0009 L23: -0.2477
REMARK 3 S TENSOR
REMARK 3 S11: -0.0674 S12: -0.2997 S13: -0.0771
REMARK 3 S21: -0.0021 S22: -0.0581 S23: 0.0342
REMARK 3 S31: 0.0850 S32: 0.4300 S33: 0.1218
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN 'L' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0476-127.4074 38.1904
REMARK 3 T TENSOR
REMARK 3 T11: 1.0572 T22: 1.0058
REMARK 3 T33: 1.0886 T12: 0.2077
REMARK 3 T13: -0.0277 T23: 0.0900
REMARK 3 L TENSOR
REMARK 3 L11: 4.7294 L22: 3.2253
REMARK 3 L33: 7.7809 L12: -0.5114
REMARK 3 L13: -0.7142 L23: 0.6912
REMARK 3 S TENSOR
REMARK 3 S11: -0.3289 S12: 0.2675 S13: -0.5311
REMARK 3 S21: 0.1950 S22: 0.4860 S23: 0.4226
REMARK 3 S31: 0.8871 S32: -0.8202 S33: -0.0152
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN 'M' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3273 -14.0367 41.1586
REMARK 3 T TENSOR
REMARK 3 T11: 0.8133 T22: 0.9656
REMARK 3 T33: 0.6820 T12: -0.1039
REMARK 3 T13: -0.0685 T23: -0.0451
REMARK 3 L TENSOR
REMARK 3 L11: 2.9588 L22: 7.4544
REMARK 3 L33: 3.9353 L12: 2.4218
REMARK 3 L13: -1.2767 L23: -1.9365
REMARK 3 S TENSOR
REMARK 3 S11: -0.0850 S12: -0.3690 S13: 0.1307
REMARK 3 S21: 0.2722 S22: 0.0770 S23: -0.1009
REMARK 3 S31: 0.2629 S32: 0.3288 S33: 0.0420
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN 'N' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.5596 -14.3546 38.2890
REMARK 3 T TENSOR
REMARK 3 T11: 1.0306 T22: 0.9975
REMARK 3 T33: 0.6903 T12: -0.2270
REMARK 3 T13: -0.0440 T23: 0.1159
REMARK 3 L TENSOR
REMARK 3 L11: 4.2106 L22: 5.2171
REMARK 3 L33: 4.4149 L12: 1.5131
REMARK 3 L13: -1.0178 L23: -0.3458
REMARK 3 S TENSOR
REMARK 3 S11: -0.0333 S12: 0.1994 S13: 0.2876
REMARK 3 S21: -0.2706 S22: 0.3046 S23: 0.9899
REMARK 3 S31: 0.3876 S32: -0.2787 S33: 0.2184
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN 'O' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2380 -18.2940 19.8880
REMARK 3 T TENSOR
REMARK 3 T11: 1.5884 T22: 1.1551
REMARK 3 T33: 0.6875 T12: -0.2703
REMARK 3 T13: 0.1159 T23: -0.0745
REMARK 3 L TENSOR
REMARK 3 L11: 4.4360 L22: 7.3347
REMARK 3 L33: 3.7237 L12: 2.3248
REMARK 3 L13: -1.6747 L23: 0.5280
REMARK 3 S TENSOR
REMARK 3 S11: -0.6990 S12: 1.1741 S13: -0.3620
REMARK 3 S21: -1.5179 S22: 0.8960 S23: -0.9008
REMARK 3 S31: 0.8098 S32: 0.0452 S33: -0.4381
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN 'P' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2830 -12.4579 18.3955
REMARK 3 T TENSOR
REMARK 3 T11: 1.6344 T22: 1.3675
REMARK 3 T33: 0.6208 T12: -0.6100
REMARK 3 T13: 0.0740 T23: 0.0720
REMARK 3 L TENSOR
REMARK 3 L11: 6.5514 L22: 6.5742
REMARK 3 L33: 3.4143 L12: 0.8856
REMARK 3 L13: 1.1745 L23: 0.8278
REMARK 3 S TENSOR
REMARK 3 S11: -0.8310 S12: 1.1833 S13: 1.0060
REMARK 3 S21: -2.3773 S22: 0.7692 S23: -0.2888
REMARK 3 S31: 0.6000 S32: 0.0069 S33: -0.9625
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN 'Q' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -64.1050 -97.5599 16.5258
REMARK 3 T TENSOR
REMARK 3 T11: 1.0087 T22: 0.9200
REMARK 3 T33: 1.1355 T12: 0.0128
REMARK 3 T13: -0.0379 T23: -0.0507
REMARK 3 L TENSOR
REMARK 3 L11: 7.7703 L22: 7.7288
REMARK 3 L33: 4.9824 L12: 2.3832
REMARK 3 L13: -1.6105 L23: 0.9405
REMARK 3 S TENSOR
REMARK 3 S11: -0.2090 S12: -1.0220 S13: 0.2851
REMARK 3 S21: 0.8910 S22: -0.1613 S23: 0.3422
REMARK 3 S31: 0.1533 S32: 0.6553 S33: 0.4359
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN 'R' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -68.0192 -97.4051 11.0092
REMARK 3 T TENSOR
REMARK 3 T11: 0.9478 T22: 0.9519
REMARK 3 T33: 0.9868 T12: 0.0607
REMARK 3 T13: -0.1069 T23: -0.0530
REMARK 3 L TENSOR
REMARK 3 L11: 5.6098 L22: 6.2508
REMARK 3 L33: 3.6666 L12: -0.7986
REMARK 3 L13: -0.0184 L23: 1.2694
REMARK 3 S TENSOR
REMARK 3 S11: -0.3351 S12: -0.0411 S13: 0.1313
REMARK 3 S21: 0.3570 S22: 0.1983 S23: 1.1516
REMARK 3 S31: -0.2646 S32: -0.4450 S33: 0.1732
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN 'S' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -49.1261-110.0062 4.0031
REMARK 3 T TENSOR
REMARK 3 T11: 0.9831 T22: 1.0670
REMARK 3 T33: 1.0022 T12: -0.0843
REMARK 3 T13: 0.0073 T23: -0.0785
REMARK 3 L TENSOR
REMARK 3 L11: 5.9356 L22: 5.3699
REMARK 3 L33: 2.9779 L12: -0.6196
REMARK 3 L13: -1.8343 L23: 1.2711
REMARK 3 S TENSOR
REMARK 3 S11: -0.4364 S12: 0.3087 S13: -0.6783
REMARK 3 S21: 0.1916 S22: 0.4438 S23: -0.5716
REMARK 3 S31: 0.6852 S32: 0.6225 S33: 0.0994
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN 'T' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -48.7303-104.5571 -0.0091
REMARK 3 T TENSOR
REMARK 3 T11: 0.8124 T22: 1.1851
REMARK 3 T33: 1.1674 T12: -0.2099
REMARK 3 T13: 0.0542 T23: -0.1282
REMARK 3 L TENSOR
REMARK 3 L11: 8.2625 L22: 6.0287
REMARK 3 L33: 5.6286 L12: -1.2277
REMARK 3 L13: -1.6460 L23: 2.6491
REMARK 3 S TENSOR
REMARK 3 S11: -0.3851 S12: 1.1105 S13: 0.0159
REMARK 3 S21: -0.4296 S22: 0.4651 S23: -0.6306
REMARK 3 S31: 0.1216 S32: 0.9268 S33: -0.2153
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN 'U' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -65.6957-162.1612 59.9325
REMARK 3 T TENSOR
REMARK 3 T11: 0.9702 T22: 0.7767
REMARK 3 T33: 1.1754 T12: -0.0535
REMARK 3 T13: -0.0662 T23: -0.0858
REMARK 3 L TENSOR
REMARK 3 L11: 4.5454 L22: 4.1648
REMARK 3 L33: 7.0552 L12: -0.0809
REMARK 3 L13: -0.6480 L23: 0.1657
REMARK 3 S TENSOR
REMARK 3 S11: -0.0110 S12: 0.4639 S13: -0.0627
REMARK 3 S21: -0.4059 S22: 0.0507 S23: -0.6038
REMARK 3 S31: -0.4841 S32: 0.4578 S33: -0.0605
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN 'V' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -66.7149-166.6816 65.0090
REMARK 3 T TENSOR
REMARK 3 T11: 0.7966 T22: 0.7884
REMARK 3 T33: 1.1726 T12: -0.0389
REMARK 3 T13: -0.1956 T23: 0.0743
REMARK 3 L TENSOR
REMARK 3 L11: 4.4626 L22: 5.4431
REMARK 3 L33: 7.4958 L12: 0.2256
REMARK 3 L13: 1.8835 L23: 1.7482
REMARK 3 S TENSOR
REMARK 3 S11: -0.1693 S12: -0.0795 S13: 0.0740
REMARK 3 S21: 0.2282 S22: 0.2155 S23: -0.6644
REMARK 3 S31: -0.4088 S32: 0.3413 S33: -0.0866
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN 'W' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -78.7539-176.2703 47.0976
REMARK 3 T TENSOR
REMARK 3 T11: 1.0113 T22: 0.7362
REMARK 3 T33: 0.9806 T12: -0.0611
REMARK 3 T13: -0.0626 T23: -0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 5.2455 L22: 4.4885
REMARK 3 L33: 4.4397 L12: 0.2030
REMARK 3 L13: 1.4893 L23: 1.8766
REMARK 3 S TENSOR
REMARK 3 S11: -0.2098 S12: 0.7487 S13: -0.2612
REMARK 3 S21: -0.9649 S22: 0.0471 S23: 0.2075
REMARK 3 S31: -0.0735 S32: 0.0350 S33: 0.1757
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN 'X' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -83.5972-175.0805 51.5107
REMARK 3 T TENSOR
REMARK 3 T11: 0.9455 T22: 0.7543
REMARK 3 T33: 1.0443 T12: 0.0020
REMARK 3 T13: -0.0497 T23: -0.0825
REMARK 3 L TENSOR
REMARK 3 L11: 5.9429 L22: 5.7598
REMARK 3 L33: 2.7107 L12: 0.6223
REMARK 3 L13: 1.9471 L23: 1.5253
REMARK 3 S TENSOR
REMARK 3 S11: -0.1260 S12: 0.0956 S13: -0.1028
REMARK 3 S21: -0.6210 S22: 0.0605 S23: 0.7156
REMARK 3 S31: -0.1749 S32: -0.4094 S33: 0.1303
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (CHAIN 'Y' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -70.3264-119.4783 -9.3175
REMARK 3 T TENSOR
REMARK 3 T11: 0.7679 T22: 1.0753
REMARK 3 T33: 0.7179 T12: -0.0513
REMARK 3 T13: 0.0488 T23: -0.0620
REMARK 3 L TENSOR
REMARK 3 L11: 2.5771 L22: 4.3165
REMARK 3 L33: 8.6429 L12: 0.4836
REMARK 3 L13: 0.5604 L23: -1.8946
REMARK 3 S TENSOR
REMARK 3 S11: -0.2786 S12: 0.4138 S13: 0.2668
REMARK 3 S21: -0.4375 S22: -0.0017 S23: -0.2103
REMARK 3 S31: 0.0885 S32: 0.9353 S33: 0.1785
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: (CHAIN 'Z' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -68.7204-126.1382 -8.3039
REMARK 3 T TENSOR
REMARK 3 T11: 0.9142 T22: 0.9462
REMARK 3 T33: 0.6367 T12: 0.0057
REMARK 3 T13: -0.0077 T23: -0.0319
REMARK 3 L TENSOR
REMARK 3 L11: 3.3498 L22: 5.4521
REMARK 3 L33: 6.6832 L12: 2.4833
REMARK 3 L13: -1.2072 L23: 0.7873
REMARK 3 S TENSOR
REMARK 3 S11: -0.3650 S12: 0.7062 S13: -0.8057
REMARK 3 S21: -0.4988 S22: 0.2869 S23: -0.6583
REMARK 3 S31: 0.6864 S32: 0.8647 S33: 0.0938
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: (CHAIN '1' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -81.5493-121.5412 10.8550
REMARK 3 T TENSOR
REMARK 3 T11: 0.7016 T22: 0.9532
REMARK 3 T33: 0.5458 T12: 0.0039
REMARK 3 T13: -0.0301 T23: 0.0737
REMARK 3 L TENSOR
REMARK 3 L11: 6.3808 L22: 8.4593
REMARK 3 L33: 6.0478 L12: -0.6470
REMARK 3 L13: -1.4040 L23: -0.5703
REMARK 3 S TENSOR
REMARK 3 S11: -0.3410 S12: -0.6987 S13: 0.0177
REMARK 3 S21: 0.5026 S22: 0.3818 S23: 0.7279
REMARK 3 S31: 0.2389 S32: -0.1767 S33: -0.0206
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: (CHAIN '2' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -75.3797-122.7257 13.5990
REMARK 3 T TENSOR
REMARK 3 T11: 0.7629 T22: 0.9753
REMARK 3 T33: 0.7171 T12: 0.0059
REMARK 3 T13: -0.0414 T23: 0.0579
REMARK 3 L TENSOR
REMARK 3 L11: 5.9090 L22: 6.9465
REMARK 3 L33: 4.9130 L12: 1.2247
REMARK 3 L13: -0.3718 L23: -2.6086
REMARK 3 S TENSOR
REMARK 3 S11: 0.0960 S12: -1.0540 S13: -0.5339
REMARK 3 S21: 0.3470 S22: -0.3866 S23: -0.6419
REMARK 3 S31: 0.2496 S32: 0.5563 S33: 0.2008
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: (CHAIN '3' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -94.2978-138.0556 -16.8578
REMARK 3 T TENSOR
REMARK 3 T11: 1.0197 T22: 0.8914
REMARK 3 T33: 0.9914 T12: 0.0815
REMARK 3 T13: -0.1515 T23: -0.2115
REMARK 3 L TENSOR
REMARK 3 L11: 5.3893 L22: 3.0639
REMARK 3 L33: 5.6332 L12: -0.1744
REMARK 3 L13: -2.6979 L23: -0.8733
REMARK 3 S TENSOR
REMARK 3 S11: 0.2046 S12: 0.7060 S13: -1.1336
REMARK 3 S21: -0.6810 S22: -0.4023 S23: 0.4126
REMARK 3 S31: 0.3995 S32: -0.3060 S33: 0.2481
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: (CHAIN '4' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -95.1030-132.2015 -13.5812
REMARK 3 T TENSOR
REMARK 3 T11: 0.9605 T22: 0.9257
REMARK 3 T33: 0.7629 T12: 0.0746
REMARK 3 T13: 0.0563 T23: -0.0883
REMARK 3 L TENSOR
REMARK 3 L11: 5.9233 L22: 5.3688
REMARK 3 L33: 5.0217 L12: 2.5319
REMARK 3 L13: 0.2574 L23: -1.2782
REMARK 3 S TENSOR
REMARK 3 S11: 0.2347 S12: 0.1298 S13: 0.9268
REMARK 3 S21: -0.6511 S22: -0.2418 S23: 0.6061
REMARK 3 S31: -0.0909 S32: 0.2565 S33: 0.1188
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: (CHAIN '5' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -89.7103-147.3365 3.8301
REMARK 3 T TENSOR
REMARK 3 T11: 0.9542 T22: 0.8095
REMARK 3 T33: 0.7383 T12: -0.0609
REMARK 3 T13: 0.0486 T23: -0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 3.1898 L22: 4.0101
REMARK 3 L33: 6.8503 L12: 1.2320
REMARK 3 L13: 0.3805 L23: 0.7316
REMARK 3 S TENSOR
REMARK 3 S11: -0.0257 S12: -0.1991 S13: -0.5252
REMARK 3 S21: 0.2193 S22: 0.0435 S23: -0.4672
REMARK 3 S31: 1.0994 S32: 0.5559 S33: 0.0800
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: (CHAIN '6' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -95.9927-145.5368 5.6362
REMARK 3 T TENSOR
REMARK 3 T11: 0.8722 T22: 0.7288
REMARK 3 T33: 0.9811 T12: -0.0360
REMARK 3 T13: -0.0610 T23: -0.0472
REMARK 3 L TENSOR
REMARK 3 L11: 4.0364 L22: 2.4800
REMARK 3 L33: 7.4940 L12: -0.1486
REMARK 3 L13: -2.0357 L23: -0.8963
REMARK 3 S TENSOR
REMARK 3 S11: 0.0595 S12: -0.0997 S13: -0.4101
REMARK 3 S21: 0.2608 S22: -0.0940 S23: 0.2682
REMARK 3 S31: 1.2655 S32: -0.1365 S33: -0.0236
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: (CHAIN '7' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.8173-111.2060 13.7318
REMARK 3 T TENSOR
REMARK 3 T11: 1.1983 T22: 1.1630
REMARK 3 T33: 1.1754 T12: 0.4299
REMARK 3 T13: -0.0563 T23: 0.1004
REMARK 3 L TENSOR
REMARK 3 L11: 4.5809 L22: 6.0916
REMARK 3 L33: 5.8335 L12: -0.4392
REMARK 3 L13: -0.7206 L23: 1.1307
REMARK 3 S TENSOR
REMARK 3 S11: -0.3406 S12: -0.1226 S13: 0.9001
REMARK 3 S21: -0.3310 S22: -0.4516 S23: 0.9811
REMARK 3 S31: -0.4106 S32: -1.4060 S33: 0.8055
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: (CHAIN '8' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.5249-106.0364 11.0408
REMARK 3 T TENSOR
REMARK 3 T11: 1.3959 T22: 1.4147
REMARK 3 T33: 1.3553 T12: 0.5527
REMARK 3 T13: 0.0625 T23: 0.1349
REMARK 3 L TENSOR
REMARK 3 L11: 3.6566 L22: 5.1453
REMARK 3 L33: 5.6780 L12: -2.4314
REMARK 3 L13: -1.1504 L23: -1.4674
REMARK 3 S TENSOR
REMARK 3 S11: 0.7131 S12: 0.8455 S13: 0.5775
REMARK 3 S21: -0.7780 S22: -0.7884 S23: 0.6655
REMARK 3 S31: -1.6415 S32: -0.9501 S33: 0.0825
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: (CHAIN '9' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1465-122.6162 11.3121
REMARK 3 T TENSOR
REMARK 3 T11: 1.0336 T22: 1.1449
REMARK 3 T33: 1.1095 T12: 0.2817
REMARK 3 T13: 0.0946 T23: 0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 3.6285 L22: 5.2240
REMARK 3 L33: 6.2214 L12: 0.2214
REMARK 3 L13: 0.8569 L23: -1.0133
REMARK 3 S TENSOR
REMARK 3 S11: -0.1761 S12: 0.5936 S13: -0.2465
REMARK 3 S21: -0.1697 S22: 0.2890 S23: -0.1305
REMARK 3 S31: 0.0267 S32: 0.2808 S33: 0.0252
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: (CHAIN 'A' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7062-117.8346 15.5648
REMARK 3 T TENSOR
REMARK 3 T11: 1.0725 T22: 0.9492
REMARK 3 T33: 1.1983 T12: 0.2394
