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HEADER OXIDOREDUCTASE 18-JAN-13 4ITV
TITLE STRUCTURE OF A 16 NM PROTEIN CAGE DESIGNED BY FUSING SYMMETRIC
TITLE 2 OLIGOMERIC DOMAINS, TRIPLE MUTANT, P212121 FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NON-HAEM BROMOPEROXIDASE BPO-A2, MATRIX PROTEIN 1;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 SYNONYM: BPO2, BROMIDE PEROXIDASE, M1;
COMPND 5 EC: 1.11.1.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES AUREOFACIENS, INFLUENZA A VIRUS;
SOURCE 3 ORGANISM_TAXID: 1894, 211044;
SOURCE 4 STRAIN: A/PUERTO RICO/8/1934 H1N1;
SOURCE 5 GENE: BPOA2, BROMOPEROXIDASE A2 AND M1 MATRIX, M;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS PROTEIN DESIGN, BIONANOTECHNOLOGY, PROTEIN ASSEMBLY, SYMMETRIC
KEYWDS 2 OLIGOMERIC DOMAINS, BIOMATERIALS, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-T.LAI,M.R.SAWAYA,T.O.YEATES
REVDAT 1 24-JUL-13 4ITV 0
JRNL AUTH Y.T.LAI,K.L.TSAI,M.R.SAWAYA,F.J.ASTURIAS,T.O.YEATES
JRNL TITL STRUCTURE AND FLEXIBILITY OF NANOSCALE PROTEIN CAGES
JRNL TITL 2 DESIGNED BY SYMMETRIC SELF-ASSEMBLY.
JRNL REF J.AM.CHEM.SOC. V. 135 7738 2013
JRNL REFN ISSN 0002-7863
JRNL PMID 23621606
JRNL DOI 10.1021/JA402277F
REMARK 2
REMARK 2 RESOLUTION. 3.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 96.14
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 76445
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3821
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 96.1740 - 10.7903 0.95 2806 147 0.2257 0.2372
REMARK 3 2 10.7903 - 8.5663 0.98 2770 146 0.1497 0.1858
REMARK 3 3 8.5663 - 7.4839 0.99 2759 145 0.1796 0.2112
REMARK 3 4 7.4839 - 6.7999 0.99 2746 145 0.1968 0.2219
REMARK 3 5 6.7999 - 6.3126 1.00 2762 145 0.2184 0.2650
REMARK 3 6 6.3126 - 5.9405 0.95 2635 139 0.2256 0.2691
REMARK 3 7 5.9405 - 5.6430 0.97 2662 140 0.2163 0.2681
REMARK 3 8 5.6430 - 5.3974 0.99 2700 142 0.1877 0.2152
REMARK 3 9 5.3974 - 5.1896 0.99 2721 143 0.1944 0.2471
REMARK 3 10 5.1896 - 5.0105 0.99 2699 142 0.1880 0.2271
REMARK 3 11 5.0105 - 4.8539 1.00 2721 144 0.1823 0.2219
REMARK 3 12 4.8539 - 4.7151 1.00 2693 141 0.1870 0.2429
REMARK 3 13 4.7151 - 4.5910 1.00 2740 145 0.2003 0.2192
REMARK 3 14 4.5910 - 4.4790 1.00 2699 142 0.1997 0.2528
REMARK 3 15 4.4790 - 4.3772 1.00 2695 142 0.1960 0.2490
REMARK 3 16 4.3772 - 4.2840 1.00 2720 143 0.1970 0.2248
REMARK 3 17 4.2840 - 4.1983 1.00 2715 142 0.2045 0.2443
REMARK 3 18 4.1983 - 4.1191 0.98 2635 138 0.2209 0.2425
REMARK 3 19 4.1191 - 4.0455 0.95 2590 137 0.2242 0.2483
REMARK 3 20 4.0455 - 3.9770 0.98 2629 138 0.2445 0.2704
REMARK 3 21 3.9770 - 3.9128 0.98 2676 141 0.2383 0.2896
REMARK 3 22 3.9128 - 3.8526 0.99 2668 140 0.2421 0.2712
REMARK 3 23 3.8526 - 3.7959 0.99 2655 140 0.2495 0.2970
REMARK 3 24 3.7959 - 3.7425 0.99 2672 141 0.2596 0.2557
REMARK 3 25 3.7425 - 3.6919 0.99 2676 141 0.2703 0.3456
REMARK 3 26 3.6919 - 3.6439 0.99 2672 140 0.2851 0.2843
REMARK 3 27 3.6439 - 3.5984 0.92 2508 132 0.3007 0.3170
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 102.21
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 151.86
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 : 0.003 41700
REMARK 3 ANGLE : 0.609 56748
REMARK 3 CHIRALITY : 0.042 6408
REMARK 3 PLANARITY : 0.004 7392
REMARK 3 DIHEDRAL : 13.192 14808
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain A and resid 1:276
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6574 47.4243 342.8757
REMARK 3 T TENSOR
REMARK 3 T11: 0.4704 T22: 0.6516
REMARK 3 T33: 0.5304 T12: 0.0174
REMARK 3 T13: 0.0985 T23: -0.1412
REMARK 3 L TENSOR
REMARK 3 L11: 2.1771 L22: 3.0007
REMARK 3 L33: 4.2935 L12: 0.2296
REMARK 3 L13: 0.9068 L23: -1.0112
REMARK 3 S TENSOR
REMARK 3 S11: 0.0650 S12: -0.0024 S13: -0.1097
REMARK 3 S21: 0.3422 S22: 0.0382 S23: 0.2248
REMARK 3 S31: -0.1449 S32: -0.2475 S33: -0.1015
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain A and resid 277:440
REMARK 3 ORIGIN FOR THE GROUP (A): -13.5297 39.8594 371.1818
REMARK 3 T TENSOR
REMARK 3 T11: 0.7864 T22: 1.0670
REMARK 3 T33: 0.4977 T12: -0.0111
REMARK 3 T13: 0.0303 T23: 0.1172
REMARK 3 L TENSOR
REMARK 3 L11: 9.6883 L22: 7.2286
REMARK 3 L33: 6.9035 L12: -3.4478
REMARK 3 L13: 4.3767 L23: -2.1427
REMARK 3 S TENSOR
REMARK 3 S11: 0.2640 S12: -0.4347 S13: 0.2359
REMARK 3 S21: 0.0561 S22: -0.5666 S23: -0.2228
REMARK 3 S31: 0.1671 S32: 0.3730 S33: 0.2995
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain B and resid 1:276
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7285 67.6750 311.3918
REMARK 3 T TENSOR
REMARK 3 T11: 0.9935 T22: 0.7836
REMARK 3 T33: 0.5820 T12: 0.0191
REMARK 3 T13: -0.0976 T23: 0.0239
REMARK 3 L TENSOR
REMARK 3 L11: 3.2655 L22: 3.8213
REMARK 3 L33: 2.8960 L12: 0.5232
REMARK 3 L13: 0.6322 L23: 0.8886
REMARK 3 S TENSOR
REMARK 3 S11: -0.2603 S12: 0.6281 S13: 0.4601
REMARK 3 S21: -0.8909 S22: -0.0166 S23: 0.2020
REMARK 3 S31: -0.7725 S32: -0.0452 S33: 0.2694
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain B and resid 277:440
REMARK 3 ORIGIN FOR THE GROUP (A): 21.3875 88.8284 346.7508
REMARK 3 T TENSOR
REMARK 3 T11: 1.0862 T22: 0.6077
REMARK 3 T33: 0.5780 T12: 0.1717
REMARK 3 T13: -0.1282 T23: -0.0856
REMARK 3 L TENSOR
REMARK 3 L11: 8.4675 L22: 5.7022
REMARK 3 L33: 8.2636 L12: 4.9857
REMARK 3 L13: -4.3462 L23: -3.6892
REMARK 3 S TENSOR
REMARK 3 S11: -0.1719 S12: 0.0181 S13: 0.1989
REMARK 3 S21: -0.2130 S22: 0.0025 S23: -0.0665
REMARK 3 S31: -0.5529 S32: 0.2017 S33: 0.1142
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain C and resid 1:276
REMARK 3 ORIGIN FOR THE GROUP (A): -9.8318 40.1002 317.4054
REMARK 3 T TENSOR
REMARK 3 T11: 0.5009 T22: 0.9934
REMARK 3 T33: 1.0150 T12: -0.0106
REMARK 3 T13: -0.0688 T23: -0.1823
REMARK 3 L TENSOR
REMARK 3 L11: 3.0607 L22: 3.2909
REMARK 3 L33: 4.4102 L12: -0.7312
REMARK 3 L13: 1.2844 L23: -0.0473
REMARK 3 S TENSOR
REMARK 3 S11: 0.0657 S12: 0.0836 S13: -0.2959
REMARK 3 S21: -0.2435 S22: -0.1353 S23: 0.9671
REMARK 3 S31: 0.1328 S32: -0.8142 S33: 0.0606
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain C and resid 277:440
REMARK 3 ORIGIN FOR THE GROUP (A): -38.9201 66.5276 304.3239
REMARK 3 T TENSOR
REMARK 3 T11: 1.2248 T22: 0.9882
REMARK 3 T33: 1.7462 T12: -0.1065
REMARK 3 T13: -0.0340 T23: -0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 9.7289 L22: 2.7352
REMARK 3 L33: 7.5378 L12: -4.6225
REMARK 3 L13: -0.1786 L23: -0.2399
REMARK 3 S TENSOR
REMARK 3 S11: 0.1061 S12: 0.1743 S13: 1.2948
REMARK 3 S21: 0.1158 S22: -0.1491 S23: -0.9076
REMARK 3 S31: -1.7572 S32: 0.2657 S33: 0.0596
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain D and resid 1:276
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7307 111.5375 372.5944
REMARK 3 T TENSOR
REMARK 3 T11: 1.3055 T22: 0.8139
REMARK 3 T33: 0.9394 T12: 0.2179
REMARK 3 T13: -0.2820 T23: -0.2834
REMARK 3 L TENSOR
REMARK 3 L11: 3.1089 L22: 3.6498
REMARK 3 L33: 2.7117 L12: -0.1242
REMARK 3 L13: -0.6366 L23: -0.1224
REMARK 3 S TENSOR
REMARK 3 S11: 0.0122 S12: -0.1951 S13: 0.7969
REMARK 3 S21: -1.0602 S22: -0.1644 S23: 0.1721
REMARK 3 S31: -0.6060 S32: -0.4290 S33: 0.1131
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: chain D and resid 277:440
REMARK 3 ORIGIN FOR THE GROUP (A): -19.2818 118.4290 350.5170
REMARK 3 T TENSOR
REMARK 3 T11: 1.7247 T22: 1.5004
REMARK 3 T33: 1.8437 T12: 0.4509
REMARK 3 T13: -0.3932 T23: -0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 4.3372 L22: 2.1299
REMARK 3 L33: 6.1002 L12: 3.3062
REMARK 3 L13: -0.7663 L23: -1.8169
REMARK 3 S TENSOR
REMARK 3 S11: 0.1487 S12: -0.0020 S13: 0.6622
REMARK 3 S21: -0.6174 S22: 0.3547 S23: 1.3494
REMARK 3 S31: 0.0670 S32: -0.9529 S33: -0.6592
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: chain E and resid 1:276
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3009 91.2894 403.7505
REMARK 3 T TENSOR
REMARK 3 T11: 0.9586 T22: 1.3873
REMARK 3 T33: 0.6571 T12: 0.0207
REMARK 3 T13: -0.0163 T23: -0.2964
REMARK 3 L TENSOR
REMARK 3 L11: 2.6372 L22: 3.4281
REMARK 3 L33: 2.2745 L12: -0.1882
REMARK 3 L13: -0.3116 L23: 0.8623
REMARK 3 S TENSOR
REMARK 3 S11: -0.1032 S12: -1.1884 S13: 0.2643
REMARK 3 S21: 0.6257 S22: -0.1497 S23: 0.3118
REMARK 3 S31: 0.0294 S32: -0.4062 S33: 0.2316
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: chain E and resid 277:440
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9153 69.5511 369.6195
REMARK 3 T TENSOR
REMARK 3 T11: 0.7204 T22: 0.5939
REMARK 3 T33: 0.5527 T12: -0.0849
REMARK 3 T13: 0.0177 T23: -0.0610
REMARK 3 L TENSOR
REMARK 3 L11: 9.6872 L22: 8.6757
REMARK 3 L33: 9.4059 L12: -4.9146
REMARK 3 L13: 2.6034 L23: -0.6243
REMARK 3 S TENSOR
REMARK 3 S11: -0.1303 S12: -0.0251 S13: -0.0500
REMARK 3 S21: -0.1151 S22: -0.0725 S23: -0.0128
REMARK 3 S31: 0.0539 S32: 0.2997 S33: 0.2063
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: chain F and resid 1:276
REMARK 3 ORIGIN FOR THE GROUP (A): -13.4942 119.1120 395.9190
REMARK 3 T TENSOR
REMARK 3 T11: 1.0676 T22: 2.2517
REMARK 3 T33: 1.7951 T12: 0.5981
REMARK 3 T13: -0.3914 T23: -0.9365
REMARK 3 L TENSOR
REMARK 3 L11: 1.7184 L22: 2.2028
REMARK 3 L33: 3.2453 L12: -0.1551
REMARK 3 L13: -0.8479 L23: 0.1728
REMARK 3 S TENSOR
REMARK 3 S11: -0.2363 S12: -0.8245 S13: 1.0655
REMARK 3 S21: -0.0087 S22: -0.3215 S23: 0.9411
REMARK 3 S31: -0.7582 S32: -1.5198 S33: 0.4386
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: chain F and resid 277:440
REMARK 3 ORIGIN FOR THE GROUP (A): -44.3706 92.1873 406.7296
REMARK 3 T TENSOR
REMARK 3 T11: 2.2138 T22: 2.1948
REMARK 3 T33: 2.3624 T12: -0.4030