REMARK 3 T13: 0.0382 T23: -0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 3.5044 L22: 6.0876
REMARK 3 L33: 6.9870 L12: -0.7993
REMARK 3 L13: -0.9636 L23: -1.4899
REMARK 3 S TENSOR
REMARK 3 S11: 0.2239 S12: -0.0431 S13: -0.4506
REMARK 3 S21: -0.0224 S22: -0.2524 S23: -0.5531
REMARK 3 S31: -0.5778 S32: 0.6075 S33: -0.0084
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: (CHAIN 'B' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -32.1992 -55.0269 8.6917
REMARK 3 T TENSOR
REMARK 3 T11: 1.0828 T22: 0.8658
REMARK 3 T33: 1.2685 T12: -0.0138
REMARK 3 T13: -0.2235 T23: 0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 4.5766 L22: 10.0094
REMARK 3 L33: 5.0253 L12: 1.4485
REMARK 3 L13: 0.9334 L23: -1.3476
REMARK 3 S TENSOR
REMARK 3 S11: 0.0300 S12: 0.7253 S13: 0.0538
REMARK 3 S21: -1.0815 S22: 0.5977 S23: 1.2742
REMARK 3 S31: -0.0865 S32: -0.1382 S33: -0.7128
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: (CHAIN 'C' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -34.1695 -50.9163 13.5220
REMARK 3 T TENSOR
REMARK 3 T11: 1.2216 T22: 0.8414
REMARK 3 T33: 1.7384 T12: -0.0984
REMARK 3 T13: -0.0984 T23: 0.0999
REMARK 3 L TENSOR
REMARK 3 L11: 4.8276 L22: 4.9878
REMARK 3 L33: 6.7938 L12: 0.8237
REMARK 3 L13: 1.9556 L23: -0.0902
REMARK 3 S TENSOR
REMARK 3 S11: -0.6576 S12: -0.0275 S13: -0.4114
REMARK 3 S21: 0.2549 S22: 0.4805 S23: 1.4155
REMARK 3 S31: -0.5599 S32: -0.2460 S33: 0.1380
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: (CHAIN 'D' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -18.2997 -64.6574 24.5685
REMARK 3 T TENSOR
REMARK 3 T11: 1.4214 T22: 0.9069
REMARK 3 T33: 1.8917 T12: -0.1148
REMARK 3 T13: -0.7248 T23: 0.0494
REMARK 3 L TENSOR
REMARK 3 L11: 6.3814 L22: 8.5890
REMARK 3 L33: 5.7073 L12: 2.9273
REMARK 3 L13: 1.7278 L23: -3.5067
REMARK 3 S TENSOR
REMARK 3 S11: 0.3047 S12: -0.4902 S13: -0.9729
REMARK 3 S21: 2.1041 S22: 0.2246 S23: -3.0154
REMARK 3 S31: 0.3351 S32: 0.8658 S33: -0.0693
REMARK 3 TLS GROUP : 40
REMARK 3 SELECTION: (CHAIN 'E' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -24.1779 -65.9003 28.1336
REMARK 3 T TENSOR
REMARK 3 T11: 1.5929 T22: 1.0179
REMARK 3 T33: 1.2637 T12: 0.0030
REMARK 3 T13: -0.2483 T23: 0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 4.4684 L22: 3.8523
REMARK 3 L33: 5.0050 L12: 0.6071
REMARK 3 L13: 1.6977 L23: -2.5626
REMARK 3 S TENSOR
REMARK 3 S11: 0.4814 S12: -0.7703 S13: -0.7076
REMARK 3 S21: 1.4965 S22: -0.0884 S23: -0.3739
REMARK 3 S31: 0.5095 S32: -0.4009 S33: -0.4493
REMARK 3 TLS GROUP : 41
REMARK 3 SELECTION: (CHAIN 'F' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -87.0068-147.6222 65.7365
REMARK 3 T TENSOR
REMARK 3 T11: 1.4513 T22: 1.4124
REMARK 3 T33: 0.9655 T12: 0.3410
REMARK 3 T13: -0.2026 T23: 0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 5.9043 L22: 5.1787
REMARK 3 L33: 4.1034 L12: -2.2186
REMARK 3 L13: 1.7352 L23: -1.5235
REMARK 3 S TENSOR
REMARK 3 S11: -0.9565 S12: -1.8940 S13: -0.1526
REMARK 3 S21: 1.3101 S22: 0.8714 S23: 0.0024
REMARK 3 S31: -0.5811 S32: -0.8326 S33: 0.1075
REMARK 3 TLS GROUP : 42
REMARK 3 SELECTION: (CHAIN 'G' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -83.7804-141.9026 63.7063
REMARK 3 T TENSOR
REMARK 3 T11: 1.6480 T22: 1.2083
REMARK 3 T33: 1.0056 T12: 0.4210
REMARK 3 T13: -0.3548 T23: -0.1383
REMARK 3 L TENSOR
REMARK 3 L11: 5.0127 L22: 8.7107
REMARK 3 L33: 6.9217 L12: -2.3012
REMARK 3 L13: 2.3600 L23: -2.5155
REMARK 3 S TENSOR
REMARK 3 S11: -1.4576 S12: -1.9569 S13: 0.4810
REMARK 3 S21: 2.1529 S22: 0.9305 S23: -1.2390
REMARK 3 S31: -1.8941 S32: -1.1116 S33: 0.2566
REMARK 3 TLS GROUP : 43
REMARK 3 SELECTION: (CHAIN 'H' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -93.9615-149.7555 43.7457
REMARK 3 T TENSOR
REMARK 3 T11: 0.9211 T22: 1.0049
REMARK 3 T33: 0.8427 T12: -0.0524
REMARK 3 T13: 0.0380 T23: 0.1299
REMARK 3 L TENSOR
REMARK 3 L11: 3.9607 L22: 5.3441
REMARK 3 L33: 8.3239 L12: -4.6111
REMARK 3 L13: 1.7371 L23: -2.1261
REMARK 3 S TENSOR
REMARK 3 S11: 0.1266 S12: -0.6346 S13: -0.5535
REMARK 3 S21: -0.5760 S22: 0.3910 S23: 0.8635
REMARK 3 S31: 0.5756 S32: -1.6826 S33: -0.3892
REMARK 3 TLS GROUP : 44
REMARK 3 SELECTION: (CHAIN 'I' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -87.4944-150.0126 42.2667
REMARK 3 T TENSOR
REMARK 3 T11: 1.0363 T22: 0.7332
REMARK 3 T33: 0.8545 T12: 0.0183
REMARK 3 T13: -0.0382 T23: 0.1010
REMARK 3 L TENSOR
REMARK 3 L11: 8.3080 L22: 4.5257
REMARK 3 L33: 8.6969 L12: -4.0207
REMARK 3 L13: 1.5366 L23: -2.7653
REMARK 3 S TENSOR
REMARK 3 S11: 0.6139 S12: 0.3300 S13: -0.1629
REMARK 3 S21: -0.5286 S22: -0.1605 S23: 0.5561
REMARK 3 S31: 0.9595 S32: -0.2472 S33: -0.2957
REMARK 3 TLS GROUP : 45
REMARK 3 SELECTION: (CHAIN 'J' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A):-115.6324-163.8026 -4.0881
REMARK 3 T TENSOR
REMARK 3 T11: 1.6409 T22: 1.4810
REMARK 3 T33: 2.0013 T12: -0.4563
REMARK 3 T13: -0.2471 T23: -0.0474
REMARK 3 L TENSOR
REMARK 3 L11: 9.2208 L22: 4.9790
REMARK 3 L33: 4.6032 L12: 2.2288
REMARK 3 L13: 0.0509 L23: -0.9579
REMARK 3 S TENSOR
REMARK 3 S11: 0.4617 S12: -0.8224 S13: -1.5018
REMARK 3 S21: 0.9633 S22: -0.4676 S23: -0.2570
REMARK 3 S31: 1.1334 S32: 0.4140 S33: -0.4094
REMARK 3 TLS GROUP : 46
REMARK 3 SELECTION: (CHAIN 'K' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A):-109.8840-164.2482 -7.5994
REMARK 3 T TENSOR
REMARK 3 T11: 1.8574 T22: 1.4068
REMARK 3 T33: 1.9175 T12: -0.2414
REMARK 3 T13: -0.4173 T23: 0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 5.9057 L22: 7.2516
REMARK 3 L33: 2.3385 L12: 1.4462
REMARK 3 L13: 1.9891 L23: -1.6586
REMARK 3 S TENSOR
REMARK 3 S11: 1.3708 S12: 0.1541 S13: -1.8264
REMARK 3 S21: 0.9797 S22: -0.9358 S23: -0.9574
REMARK 3 S31: 1.2774 S32: 0.2911 S33: -1.1966
REMARK 3 TLS GROUP : 47
REMARK 3 SELECTION: (CHAIN 'L' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A):-119.7746-143.9352 -14.8784
REMARK 3 T TENSOR
REMARK 3 T11: 1.3616 T22: 1.4596
REMARK 3 T33: 2.2534 T12: -0.2414
REMARK 3 T13: -0.1347 T23: -0.1199
REMARK 3 L TENSOR
REMARK 3 L11: 6.2167 L22: 3.4344
REMARK 3 L33: 4.6298 L12: 3.9537
REMARK 3 L13: 3.5499 L23: 0.5305
REMARK 3 S TENSOR
REMARK 3 S11: -0.8301 S12: 0.7429 S13: 2.6235
REMARK 3 S21: -0.2218 S22: 0.7149 S23: 0.3400
REMARK 3 S31: -0.5028 S32: -0.2253 S33: 0.2094
REMARK 3 TLS GROUP : 48
REMARK 3 SELECTION: (CHAIN 'M' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A):-119.7570-147.3393 -20.8420
REMARK 3 T TENSOR
REMARK 3 T11: 1.5819 T22: 1.4658
REMARK 3 T33: 1.9949 T12: -0.2528
REMARK 3 T13: -0.3242 T23: 0.0808
REMARK 3 L TENSOR
REMARK 3 L11: 3.1797 L22: 7.0615
REMARK 3 L33: 4.2459 L12: 0.7043
REMARK 3 L13: 1.9198 L23: 1.0954
REMARK 3 S TENSOR
REMARK 3 S11: -0.4257 S12: 0.6244 S13: 1.1246
REMARK 3 S21: -1.1341 S22: 0.1354 S23: 0.9326
REMARK 3 S31: -0.3737 S32: -0.3902 S33: -0.4786
REMARK 3 TLS GROUP : 49
REMARK 3 SELECTION: (CHAIN 'N' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0498-115.6936 -13.2833
REMARK 3 T TENSOR
REMARK 3 T11: 1.7107 T22: 3.8658
REMARK 3 T33: 1.6964 T12: -0.1243
REMARK 3 T13: -0.0524 T23: -0.4611
REMARK 3 L TENSOR
REMARK 3 L11: 2.9703 L22: 0.9967
REMARK 3 L33: 7.5763 L12: -1.1964
REMARK 3 L13: -0.9009 L23: -1.6206
REMARK 3 S TENSOR
REMARK 3 S11: 0.3368 S12: 1.7329 S13: -0.1424
REMARK 3 S21: -0.1794 S22: -0.5784 S23: 1.6957
REMARK 3 S31: -0.0117 S32: -4.3618 S33: 0.2010
REMARK 3 TLS GROUP : 50
REMARK 3 SELECTION: (CHAIN 'O' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6469-109.5067 -16.6645
REMARK 3 T TENSOR
REMARK 3 T11: 1.7780 T22: 3.6632
REMARK 3 T33: 1.6980 T12: 0.2345
REMARK 3 T13: -0.2211 T23: -0.2790
REMARK 3 L TENSOR
REMARK 3 L11: 4.4944 L22: 5.8374
REMARK 3 L33: 9.3316 L12: 1.3661
REMARK 3 L13: -4.8471 L23: -2.7120
REMARK 3 S TENSOR
REMARK 3 S11: -0.4170 S12: 1.6012 S13: -0.7845
REMARK 3 S21: -0.1751 S22: 0.1218 S23: 1.8817
REMARK 3 S31: -0.3762 S32: -4.6480 S33: 0.2189
REMARK 3 TLS GROUP : 51
REMARK 3 SELECTION: (CHAIN 'P' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4808-114.9313 -14.5949
REMARK 3 T TENSOR
REMARK 3 T11: 1.5700 T22: 1.8283
REMARK 3 T33: 1.5519 T12: 0.4076
REMARK 3 T13: 0.1882 T23: 0.2268
REMARK 3 L TENSOR
REMARK 3 L11: 7.2680 L22: 4.3139
REMARK 3 L33: 6.1850 L12: 1.9569
REMARK 3 L13: -0.8919 L23: 3.6221
REMARK 3 S TENSOR
REMARK 3 S11: -1.1823 S12: -0.0425 S13: -0.7696
REMARK 3 S21: 0.8868 S22: 0.2804 S23: -1.3084
REMARK 3 S31: -0.4401 S32: 0.4904 S33: 0.6464
REMARK 3 TLS GROUP : 52
REMARK 3 SELECTION: (CHAIN 'Q' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8923-109.0714 -11.0907
REMARK 3 T TENSOR
REMARK 3 T11: 1.4884 T22: 1.8496
REMARK 3 T33: 1.7858 T12: -0.0478
REMARK 3 T13: -0.0118 T23: 0.2247
REMARK 3 L TENSOR
REMARK 3 L11: 5.4403 L22: 2.0996
REMARK 3 L33: 6.5028 L12: -0.1156
REMARK 3 L13: 0.0766 L23: 1.4652
REMARK 3 S TENSOR
REMARK 3 S11: 0.0260 S12: -0.7823 S13: 0.7633
REMARK 3 S21: 0.6595 S22: -0.7786 S23: -0.2915
REMARK 3 S31: -0.5890 S32: 1.2211 S33: 0.5733
REMARK 3 TLS GROUP : 53
REMARK 3 SELECTION: (CHAIN 'R' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -11.2226 -37.1109 11.9902
REMARK 3 T TENSOR
REMARK 3 T11: 1.3023 T22: 1.1321
REMARK 3 T33: 0.6567 T12: -0.0922
REMARK 3 T13: -0.0500 T23: -0.1369
REMARK 3 L TENSOR
REMARK 3 L11: 4.7066 L22: 6.2102
REMARK 3 L33: 2.8322 L12: 1.1456
REMARK 3 L13: 1.0962 L23: -0.2154
REMARK 3 S TENSOR
REMARK 3 S11: -0.4631 S12: 1.3029 S13: -0.7144
REMARK 3 S21: -0.9781 S22: 0.2104 S23: -0.0172
REMARK 3 S31: 0.7144 S32: 0.0078 S33: 0.1723
REMARK 3 TLS GROUP : 54
REMARK 3 SELECTION: (CHAIN 'S' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.1164 -31.3132 14.2464
REMARK 3 T TENSOR
REMARK 3 T11: 1.3960 T22: 1.1700
REMARK 3 T33: 0.6700 T12: -0.2679
REMARK 3 T13: -0.0446 T23: 0.0539
REMARK 3 L TENSOR
REMARK 3 L11: 3.2034 L22: 4.5153
REMARK 3 L33: 5.9692 L12: 1.7786
REMARK 3 L13: 0.2060 L23: -0.3263
REMARK 3 S TENSOR
REMARK 3 S11: -0.3159 S12: 1.2751 S13: 0.5089
REMARK 3 S21: -0.7295 S22: 0.3552 S23: 0.2387
REMARK 3 S31: -0.4545 S32: 0.4067 S33: 0.1039
REMARK 3 TLS GROUP : 55
REMARK 3 SELECTION: (CHAIN 'T' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.8348 -41.1418 34.3383
REMARK 3 T TENSOR
REMARK 3 T11: 1.4164 T22: 0.9615
REMARK 3 T33: 0.8493 T12: -0.2025
REMARK 3 T13: -0.0550 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 5.5117 L22: 4.0333
REMARK 3 L33: 5.7899 L12: 2.0995
REMARK 3 L13: 0.7727 L23: 0.0793
REMARK 3 S TENSOR
REMARK 3 S11: 0.1906 S12: -0.3017 S13: -0.5742
REMARK 3 S21: 0.6296 S22: 0.1082 S23: -1.0420
REMARK 3 S31: 0.5274 S32: 0.8928 S33: -0.2029
REMARK 3 TLS GROUP : 56
REMARK 3 SELECTION: (CHAIN 'U' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -13.5768 -41.0682 35.1468
REMARK 3 T TENSOR
REMARK 3 T11: 1.3806 T22: 0.9578
REMARK 3 T33: 0.8038 T12: -0.2198
REMARK 3 T13: -0.1295 T23: 0.0783
REMARK 3 L TENSOR
REMARK 3 L11: 4.9455 L22: 4.3478
REMARK 3 L33: 9.2430 L12: 1.8929
REMARK 3 L13: 0.5941 L23: 2.7597
REMARK 3 S TENSOR
REMARK 3 S11: 0.7690 S12: -0.4788 S13: -0.3620
REMARK 3 S21: 0.4279 S22: -0.2418 S23: -0.4219
REMARK 3 S31: 1.1752 S32: 0.3374 S33: -0.4695
REMARK 3 TLS GROUP : 57
REMARK 3 SELECTION: (CHAIN 'V' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -69.8962-196.3694 63.8888
REMARK 3 T TENSOR
REMARK 3 T11: 1.0643 T22: 0.8202
REMARK 3 T33: 1.1141 T12: -0.0399
REMARK 3 T13: -0.1522 T23: -0.0791
REMARK 3 L TENSOR
REMARK 3 L11: 6.8490 L22: 3.5136
REMARK 3 L33: 3.7380 L12: -0.0723
REMARK 3 L13: 2.7657 L23: -0.1580
REMARK 3 S TENSOR
REMARK 3 S11: -0.1454 S12: -0.0187 S13: -0.1212
REMARK 3 S21: 0.4860 S22: 0.3615 S23: 0.1872
REMARK 3 S31: 0.3806 S32: -0.4351 S33: -0.0669
REMARK 3 TLS GROUP : 58
REMARK 3 SELECTION: (CHAIN 'W' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -67.7157-200.7155 59.0168
REMARK 3 T TENSOR
REMARK 3 T11: 1.1745 T22: 0.9140
REMARK 3 T33: 1.3311 T12: -0.0196
REMARK 3 T13: -0.0963 T23: -0.0791
REMARK 3 L TENSOR
REMARK 3 L11: 4.0871 L22: 3.7474
REMARK 3 L33: 7.9322 L12: 0.0767
REMARK 3 L13: 2.1477 L23: 1.5393
REMARK 3 S TENSOR
REMARK 3 S11: 0.4650 S12: 0.6427 S13: -1.2566
REMARK 3 S21: 0.2965 S22: 0.0930 S23: -0.1730
REMARK 3 S31: 1.3542 S32: 0.7754 S33: -0.5996
REMARK 3 TLS GROUP : 59
REMARK 3 SELECTION: (CHAIN 'X' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -48.4936-187.5420 62.5198
REMARK 3 T TENSOR
REMARK 3 T11: 0.9685 T22: 1.2852
REMARK 3 T33: 1.7128 T12: 0.1029
REMARK 3 T13: -0.1330 T23: -0.0829
REMARK 3 L TENSOR
REMARK 3 L11: 4.8639 L22: 3.8783
REMARK 3 L33: 3.7138 L12: 0.9674
REMARK 3 L13: 0.4669 L23: 1.3577
REMARK 3 S TENSOR
REMARK 3 S11: -0.2077 S12: 0.2135 S13: -0.2707
REMARK 3 S21: -0.2974 S22: 0.9553 S23: -1.0332
REMARK 3 S31: -0.0234 S32: 1.3167 S33: -0.6597
REMARK 3 TLS GROUP : 60
REMARK 3 SELECTION: (CHAIN 'Y' AND RESID 890 THROUGH 966)
REMARK 3 ORIGIN FOR THE GROUP (A): -50.1694-186.1298 56.0097
REMARK 3 T TENSOR
REMARK 3 T11: 0.8904 T22: 1.3934
REMARK 3 T33: 1.3416 T12: -0.0585
REMARK 3 T13: -0.1877 T23: -0.0333
REMARK 3 L TENSOR
REMARK 3 L11: 2.0320 L22: 4.2119
REMARK 3 L33: 3.8856 L12: 1.3822
REMARK 3 L13: -1.5575 L23: 0.6230
REMARK 3 S TENSOR
REMARK 3 S11: -0.0767 S12: 0.4329 S13: 0.7987
REMARK 3 S21: -0.4852 S22: 0.6961 S23: -0.6293
REMARK 3 S31: -0.1196 S32: 0.9437 S33: -0.5644
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 5LHY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1200000759.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 119458