REMARK 3 T13: 0.1869 T23: -0.3219
REMARK 3 L TENSOR
REMARK 3 L11: 2.2379 L22: 8.8592
REMARK 3 L33: 3.3616 L12: 8.5785
REMARK 3 L13: 5.9240 L23: 5.2481
REMARK 3 S TENSOR
REMARK 3 S11: -1.1809 S12: 0.4711 S13: -1.6168
REMARK 3 S21: -1.8680 S22: 0.6099 S23: -0.4297
REMARK 3 S31: 0.4739 S32: -0.8917 S33: 0.7105
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: chain G and resid 1:276
REMARK 3 ORIGIN FOR THE GROUP (A): -42.0911 116.9717 320.8955
REMARK 3 T TENSOR
REMARK 3 T11: 1.3797 T22: 0.8064
REMARK 3 T33: 1.7778 T12: -0.0987
REMARK 3 T13: 0.5346 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 3.1769 L22: 0.7870
REMARK 3 L33: 3.4280 L12: 0.9890
REMARK 3 L13: -0.7869 L23: 0.0527
REMARK 3 S TENSOR
REMARK 3 S11: 0.0140 S12: 0.0616 S13: 0.6168
REMARK 3 S21: -0.6155 S22: 0.2494 S23: -0.4566
REMARK 3 S31: -0.6917 S32: 0.6588 S33: -0.2636
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: chain G and resid 277:440
REMARK 3 ORIGIN FOR THE GROUP (A): -12.2704 88.6354 311.7000
REMARK 3 T TENSOR
REMARK 3 T11: 1.7997 T22: 1.5276
REMARK 3 T33: 2.2332 T12: 0.2011
REMARK 3 T13: 0.0577 T23: 0.1032
REMARK 3 L TENSOR
REMARK 3 L11: 5.9084 L22: 8.9762
REMARK 3 L33: 2.1900 L12: -5.5679
REMARK 3 L13: -0.1804 L23: -0.7296
REMARK 3 S TENSOR
REMARK 3 S11: -0.0697 S12: -0.1109 S13: -1.9254
REMARK 3 S21: 0.7173 S22: 0.1989 S23: 2.3494
REMARK 3 S31: 1.0439 S32: 0.8312 S33: -0.0652
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: chain H and resid 1:276
REMARK 3 ORIGIN FOR THE GROUP (A): -71.1740 110.6979 343.4952
REMARK 3 T TENSOR
REMARK 3 T11: 1.0135 T22: 0.5470
REMARK 3 T33: 0.9659 T12: 0.0441
REMARK 3 T13: 0.1206 T23: 0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 4.6378 L22: 1.5171
REMARK 3 L33: 4.1746 L12: 1.1601
REMARK 3 L13: -0.5204 L23: 0.3467
REMARK 3 S TENSOR
REMARK 3 S11: 0.0271 S12: 0.1056 S13: 0.6852
REMARK 3 S21: -0.0119 S22: 0.0434 S23: -0.2027
REMARK 3 S31: -0.4407 S32: -0.0912 S33: -0.0959
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: chain H and resid 277:440
REMARK 3 ORIGIN FOR THE GROUP (A): -44.4635 117.1763 376.3639
REMARK 3 T TENSOR
REMARK 3 T11: 2.9103 T22: 3.2256
REMARK 3 T33: 1.7077 T12: 0.2053
REMARK 3 T13: -0.3441 T23: 0.2195
REMARK 3 L TENSOR
REMARK 3 L11: 4.9177 L22: 7.7299
REMARK 3 L33: 5.1642 L12: -2.8795
REMARK 3 L13: 3.9054 L23: -0.4234
REMARK 3 S TENSOR
REMARK 3 S11: -0.4091 S12: 0.6756 S13: 0.3267
REMARK 3 S21: 3.3830 S22: 0.0084 S23: -1.7065
REMARK 3 S31: 0.6578 S32: 1.6672 S33: 0.4819
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: chain I and resid 1:276
REMARK 3 ORIGIN FOR THE GROUP (A): -64.6505 87.6440 314.6246
REMARK 3 T TENSOR
REMARK 3 T11: 1.8567 T22: 0.7840
REMARK 3 T33: 1.0343 T12: -0.1355
REMARK 3 T13: 0.4947 T23: -0.0322
REMARK 3 L TENSOR
REMARK 3 L11: 3.6889 L22: 3.7073
REMARK 3 L33: 2.4593 L12: -0.9976
REMARK 3 L13: 0.1309 L23: 0.6092
REMARK 3 S TENSOR
REMARK 3 S11: -0.3413 S12: 0.5957 S13: -0.3487
REMARK 3 S21: -1.0070 S22: 0.1345 S23: -0.6546
REMARK 3 S31: 0.4911 S32: -0.1226 S33: 0.2024
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: chain I and resid 277:440
REMARK 3 ORIGIN FOR THE GROUP (A): -75.8716 68.9726 349.8814
REMARK 3 T TENSOR
REMARK 3 T11: 0.9601 T22: 0.5514
REMARK 3 T33: 0.8074 T12: 0.0576
REMARK 3 T13: 0.2084 T23: 0.0858
REMARK 3 L TENSOR
REMARK 3 L11: 8.8431 L22: 8.0017
REMARK 3 L33: 7.6822 L12: 5.7586
REMARK 3 L13: 2.6076 L23: 2.8227
REMARK 3 S TENSOR
REMARK 3 S11: -0.1972 S12: 0.2142 S13: -0.1426
REMARK 3 S21: -0.3540 S22: 0.1429 S23: -0.5563
REMARK 3 S31: 0.3045 S32: -0.2964 S33: 0.0581
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: chain J and resid 1:276
REMARK 3 ORIGIN FOR THE GROUP (A): -73.2385 48.8048 378.4184
REMARK 3 T TENSOR
REMARK 3 T11: 0.6885 T22: 0.9025
REMARK 3 T33: 1.0281 T12: 0.0798
REMARK 3 T13: 0.0201 T23: 0.2320
REMARK 3 L TENSOR
REMARK 3 L11: 2.7867 L22: 5.3761
REMARK 3 L33: 4.2390 L12: 0.2033
REMARK 3 L13: 1.5260 L23: 0.6392
REMARK 3 S TENSOR
REMARK 3 S11: 0.0663 S12: -0.6939 S13: -0.6529
REMARK 3 S21: 0.0830 S22: 0.2252 S23: -0.7365
REMARK 3 S31: 0.2649 S32: -0.3230 S33: -0.2270
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: chain J and resid 277:440
REMARK 3 ORIGIN FOR THE GROUP (A): -38.4788 41.4866 355.9113
REMARK 3 T TENSOR
REMARK 3 T11: 0.7165 T22: 0.8033
REMARK 3 T33: 0.7568 T12: 0.1995
REMARK 3 T13: -0.0898 T23: -0.1233
REMARK 3 L TENSOR
REMARK 3 L11: 6.2886 L22: 5.8669
REMARK 3 L33: 8.6641 L12: 4.7704
REMARK 3 L13: 4.0071 L23: 1.5920
REMARK 3 S TENSOR
REMARK 3 S11: 0.2086 S12: -0.6017 S13: 0.5637
REMARK 3 S21: -0.1182 S22: -0.7371 S23: 0.5722
REMARK 3 S31: -0.0680 S32: -0.6500 S33: 0.5145
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: chain K and resid 1:276
REMARK 3 ORIGIN FOR THE GROUP (A): -72.1317 71.8556 407.9764
REMARK 3 T TENSOR
REMARK 3 T11: 2.0088 T22: 1.4956
REMARK 3 T33: 0.9549 T12: 0.2664
REMARK 3 T13: -0.2698 T23: -0.0594
REMARK 3 L TENSOR
REMARK 3 L11: 1.3947 L22: 4.6397
REMARK 3 L33: 3.5631 L12: -0.3608
REMARK 3 L13: 0.6518 L23: -0.2227
REMARK 3 S TENSOR
REMARK 3 S11: -0.3296 S12: -1.2439 S13: 0.2087
REMARK 3 S21: 2.3041 S22: 0.1982 S23: -0.6060
REMARK 3 S31: -0.7719 S32: -0.5772 S33: 0.0953
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: chain K and resid 277:440
REMARK 3 ORIGIN FOR THE GROUP (A): -77.8272 90.2238 371.0915
REMARK 3 T TENSOR
REMARK 3 T11: 0.8889 T22: 0.7591
REMARK 3 T33: 0.7402 T12: -0.0795
REMARK 3 T13: 0.0266 T23: -0.1063
REMARK 3 L TENSOR
REMARK 3 L11: 9.4993 L22: 6.3044
REMARK 3 L33: 9.3972 L12: -6.1516
REMARK 3 L13: -1.1326 L23: 0.4951
REMARK 3 S TENSOR
REMARK 3 S11: -0.1913 S12: -0.6978 S13: 0.0939
REMARK 3 S21: 0.4381 S22: 0.3698 S23: -0.1725
REMARK 3 S31: -0.5344 S32: -0.5784 S33: -0.2245
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: chain L and resid 1:276
REMARK 3 ORIGIN FOR THE GROUP (A): -47.5731 43.6277 405.1817
REMARK 3 T TENSOR
REMARK 3 T11: 1.6197 T22: 1.4753
REMARK 3 T33: 2.7177 T12: 0.1642
REMARK 3 T13: -0.9854 T23: 0.3133
REMARK 3 L TENSOR
REMARK 3 L11: 2.0957 L22: 2.0351
REMARK 3 L33: 2.6985 L12: 0.3271
REMARK 3 L13: 0.8958 L23: -0.2537
REMARK 3 S TENSOR
REMARK 3 S11: 0.0285 S12: -0.6933 S13: -0.6052
REMARK 3 S21: 1.3902 S22: 0.0871 S23: -2.1311
REMARK 3 S31: 0.1280 S32: 0.3049 S33: -0.0914
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: chain L and resid 277:440
REMARK 3 ORIGIN FOR THE GROUP (A): -18.2103 71.2114 418.2901
REMARK 3 T TENSOR
REMARK 3 T11: 2.6837 T22: 3.3908
REMARK 3 T33: 3.5728 T12: -0.4479
REMARK 3 T13: 0.3184 T23: 0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 1.8743 L22: 2.7997
REMARK 3 L33: 0.3596 L12: 1.7995
REMARK 3 L13: -0.4267 L23: 0.5201
REMARK 3 S TENSOR
REMARK 3 S11: 0.0063 S12: -1.1429 S13: 1.8253
REMARK 3 S21: -1.1567 S22: 0.3268 S23: -0.5665
REMARK 3 S31: -1.1552 S32: 2.3330 S33: -0.3652
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 4ITV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-13.
REMARK 100 THE RCSB ID CODE IS RCSB077202.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97910
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76475
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.598
REMARK 200 RESOLUTION RANGE LOW (A) : 160.575
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.6100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.61900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1BRO AND 1AA7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA CITRATE PH 4.4, 10% PEG 3000,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 65.81000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 160.57500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 78.30500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 160.57500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 65.81000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 78.30500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 35620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 187760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -97.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, J, G, I, K, L, H, B, E,
REMARK 350 AND CHAINS: D, F, 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 0
REMARK 465 GLN A 441
REMARK 465 HIS A 442
REMARK 465 ARG A 443
REMARK 465 SER A 444
REMARK 465 HIS A 445
REMARK 465 ARG A 446
REMARK 465 GLN A 447
REMARK 465 LEU A 448
REMARK 465 GLU A 449
REMARK 465 HIS A 450
REMARK 465 HIS A 451
REMARK 465 HIS A 452
REMARK 465 HIS A 453
REMARK 465 HIS A 454
REMARK 465 HIS A 455
REMARK 465 MET B 0
REMARK 465 GLN B 441
REMARK 465 HIS B 442
REMARK 465 ARG B 443
REMARK 465 SER B 444
REMARK 465 HIS B 445
REMARK 465 ARG B 446
REMARK 465 GLN B 447
REMARK 465 LEU B 448
REMARK 465 GLU B 449
REMARK 465 HIS B 450
REMARK 465 HIS B 451
REMARK 465 HIS B 452
REMARK 465 HIS B 453
REMARK 465 HIS B 454
REMARK 465 HIS B 455
REMARK 465 MET C 0
REMARK 465 GLN C 441
REMARK 465 HIS C 442
REMARK 465 ARG C 443
REMARK 465 SER C 444
REMARK 465 HIS C 445
REMARK 465 ARG C 446
REMARK 465 GLN C 447
REMARK 465 LEU C 448
REMARK 465 GLU C 449
REMARK 465 HIS C 450
REMARK 465 HIS C 451
REMARK 465 HIS C 452
REMARK 465 HIS C 453
REMARK 465 HIS C 454
REMARK 465 HIS C 455
REMARK 465 MET D 0
REMARK 465 GLN D 441
REMARK 465 HIS D 442
REMARK 465 ARG D 443
REMARK 465 SER D 444
REMARK 465 HIS D 445
REMARK 465 ARG D 446
REMARK 465 GLN D 447
REMARK 465 LEU D 448
REMARK 465 GLU D 449
REMARK 465 HIS D 450
REMARK 465 HIS D 451
REMARK 465 HIS D 452
REMARK 465 HIS D 453
REMARK 465 HIS D 454
REMARK 465 HIS D 455
REMARK 465 MET E 0
REMARK 465 GLN E 441
REMARK 465 HIS E 442
REMARK 465 ARG E 443
REMARK 465 SER E 444
REMARK 465 HIS E 445
REMARK 465 ARG E 446
REMARK 465 GLN E 447
REMARK 465 LEU E 448
REMARK 465 GLU E 449
REMARK 465 HIS E 450
REMARK 465 HIS E 451
REMARK 465 HIS E 452
REMARK 465 HIS E 453
REMARK 465 HIS E 454
REMARK 465 HIS E 455
REMARK 465 MET F 0
REMARK 465 GLN F 441
REMARK 465 HIS F 442
REMARK 465 ARG F 443
REMARK 465 SER F 444
REMARK 465 HIS F 445
REMARK 465 ARG F 446
REMARK 465 GLN F 447
REMARK 465 LEU F 448
REMARK 465 GLU F 449
REMARK 465 HIS F 450
REMARK 465 HIS F 451
REMARK 465 HIS F 452
REMARK 465 HIS F 453
REMARK 465 HIS F 454
REMARK 465 HIS F 455
REMARK 465 MET G 0
REMARK 465 GLN G 441
REMARK 465 HIS G 442
REMARK 465 ARG G 443
REMARK 465 SER G 444
REMARK 465 HIS G 445
REMARK 465 ARG G 446
REMARK 465 GLN G 447
REMARK 465 LEU G 448
REMARK 465 GLU G 449
REMARK 465 HIS G 450
REMARK 465 HIS G 451
REMARK 465 HIS G 452
REMARK 465 HIS G 453
REMARK 465 HIS G 454
REMARK 465 HIS G 455
REMARK 465 MET H 0
REMARK 465 GLN H 441
REMARK 465 HIS H 442
REMARK 465 ARG H 443
REMARK 465 SER H 444
REMARK 465 HIS H 445
REMARK 465 ARG H 446
REMARK 465 GLN H 447
REMARK 465 LEU H 448
REMARK 465 GLU H 449
REMARK 465 HIS H 450
REMARK 465 HIS H 451
REMARK 465 HIS H 452
REMARK 465 HIS H 453
REMARK 465 HIS H 454
REMARK 465 HIS H 455
REMARK 465 MET I 0
REMARK 465 GLN I 441
REMARK 465 HIS I 442
REMARK 465 ARG I 443
REMARK 465 SER I 444
REMARK 465 HIS I 445
REMARK 465 ARG I 446
REMARK 465 GLN I 447
REMARK 465 LEU I 448
REMARK 465 GLU I 449
REMARK 465 HIS I 450
REMARK 465 HIS I 451
REMARK 465 HIS I 452
REMARK 465 HIS I 453
REMARK 465 HIS I 454
REMARK 465 HIS I 455
REMARK 465 MET J 0
REMARK 465 GLN J 441
REMARK 465 HIS J 442
REMARK 465 ARG J 443
REMARK 465 SER J 444
REMARK 465 HIS J 445
REMARK 465 ARG J 446
REMARK 465 GLN J 447
REMARK 465 LEU J 448
REMARK 465 GLU J 449
REMARK 465 HIS J 450
REMARK 465 HIS J 451
REMARK 465 HIS J 452
REMARK 465 HIS J 453
REMARK 465 HIS J 454
REMARK 465 HIS J 455
REMARK 465 MET K 0
REMARK 465 GLN K 441
REMARK 465 HIS K 442
REMARK 465 ARG K 443
REMARK 465 SER K 444
REMARK 465 HIS K 445
REMARK 465 ARG K 446
REMARK 465 GLN K 447
REMARK 465 LEU K 448
REMARK 465 GLU K 449
REMARK 465 HIS K 450
REMARK 465 HIS K 451
REMARK 465 HIS K 452
REMARK 465 HIS K 453
REMARK 465 HIS K 454
REMARK 465 HIS K 455
REMARK 465 MET L 0
REMARK 465 GLN L 441
REMARK 465 HIS L 442
REMARK 465 ARG L 443
REMARK 465 SER L 444
REMARK 465 HIS L 445
REMARK 465 ARG L 446
REMARK 465 GLN L 447
REMARK 465 LEU L 448
REMARK 465 GLU L 449
REMARK 465 HIS L 450
REMARK 465 HIS L 451
REMARK 465 HIS L 452
REMARK 465 HIS L 453
REMARK 465 HIS L 454
REMARK 465 HIS L 455
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 ASN A 9 -148.45 29.30
REMARK 500 LEU A 34 -158.05 -88.66
REMARK 500 GLN A 66 78.01 -118.78
REMARK 500 TYR A 71 71.37 -102.68
REMARK 500 SER A 98 -120.84 51.72
REMARK 500 THR A 113 47.53 -86.82
REMARK 500 GLU A 126 150.51 -48.94
REMARK 500 THR A 176 -70.23 -108.10
REMARK 500 TYR A 206 42.44 -93.07
REMARK 500 THR A 236 -74.26 -124.99
REMARK 500 PRO A 256 -167.62 -73.74
REMARK 500 ASN A 319 102.62 -54.10
REMARK 500 ARG A 417 18.69 59.49
REMARK 500 ASN B 9 -130.42 53.67
REMARK 500 LEU B 34 -158.44 -88.64
REMARK 500 GLN B 66 77.72 -118.05
REMARK 500 TYR B 71 72.02 -101.67
REMARK 500 SER B 98 -120.11 51.91
REMARK 500 THR B 113 48.15 -86.42
REMARK 500 THR B 176 -70.57 -108.69
REMARK 500 TYR B 206 41.73 -92.39
REMARK 500 THR B 236 -72.98 -126.26
REMARK 500 PRO B 256 -167.47 -74.62
REMARK 500 ASN B 319 103.16 -55.25
REMARK 500 ARG B 417 18.68 59.47
REMARK 500 ASN C 9 -150.10 52.62
REMARK 500 TYR C 17 -169.68 -106.86
REMARK 500 LEU C 34 -157.36 -88.36
REMARK 500 GLN C 66 77.73 -119.34
REMARK 500 TYR C 71 71.16 -101.81
REMARK 500 SER C 98 -121.32 52.42
REMARK 500 THR C 113 47.95 -86.76
REMARK 500 GLU C 126 150.44 -49.42
REMARK 500 THR C 176 -70.39 -107.53
REMARK 500 TYR C 206 42.13 -92.35
REMARK 500 THR C 236 -73.43 -125.63
REMARK 500 PRO C 256 -167.87 -74.20
REMARK 500 ASN C 319 102.40 -52.76
REMARK 500 ARG C 417 19.85 58.87
REMARK 500 ASN D 9 -150.06 31.52
REMARK 500 LEU D 34 -157.76 -88.37
REMARK 500 GLN D 66 78.29 -119.28
REMARK 500 TYR D 71 70.66 -102.44
REMARK 500 SER D 98 -120.45 51.90
REMARK 500 THR D 113 47.84 -86.84
REMARK 500 THR D 176 -70.42 -107.96
REMARK 500 TYR D 206 41.74 -92.81
REMARK 500 THR D 236 -73.21 -124.85
REMARK 500 LEU D 244 76.42 -150.12
REMARK 500 PRO D 256 -167.23 -73.73
REMARK 500
REMARK 500 THIS ENTRY HAS 165 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4IQ4 RELATED DB: PDB
REMARK 900 RELATED ID: 3VDX RELATED DB: PDB
REMARK 900 RELATED ID: 4D9J RELATED DB: PDB
REMARK 900 RELATED ID: 4IVJ RELATED DB: PDB
DBREF 4ITV A 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4ITV A 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4ITV B 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4ITV B 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4ITV C 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4ITV C 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4ITV D 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4ITV D 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4ITV E 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4ITV E 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4ITV F 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4ITV F 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4ITV G 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4ITV G 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4ITV H 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4ITV H 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4ITV I 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4ITV I 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4ITV J 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4ITV J 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4ITV K 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4ITV K 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4ITV L 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4ITV L 286 447 UNP P03485 M1_I34A1 3 164
SEQADV 4ITV THR A 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4ITV ALA A 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4ITV ALA A 278 UNP P03485 LINKER
SEQADV 4ITV GLN A 279 UNP P03485 LINKER
SEQADV 4ITV GLU A 280 UNP P03485 LINKER
SEQADV 4ITV ALA A 281 UNP P03485 LINKER
SEQADV 4ITV GLN A 282 UNP P03485 LINKER
SEQADV 4ITV LYS A 283 UNP P03485 LINKER
SEQADV 4ITV GLN A 284 UNP P03485 LINKER
SEQADV 4ITV LYS A 285 UNP P03485 LINKER
SEQADV 4ITV LEU A 448 UNP P03485 EXPRESSION TAG
SEQADV 4ITV GLU A 449 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS A 450 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS A 451 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS A 452 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS A 453 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS A 454 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS A 455 UNP P03485 EXPRESSION TAG
SEQADV 4ITV THR B 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4ITV ALA B 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4ITV ALA B 278 UNP P03485 LINKER
SEQADV 4ITV GLN B 279 UNP P03485 LINKER
SEQADV 4ITV GLU B 280 UNP P03485 LINKER
SEQADV 4ITV ALA B 281 UNP P03485 LINKER
SEQADV 4ITV GLN B 282 UNP P03485 LINKER
SEQADV 4ITV LYS B 283 UNP P03485 LINKER
SEQADV 4ITV GLN B 284 UNP P03485 LINKER
SEQADV 4ITV LYS B 285 UNP P03485 LINKER
SEQADV 4ITV LEU B 448 UNP P03485 EXPRESSION TAG
SEQADV 4ITV GLU B 449 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS B 450 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS B 451 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS B 452 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS B 453 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS B 454 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS B 455 UNP P03485 EXPRESSION TAG
SEQADV 4ITV THR C 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4ITV ALA C 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4ITV ALA C 278 UNP P03485 LINKER
SEQADV 4ITV GLN C 279 UNP P03485 LINKER
SEQADV 4ITV GLU C 280 UNP P03485 LINKER
SEQADV 4ITV ALA C 281 UNP P03485 LINKER
SEQADV 4ITV GLN C 282 UNP P03485 LINKER
SEQADV 4ITV LYS C 283 UNP P03485 LINKER
SEQADV 4ITV GLN C 284 UNP P03485 LINKER
SEQADV 4ITV LYS C 285 UNP P03485 LINKER
SEQADV 4ITV LEU C 448 UNP P03485 EXPRESSION TAG
SEQADV 4ITV GLU C 449 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS C 450 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS C 451 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS C 452 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS C 453 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS C 454 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS C 455 UNP P03485 EXPRESSION TAG
SEQADV 4ITV THR D 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4ITV ALA D 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4ITV ALA D 278 UNP P03485 LINKER
SEQADV 4ITV GLN D 279 UNP P03485 LINKER
SEQADV 4ITV GLU D 280 UNP P03485 LINKER
SEQADV 4ITV ALA D 281 UNP P03485 LINKER
SEQADV 4ITV GLN D 282 UNP P03485 LINKER
SEQADV 4ITV LYS D 283 UNP P03485 LINKER
SEQADV 4ITV GLN D 284 UNP P03485 LINKER
SEQADV 4ITV LYS D 285 UNP P03485 LINKER
SEQADV 4ITV LEU D 448 UNP P03485 EXPRESSION TAG