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.310
REMARK 200 RESOLUTION RANGE LOW (A) : 110.180
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.31
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.35300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER, MOLREP
REMARK 200 STARTING MODEL: CHAINSAW MODEL BASED ON 1MBY
REMARK 200
REMARK 200 REMARK: CUBES
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 NL PROTEIN SOLUTION (52.3 MG/ML
REMARK 280 PROTEIN IN 20 MM TRIS PH 7.5, 150 MM NACL, 2 MM DTT) AND 100 NL
REMARK 280 MOTHER LIQUOR (32.27% V/V PPG400, 100 MM NACL, 50 MM MGCL2,
REMARK 280 UNBUFFERED), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 162.86500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 110.17500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 110.17500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 244.29750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 110.17500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 110.17500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 81.43250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 110.17500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 110.17500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 244.29750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 110.17500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 110.17500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 81.43250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 162.86500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,
REMARK 300 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28,
REMARK 300 29, 30
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, P
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, R
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 10
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, T
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 11
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: U, V
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 12
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: W, X
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 13
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Y, Z
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 14
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 1, 2
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 15
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 3, 4
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 16
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 5, 6
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 17
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 7, 8
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 18
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 9, a
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 19
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: b, c
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 20
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: d, e
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 21
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: f, g
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 22
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: h, i
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 23
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: j, k
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 24
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: l, m
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 25
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: n, o
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 26
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: p, q
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 27
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: r, s
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 28
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: t, u
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 29
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: v, w
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 30
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: x, y
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 880
REMARK 465 PRO A 881
REMARK 465 MET A 882
REMARK 465 GLY A 883
REMARK 465 SER A 884
REMARK 465 ALA A 885
REMARK 465 GLN A 886
REMARK 465 LEU A 887
REMARK 465 LEU A 888
REMARK 465 LYS A 889
REMARK 465 PRO A 967
REMARK 465 ASN A 968
REMARK 465 PHE A 969
REMARK 465 HIS A 970
REMARK 465 GLY B 880
REMARK 465 PRO B 881
REMARK 465 MET B 882
REMARK 465 GLY B 883
REMARK 465 SER B 884
REMARK 465 ALA B 885
REMARK 465 GLN B 886
REMARK 465 LEU B 887
REMARK 465 LEU B 888
REMARK 465 LYS B 889
REMARK 465 PRO B 967
REMARK 465 ASN B 968
REMARK 465 PHE B 969
REMARK 465 HIS B 970
REMARK 465 GLY C 880
REMARK 465 PRO C 881
REMARK 465 MET C 882
REMARK 465 GLY C 883
REMARK 465 SER C 884
REMARK 465 ALA C 885
REMARK 465 GLN C 886
REMARK 465 LEU C 887
REMARK 465 LEU C 888
REMARK 465 LYS C 889
REMARK 465 PRO C 967
REMARK 465 ASN C 968
REMARK 465 PHE C 969
REMARK 465 HIS C 970
REMARK 465 GLY D 880
REMARK 465 PRO D 881
REMARK 465 MET D 882
REMARK 465 GLY D 883
REMARK 465 SER D 884
REMARK 465 ALA D 885
REMARK 465 GLN D 886
REMARK 465 LEU D 887
REMARK 465 LEU D 888
REMARK 465 LYS D 889
REMARK 465 PRO D 967
REMARK 465 ASN D 968
REMARK 465 PHE D 969
REMARK 465 HIS D 970
REMARK 465 GLY E 880
REMARK 465 PRO E 881
REMARK 465 MET E 882
REMARK 465 GLY E 883
REMARK 465 SER E 884
REMARK 465 ALA E 885
REMARK 465 GLN E 886
REMARK 465 LEU E 887
REMARK 465 LEU E 888
REMARK 465 LYS E 889
REMARK 465 PRO E 967
REMARK 465 ASN E 968
REMARK 465 PHE E 969
REMARK 465 HIS E 970
REMARK 465 GLY F 880
REMARK 465 PRO F 881
REMARK 465 MET F 882
REMARK 465 GLY F 883
REMARK 465 SER F 884
REMARK 465 ALA F 885
REMARK 465 GLN F 886
REMARK 465 LEU F 887
REMARK 465 LEU F 888
REMARK 465 LYS F 889
REMARK 465 PRO F 967
REMARK 465 ASN F 968
REMARK 465 PHE F 969
REMARK 465 HIS F 970
REMARK 465 GLY G 880
REMARK 465 PRO G 881
REMARK 465 MET G 882
REMARK 465 GLY G 883
REMARK 465 SER G 884
REMARK 465 ALA G 885
REMARK 465 GLN G 886
REMARK 465 LEU G 887
REMARK 465 LEU G 888
REMARK 465 LYS G 889
REMARK 465 PRO G 967
REMARK 465 ASN G 968
REMARK 465 PHE G 969
REMARK 465 HIS G 970
REMARK 465 GLY H 880
REMARK 465 PRO H 881
REMARK 465 MET H 882
REMARK 465 GLY H 883
REMARK 465 SER H 884
REMARK 465 ALA H 885
REMARK 465 GLN H 886
REMARK 465 LEU H 887
REMARK 465 LEU H 888
REMARK 465 LYS H 889
REMARK 465 PRO H 967
REMARK 465 ASN H 968
REMARK 465 PHE H 969
REMARK 465 HIS H 970
REMARK 465 GLY I 880
REMARK 465 PRO I 881
REMARK 465 MET I 882
REMARK 465 GLY I 883
REMARK 465 SER I 884
REMARK 465 ALA I 885
REMARK 465 GLN I 886
REMARK 465 LEU I 887
REMARK 465 LEU I 888
REMARK 465 LYS I 889
REMARK 465 PRO I 967
REMARK 465 ASN I 968
REMARK 465 PHE I 969
REMARK 465 HIS I 970
REMARK 465 GLY J 880
REMARK 465 PRO J 881
REMARK 465 MET J 882
REMARK 465 GLY J 883
REMARK 465 SER J 884
REMARK 465 ALA J 885
REMARK 465 GLN J 886
REMARK 465 LEU J 887
REMARK 465 LEU J 888
REMARK 465 LYS J 889
REMARK 465 PRO J 967
REMARK 465 ASN J 968
REMARK 465 PHE J 969
REMARK 465 HIS J 970
REMARK 465 GLY K 880
REMARK 465 PRO K 881
REMARK 465 MET K 882
REMARK 465 GLY K 883
REMARK 465 SER K 884
REMARK 465 ALA K 885
REMARK 465 GLN K 886
REMARK 465 LEU K 887
REMARK 465 LEU K 888
REMARK 465 LYS K 889
REMARK 465 PRO K 967
REMARK 465 ASN K 968
REMARK 465 PHE K 969
REMARK 465 HIS K 970
REMARK 465 GLY L 880
REMARK 465 PRO L 881
REMARK 465 MET L 882
REMARK 465 GLY L 883
REMARK 465 SER L 884
REMARK 465 ALA L 885
REMARK 465 GLN L 886
REMARK 465 LEU L 887
REMARK 465 LEU L 888
REMARK 465 LYS L 889
REMARK 465 PRO L 967
REMARK 465 ASN L 968
REMARK 465 PHE L 969
REMARK 465 HIS L 970
REMARK 465 GLY M 880
REMARK 465 PRO M 881
REMARK 465 MET M 882
REMARK 465 GLY M 883
REMARK 465 SER M 884
REMARK 465 ALA M 885
REMARK 465 GLN M 886
REMARK 465 LEU M 887
REMARK 465 LEU M 888
REMARK 465 LYS M 889
REMARK 465 PRO M 967
REMARK 465 ASN M 968
REMARK 465 PHE M 969
REMARK 465 HIS M 970
REMARK 465 GLY N 880
REMARK 465 PRO N 881
REMARK 465 MET N 882
REMARK 465 GLY N 883
REMARK 465 SER N 884
REMARK 465 ALA N 885
REMARK 465 GLN N 886
REMARK 465 LEU N 887
REMARK 465 LEU N 888
REMARK 465 LYS N 889
REMARK 465 PRO N 967
REMARK 465 ASN N 968
REMARK 465 PHE N 969
REMARK 465 HIS N 970
REMARK 465 GLY O 880
REMARK 465 PRO O 881
REMARK 465 MET O 882
REMARK 465 GLY O 883
REMARK 465 SER O 884
REMARK 465 ALA O 885
REMARK 465 GLN O 886
REMARK 465 LEU O 887
REMARK 465 LEU O 888
REMARK 465 LYS O 889
REMARK 465 PRO O 967
REMARK 465 ASN O 968
REMARK 465 PHE O 969
REMARK 465 HIS O 970
REMARK 465 GLY P 880
REMARK 465 PRO P 881
REMARK 465 MET P 882
REMARK 465 GLY P 883
REMARK 465 SER P 884
REMARK 465 ALA P 885
REMARK 465 GLN P 886
REMARK 465 LEU P 887
REMARK 465 LEU P 888
REMARK 465 LYS P 889
REMARK 465 PRO P 967
REMARK 465 ASN P 968
REMARK 465 PHE P 969
REMARK 465 HIS P 970
REMARK 465 GLY Q 880
REMARK 465 PRO Q 881
REMARK 465 MET Q 882
REMARK 465 GLY Q 883
REMARK 465 SER Q 884
REMARK 465 ALA Q 885
REMARK 465 GLN Q 886
REMARK 465 LEU Q 887
REMARK 465 LEU Q 888
REMARK 465 LYS Q 889
REMARK 465 PRO Q 967
REMARK 465 ASN Q 968
REMARK 465 PHE Q 969
REMARK 465 HIS Q 970
REMARK 465 GLY R 880
REMARK 465 PRO R 881
REMARK 465 MET R 882
REMARK 465 GLY R 883
REMARK 465 SER R 884
REMARK 465 ALA R 885
REMARK 465 GLN R 886
REMARK 465 LEU R 887
REMARK 465 LEU R 888
REMARK 465 LYS R 889
REMARK 465 PRO R 967
REMARK 465 ASN R 968
REMARK 465 PHE R 969
REMARK 465 HIS R 970
REMARK 465 GLY S 880
REMARK 465 PRO S 881
REMARK 465 MET S 882
REMARK 465 GLY S 883
REMARK 465 SER S 884
REMARK 465 ALA S 885
REMARK 465 GLN S 886
REMARK 465 LEU S 887
REMARK 465 LEU S 888
REMARK 465 LYS S 889
REMARK 465 PRO S 967
REMARK 465 ASN S 968
REMARK 465 PHE S 969
REMARK 465 HIS S 970
REMARK 465 GLY T 880
REMARK 465 PRO T 881
REMARK 465 MET T 882
REMARK 465 GLY T 883
REMARK 465 SER T 884
REMARK 465 ALA T 885
REMARK 465 GLN T 886
REMARK 465 LEU T 887
REMARK 465 LEU T 888
REMARK 465 LYS T 889
REMARK 465 PRO T 967
REMARK 465 ASN T 968
REMARK 465 PHE T 969
REMARK 465 HIS T 970
REMARK 465 GLY U 880
REMARK 465 PRO U 881
REMARK 465 MET U 882
REMARK 465 GLY U 883
REMARK 465 SER U 884
REMARK 465 ALA U 885
REMARK 465 GLN U 886
REMARK 465 LEU U 887
REMARK 465 LEU U 888
REMARK 465 LYS U 889
REMARK 465 PRO U 967
REMARK 465 ASN U 968
REMARK 465 PHE U 969
REMARK 465 HIS U 970
REMARK 465 GLY V 880
REMARK 465 PRO V 881
REMARK 465 MET V 882
REMARK 465 GLY V 883
REMARK 465 SER V 884
REMARK 465 ALA V 885
REMARK 465 GLN V 886
REMARK 465 LEU V 887
REMARK 465 LEU V 888
REMARK 465 LYS V 889
REMARK 465 PRO V 967
REMARK 465 ASN V 968
REMARK 465 PHE V 969
REMARK 465 HIS V 970
REMARK 465 GLY W 880
REMARK 465 PRO W 881
REMARK 465 MET W 882
REMARK 465 GLY W 883
REMARK 465 SER W 884
REMARK 465 ALA W 885
REMARK 465 GLN W 886
REMARK 465 LEU W 887
REMARK 465 LEU W 888
REMARK 465 LYS W 889
REMARK 465 PRO W 967
REMARK 465 ASN W 968
REMARK 465 PHE W 969
REMARK 465 HIS W 970
REMARK 465 GLY X 880
REMARK 465 PRO X 881
REMARK 465 MET X 882
REMARK 465 GLY X 883
REMARK 465 SER X 884
REMARK 465 ALA X 885
REMARK 465 GLN X 886
REMARK 465 LEU X 887
REMARK 465 LEU X 888
REMARK 465 LYS X 889
REMARK 465 PRO X 967
REMARK 465 ASN X 968
REMARK 465 PHE X 969
REMARK 465 HIS X 970
REMARK 465 GLY Y 880
REMARK 465 PRO Y 881
REMARK 465 MET Y 882
REMARK 465 GLY Y 883
REMARK 465 SER Y 884
REMARK 465 ALA Y 885
REMARK 465 GLN Y 886
REMARK 465 LEU Y 887
REMARK 465 LEU Y 888
REMARK 465 LYS Y 889
REMARK 465 PRO Y 967
REMARK 465 ASN Y 968
REMARK 465 PHE Y 969
REMARK 465 HIS Y 970
REMARK 465 GLY Z 880
REMARK 465 PRO Z 881
REMARK 465 MET Z 882
REMARK 465 GLY Z 883
REMARK 465 SER Z 884
REMARK 465 ALA Z 885
REMARK 465 GLN Z 886
REMARK 465 LEU Z 887
REMARK 465 LEU Z 888
REMARK 465 LYS Z 889
REMARK 465 PRO Z 967
REMARK 465 ASN Z 968
REMARK 465 PHE Z 969
REMARK 465 HIS Z 970
REMARK 465 GLY 1 880
REMARK 465 PRO 1 881
REMARK 465 MET 1 882
REMARK 465 GLY 1 883
REMARK 465 SER 1 884
REMARK 465 ALA 1 885
REMARK 465 GLN 1 886
REMARK 465 LEU 1 887
REMARK 465 LEU 1 888
REMARK 465 LYS 1 889
REMARK 465 PRO 1 967
REMARK 465 ASN 1 968
REMARK 465 PHE 1 969
REMARK 465 HIS 1 970
REMARK 465 GLY 2 880
REMARK 465 PRO 2 881
REMARK 465 MET 2 882
REMARK 465 GLY 2 883
REMARK 465 SER 2 884
REMARK 465 ALA 2 885
REMARK 465 GLN 2 886
REMARK 465 LEU 2 887
REMARK 465 LEU 2 888
REMARK 465 LYS 2 889
REMARK 465 PRO 2 967
REMARK 465 ASN 2 968
REMARK 465 PHE 2 969
REMARK 465 HIS 2 970
REMARK 465 GLY 3 880
REMARK 465 PRO 3 881
REMARK 465 MET 3 882
REMARK 465 GLY 3 883
REMARK 465 SER 3 884
REMARK 465 ALA 3 885
REMARK 465 GLN 3 886
REMARK 465 LEU 3 887
REMARK 465 LEU 3 888
REMARK 465 LYS 3 889
REMARK 465 PRO 3 967
REMARK 465 ASN 3 968
REMARK 465 PHE 3 969
REMARK 465 HIS 3 970
REMARK 465 GLY 4 880
REMARK 465 PRO 4 881
REMARK 465 MET 4 882
REMARK 465 GLY 4 883
REMARK 465 SER 4 884
REMARK 465 ALA 4 885
REMARK 465 GLN 4 886
REMARK 465 LEU 4 887
REMARK 465 LEU 4 888
REMARK 465 LYS 4 889
REMARK 465 PRO 4 967
REMARK 465 ASN 4 968
REMARK 465 PHE 4 969
REMARK 465 HIS 4 970
REMARK 465 GLY 5 880
REMARK 465 PRO 5 881
REMARK 465 MET 5 882
REMARK 465 GLY 5 883
REMARK 465 SER 5 884
REMARK 465 ALA 5 885
REMARK 465 GLN 5 886
REMARK 465 LEU 5 887
REMARK 465 LEU 5 888
REMARK 465 LYS 5 889
REMARK 465 PRO 5 967
REMARK 465 ASN 5 968
REMARK 465 PHE 5 969
REMARK 465 HIS 5 970
REMARK 465 GLY 6 880
REMARK 465 PRO 6 881
REMARK 465 MET 6 882
REMARK 465 GLY 6 883
REMARK 465 SER 6 884
REMARK 465 ALA 6 885
REMARK 465 GLN 6 886
REMARK 465 LEU 6 887
REMARK 465 LEU 6 888
REMARK 465 LYS 6 889
REMARK 465 PRO 6 967
REMARK 465 ASN 6 968
REMARK 465 PHE 6 969
REMARK 465 HIS 6 970
REMARK 465 GLY 7 880
REMARK 465 PRO 7 881
REMARK 465 MET 7 882
REMARK 465 GLY 7 883
REMARK 465 SER 7 884
REMARK 465 ALA 7 885
REMARK 465 GLN 7 886
REMARK 465 LEU 7 887
REMARK 465 LEU 7 888
REMARK 465 LYS 7 889
REMARK 465 PRO 7 967
REMARK 465 ASN 7 968
REMARK 465 PHE 7 969
REMARK 465 HIS 7 970
REMARK 465 GLY 8 880
REMARK 465 PRO 8 881
REMARK 465 MET 8 882
REMARK 465 GLY 8 883
REMARK 465 SER 8 884
REMARK 465 ALA 8 885
REMARK 465 GLN 8 886
REMARK 465 LEU 8 887
REMARK 465 LEU 8 888
REMARK 465 LYS 8 889
REMARK 465 PRO 8 967
REMARK 465 ASN 8 968
REMARK 465 PHE 8 969
REMARK 465 HIS 8 970
REMARK 465 GLY 9 880
REMARK 465 PRO 9 881
REMARK 465 MET 9 882
REMARK 465 GLY 9 883
REMARK 465 SER 9 884
REMARK 465 ALA 9 885
REMARK 465 GLN 9 886
REMARK 465 LEU 9 887
REMARK 465 LEU 9 888
REMARK 465 LYS 9 889
REMARK 465 PRO 9 967
REMARK 465 ASN 9 968
REMARK 465 PHE 9 969
REMARK 465 HIS 9 970
REMARK 465 GLY a 880
REMARK 465 PRO a 881
REMARK 465 MET a 882
REMARK 465 GLY a 883
REMARK 465 SER a 884
REMARK 465 ALA a 885
REMARK 465 GLN a 886
REMARK 465 LEU a 887
REMARK 465 LEU a 888
REMARK 465 LYS a 889
REMARK 465 PRO a 967
REMARK 465 ASN a 968
REMARK 465 PHE a 969
REMARK 465 HIS a 970
REMARK 465 GLY b 880
REMARK 465 PRO b 881
REMARK 465 MET b 882
REMARK 465 GLY b 883
REMARK 465 SER b 884
REMARK 465 ALA b 885
REMARK 465 GLN b 886
REMARK 465 LEU b 887
REMARK 465 LEU b 888
REMARK 465 LYS b 889
REMARK 465 PRO b 967
REMARK 465 ASN b 968
REMARK 465 PHE b 969
REMARK 465 HIS b 970
REMARK 465 GLY c 880
REMARK 465 PRO c 881
REMARK 465 MET c 882
REMARK 465 GLY c 883
REMARK 465 SER c 884
REMARK 465 ALA c 885
REMARK 465 GLN c 886
REMARK 465 LEU c 887
REMARK 465 LEU c 888
REMARK 465 LYS c 889
REMARK 465 PRO c 967
REMARK 465 ASN c 968
REMARK 465 PHE c 969
REMARK 465 HIS c 970
REMARK 465 GLY d 880
REMARK 465 PRO d 881
REMARK 465 MET d 882
REMARK 465 GLY d 883
REMARK 465 SER d 884
REMARK 465 ALA d 885
REMARK 465 GLN d 886
REMARK 465 LEU d 887
REMARK 465 LEU d 888
REMARK 465 LYS d 889
REMARK 465 PRO d 967
REMARK 465 ASN d 968
REMARK 465 PHE d 969
REMARK 465 HIS d 970
REMARK 465 GLY e 880
REMARK 465 PRO e 881
REMARK 465 MET e 882
REMARK 465 GLY e 883
REMARK 465 SER e 884
REMARK 465 ALA e 885
REMARK 465 GLN e 886
REMARK 465 LEU e 887
REMARK 465 LEU e 888
REMARK 465 LYS e 889
REMARK 465 PRO e 967
REMARK 465 ASN e 968
REMARK 465 PHE e 969
REMARK 465 HIS e 970
REMARK 465 GLY f 880
REMARK 465 PRO f 881
REMARK 465 MET f 882
REMARK 465 GLY f 883
REMARK 465 SER f 884
REMARK 465 ALA f 885
REMARK 465 GLN f 886
REMARK 465 LEU f 887
REMARK 465 LEU f 888
REMARK 465 LYS f 889
REMARK 465 PRO f 967
REMARK 465 ASN f 968
REMARK 465 PHE f 969
REMARK 465 HIS f 970
REMARK 465 GLY g 880
REMARK 465 PRO g 881
REMARK 465 MET g 882
REMARK 465 GLY g 883
REMARK 465 SER g 884
REMARK 465 ALA g 885
REMARK 465 GLN g 886
REMARK 465 LEU g 887
REMARK 465 LEU g 888
REMARK 465 LYS g 889
REMARK 465 PRO g 967
REMARK 465 ASN g 968
REMARK 465 PHE g 969
REMARK 465 HIS g 970
REMARK 465 GLY h 880
REMARK 465 PRO h 881
REMARK 465 MET h 882
REMARK 465 GLY h 883
REMARK 465 SER h 884
REMARK 465 ALA h 885
REMARK 465 GLN h 886
REMARK 465 LEU h 887
REMARK 465 LEU h 888
REMARK 465 LYS h 889
REMARK 465 PRO h 967
REMARK 465 ASN h 968
REMARK 465 PHE h 969
REMARK 465 HIS h 970
REMARK 465 GLY i 880
REMARK 465 PRO i 881
REMARK 465 MET i 882
REMARK 465 GLY i 883
REMARK 465 SER i 884
REMARK 465 ALA i 885
REMARK 465 GLN i 886
REMARK 465 LEU i 887
REMARK 465 LEU i 888
REMARK 465 LYS i 889
REMARK 465 PRO i 967
REMARK 465 ASN i 968
REMARK 465 PHE i 969
REMARK 465 HIS i 970
REMARK 465 GLY j 880
REMARK 465 PRO j 881
REMARK 465 MET j 882
REMARK 465 GLY j 883
REMARK 465 SER j 884
REMARK 465 ALA j 885
REMARK 465 GLN j 886
REMARK 465 LEU j 887
REMARK 465 LEU j 888
REMARK 465 LYS j 889
REMARK 465 PRO j 967
REMARK 465 ASN j 968
REMARK 465 PHE j 969
REMARK 465 HIS j 970
REMARK 465 GLY k 880
REMARK 465 PRO k 881
REMARK 465 MET k 882
REMARK 465 GLY k 883
REMARK 465 SER k 884
REMARK 465 ALA k 885
REMARK 465 GLN k 886
REMARK 465 LEU k 887
REMARK 465 LEU k 888
REMARK 465 LYS k 889
REMARK 465 PRO k 967
REMARK 465 ASN k 968
REMARK 465 PHE k 969
REMARK 465 HIS k 970
REMARK 465 GLY l 880
REMARK 465 PRO l 881
REMARK 465 MET l 882
REMARK 465 GLY l 883
REMARK 465 SER l 884
REMARK 465 ALA l 885
REMARK 465 GLN l 886
REMARK 465 LEU l 887
REMARK 465 LEU l 888
REMARK 465 LYS l 889
REMARK 465 PRO l 967
REMARK 465 ASN l 968
REMARK 465 PHE l 969
REMARK 465 HIS l 970
REMARK 465 GLY m 880
REMARK 465 PRO m 881
REMARK 465 MET m 882
REMARK 465 GLY m 883
REMARK 465 SER m 884
REMARK 465 ALA m 885
REMARK 465 GLN m 886
REMARK 465 LEU m 887
REMARK 465 LEU m 888
REMARK 465 LYS m 889
REMARK 465 PRO m 967
REMARK 465 ASN m 968
REMARK 465 PHE m 969
REMARK 465 HIS m 970
REMARK 465 GLY n 880
REMARK 465 PRO n 881
REMARK 465 MET n 882
REMARK 465 GLY n 883
REMARK 465 SER n 884
REMARK 465 ALA n 885
REMARK 465 GLN n 886
REMARK 465 LEU n 887
REMARK 465 LEU n 888
REMARK 465 LYS n 889
REMARK 465 PRO n 967
REMARK 465 ASN n 968
REMARK 465 PHE n 969
REMARK 465 HIS n 970
REMARK 465 GLY o 880
REMARK 465 PRO o 881
REMARK 465 MET o 882
REMARK 465 GLY o 883
REMARK 465 SER o 884
REMARK 465 ALA o 885
REMARK 465 GLN o 886
REMARK 465 LEU o 887
REMARK 465 LEU o 888
REMARK 465 LYS o 889
REMARK 465 PRO o 967
REMARK 465 ASN o 968
REMARK 465 PHE o 969
REMARK 465 HIS o 970
REMARK 465 GLY p 880
REMARK 465 PRO p 881
REMARK 465 MET p 882
REMARK 465 GLY p 883
REMARK 465 SER p 884
REMARK 465 ALA p 885
REMARK 465 GLN p 886
REMARK 465 LEU p 887
REMARK 465 LEU p 888
REMARK 465 LYS p 889
REMARK 465 PRO p 967
REMARK 465 ASN p 968
REMARK 465 PHE p 969
REMARK 465 HIS p 970
REMARK 465 GLY q 880
REMARK 465 PRO q 881
REMARK 465 MET q 882
REMARK 465 GLY q 883
REMARK 465 SER q 884
REMARK 465 ALA q 885
REMARK 465 GLN q 886
REMARK 465 LEU q 887
REMARK 465 LEU q 888
REMARK 465 LYS q 889
REMARK 465 PRO q 967
REMARK 465 ASN q 968
REMARK 465 PHE q 969
REMARK 465 HIS q 970
REMARK 465 GLY r 880
REMARK 465 PRO r 881
REMARK 465 MET r 882
REMARK 465 GLY r 883
REMARK 465 SER r 884
REMARK 465 ALA r 885
REMARK 465 GLN r 886
REMARK 465 LEU r 887
REMARK 465 LEU r 888
REMARK 465 LYS r 889
REMARK 465 PRO r 967
REMARK 465 ASN r 968
REMARK 465 PHE r 969
REMARK 465 HIS r 970
REMARK 465 GLY s 880
REMARK 465 PRO s 881
REMARK 465 MET s 882
REMARK 465 GLY s 883
REMARK 465 SER s 884
REMARK 465 ALA s 885
REMARK 465 GLN s 886
REMARK 465 LEU s 887
REMARK 465 LEU s 888
REMARK 465 LYS s 889
REMARK 465 PRO s 967
REMARK 465 ASN s 968
REMARK 465 PHE s 969
REMARK 465 HIS s 970
REMARK 465 GLY t 880
REMARK 465 PRO t 881
REMARK 465 MET t 882
REMARK 465 GLY t 883
REMARK 465 SER t 884
REMARK 465 ALA t 885
REMARK 465 GLN t 886
REMARK 465 LEU t 887
REMARK 465 LEU t 888
REMARK 465 LYS t 889
REMARK 465 PRO t 967
REMARK 465 ASN t 968
REMARK 465 PHE t 969
REMARK 465 HIS t 970
REMARK 465 GLY u 880
REMARK 465 PRO u 881
REMARK 465 MET u 882
REMARK 465 GLY u 883
REMARK 465 SER u 884
REMARK 465 ALA u 885
REMARK 465 GLN u 886
REMARK 465 LEU u 887
REMARK 465 LEU u 888
REMARK 465 LYS u 889
REMARK 465 PRO u 967
REMARK 465 ASN u 968
REMARK 465 PHE u 969
REMARK 465 HIS u 970
REMARK 465 GLY v 880
REMARK 465 PRO v 881
REMARK 465 MET v 882
REMARK 465 GLY v 883
REMARK 465 SER v 884
REMARK 465 ALA v 885
REMARK 465 GLN v 886
REMARK 465 LEU v 887
REMARK 465 LEU v 888
REMARK 465 LYS v 889
REMARK 465 PRO v 967
REMARK 465 ASN v 968
REMARK 465 PHE v 969
REMARK 465 HIS v 970
REMARK 465 GLY w 880
REMARK 465 PRO w 881
REMARK 465 MET w 882
REMARK 465 GLY w 883
REMARK 465 SER w 884
REMARK 465 ALA w 885
REMARK 465 GLN w 886
REMARK 465 LEU w 887
REMARK 465 LEU w 888
REMARK 465 LYS w 889
REMARK 465 PRO w 967
REMARK 465 ASN w 968
REMARK 465 PHE w 969
REMARK 465 HIS w 970
REMARK 465 GLY x 880
REMARK 465 PRO x 881
REMARK 465 MET x 882
REMARK 465 GLY x 883
REMARK 465 SER x 884
REMARK 465 ALA x 885
REMARK 465 GLN x 886
REMARK 465 LEU x 887
REMARK 465 LEU x 888
REMARK 465 LYS x 889
REMARK 465 PRO x 967
REMARK 465 ASN x 968
REMARK 465 PHE x 969
REMARK 465 HIS x 970
REMARK 465 GLY y 880
REMARK 465 PRO y 881
REMARK 465 MET y 882
REMARK 465 GLY y 883
REMARK 465 SER y 884
REMARK 465 ALA y 885
REMARK 465 GLN y 886
REMARK 465 LEU y 887
REMARK 465 LEU y 888
REMARK 465 LYS y 889
REMARK 465 PRO y 967
REMARK 465 ASN y 968
REMARK 465 PHE y 969
REMARK 465 HIS y 970
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 OG SER j 930 OD1 ASN j 932 2.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN A 901 -159.99 -94.85
REMARK 500 GLN B 901 -159.45 -94.67
REMARK 500 ASN C 964 78.23 -119.99
REMARK 500 GLN E 901 -159.75 -94.78
REMARK 500 GLN F 901 -158.73 -93.45
REMARK 500 GLN G 901 -159.20 -94.59
REMARK 500 GLN H 901 -159.92 -94.60
REMARK 500 GLN J 901 -159.85 -95.29
REMARK 500 ASN J 964 76.79 -119.72
REMARK 500 ASN K 964 77.89 -119.04
REMARK 500 GLN L 901 -159.65 -94.86
REMARK 500 GLN M 901 -159.24 -94.17
REMARK 500 GLN N 901 -158.78 -95.23
REMARK 500 GLN O 901 -159.65 -94.77
REMARK 500 GLN P 901 -159.36 -94.47
REMARK 500 GLN Q 901 -159.99 -95.16
REMARK 500 GLN R 901 -159.63 -95.31
REMARK 500 GLN S 901 -159.79 -95.41
REMARK 500 ASN T 964 77.75 -119.84
REMARK 500 GLN U 901 -159.39 -94.73
REMARK 500 GLN W 901 -159.47 -95.35
REMARK 500 GLN Z 901 -159.99 -95.10
REMARK 500 GLN 1 901 -159.62 -94.51
REMARK 500 GLN 2 901 -159.47 -94.68
REMARK 500 GLN 3 901 -159.39 -94.79
REMARK 500 GLN 5 901 -159.76 -94.81
REMARK 500 ASN 6 964 78.21 -119.74
REMARK 500 ASN 8 964 77.81 -119.77
REMARK 500 GLN 9 901 -159.48 -95.20
REMARK 500 GLN a 901 -159.74 -93.99
REMARK 500 GLN d 901 -159.92 -94.96
REMARK 500 GLN e 901 -159.96 -95.13
REMARK 500 GLN f 901 -159.92 -96.12
REMARK 500 GLN h 901 -159.49 -95.22
REMARK 500 ASN k 964 76.96 -119.45
REMARK 500 ASN n 964 78.33 -119.37
REMARK 500 GLN r 901 -159.93 -95.16
REMARK 500 GLN t 901 -159.97 -95.02
REMARK 500 GLN u 901 -159.89 -94.58
REMARK 500 GLN v 901 -159.67 -94.59
REMARK 500 GLN w 901 -159.89 -95.09
REMARK 500 GLN x 901 -159.54 -95.33
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5LHY A 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY B 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY C 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY D 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY E 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY F 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY G 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY H 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY I 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY J 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY K 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY L 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY M 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY N 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY O 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY P 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY Q 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY R 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY S 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY T 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY U 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY V 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY W 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY X 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY Y 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY Z 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY 1 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY 2 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY 3 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY 4 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY 5 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY 6 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY 7 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY 8 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY 9 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY a 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY b 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY c 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY d 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY e 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY f 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY g 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY h 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY i 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY j 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY k 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY l 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY m 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY n 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY o 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY p 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY q 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY r 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY s 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY t 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY u 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY v 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY w 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY x 884 970 UNP O00444 PLK4_HUMAN 884 970