SEQADV 4ITV GLU D 449 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS D 450 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS D 451 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS D 452 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS D 453 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS D 454 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS D 455 UNP P03485 EXPRESSION TAG
SEQADV 4ITV THR E 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4ITV ALA E 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4ITV ALA E 278 UNP P03485 LINKER
SEQADV 4ITV GLN E 279 UNP P03485 LINKER
SEQADV 4ITV GLU E 280 UNP P03485 LINKER
SEQADV 4ITV ALA E 281 UNP P03485 LINKER
SEQADV 4ITV GLN E 282 UNP P03485 LINKER
SEQADV 4ITV LYS E 283 UNP P03485 LINKER
SEQADV 4ITV GLN E 284 UNP P03485 LINKER
SEQADV 4ITV LYS E 285 UNP P03485 LINKER
SEQADV 4ITV LEU E 448 UNP P03485 EXPRESSION TAG
SEQADV 4ITV GLU E 449 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS E 450 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS E 451 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS E 452 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS E 453 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS E 454 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS E 455 UNP P03485 EXPRESSION TAG
SEQADV 4ITV THR F 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4ITV ALA F 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4ITV ALA F 278 UNP P03485 LINKER
SEQADV 4ITV GLN F 279 UNP P03485 LINKER
SEQADV 4ITV GLU F 280 UNP P03485 LINKER
SEQADV 4ITV ALA F 281 UNP P03485 LINKER
SEQADV 4ITV GLN F 282 UNP P03485 LINKER
SEQADV 4ITV LYS F 283 UNP P03485 LINKER
SEQADV 4ITV GLN F 284 UNP P03485 LINKER
SEQADV 4ITV LYS F 285 UNP P03485 LINKER
SEQADV 4ITV LEU F 448 UNP P03485 EXPRESSION TAG
SEQADV 4ITV GLU F 449 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS F 450 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS F 451 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS F 452 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS F 453 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS F 454 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS F 455 UNP P03485 EXPRESSION TAG
SEQADV 4ITV THR G 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4ITV ALA G 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4ITV ALA G 278 UNP P03485 LINKER
SEQADV 4ITV GLN G 279 UNP P03485 LINKER
SEQADV 4ITV GLU G 280 UNP P03485 LINKER
SEQADV 4ITV ALA G 281 UNP P03485 LINKER
SEQADV 4ITV GLN G 282 UNP P03485 LINKER
SEQADV 4ITV LYS G 283 UNP P03485 LINKER
SEQADV 4ITV GLN G 284 UNP P03485 LINKER
SEQADV 4ITV LYS G 285 UNP P03485 LINKER
SEQADV 4ITV LEU G 448 UNP P03485 EXPRESSION TAG
SEQADV 4ITV GLU G 449 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS G 450 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS G 451 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS G 452 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS G 453 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS G 454 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS G 455 UNP P03485 EXPRESSION TAG
SEQADV 4ITV THR H 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4ITV ALA H 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4ITV ALA H 278 UNP P03485 LINKER
SEQADV 4ITV GLN H 279 UNP P03485 LINKER
SEQADV 4ITV GLU H 280 UNP P03485 LINKER
SEQADV 4ITV ALA H 281 UNP P03485 LINKER
SEQADV 4ITV GLN H 282 UNP P03485 LINKER
SEQADV 4ITV LYS H 283 UNP P03485 LINKER
SEQADV 4ITV GLN H 284 UNP P03485 LINKER
SEQADV 4ITV LYS H 285 UNP P03485 LINKER
SEQADV 4ITV LEU H 448 UNP P03485 EXPRESSION TAG
SEQADV 4ITV GLU H 449 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS H 450 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS H 451 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS H 452 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS H 453 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS H 454 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS H 455 UNP P03485 EXPRESSION TAG
SEQADV 4ITV THR I 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4ITV ALA I 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4ITV ALA I 278 UNP P03485 LINKER
SEQADV 4ITV GLN I 279 UNP P03485 LINKER
SEQADV 4ITV GLU I 280 UNP P03485 LINKER
SEQADV 4ITV ALA I 281 UNP P03485 LINKER
SEQADV 4ITV GLN I 282 UNP P03485 LINKER
SEQADV 4ITV LYS I 283 UNP P03485 LINKER
SEQADV 4ITV GLN I 284 UNP P03485 LINKER
SEQADV 4ITV LYS I 285 UNP P03485 LINKER
SEQADV 4ITV LEU I 448 UNP P03485 EXPRESSION TAG
SEQADV 4ITV GLU I 449 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS I 450 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS I 451 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS I 452 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS I 453 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS I 454 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS I 455 UNP P03485 EXPRESSION TAG
SEQADV 4ITV THR J 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4ITV ALA J 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4ITV ALA J 278 UNP P03485 LINKER
SEQADV 4ITV GLN J 279 UNP P03485 LINKER
SEQADV 4ITV GLU J 280 UNP P03485 LINKER
SEQADV 4ITV ALA J 281 UNP P03485 LINKER
SEQADV 4ITV GLN J 282 UNP P03485 LINKER
SEQADV 4ITV LYS J 283 UNP P03485 LINKER
SEQADV 4ITV GLN J 284 UNP P03485 LINKER
SEQADV 4ITV LYS J 285 UNP P03485 LINKER
SEQADV 4ITV LEU J 448 UNP P03485 EXPRESSION TAG
SEQADV 4ITV GLU J 449 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS J 450 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS J 451 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS J 452 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS J 453 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS J 454 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS J 455 UNP P03485 EXPRESSION TAG
SEQADV 4ITV THR K 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4ITV ALA K 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4ITV ALA K 278 UNP P03485 LINKER
SEQADV 4ITV GLN K 279 UNP P03485 LINKER
SEQADV 4ITV GLU K 280 UNP P03485 LINKER
SEQADV 4ITV ALA K 281 UNP P03485 LINKER
SEQADV 4ITV GLN K 282 UNP P03485 LINKER
SEQADV 4ITV LYS K 283 UNP P03485 LINKER
SEQADV 4ITV GLN K 284 UNP P03485 LINKER
SEQADV 4ITV LYS K 285 UNP P03485 LINKER
SEQADV 4ITV LEU K 448 UNP P03485 EXPRESSION TAG
SEQADV 4ITV GLU K 449 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS K 450 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS K 451 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS K 452 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS K 453 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS K 454 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS K 455 UNP P03485 EXPRESSION TAG
SEQADV 4ITV THR L 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4ITV ALA L 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4ITV ALA L 278 UNP P03485 LINKER
SEQADV 4ITV GLN L 279 UNP P03485 LINKER
SEQADV 4ITV GLU L 280 UNP P03485 LINKER
SEQADV 4ITV ALA L 281 UNP P03485 LINKER
SEQADV 4ITV GLN L 282 UNP P03485 LINKER
SEQADV 4ITV LYS L 283 UNP P03485 LINKER
SEQADV 4ITV GLN L 284 UNP P03485 LINKER
SEQADV 4ITV LYS L 285 UNP P03485 LINKER
SEQADV 4ITV LEU L 448 UNP P03485 EXPRESSION TAG
SEQADV 4ITV GLU L 449 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS L 450 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS L 451 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS L 452 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS L 453 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS L 454 UNP P03485 EXPRESSION TAG
SEQADV 4ITV HIS L 455 UNP P03485 EXPRESSION TAG
SEQRES 1 A 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 A 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 A 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 A 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 A 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 A 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 A 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 A 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 A 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 A 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 A 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 A 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 A 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 A 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 A 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 A 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 A 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 A 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 A 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 A 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 A 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 A 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 A 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 A 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 A 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 A 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 A 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 A 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 A 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 A 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 A 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 A 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 A 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 A 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 A 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 A 456 HIS