DBREF 5LHY y 884 970 UNP O00444 PLK4_HUMAN 884 970
SEQADV 5LHY GLY A 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO A 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET A 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY A 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY B 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO B 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET B 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY B 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY C 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO C 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET C 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY C 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY D 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO D 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET D 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY D 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY E 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO E 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET E 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY E 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY F 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO F 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET F 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY F 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY G 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO G 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET G 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY G 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY H 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO H 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET H 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY H 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY I 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO I 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET I 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY I 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY J 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO J 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET J 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY J 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY K 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO K 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET K 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY K 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY L 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO L 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET L 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY L 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY M 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO M 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET M 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY M 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY N 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO N 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET N 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY N 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY O 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO O 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET O 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY O 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY P 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO P 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET P 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY P 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY Q 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO Q 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET Q 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY Q 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY R 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO R 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET R 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY R 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY S 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO S 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET S 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY S 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY T 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO T 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET T 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY T 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY U 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO U 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET U 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY U 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY V 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO V 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET V 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY V 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY W 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO W 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET W 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY W 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY X 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO X 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET X 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY X 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY Y 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO Y 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET Y 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY Y 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY Z 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO Z 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET Z 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY Z 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY 1 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO 1 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET 1 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY 1 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY 2 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO 2 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET 2 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY 2 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY 3 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO 3 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET 3 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY 3 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY 4 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO 4 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET 4 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY 4 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY 5 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO 5 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET 5 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY 5 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY 6 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO 6 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET 6 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY 6 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY 7 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO 7 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET 7 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY 7 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY 8 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO 8 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET 8 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY 8 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY 9 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO 9 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET 9 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY 9 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY a 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO a 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET a 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY a 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY b 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO b 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET b 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY b 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY c 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO c 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET c 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY c 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY d 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO d 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET d 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY d 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY e 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO e 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET e 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY e 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY f 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO f 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET f 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY f 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY g 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO g 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET g 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY g 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY h 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO h 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET h 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY h 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY i 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO i 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET i 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY i 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY j 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO j 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET j 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY j 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY k 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO k 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET k 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY k 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY l 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO l 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET l 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY l 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY m 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO m 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET m 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY m 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY n 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO n 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET n 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY n 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY o 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO o 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET o 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY o 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY p 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO p 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET p 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY p 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY q 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO q 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET q 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY q 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY r 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO r 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET r 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY r 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY s 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO s 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET s 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY s 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY t 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO t 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET t 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY t 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY u 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO u 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET u 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY u 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY v 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO v 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET v 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY v 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY w 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO w 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET w 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY w 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY x 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO x 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET x 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY x 883 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY y 880 UNP O00444 EXPRESSION TAG
SEQADV 5LHY PRO y 881 UNP O00444 EXPRESSION TAG
SEQADV 5LHY MET y 882 UNP O00444 EXPRESSION TAG
SEQADV 5LHY GLY y 883 UNP O00444 EXPRESSION TAG
SEQRES 1 A 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 A 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 A 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 A 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 A 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 A 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 A 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 B 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 B 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 B 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 B 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 B 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 B 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 B 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 C 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 C 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 C 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 C 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 C 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 C 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 C 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 D 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 D 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 D 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 D 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 D 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 D 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 D 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 E 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 E 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 E 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 E 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 E 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 E 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 E 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 F 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 F 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 F 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 F 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 F 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 F 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 F 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 G 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 G 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 G 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 G 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 G 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 G 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 G 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 H 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 H 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 H 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 H 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 H 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 H 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 H 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 I 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 I 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 I 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 I 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 I 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 I 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 I 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 J 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 J 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 J 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 J 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 J 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 J 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 J 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 K 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 K 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 K 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 K 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 K 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 K 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 K 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 L 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 L 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 L 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 L 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 L 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 L 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 L 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 M 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 M 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 M 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 M 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 M 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 M 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 M 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 N 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 N 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 N 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 N 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 N 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 N 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 N 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 O 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 O 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 O 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 O 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 O 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 O 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 O 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 P 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 P 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 P 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 P 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 P 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 P 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 P 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 Q 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 Q 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 Q 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 Q 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 Q 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 Q 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 Q 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 R 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 R 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 R 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 R 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 R 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 R 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 R 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 S 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 S 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 S 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 S 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 S 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 S 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 S 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 T 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 T 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 T 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 T 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 T 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 T 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 T 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 U 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 U 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 U 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 U 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 U 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 U 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 U 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 V 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 V 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 V 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 V 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 V 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 V 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 V 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 W 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 W 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 W 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 W 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 W 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 W 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 W 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 X 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 X 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 X 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 X 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 X 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 X 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 X 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 Y 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 Y 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 Y 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 Y 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 Y 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 Y 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 Y 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 Z 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 Z 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 Z 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 Z 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 Z 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 Z 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 Z 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 1 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 1 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 1 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 1 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 1 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 1 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 1 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 2 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 2 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 2 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 2 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 2 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 2 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 2 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 3 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 3 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 3 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 3 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 3 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 3 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 3 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 4 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 4 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 4 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 4 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 4 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 4 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 4 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 5 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 5 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 5 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 5 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 5 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 5 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 5 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 6 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 6 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 6 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 6 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 