SEQRES 1 B 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 B 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 B 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 B 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 B 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 B 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 B 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 B 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 B 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 B 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 B 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 B 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 B 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 B 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 B 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 B 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 B 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 B 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 B 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 B 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 B 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 B 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 B 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 B 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 B 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 B 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 B 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 B 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 B 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 B 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 B 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 B 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 B 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 B 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 B 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 B 456 HIS
SEQRES 1 C 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 C 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 C 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 C 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 C 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 C 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 C 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 C 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 C 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 C 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 C 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 C 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 C 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 C 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 C 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 C 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 C 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 C 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 C 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 C 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 C 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 C 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 C 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 C 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 C 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 C 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 C 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 C 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 C 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 C 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 C 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 C 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 C 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 C 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 C 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 C 456 HIS
SEQRES 1 D 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 D 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 D 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 D 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 D 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 D 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 D 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 D 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 D 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 D 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 D 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 D 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 D 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 D 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 D 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 D 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 D 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 D 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 D 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 D 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 D 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 D 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 D 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 D 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 D 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 D 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 D 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 D 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 D 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 D 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 D 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 D 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 D 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 D 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 D 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 D 456 HIS
SEQRES 1 E 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 E 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 E 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 E 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 E 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 E 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 E 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 E 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 E 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 E 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 E 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 E 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 E 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 E 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 E 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 E 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 E 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 E 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 E 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 E 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 E 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 E 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 E 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 E 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 E 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 E 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 E 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 E 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 E 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 E 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 E 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 E 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 E 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 E 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 E 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 E 456 HIS
SEQRES 1 F 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 F 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 F 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 F 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 F 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 F 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 F 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 F 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 F 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 F 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 F 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 F 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 F 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 F 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 F 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 F 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 F 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 F 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 F 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 F 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 F 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 F 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 F 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 F 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 F 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 F 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 F 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 F 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 F 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 F 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 F 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 F 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 F 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 F 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 F 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 F 456 HIS
SEQRES 1 G 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 G 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 G 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 G 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 G 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 G 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 G 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 G 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 G 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 G 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 G 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 G 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 G 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 G 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 G 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 G 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 G 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 G 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 G 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 G 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 G 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 G 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 G 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 G 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 G 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 G 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 G 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 G 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 G 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 G 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 G 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 G 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 G 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 G 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 G 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 G 456 HIS
SEQRES 1 H 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 H 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 H 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 H 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 H 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 H 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 H 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 H 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 H 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 H 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 H 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 H 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 H 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 H 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 H 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 H 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 H 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 H 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 H 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 H 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 H 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 H 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 H 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 H 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 H 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 H 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 H 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 H 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 H 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 H 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 H 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 H 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 H 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 H 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 H 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 H 456 HIS
SEQRES 1 I 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 I 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 I 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 I 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 I 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 I 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 I 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 I 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 I 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 I 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 I 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 I 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 I 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 I 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 I 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 I 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 I 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 I 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 I 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 I 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 I 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 I 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 I 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 I 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 I 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 I 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 I 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 I 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 I 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 I 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 I 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 I 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 I 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 I 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 I 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 I 456 HIS
SEQRES 1 J 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 J 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 J 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 J 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 J 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 J 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 J 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 J 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 J 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 J 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 J 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 J 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 J 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 J 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 J 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 J 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 J 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 J 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 J 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 J 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 J 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 J 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 J 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 J 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 J 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 J 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 J 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 J 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 J 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 J 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 J 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 J 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 J 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 J 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 J 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 J 456 HIS
SEQRES 1 K 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 K 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 K 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 K 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 K 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 K 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 K 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 K 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 K 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 K 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 K 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 K 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 K 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 K 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 K 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 K 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 K 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 K 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 K 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 K 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 K 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 K 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 K 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 K 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 K 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 K 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 K 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 K 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 K 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 K 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 K 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 K 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 K 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 K 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 K 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 K 456 HIS