6 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 6 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 6 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 7 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 7 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 7 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 7 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 7 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 7 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 7 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 8 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 8 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 8 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 8 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 8 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 8 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 8 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 9 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 9 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 9 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 9 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 9 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 9 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 9 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 a 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 a 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 a 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 a 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 a 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 a 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 a 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 b 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 b 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 b 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 b 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 b 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 b 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 b 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 c 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 c 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 c 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 c 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 c 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 c 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 c 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 d 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 d 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 d 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 d 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 d 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 d 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 d 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 e 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 e 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 e 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 e 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 e 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 e 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 e 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 f 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 f 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 f 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 f 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 f 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 f 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 f 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 g 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 g 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 g 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 g 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 g 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 g 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 g 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 h 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 h 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 h 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 h 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 h 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 h 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 h 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 i 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 i 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 i 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 i 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 i 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 i 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 i 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 j 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 j 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 j 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 j 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 j 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 j 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 j 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 k 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 k 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 k 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 k 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 k 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 k 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 k 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 l 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 l 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 l 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 l 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 l 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 l 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 l 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 m 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 m 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 m 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 m 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 m 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 m 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 m 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 n 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 n 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 n 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 n 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 n 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 n 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 n 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 o 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 o 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 o 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 o 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 o 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 o 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 o 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 p 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 p 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 p 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 p 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 p 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 p 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 p 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 q 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 q 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 q 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 q 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 q 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 q 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 q 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 r 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 r 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 r 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 r 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 r 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 r 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 r 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 s 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 s 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 s 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 s 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 s 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 s 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 s 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 t 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 t 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 t 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 t 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 t 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 t 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 t 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 u 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 u 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 u 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 u 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 u 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 u 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 u 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 v 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 v 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 v 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 v 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 v 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 v 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 v 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 w 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 w 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 w 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 w 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 w 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 w 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 w 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 x 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 x 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 x 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 x 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 x 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 x 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 x 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
SEQRES 1 y 91 GLY PRO MET GLY SER ALA GLN LEU LEU LYS SER VAL PHE
SEQRES 2 y 91 VAL LYS ASN VAL GLY TRP ALA THR GLN LEU THR SER GLY
SEQRES 3 y 91 ALA VAL TRP VAL GLN PHE ASN ASP GLY SER GLN LEU VAL
SEQRES 4 y 91 VAL GLN ALA GLY VAL SER SER ILE SER TYR THR SER PRO
SEQRES 5 y 91 ASN GLY GLN THR THR ARG TYR GLY GLU ASN GLU LYS LEU
SEQRES 6 y 91 PRO ASP TYR ILE LYS GLN LYS LEU GLN CYS LEU SER SER
SEQRES 7 y 91 ILE LEU LEU MET PHE SER ASN PRO THR PRO ASN PHE HIS
HELIX 1 AA1 PRO A 945 GLN A 953 1 9
HELIX 2 AA2 PRO B 945 CYS B 954 1 10
HELIX 3 AA3 PRO C 945 CYS C 954 1 10
HELIX 4 AA4 PRO D 945 GLN D 953 1 9
HELIX 5 AA5 PRO E 945 CYS E 954 1 10
HELIX 6 AA6 PRO F 945 SER F 956 1 12
HELIX 7 AA7 PRO G 945 CYS G 954 1 10
HELIX 8 AA8 PRO H 945 CYS H 954 1 10
HELIX 9 AA9 PRO I 945 CYS I 954 1 10
HELIX 10 AB1 PRO J 945 GLN J 953 1 9
HELIX 11 AB2 PRO K 945 CYS K 954 1 10
HELIX 12 AB3 PRO L 945 CYS L 954 1 10
HELIX 13 AB4 PRO M 945 CYS M 954 1 10
HELIX 14 AB5 PRO N 945 CYS N 954 1 10
HELIX 15 AB6 PRO O 945 CYS O 954 1 10
HELIX 16 AB7 PRO P 945 CYS P 954 1 10
HELIX 17 AB8 PRO Q 945 CYS Q 954 1 10
HELIX 18 AB9 PRO R 945 CYS R 954 1 10
HELIX 19 AC1 PRO S 945 GLN S 953 1 9
HELIX 20 AC2 PRO T 945 CYS T 954 1 10
HELIX 21 AC3 PRO U 945 CYS U 954 1 10
HELIX 22 AC4 PRO V 945 CYS V 954 1 10
HELIX 23 AC5 PRO W 945 CYS W 954 1 10
HELIX 24 AC6 PRO X 945 CYS X 954 1 10
HELIX 25 AC7 PRO Y 945 CYS Y 954 1 10
HELIX 26 AC8 PRO Z 945 CYS Z 954 1 10
HELIX 27 AC9 PRO 1 945 GLN 1 953 1 9
HELIX 28 AD1 PRO 2 945 CYS 2 954 1 10
HELIX 29 AD2 PRO 3 945 CYS 3 954 1 10
HELIX 30 AD3 PRO 4 945 CYS 4 954 1 10
HELIX 31 AD4 PRO 5 945 CYS 5 954 1 10
HELIX 32 AD5 PRO 6 945 CYS 6 954 1 10
HELIX 33 AD6 PRO 7 945 GLN 7 953 1 9
HELIX 34 AD7 PRO 8 945 CYS 8 954 1 10
HELIX 35 AD8 PRO 9 945 CYS 9 954 1 10
HELIX 36 AD9 PRO a 945 GLN a 953 1 9
HELIX 37 AE1 PRO b 945 GLN b 953 1 9
HELIX 38 AE2 PRO c 945 CYS c 954 1 10
HELIX 39 AE3 PRO d 945 GLN d 953 1 9
HELIX 40 AE4 PRO e 945 CYS e 954 1 10
HELIX 41 AE5 PRO f 945 CYS f 954 1 10
HELIX 42 AE6 PRO g 945 GLN g 953 1 9
HELIX 43 AE7 PRO h 945 CYS h 954 1 10
HELIX 44 AE8 PRO i 945 CYS i 954 1 10
HELIX 45 AE9 PRO j 945 CYS j 954 1 10
HELIX 46 AF1 PRO k 945 GLN k 953 1 9
HELIX 47 AF2 PRO l 945 CYS l 954 1 10
HELIX 48 AF3 PRO m 945 GLN m 953 1 9
HELIX 49 AF4 PRO n 945 CYS n 954 1 10
HELIX 50 AF5 PRO o 945 GLN o 953 1 9
HELIX 51 AF6 PRO p 945 CYS p 954 1 10
HELIX 52 AF7 PRO q 945 CYS q 954 1 10
HELIX 53 AF8 PRO r 945 CYS r 954 1 10
HELIX 54 AF9 PRO s 945 CYS s 954 1 10
HELIX 55 AG1 PRO t 945 CYS t 954 1 10