SEQRES 1 L 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 L 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 L 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 L 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 L 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 L 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 L 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 L 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 L 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 L 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 L 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 L 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 L 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 L 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 L 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 L 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 L 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 L 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 L 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 L 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 L 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 L 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 L 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 L 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 L 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 L 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 L 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 L 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 L 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 L 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 L 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 L 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 L 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 L 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 L 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 L 456 HIS
HELIX 1 1 SER A 35 SER A 38 5 4
HELIX 2 2 TRP A 39 ALA A 49 1 11
HELIX 3 3 ASP A 72 ASP A 88 1 17
HELIX 4 4 SER A 98 GLY A 112 1 15
HELIX 5 5 PRO A 141 ASP A 155 1 15
HELIX 6 6 ASP A 155 TYR A 168 1 14
HELIX 7 7 ASN A 169 LEU A 174 1 6
HELIX 8 8 SER A 179 GLY A 193 1 15
HELIX 9 9 GLY A 194 ALA A 201 1 8
HELIX 10 10 PRO A 202 TRP A 205 5 4
HELIX 11 11 ASP A 212 ILE A 216 5 5
HELIX 12 12 THR A 236 LEU A 244 1 9
HELIX 13 13 GLY A 258 HIS A 263 1 6
HELIX 14 14 HIS A 263 SER A 296 1 34
HELIX 15 15 GLY A 301 GLY A 317 1 17
HELIX 16 16 ASP A 321 THR A 331 1 11
HELIX 17 17 SER A 336 VAL A 351 1 16
HELIX 18 18 ARG A 360 ASN A 365 1 6
HELIX 19 19 ASP A 372 ARG A 388 1 17
HELIX 20 20 THR A 391 LEU A 400 1 10
HELIX 21 21 SER A 403 ASN A 416 1 14
HELIX 22 22 THR A 422 SER A 440 1 19
HELIX 23 23 SER B 35 SER B 38 5 4
HELIX 24 24 TRP B 39 ALA B 49 1 11
HELIX 25 25 ASP B 72 ASP B 88 1 17
HELIX 26 26 SER B 98 GLY B 112 1 15
HELIX 27 27 PRO B 141 TYR B 168 1 28
HELIX 28 28 ASN B 169 LEU B 174 1 6
HELIX 29 29 SER B 179 GLY B 193 1 15
HELIX 30 30 GLY B 194 ALA B 201 1 8
HELIX 31 31 ALA B 201 TYR B 206 1 6
HELIX 32 32 ASP B 212 ILE B 216 5 5
HELIX 33 33 PRO B 232 LEU B 244 1 13
HELIX 34 34 GLY B 258 HIS B 263 1 6
HELIX 35 35 HIS B 263 SER B 296 1 34
HELIX 36 36 GLY B 301 GLY B 317 1 17
HELIX 37 37 ASP B 321 THR B 331 1 11
HELIX 38 38 SER B 336 VAL B 351 1 16
HELIX 39 39 ARG B 360 ASN B 365 1 6
HELIX 40 40 ASP B 372 ARG B 388 1 17
HELIX 41 41 THR B 391 LEU B 400 1 10
HELIX 42 42 SER B 403 ASN B 416 1 14
HELIX 43 43 THR B 422 SER B 440 1 19
HELIX 44 44 SER C 35 SER C 38 5 4
HELIX 45 45 TRP C 39 ALA C 49 1 11
HELIX 46 46 ASP C 72 ASP C 88 1 17
HELIX 47 47 MET C 99 GLY C 112 1 14
HELIX 48 48 PRO C 141 ASP C 155 1 15
HELIX 49 49 ASP C 155 TYR C 168 1 14
HELIX 50 50 ASN C 169 LEU C 174 1 6
HELIX 51 51 SER C 179 GLY C 193 1 15
HELIX 52 52 GLY C 194 ALA C 201 1 8
HELIX 53 53 PRO C 202 TRP C 205 5 4
HELIX 54 54 ASP C 212 ILE C 216 5 5
HELIX 55 55 THR C 236 LEU C 244 1 9
HELIX 56 56 GLY C 258 HIS C 263 1 6
HELIX 57 57 HIS C 263 SER C 296 1 34
HELIX 58 58 GLY C 301 GLY C 317 1 17
HELIX 59 59 ASP C 321 THR C 331 1 11
HELIX 60 60 SER C 336 VAL C 351 1 16
HELIX 61 61 ARG C 360 ASN C 365 1 6
HELIX 62 62 ASP C 372 ARG C 388 1 17
HELIX 63 63 THR C 391 LEU C 400 1 10
HELIX 64 64 SER C 403 ASN C 416 1 14
HELIX 65 65 THR C 422 ALA C 438 1 17
HELIX 66 66 SER D 35 SER D 38 5 4
HELIX 67 67 TRP D 39 ALA D 49 1 11
HELIX 68 68 ASP D 72 ASP D 88 1 17
HELIX 69 69 SER D 98 GLY D 112 1 15
HELIX 70 70 PRO D 141 TYR D 168 1 28
HELIX 71 71 ASN D 169 LEU D 174 1 6
HELIX 72 72 SER D 179 GLY D 193 1 15
HELIX 73 73 GLY D 194 ALA D 201 1 8
HELIX 74 74 PRO D 202 TRP D 205 5 4
HELIX 75 75 ASP D 212 ILE D 216 5 5
HELIX 76 76 PRO D 232 LEU D 244 1 13
HELIX 77 77 GLY D 258 HIS D 263 1 6
HELIX 78 78 HIS D 263 SER D 296 1 34
HELIX 79 79 GLY D 301 GLY D 317 1 17
HELIX 80 80 ASP D 321 THR D 331 1 11
HELIX 81 81 SER D 336 VAL D 351 1 16
HELIX 82 82 ARG D 360 ASN D 368 1 9
HELIX 83 83 ASP D 372 ARG D 388 1 17
HELIX 84 84 THR D 391 LEU D 400 1 10
HELIX 85 85 SER D 403 ASN D 416 1 14
HELIX 86 86 THR D 422 ALA D 438 1 17
HELIX 87 87 SER E 35 SER E 38 5 4
HELIX 88 88 TRP E 39 ALA E 49 1 11
HELIX 89 89 ASP E 72 ASP E 88 1 17
HELIX 90 90 MET E 99 GLY E 112 1 14
HELIX 91 91 PRO E 141 TYR E 168 1 28
HELIX 92 92 ASN E 169 LEU E 174 1 6
HELIX 93 93 SER E 179 GLY E 193 1 15
HELIX 94 94 GLY E 194 ALA E 201 1 8
HELIX 95 95 PRO E 202 TRP E 205 5 4
HELIX 96 96 ASP E 212 ILE E 216 5 5
HELIX 97 97 PRO E 232 LEU E 244 1 13
HELIX 98 98 GLY E 258 HIS E 263 1 6
HELIX 99 99 HIS E 263 SER E 296 1 34
HELIX 100 100 GLY E 301 GLY E 317 1 17
HELIX 101 101 ASP E 321 THR E 331 1 11
HELIX 102 102 SER E 336 VAL E 351 1 16
HELIX 103 103 ARG E 360 ASN E 365 1 6
HELIX 104 104 ASP E 372 ARG E 388 1 17
HELIX 105 105 THR E 391 LEU E 400 1 10
HELIX 106 106 SER E 403 ASN E 416 1 14
HELIX 107 107 THR E 422 ALA E 438 1 17
HELIX 108 108 SER F 35 SER F 38 5 4
HELIX 109 109 TRP F 39 ALA F 49 1 11
HELIX 110 110 ASP F 72 LEU F 87 1 16
HELIX 111 111 MET F 99 GLY F 112 1 14
HELIX 112 112 PRO F 141 TYR F 168 1 28
HELIX 113 113 ASN F 169 LEU F 174 1 6
HELIX 114 114 SER F 179 GLY F 193 1 15
HELIX 115 115 GLY F 194 ALA F 201 1 8
HELIX 116 116 PRO F 202 TRP F 205 5 4
HELIX 117 117 ASP F 212 ILE F 216 5 5
HELIX 118 118 PRO F 232 LEU F 244 1 13
HELIX 119 119 GLY F 258 HIS F 263 1 6
HELIX 120 120 HIS F 263 SER F 296 1 34
HELIX 121 121 GLY F 301 GLY F 317 1 17
HELIX 122 122 ASP F 321 THR F 331 1 11
HELIX 123 123 SER F 336 VAL F 351 1 16
HELIX 124 124 ARG F 360 ASN F 365 1 6
HELIX 125 125 ASP F 372 ARG F 388 1 17
HELIX 126 126 THR F 391 LEU F 400 1 10
HELIX 127 127 SER F 403 ASN F 416 1 14
HELIX 128 128 THR F 422 SER F 440 1 19
HELIX 129 129 SER G 35 SER G 38 5 4
HELIX 130 130 TRP G 39 ALA G 49 1 11
HELIX 131 131 ASP G 72 ASP G 88 1 17
HELIX 132 132 MET G 99 GLY G 112 1 14
HELIX 133 133 PRO G 141 TYR G 168 1 28
HELIX 134 134 ASN G 169 LEU G 174 1 6
HELIX 135 135 SER G 179 GLY G 193 1 15
HELIX 136 136 GLY G 194 ALA G 201 1 8
HELIX 137 137 PRO G 202 TRP G 205 5 4
HELIX 138 138 ASP G 212 ILE G 216 5 5
HELIX 139 139 PRO G 232 LEU G 244 1 13
HELIX 140 140 GLY G 258 HIS G 263 1 6
HELIX 141 141 HIS G 263 SER G 296 1 34
HELIX 142 142 GLY G 301 GLY G 317 1 17
HELIX 143 143 ASP G 321 THR G 331 1 11
HELIX 144 144 SER G 336 VAL G 351 1 16
HELIX 145 145 ARG G 360 ASN G 365 1 6
HELIX 146 146 ASP G 372 ARG G 388 1 17
HELIX 147 147 THR G 391 LEU G 400 1 10
HELIX 148 148 SER G 403 ASN G 416 1 14
HELIX 149 149 THR G 422 ALA G 438 1 17
HELIX 150 150 SER H 35 SER H 38 5 4
HELIX 151 151 TRP H 39 ALA H 49 1 11
HELIX 152 152 ASP H 72 ASP H 88 1 17
HELIX 153 153 SER H 98 GLY H 112 1 15
HELIX 154 154 PRO H 141 ASP H 155 1 15
HELIX 155 155 ASP H 155 TYR H 168 1 14
HELIX 156 156 ASN H 169 LEU H 174 1 6
HELIX 157 157 SER H 179 GLY H 193 1 15
HELIX 158 158 GLY H 194 ALA H 201 1 8
HELIX 159 159 PRO H 202 TRP H 205 5 4
HELIX 160 160 ASP H 212 ILE H 216 5 5
HELIX 161 161 PRO H 232 LEU H 244 1 13
HELIX 162 162 GLY H 258 HIS H 263 1 6
HELIX 163 163 HIS H 263 SER H 296 1 34
HELIX 164 164 GLY H 301 GLY H 317 1 17
HELIX 165 165 ASP H 321 THR H 331 1 11
HELIX 166 166 SER H 336 VAL H 351 1 16
HELIX 167 167 ARG H 360 ASN H 365 1 6
HELIX 168 168 ASP H 372 ARG H 388 1 17
HELIX 169 169 THR H 391 LEU H 400 1 10
HELIX 170 170 SER H 403 ASN H 416 1 14
HELIX 171 171 THR H 422 ALA H 438 1 17
HELIX 172 172 SER I 35 SER I 38 5 4
HELIX 173 173 TRP I 39 ALA I 49 1 11
HELIX 174 174 ASP I 72 ASP I 88 1 17
HELIX 175 175 MET I 99 GLY I 112 1 14
HELIX 176 176 PRO I 141 ASP I 155 1 15
HELIX 177 177 ASP I 155 TYR I 168 1 14
HELIX 178 178 ASN I 169 LEU I 174 1 6