HELIX 56 AG2 PRO u 945 CYS u 954 1 10
HELIX 57 AG3 PRO v 945 CYS v 954 1 10
HELIX 58 AG4 PRO w 945 CYS w 954 1 10
HELIX 59 AG5 PRO x 945 CYS x 954 1 10
HELIX 60 AG6 PRO y 945 CYS y 954 1 10
SHEET 1 A 4 ILE A 958 PHE A 962 0
SHEET 2 A 4 VAL A 893 THR A 900 -1
SHEET 3 A 4 SER A 904 PHE A 911 -1
SHEET 4 A 4 GLN A 916 GLY A 922 -1
SHEET 1 B 2 ILE A 926 THR A 929 0
SHEET 2 B 2 THR A 935 TYR A 938 -1
SHEET 1 C 4 ILE B 958 MET B 961 0
SHEET 2 C 4 VAL B 893 THR B 900 -1
SHEET 3 C 4 SER B 904 PHE B 911 -1
SHEET 4 C 4 GLN B 916 GLY B 922 -1
SHEET 1 D 2 ILE B 926 THR B 929 0
SHEET 2 D 2 THR B 935 TYR B 938 -1
SHEET 1 E 4 ILE C 958 PHE C 962 0
SHEET 2 E 4 VAL C 893 THR C 900 -1
SHEET 3 E 4 SER C 904 PHE C 911 -1
SHEET 4 E 4 GLN C 916 GLY C 922 -1
SHEET 1 F 2 ILE C 926 THR C 929 0
SHEET 2 F 2 THR C 935 TYR C 938 -1
SHEET 1 G 4 ILE D 958 PHE D 962 0
SHEET 2 G 4 VAL D 893 THR D 900 -1
SHEET 3 G 4 SER D 904 PHE D 911 -1
SHEET 4 G 4 GLN D 916 GLY D 922 -1
SHEET 1 H 2 ILE D 926 THR D 929 0
SHEET 2 H 2 THR D 935 TYR D 938 -1
SHEET 1 I 4 ILE E 958 PHE E 962 0
SHEET 2 I 4 VAL E 893 THR E 900 -1
SHEET 3 I 4 SER E 904 PHE E 911 -1
SHEET 4 I 4 GLN E 916 GLY E 922 -1
SHEET 1 J 2 ILE E 926 THR E 929 0
SHEET 2 J 2 THR E 935 TYR E 938 -1
SHEET 1 K 4 ILE F 958 PHE F 962 0
SHEET 2 K 4 VAL F 893 THR F 900 -1
SHEET 3 K 4 SER F 904 PHE F 911 -1
SHEET 4 K 4 GLN F 916 GLY F 922 -1
SHEET 1 L 2 ILE F 926 THR F 929 0
SHEET 2 L 2 THR F 935 TYR F 938 -1
SHEET 1 M 4 ILE G 958 PHE G 962 0
SHEET 2 M 4 VAL G 893 THR G 900 -1
SHEET 3 M 4 SER G 904 PHE G 911 -1
SHEET 4 M 4 GLN G 916 GLY G 922 -1
SHEET 1 N 2 ILE G 926 THR G 929 0
SHEET 2 N 2 THR G 935 TYR G 938 -1
SHEET 1 O 4 ILE H 958 PHE H 962 0
SHEET 2 O 4 VAL H 893 THR H 900 -1
SHEET 3 O 4 SER H 904 PHE H 911 -1
SHEET 4 O 4 GLN H 916 GLY H 922 -1
SHEET 1 P 2 ILE H 926 THR H 929 0
SHEET 2 P 2 THR H 935 TYR H 938 -1
SHEET 1 Q 4 ILE I 958 PHE I 962 0
SHEET 2 Q 4 VAL I 893 THR I 900 -1
SHEET 3 Q 4 SER I 904 PHE I 911 -1
SHEET 4 Q 4 GLN I 916 GLY I 922 -1
SHEET 1 R 2 ILE I 926 THR I 929 0
SHEET 2 R 2 THR I 935 TYR I 938 -1
SHEET 1 S 4 ILE J 958 PHE J 962 0
SHEET 2 S 4 VAL J 893 THR J 900 -1
SHEET 3 S 4 SER J 904 PHE J 911 -1
SHEET 4 S 4 GLN J 916 GLY J 922 -1
SHEET 1 T 2 ILE J 926 THR J 929 0
SHEET 2 T 2 THR J 935 TYR J 938 -1
SHEET 1 U 4 ILE K 958 PHE K 962 0
SHEET 2 U 4 VAL K 893 THR K 900 -1
SHEET 3 U 4 SER K 904 PHE K 911 -1
SHEET 4 U 4 GLN K 916 GLY K 922 -1
SHEET 1 V 2 ILE K 926 THR K 929 0
SHEET 2 V 2 THR K 935 TYR K 938 -1
SHEET 1 W 4 ILE L 958 PHE L 962 0
SHEET 2 W 4 VAL L 893 THR L 900 -1
SHEET 3 W 4 SER L 904 PHE L 911 -1
SHEET 4 W 4 GLN L 916 GLY L 922 -1
SHEET 1 X 2 ILE L 926 THR L 929 0
SHEET 2 X 2 THR L 935 TYR L 938 -1
SHEET 1 Y 4 ILE M 958 PHE M 962 0
SHEET 2 Y 4 VAL M 893 THR M 900 -1
SHEET 3 Y 4 SER M 904 PHE M 911 -1
SHEET 4 Y 4 GLN M 916 GLY M 922 -1
SHEET 1 Z 2 ILE M 926 THR M 929 0
SHEET 2 Z 2 THR M 935 TYR M 938 -1
SHEET 1 AA 4 ILE N 958 PHE N 962 0
SHEET 2 AA 4 VAL N 893 THR N 900 -1
SHEET 3 AA 4 SER N 904 PHE N 911 -1
SHEET 4 AA 4 GLN N 916 GLY N 922 -1
SHEET 1 AB 2 ILE N 926 THR N 929 0
SHEET 2 AB 2 THR N 935 TYR N 938 -1
SHEET 1 AC 4 ILE O 958 PHE O 962 0
SHEET 2 AC 4 VAL O 893 THR O 900 -1
SHEET 3 AC 4 SER O 904 PHE O 911 -1
SHEET 4 AC 4 GLN O 916 GLY O 922 -1
SHEET 1 AD 2 ILE O 926 THR O 929 0
SHEET 2 AD 2 THR O 935 TYR O 938 -1
SHEET 1 AE 4 ILE P 958 PHE P 962 0
SHEET 2 AE 4 VAL P 893 THR P 900 -1
SHEET 3 AE 4 SER P 904 PHE P 911 -1
SHEET 4 AE 4 GLN P 916 GLY P 922 -1
SHEET 1 AF 2 ILE P 926 THR P 929 0
SHEET 2 AF 2 THR P 935 TYR P 938 -1
SHEET 1 AG 4 ILE Q 958 PHE Q 962 0
SHEET 2 AG 4 VAL Q 893 THR Q 900 -1
SHEET 3 AG 4 SER Q 904 PHE Q 911 -1
SHEET 4 AG 4 GLN Q 916 GLY Q 922 -1
SHEET 1 AH 2 ILE Q 926 THR Q 929 0
SHEET 2 AH 2 THR Q 935 TYR Q 938 -1
SHEET 1 AI 4 ILE R 958 PHE R 962 0
SHEET 2 AI 4 VAL R 893 THR R 900 -1
SHEET 3 AI 4 SER R 904 PHE R 911 -1
SHEET 4 AI 4 GLN R 916 GLY R 922 -1
SHEET 1 AJ 2 ILE R 926 THR R 929 0
SHEET 2 AJ 2 THR R 935 TYR R 938 -1
SHEET 1 AK 4 ILE S 958 PHE S 962 0
SHEET 2 AK 4 VAL S 893 THR S 900 -1
SHEET 3 AK 4 SER S 904 PHE S 911 -1
SHEET 4 AK 4 GLN S 916 GLY S 922 -1
SHEET 1 AL 2 ILE S 926 THR S 929 0
SHEET 2 AL 2 THR S 935 TYR S 938 -1
SHEET 1 AM 4 ILE T 958 PHE T 962 0
SHEET 2 AM 4 VAL T 893 THR T 900 -1
SHEET 3 AM 4 SER T 904 PHE T 911 -1
SHEET 4 AM 4 GLN T 916 GLY T 922 -1
SHEET 1 AN 2 ILE T 926 THR T 929 0
SHEET 2 AN 2 THR T 935 TYR T 938 -1
SHEET 1 AO 4 ILE U 958 PHE U 962 0
SHEET 2 AO 4 VAL U 893 THR U 900 -1
SHEET 3 AO 4 SER U 904 PHE U 911 -1
SHEET 4 AO 4 GLN U 916 GLY U 922 -1
SHEET 1 AP 2 ILE U 926 THR U 929 0
SHEET 2 AP 2 THR U 935 TYR U 938 -1
SHEET 1 AQ 4 ILE V 958 PHE V 962 0
SHEET 2 AQ 4 VAL V 893 THR V 900 -1
SHEET 3 AQ 4 SER V 904 PHE V 911 -1
SHEET 4 AQ 4 GLN V 916 GLY V 922 -1
SHEET 1 AR 2 ILE V 926 THR V 929 0
SHEET 2 AR 2 THR V 935 TYR V 938 -1
SHEET 1 AS 4 ILE W 958 PHE W 962 0
SHEET 2 AS 4 VAL W 893 THR W 900 -1
SHEET 3 AS 4 SER W 904 PHE W 911 -1
SHEET 4 AS 4 GLN W 916 GLY W 922 -1
SHEET 1 AT 2 ILE W 926 THR W 929 0
SHEET 2 AT 2 THR W 935 TYR W 938 -1
SHEET 1 AU 4 ILE X 958 PHE X 962 0
SHEET 2 AU 4 VAL X 893 THR X 900 -1
SHEET 3 AU 4 SER X 904 PHE X 911 -1
SHEET 4 AU 4 GLN X 916 GLY X 922 -1
SHEET 1 AV 2 ILE X 926 THR X 929 0
SHEET 2 AV 2 THR X 935 TYR X 938 -1
SHEET 1 AW 4 ILE Y 958 PHE Y 962 0
SHEET 2 AW 4 VAL Y 893 THR Y 900 -1
SHEET 3 AW 4 SER Y 904 PHE Y 911 -1
SHEET 4 AW 4 GLN Y 916 GLY Y 922 -1
SHEET 1 AX 2 ILE Y 926 THR Y 929 0
SHEET 2 AX 2 THR Y 935 TYR Y 938 -1
SHEET 1 AY 4 ILE Z 958 PHE Z 962 0
SHEET 2 AY 4 VAL Z 893 THR Z 900 -1
SHEET 3 AY 4 SER Z 904 PHE Z 911 -1
SHEET 4 AY 4 GLN Z 916 GLY Z 922 -1
SHEET 1 AZ 2 SER Z 925 THR Z 929 0
SHEET 2 AZ 2 THR Z 935 GLY Z 939 -1
SHEET 1 BA 4 ILE 1 958 PHE 1 962 0
SHEET 2 BA 4 VAL 1 893 THR 1 900 -1
SHEET 3 BA 4 SER 1 904 PHE 1 911 -1
SHEET 4 BA 4 GLN 1 916 GLY 1 922 -1
SHEET 1 BB 2 SER 1 925 THR 1 929 0
SHEET 2 BB 2 THR 1 935 GLY 1 939 -1
SHEET 1 BC 4 ILE 2 958 PHE 2 962 0
SHEET 2 BC 4 VAL 2 893 THR 2 900 -1
SHEET 3 BC 4 SER 2 904 PHE 2 911 -1
SHEET 4 BC 4 GLN 2 916 GLY 2 922 -1
SHEET 1 BD 2 ILE 2 926 THR 2 929 0
SHEET 2 BD 2 THR 2 935 TYR 2 938 -1
SHEET 1 BE 4 ILE 3 958 PHE 3 962 0
SHEET 2 BE 4 VAL 3 893 THR 3 900 -1
SHEET 3 BE 4 SER 3 904 PHE 3 911 -1
SHEET 4 BE 4 GLN 3 916 GLY 3 922 -1
SHEET 1 BF 2 ILE 3 926 THR 3 929 0
SHEET 2 BF 2 THR 3 935 TYR 3 938 -1
SHEET 1 BG 4 ILE 4 958 PHE 4 962 0
SHEET 2 BG 4 VAL 4 893 THR 4 900 -1
SHEET 3 BG 4 SER 4 904 PHE 4 911 -1
SHEET 4 BG 4 GLN 4 916 GLY 4 922 -1
SHEET 1 BH 2 ILE 4 926 THR 4 929 0
SHEET 2 BH 2 THR 4 935 TYR 4 938 -1
SHEET 1 BI 4 ILE 5 958 PHE 5 962 0
SHEET 2 BI 4 VAL 5 893 THR 5 900 -1
SHEET 3 BI 4 SER 5 904 PHE 5 911 -1
SHEET 4 BI 4 GLN 5 916 GLY 5 922 -1
SHEET 1 BJ 2 ILE 5 926 THR 5 929 0
SHEET 2 BJ 2 THR 5 935 TYR 5 938 -1
SHEET 1 BK 4 ILE 6 958 PHE 6 962 0
SHEET 2 BK 4 VAL 6 893 THR 6 900 -1
SHEET 3 BK 4 SER 6 904 PHE 6 911 -1
SHEET 4 BK 4 GLN 6 916 GLY 6 922 -1
SHEET 1 BL 2 ILE 6 926 THR 6 929 0
SHEET 2 BL 2 THR 6 935 TYR 6 938 -1
SHEET 1 BM 4 ILE 7 958 PHE 7 962 0
SHEET 2 BM 4 VAL 7 893 THR 7 900 -1
SHEET 3 BM 4 SER 7 904 PHE 7 911 -1
SHEET 4 BM 4 GLN 7 916 GLY 7 922 -1
SHEET 1 BN 2 ILE 7 926 THR 7 929 0
SHEET 2 BN 2 THR 7 935 TYR 7 938 -1
SHEET 1 BO 4 ILE 8 958 PHE 8 962 0
SHEET 2 BO 4 VAL 8 893 THR 8 900 -1
SHEET 3 BO 4 SER 8 904 PHE 8 911 -1
SHEET 4 BO 4 GLN 8 916 GLY 8 922 -1
SHEET 1 BP 2 ILE 8 926 THR 8 929 0
SHEET 2 BP 2 THR 8 935 TYR 8 938 -1
SHEET 1 BQ 4 ILE 9 958 PHE 9 962 0
SHEET 2 BQ 4 VAL 9 893 THR 9 900 -1
SHEET 3 BQ 4 SER 9 904 PHE 9 911 -1
SHEET 4 BQ 4 GLN 9 916 GLY 9 922 -1
SHEET 1 BR 2 ILE 9 926 THR 9 929 0
SHEET 2 BR 2 THR 9 935 TYR 9 938 -1
SHEET 1 BS 4 ILE a 958 PHE a 962 0
SHEET 2 BS 4 VAL a 893 THR a 900 -1
SHEET 3 BS 4 SER a 904 PHE a 911 -1
SHEET 4 BS 4 GLN a 916 GLY a 922 -1
SHEET 1 BT 2 ILE a 926 THR a 929 0
SHEET 2 BT 2 THR a 935 TYR a 938 -1
SHEET 1 BU 4 ILE b 958 PHE b 962 0
SHEET 2 BU 4 VAL b 893 THR b 900 -1
SHEET 3 BU 4 SER b 904 PHE b 911 -1
SHEET 4 BU 4 GLN b 916 GLY b 922 -1
SHEET 1 BV 2 ILE b 926 THR b 929 0
SHEET 2 BV 2 THR b 935 TYR b 938 -1
SHEET 1 BW 4 ILE c 958 PHE c 962 0
SHEET 2 BW 4 VAL c 893 THR c 900 -1
SHEET 3 BW 4 SER c 904 PHE c 911 -1
SHEET 4 BW 4 GLN c 916 GLY c 922 -1
SHEET 1 BX 2 ILE c 926 THR c 929 0
SHEET 2 BX 2 THR c 935 TYR c 938 -1
SHEET 1 BY 4 ILE d 958 PHE d 962 0
SHEET 2 BY 4 VAL d 893 THR d 900 -1
SHEET 3 BY 4 SER d 904 PHE d 911 -1
SHEET 4 BY 4 GLN d 916 GLY d 922 -1
SHEET 1 BZ 2 ILE d 926 THR d 929 0
SHEET 2 BZ 2 THR d 935 TYR d 938 -1
SHEET 1 CA 4 ILE e 958 PHE e 962 0
SHEET 2 CA 4 VAL e 893 THR e 900 -1
SHEET 3 CA 4 SER e 904 PHE e 911 -1
SHEET 4 CA 4 GLN e 916 GLY e 922 -1
SHEET 1 CB 2 ILE e 926 THR e 929 0
SHEET 2 CB 2 THR e 935 TYR e 938 -1
SHEET 1 CC 4 ILE f 958 PHE f 962 0
SHEET 2 CC 4 VAL f 893 THR f 900 -1
SHEET 3 CC 4 SER f 904 PHE f 911 -1
SHEET 4 CC 4 GLN f 916 GLY f 922 -1
SHEET 1 CD 2 ILE f 926 THR f 929 0
SHEET 2 CD 2 THR f 935 TYR f 938 -1
SHEET 1 CE 4 ILE g 958 PHE g 962 0
SHEET 2 CE 4 VAL g 893 THR g 900 -1
SHEET 3 CE 4 SER g 904 PHE g 911 -1
SHEET 4 CE 4 GLN g 916 GLY g 922 -1
SHEET 1 CF 2 ILE g 926 THR g 929 0
SHEET 2 CF 2 THR g 935 TYR g 938 -1
SHEET 1 CG 4 ILE h 958 PHE h 962 0
SHEET 2 CG 4 VAL h 893 THR h 900 -1
SHEET 3 CG 4 SER h 904 PHE h 911 -1
SHEET 4 CG 4 GLN h 916 GLY h 922 -1
SHEET 1 CH 2 ILE h 926 THR h 929 0
SHEET 2 CH 2 THR h 935 TYR h 938 -1
SHEET 1 CI 4 ILE i 958 PHE i 962 0
SHEET 2 CI 4 VAL i 893 THR i 900 -1
SHEET 3 CI 4 SER i 904 PHE i 911 -1
SHEET 4 CI 4 GLN i 916 GLY i 922 -1
SHEET 1 CJ 2 ILE i 926 THR i 929 0
SHEET 2 CJ 2 THR i 935 TYR i 938 -1
SHEET 1 CK 4 ILE j 958 PHE j 962 0
SHEET 2 CK 4 VAL j 893 THR j 900 -1
SHEET 3 CK 4 SER j 904 PHE j 911 -1
SHEET 4 CK 4 GLN j 916 GLY j 922 -1
SHEET 1 CL 2 ILE j 926 THR j 929 0
SHEET 2 CL 2 THR j 935 TYR j 938 -1
SHEET 1 CM 4 ILE k 958 PHE k 962 0
SHEET 2 CM 4 VAL k 893 THR k 900 -1
SHEET 3 CM 4 SER k 904 PHE k 911 -1
SHEET 4 CM 4 GLN k 916 GLY k 922 -1
SHEET 1 CN 2 ILE k 926 THR k 929 0
SHEET 2 CN 2 THR k 935 TYR k 938 -1
SHEET 1 CO 4 ILE l 958 PHE l 962 0
SHEET 2 CO 4 VAL l 893 THR l 900 -1
SHEET 3 CO 4 SER l 904 PHE l 911 -1
SHEET 4 CO 4 GLN l 916 GLY l 922 -1
SHEET 1 CP 2 ILE l 926 THR l 929 0
SHEET 2 CP 2 THR l 935 TYR l 938 -1
SHEET 1 CQ 4 ILE m 958 PHE m 962 0
SHEET 2 CQ 4 VAL m 893 THR m 900 -1
SHEET 3 CQ 4 SER m 904 PHE m 911 -1
SHEET 4 CQ 4 GLN m 916 GLY m 922 -1
SHEET 1 CR 2 ILE m 926 THR m 929 0
SHEET 2 CR 2 THR m 935 TYR m 938 -1
SHEET 1 CS 4 ILE n 958 PHE n 962 0
SHEET 2 CS 4 VAL n 893 THR n 900 -1
SHEET 3 CS 4 SER n 904 PHE n 911 -1
SHEET 4 CS 4 GLN n 916 GLY n 922 -1
SHEET 1 CT 2 ILE n 926 THR n 929 0
SHEET 2 CT 2 THR n 935 TYR n 938 -1
SHEET 1 CU 4 ILE o 958 PHE o 962 0
SHEET 2 CU 4 VAL o 893 THR o 900 -1
SHEET 3 CU 4 SER o 904 PHE o 911 -1
SHEET 4 CU 4 GLN o 916 GLY o 922 -1
SHEET 1 CV 2 ILE o 926 THR o 929 0
SHEET 2 CV 2 THR o 935 TYR o 938 -1
SHEET 1 CW 4 ILE p 958 PHE p 962 0
SHEET 2 CW 4 VAL p 893 THR p 900 -1
SHEET 3 CW 4 SER p 904 PHE p 911 -1
SHEET 4 CW 4 GLN p 916 GLY p 922 -1
SHEET 1 CX 2 ILE p 926 THR p 929 0
SHEET 2 CX 2 THR p 935 TYR p 938 -1
SHEET 1 CY 4 ILE q 958 PHE q 962 0
SHEET 2 CY 4 VAL q 893 THR q 900 -1
SHEET 3 CY 4 SER q 904 PHE q 911 -1
SHEET 4 CY 4 GLN q 916 GLY q 922 -1
SHEET 1 CZ 2 ILE q 926 THR q 929 0
SHEET 2 CZ 2 THR q 935 TYR q 938 -1
SHEET 1 DA 4 ILE r 958 PHE r 962 0
SHEET 2 DA 4 VAL r 893 THR r 900 -1
SHEET 3 DA 4 SER r 904 PHE r 911 -1
SHEET 4 DA 4 GLN r 916 GLY r 922 -1
SHEET 1 DB 2 ILE r 926 THR r 929 0
SHEET 2 DB 2 THR r 935 TYR r 938 -1
SHEET 1 DC 4 ILE s 958 PHE s 962 0
SHEET 2 DC 4 VAL s 893 THR s 900 -1
SHEET 3 DC 4 SER s 904 PHE s 911 -1
SHEET 4 DC 4 GLN s 916 GLY s 922 -1
SHEET 1 DD 2 ILE s 926 THR s 929 0
SHEET 2 DD 2 THR s 935 TYR s 938 -1
SHEET 1 DE 4 ILE t 958 PHE t 962 0
SHEET 2 DE 4 VAL t 893 THR t 900 -1
SHEET 3 DE 4 SER t 904 PHE t 911 -1
SHEET 4 DE 4 GLN t 916 GLY t 922 -1
SHEET 1 DF 2 ILE t 926 THR t 929 0
SHEET 2 DF 2 THR t 935 TYR t 938 -1
SHEET 1 DG 4 ILE u 958 PHE u 962 0
SHEET 2 DG 4 VAL u 893 THR u 900 -1
SHEET 3 DG 4 SER u 904 PHE u 911 -1
SHEET 4 DG 4 GLN u 916 GLY u 922 -1
SHEET 1 DH 2 ILE u 926 THR u 929 0
SHEET 2 DH 2 THR u 935 TYR u 938 -1
SHEET 1 DI 4 ILE v 958 PHE v 962 0
SHEET 2 DI 4 VAL v 893 THR v 900 -1
SHEET 3 DI 4 SER v 904 PHE v 911 -1
SHEET 4 DI 4 GLN v 916 GLY v 922 -1
SHEET 1 DJ 2 SER v 925 THR v 929 0
SHEET 2 DJ 2 THR v 935 GLY v 939 -1
SHEET 1 DK 4 ILE w 958 PHE w 962 0
SHEET 2 DK 4 VAL w 893 THR w 900 -1
SHEET 3 DK 4 SER w 904 PHE w 911 -1
SHEET 4 DK 4 GLN w 916 GLY w 922 -1
SHEET 1 DL 2 ILE w 926 THR w 929 0
SHEET 2 DL 2 THR w 935 TYR w 938 -1
SHEET 1 DM 4 ILE x 958 PHE x 962 0
SHEET 2 DM 4 VAL x 893 THR x 900 -1
SHEET 3 DM 4 SER x 904 PHE x 911 -1
SHEET 4 DM 4 GLN x 916 GLY x 922 -1
SHEET 1 DN 2 ILE x 926 THR x 929 0
SHEET 2 DN 2 THR x 935 TYR x 938 -1
SHEET 1 DO 4 ILE y 958 PHE y 962 0
SHEET 2 DO 4 VAL y 893 THR y 900 -1
SHEET 3 DO 4 SER y 904 PHE y 911 -1
SHEET 4 DO 4 GLN y 916 GLY y 922 -1
SHEET 1 DP 2 ILE y 926 THR y 929 0
SHEET 2 DP 2 THR y 935 TYR y 938 -1
CRYST1 220.350 220.350 325.730 90.00 90.00 90.00 P 43 21 2 480
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 0.004538 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004538 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003070 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