HELIX 179 179 SER I 179 GLY I 193 1 15
HELIX 180 180 GLY I 194 ALA I 201 1 8
HELIX 181 181 PRO I 202 TRP I 205 5 4
HELIX 182 182 ASP I 212 ILE I 216 5 5
HELIX 183 183 THR I 236 LEU I 244 1 9
HELIX 184 184 GLY I 258 HIS I 263 1 6
HELIX 185 185 HIS I 263 SER I 296 1 34
HELIX 186 186 GLY I 301 GLY I 317 1 17
HELIX 187 187 ASP I 321 THR I 331 1 11
HELIX 188 188 SER I 336 VAL I 351 1 16
HELIX 189 189 ARG I 360 ASN I 365 1 6
HELIX 190 190 ASP I 372 ARG I 388 1 17
HELIX 191 191 THR I 391 LEU I 400 1 10
HELIX 192 192 SER I 403 ASN I 416 1 14
HELIX 193 193 THR I 422 ALA I 438 1 17
HELIX 194 194 SER J 35 SER J 38 5 4
HELIX 195 195 TRP J 39 ALA J 49 1 11
HELIX 196 196 ASP J 72 ASP J 88 1 17
HELIX 197 197 SER J 98 GLY J 112 1 15
HELIX 198 198 PRO J 141 TYR J 168 1 28
HELIX 199 199 ASN J 169 LEU J 174 1 6
HELIX 200 200 SER J 179 GLY J 193 1 15
HELIX 201 201 GLY J 194 ALA J 201 1 8
HELIX 202 202 PRO J 202 TRP J 205 5 4
HELIX 203 203 ASP J 212 ILE J 216 5 5
HELIX 204 204 PRO J 232 LEU J 244 1 13
HELIX 205 205 GLY J 258 HIS J 263 1 6
HELIX 206 206 HIS J 263 SER J 296 1 34
HELIX 207 207 GLY J 301 GLY J 317 1 17
HELIX 208 208 ASP J 321 THR J 331 1 11
HELIX 209 209 SER J 336 VAL J 351 1 16
HELIX 210 210 ARG J 360 ASN J 365 1 6
HELIX 211 211 ASP J 372 ARG J 388 1 17
HELIX 212 212 THR J 391 LEU J 400 1 10
HELIX 213 213 SER J 403 ASN J 416 1 14
HELIX 214 214 THR J 422 SER J 440 1 19
HELIX 215 215 SER K 35 SER K 38 5 4
HELIX 216 216 TRP K 39 ALA K 49 1 11
HELIX 217 217 ASP K 72 ASP K 88 1 17
HELIX 218 218 MET K 99 GLY K 112 1 14
HELIX 219 219 PRO K 141 TYR K 168 1 28
HELIX 220 220 ASN K 169 LEU K 174 1 6
HELIX 221 221 SER K 179 GLY K 193 1 15
HELIX 222 222 GLY K 194 ALA K 201 1 8
HELIX 223 223 PRO K 202 TRP K 205 5 4
HELIX 224 224 ASP K 212 ILE K 216 5 5
HELIX 225 225 THR K 236 LEU K 244 1 9
HELIX 226 226 GLY K 258 HIS K 263 1 6
HELIX 227 227 HIS K 263 SER K 296 1 34
HELIX 228 228 GLY K 301 GLY K 317 1 17
HELIX 229 229 ASP K 321 THR K 331 1 11
HELIX 230 230 SER K 336 VAL K 351 1 16
HELIX 231 231 ARG K 360 ASN K 365 1 6
HELIX 232 232 ASP K 372 ARG K 388 1 17
HELIX 233 233 THR K 391 LEU K 400 1 10
HELIX 234 234 SER K 403 ASN K 416 1 14
HELIX 235 235 THR K 422 SER K 440 1 19
HELIX 236 236 SER L 35 SER L 38 5 4
HELIX 237 237 TRP L 39 ALA L 49 1 11
HELIX 238 238 ASP L 72 ASP L 88 1 17
HELIX 239 239 MET L 99 GLY L 112 1 14
HELIX 240 240 PRO L 141 ASP L 155 1 15
HELIX 241 241 ASP L 155 TYR L 168 1 14
HELIX 242 242 ASN L 169 LEU L 174 1 6
HELIX 243 243 SER L 179 GLY L 193 1 15
HELIX 244 244 GLY L 194 ALA L 201 1 8
HELIX 245 245 PRO L 202 TRP L 205 5 4
HELIX 246 246 ASP L 212 ILE L 216 5 5
HELIX 247 247 PRO L 232 LEU L 244 1 13
HELIX 248 248 GLY L 258 HIS L 263 1 6
HELIX 249 249 HIS L 263 SER L 296 1 34
HELIX 250 250 GLY L 301 GLY L 317 1 17
HELIX 251 251 ASP L 321 THR L 331 1 11
HELIX 252 252 SER L 336 VAL L 351 1 16
HELIX 253 253 ARG L 360 ASN L 365 1 6
HELIX 254 254 ASP L 372 ARG L 388 1 17
HELIX 255 255 THR L 391 LEU L 400 1 10
HELIX 256 256 SER L 403 ASN L 416 1 14
HELIX 257 257 THR L 422 ALA L 438 1 17
SHEET 1 A 8 PHE A 2 GLU A 8 0
SHEET 2 A 8 THR A 11 HIS A 20 -1 O ILE A 13 N VAL A 5
SHEET 3 A 8 ARG A 52 TYR A 56 -1 O VAL A 53 N HIS A 20
SHEET 4 A 8 PRO A 25 ILE A 29 1 N VAL A 26 O ARG A 52
SHEET 5 A 8 ALA A 92 PHE A 97 1 O VAL A 95 N VAL A 27
SHEET 6 A 8 ILE A 116 LEU A 122 1 O ALA A 117 N ALA A 92
SHEET 7 A 8 ALA A 220 GLY A 225 1 O LEU A 221 N PHE A 121
SHEET 8 A 8 GLU A 248 VAL A 252 1 O GLU A 248 N ILE A 222
SHEET 1 B 8 PHE B 2 GLU B 8 0
SHEET 2 B 8 THR B 11 ASP B 19 -1 O ILE B 13 N VAL B 5
SHEET 3 B 8 ARG B 52 TYR B 56 -1 O THR B 55 N GLU B 18
SHEET 4 B 8 PRO B 25 ILE B 29 1 N VAL B 26 O ARG B 52
SHEET 5 B 8 ALA B 92 PHE B 97 1 O VAL B 95 N VAL B 27
SHEET 6 B 8 ILE B 116 LEU B 122 1 O ALA B 117 N ALA B 92
SHEET 7 B 8 ALA B 220 GLY B 225 1 O LEU B 221 N PHE B 121
SHEET 8 B 8 GLU B 248 VAL B 252 1 O GLU B 248 N ILE B 222
SHEET 1 C 8 PHE C 2 GLU C 8 0
SHEET 2 C 8 THR C 11 HIS C 20 -1 O ILE C 13 N VAL C 5
SHEET 3 C 8 ARG C 52 TYR C 56 -1 O VAL C 53 N HIS C 20
SHEET 4 C 8 PRO C 25 ILE C 29 1 N VAL C 26 O ARG C 52
SHEET 5 C 8 ALA C 92 PHE C 97 1 O VAL C 95 N VAL C 27
SHEET 6 C 8 ILE C 116 LEU C 122 1 O ALA C 117 N ALA C 92
SHEET 7 C 8 ALA C 220 GLY C 225 1 O LEU C 221 N PHE C 121
SHEET 8 C 8 GLU C 248 VAL C 252 1 O GLU C 248 N ILE C 222
SHEET 1 D 8 PHE D 2 GLU D 8 0
SHEET 2 D 8 THR D 11 HIS D 20 -1 O ILE D 13 N VAL D 5
SHEET 3 D 8 ARG D 52 TYR D 56 -1 O VAL D 53 N HIS D 20
SHEET 4 D 8 PRO D 25 ILE D 29 1 N VAL D 26 O ARG D 52
SHEET 5 D 8 ALA D 92 PHE D 97 1 O VAL D 95 N VAL D 27
SHEET 6 D 8 ILE D 116 LEU D 122 1 O ALA D 117 N ALA D 92
SHEET 7 D 8 ALA D 220 GLY D 225 1 O LEU D 221 N PHE D 121
SHEET 8 D 8 GLU D 248 VAL D 252 1 O GLU D 248 N ILE D 222
SHEET 1 E 8 PHE E 2 GLU E 8 0
SHEET 2 E 8 THR E 11 ASP E 19 -1 O ILE E 13 N VAL E 5
SHEET 3 E 8 ARG E 52 TYR E 56 -1 O THR E 55 N GLU E 18
SHEET 4 E 8 PRO E 25 ILE E 29 1 N VAL E 26 O ARG E 52
SHEET 5 E 8 ALA E 92 PHE E 97 1 O VAL E 95 N VAL E 27
SHEET 6 E 8 ILE E 116 LEU E 122 1 O ALA E 117 N ALA E 92
SHEET 7 E 8 ALA E 220 GLY E 225 1 O LEU E 221 N PHE E 121
SHEET 8 E 8 GLU E 248 VAL E 252 1 O GLU E 248 N ILE E 222
SHEET 1 F 8 PHE F 2 GLU F 8 0
SHEET 2 F 8 THR F 11 ASP F 19 -1 O ILE F 13 N VAL F 5
SHEET 3 F 8 ARG F 52 TYR F 56 -1 O THR F 55 N GLU F 18
SHEET 4 F 8 PRO F 25 ILE F 29 1 N VAL F 26 O ARG F 52
SHEET 5 F 8 ALA F 92 PHE F 97 1 O VAL F 95 N ILE F 29
SHEET 6 F 8 ILE F 116 LEU F 122 1 O ALA F 117 N ALA F 92
SHEET 7 F 8 ALA F 220 GLY F 225 1 O LEU F 221 N PHE F 121
SHEET 8 F 8 GLU F 248 VAL F 252 1 O GLU F 248 N ILE F 222
SHEET 1 G 8 PHE G 2 GLN G 7 0
SHEET 2 G 8 SER G 12 ASP G 19 -1 O ILE G 13 N VAL G 5
SHEET 3 G 8 ARG G 52 TYR G 56 -1 O THR G 55 N GLU G 18
SHEET 4 G 8 PRO G 25 ILE G 29 1 N VAL G 26 O ARG G 52
SHEET 5 G 8 ALA G 92 PHE G 97 1 O VAL G 95 N ILE G 29
SHEET 6 G 8 ILE G 116 LEU G 122 1 O ALA G 117 N ALA G 92
SHEET 7 G 8 ALA G 220 GLY G 225 1 O LEU G 221 N PHE G 121
SHEET 8 G 8 GLU G 248 VAL G 252 1 O GLU G 248 N ILE G 222
SHEET 1 H 8 PHE H 2 GLU H 8 0
SHEET 2 H 8 THR H 11 HIS H 20 -1 O ILE H 13 N VAL H 5
SHEET 3 H 8 ARG H 52 TYR H 56 -1 O THR H 55 N GLU H 18
SHEET 4 H 8 PRO H 25 ILE H 29 1 N VAL H 26 O ARG H 52
SHEET 5 H 8 ALA H 92 PHE H 97 1 O VAL H 95 N VAL H 27
SHEET 6 H 8 ILE H 116 LEU H 122 1 O ALA H 117 N ALA H 92
SHEET 7 H 8 ALA H 220 GLY H 225 1 O LEU H 221 N PHE H 121
SHEET 8 H 8 GLU H 248 VAL H 252 1 O GLU H 248 N ILE H 222
SHEET 1 I 8 PHE I 2 GLN I 7 0
SHEET 2 I 8 SER I 12 HIS I 20 -1 O ILE I 13 N VAL I 5
SHEET 3 I 8 ARG I 52 TYR I 56 -1 O VAL I 53 N HIS I 20
SHEET 4 I 8 PRO I 25 ILE I 29 1 N VAL I 26 O ARG I 52
SHEET 5 I 8 ALA I 92 PHE I 97 1 O VAL I 95 N VAL I 27
SHEET 6 I 8 ILE I 116 LEU I 122 1 O ALA I 117 N ALA I 92
SHEET 7 I 8 ALA I 220 GLY I 225 1 O LEU I 221 N PHE I 121
SHEET 8 I 8 GLU I 248 VAL I 252 1 O GLU I 248 N ILE I 222
SHEET 1 J 8 PHE J 2 GLU J 8 0
SHEET 2 J 8 THR J 11 ASP J 19 -1 O ILE J 13 N VAL J 5
SHEET 3 J 8 ARG J 52 TYR J 56 -1 O THR J 55 N GLU J 18
SHEET 4 J 8 PRO J 25 ILE J 29 1 N VAL J 26 O ARG J 52
SHEET 5 J 8 ALA J 92 PHE J 97 1 O VAL J 95 N VAL J 27
SHEET 6 J 8 ILE J 116 LEU J 122 1 O ALA J 117 N ALA J 92
SHEET 7 J 8 ALA J 220 GLY J 225 1 O LEU J 221 N PHE J 121
SHEET 8 J 8 GLU J 248 VAL J 252 1 O GLU J 248 N ILE J 222
SHEET 1 K 8 PHE K 2 GLN K 7 0
SHEET 2 K 8 SER K 12 HIS K 20 -1 O ILE K 13 N VAL K 5
SHEET 3 K 8 ARG K 52 TYR K 56 -1 O THR K 55 N GLU K 18
SHEET 4 K 8 PRO K 25 ILE K 29 1 N VAL K 26 O ARG K 52
SHEET 5 K 8 ALA K 92 PHE K 97 1 O VAL K 95 N VAL K 27
SHEET 6 K 8 ILE K 116 LEU K 122 1 O ALA K 117 N ALA K 92
SHEET 7 K 8 ALA K 220 GLY K 225 1 O LEU K 221 N PHE K 121
SHEET 8 K 8 GLU K 248 VAL K 252 1 O GLU K 248 N ILE K 222
SHEET 1 L 8 PHE L 2 GLN L 7 0
SHEET 2 L 8 SER L 12 HIS L 20 -1 O ILE L 13 N VAL L 5
SHEET 3 L 8 ARG L 52 TYR L 56 -1 O THR L 55 N GLU L 18
SHEET 4 L 8 PRO L 25 ILE L 29 1 N VAL L 26 O ARG L 52
SHEET 5 L 8 ALA L 92 PHE L 97 1 O VAL L 95 N ILE L 29
SHEET 6 L 8 ILE L 116 LEU L 122 1 O ALA L 117 N ALA L 92
SHEET 7 L 8 ALA L 220 GLY L 225 1 O LEU L 221 N PHE L 121
SHEET 8 L 8 GLU L 248 VAL L 252 1 O GLU L 248 N ILE L 222
CISPEP 1 PHE A 32 PRO A 33 0 -5.89
CISPEP 2 GLU A 126 PRO A 127 0 -2.96
CISPEP 3 PHE B 32 PRO B 33 0 -6.34
CISPEP 4 GLU B 126 PRO B 127 0 -3.51
CISPEP 5 PHE C 32 PRO C 33 0 -5.82
CISPEP 6 GLU C 126 PRO C 127 0 -3.52
CISPEP 7 PHE D 32 PRO D 33 0 -6.23
CISPEP 8 GLU D 126 PRO D 127 0 -3.44
CISPEP 9 PHE E 32 PRO E 33 0 -5.85
CISPEP 10 GLU E 126 PRO E 127 0 -3.28
CISPEP 11 PHE F 32 PRO F 33 0 -5.82
CISPEP 12 GLU F 126 PRO F 127 0 -3.54
CISPEP 13 PHE G 32 PRO G 33 0 -6.01
CISPEP 14 GLU G 126 PRO G 127 0 -3.97
CISPEP 15 PHE H 32 PRO H 33 0 -5.64
CISPEP 16 GLU H 126 PRO H 127 0 -3.10
CISPEP 17 PHE I 32 PRO I 33 0 -5.82
CISPEP 18 GLU I 126 PRO I 127 0 -2.87
CISPEP 19 PHE J 32 PRO J 33 0 -5.39
CISPEP 20 GLU J 126 PRO J 127 0 -3.12
CISPEP 21 PHE K 32 PRO K 33 0 -5.94
CISPEP 22 GLU K 126 PRO K 127 0 -3.33
CISPEP 23 PHE L 32 PRO L 33 0 -6.01
CISPEP 24 GLU L 126 PRO L 127 0 -3.21
CRYST1 131.620 156.610 321.150 90.00 90.00 90.00 P 21 21 21 48
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 0.007598 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006385 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003114 0.00000
TER 3399 SER A 440
TER 6798 SER B 440
TER 10197 SER C 440
TER 13596 SER D 440
TER 16995 SER E 440
TER 20394 SER F 440
TER 23793 SER G 440
TER 27192 SER H 440
TER 30591 SER I 440
TER 33990 SER J 440
TER 37389 SER K 440
TER 40788 SER L 440
MASTER 854 0 0 257 96 0 0 640776 12 0 432
END |