HEADER IMMUNE SYSTEM 26-NOV-11 3UTT
TITLE 1E6-A*0201-ALWGPDPAAA COMPLEX, TRICLINIC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-2 ALPHA CHAIN;
COMPND 3 CHAIN: A, F;
COMPND 4 FRAGMENT: UNP RESIDUES 25-299;
COMPND 5 SYNONYM: MHC CLASS I HEAVY CHAIN, MHC CLASS I ANTIGEN A*2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 9 CHAIN: B, G;
COMPND 10 FRAGMENT: UNP RESIDUES 21-119;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: INSULIN;
COMPND 14 CHAIN: C, H;
COMPND 15 FRAGMENT: PRE-PRO-INSULIN DERIVED PEPTIDE (UNP RESIDUES 15-24);
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: 1E6 TCR ALPHA CHAIN;
COMPND 19 CHAIN: D, I;
COMPND 20 ENGINEERED: YES;
COMPND 21 MOL_ID: 5;
COMPND 22 MOLECULE: 1E6 TCR BETA CHAIN;
COMPND 23 CHAIN: E, J;
COMPND 24 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: HLA-A, HLAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA DE3;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: B2M, CDABP0092, HDCMA22P;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: ROSETTA DE3;
SOURCE 17 MOL_ID: 3;
SOURCE 18 SYNTHETIC: YES;
SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 20 ORGANISM_COMMON: HUMAN;
SOURCE 21 ORGANISM_TAXID: 9606;
SOURCE 22 MOL_ID: 4;
SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 24 ORGANISM_COMMON: HUMAN;
SOURCE 25 ORGANISM_TAXID: 9606;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 28 EXPRESSION_SYSTEM_STRAIN: ROSETTA DE3;
SOURCE 29 MOL_ID: 5;
SOURCE 30 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 31 ORGANISM_COMMON: HUMAN;
SOURCE 32 ORGANISM_TAXID: 9606;
SOURCE 33 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 34 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 35 EXPRESSION_SYSTEM_STRAIN: ROSETTA DE3
KEYWDS MAJOR HISTOCOMPATIBILITY COMPLEX, HUMAN LEUKOCYTE ANTIGEN, TYPE I
KEYWDS 2 DIABETES, T CELL RECEPTOR, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.RIZKALLAH,D.K.COLE,A.K.SEWELL,A.M.BULEK,J.ROSSJOHN,S.GRAS
REVDAT 3 17-JUL-19 3UTT 1 REMARK
REVDAT 2 07-MAR-12 3UTT 1 JRNL
REVDAT 1 25-JAN-12 3UTT 0
JRNL AUTH A.M.BULEK,D.K.COLE,A.SKOWERA,G.DOLTON,S.GRAS,F.MADURA,
JRNL AUTH 2 A.FULLER,J.J.MILES,E.GOSTICK,D.A.PRICE,J.W.DRIJFHOUT,
JRNL AUTH 3 R.R.KNIGHT,G.C.HUANG,N.LISSIN,P.E.MOLLOY,L.WOOLDRIDGE,
JRNL AUTH 4 B.K.JAKOBSEN,J.ROSSJOHN,M.PEAKMAN,P.J.RIZKALLAH,A.K.SEWELL
JRNL TITL STRUCTURAL BASIS FOR THE KILLING OF HUMAN BETA CELLS BY
JRNL TITL 2 CD8(+) T CELLS IN TYPE 1 DIABETES.
JRNL REF NAT.IMMUNOL. V. 13 283 2012
JRNL REFN ISSN 1529-2908
JRNL PMID 22245737
JRNL DOI 10.1038/NI.2206
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.1_357
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.34
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.010
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.9
REMARK 3 NUMBER OF REFLECTIONS : 51877
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2634
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 29.3382 - 5.5896 0.97 5364 256 0.1752 0.2293
REMARK 3 2 5.5896 - 4.4416 0.97 5286 300 0.1398 0.2080
REMARK 3 3 4.4416 - 3.8816 0.96 5260 287 0.1447 0.2255
REMARK 3 4 3.8816 - 3.5274 0.95 5190 287 0.1781 0.2660
REMARK 3 5 3.5274 - 3.2749 0.94 5080 298 0.2049 0.3147
REMARK 3 6 3.2749 - 3.0820 0.91 5013 291 0.2274 0.3057
REMARK 3 7 3.0820 - 2.9278 0.88 4810 247 0.2387 0.3499
REMARK 3 8 2.9278 - 2.8005 0.85 4625 231 0.2740 0.3773
REMARK 3 9 2.8005 - 2.6927 0.80 4469 220 0.2720 0.3471
REMARK 3 10 2.6927 - 2.5999 0.77 4146 217 0.2845 0.3788
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 : 0.33
REMARK 3 B_SOL : 30.40
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.200
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 12.30580
REMARK 3 B22 (A**2) : 0.79600
REMARK 3 B33 (A**2) : -13.10170
REMARK 3 B12 (A**2) : 4.88570
REMARK 3 B13 (A**2) : 3.96990
REMARK 3 B23 (A**2) : -1.50350
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 13795
REMARK 3 ANGLE : 0.671 18707
REMARK 3 CHIRALITY : 0.048 1937
REMARK 3 PLANARITY : 0.004 2457
REMARK 3 DIHEDRAL : 11.956 5051
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 22
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 1:181)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0801 7.3159 -7.9497
REMARK 3 T TENSOR
REMARK 3 T11: -0.0566 T22: 0.2798
REMARK 3 T33: 0.1495 T12: -0.0382
REMARK 3 T13: -0.0890 T23: -0.0402
REMARK 3 L TENSOR
REMARK 3 L11: 1.0618 L22: 1.1514
REMARK 3 L33: 1.6051 L12: -0.7412
REMARK 3 L13: 0.6515 L23: -0.9323
REMARK 3 S TENSOR
REMARK 3 S11: -0.1907 S12: -0.0687 S13: 0.0665
REMARK 3 S21: 0.5648 S22: 0.1262 S23: 0.1061
REMARK 3 S31: -0.2773 S32: 0.2361 S33: 0.0485
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 182:275)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8667 0.7418 26.4945
REMARK 3 T TENSOR
REMARK 3 T11: 0.3956 T22: 0.3344
REMARK 3 T33: 0.0722 T12: -0.1054
REMARK 3 T13: -0.0772 T23: -0.0422
REMARK 3 L TENSOR
REMARK 3 L11: 0.5608 L22: 0.5765
REMARK 3 L33: 0.6940 L12: 0.4757
REMARK 3 L13: 0.1187 L23: 0.1824
REMARK 3 S TENSOR
REMARK 3 S11: 0.2720 S12: 0.0855 S13: -0.0154
REMARK 3 S21: 0.5759 S22: -0.1330 S23: 0.0404
REMARK 3 S31: 0.2227 S32: -0.0318 S33: 0.0123
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN B AND RESID 0:42)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.9140 -10.8060 8.1687
REMARK 3 T TENSOR
REMARK 3 T11: 0.1635 T22: 0.2463
REMARK 3 T33: 0.0960 T12: -0.0922
REMARK 3 T13: 0.0468 T23: 0.0857
REMARK 3 L TENSOR
REMARK 3 L11: 0.6182 L22: 0.5823
REMARK 3 L33: 1.6839 L12: -0.0594
REMARK 3 L13: -0.0903 L23: 0.2757
REMARK 3 S TENSOR
REMARK 3 S11: -0.0522 S12: -0.0925 S13: 0.0508
REMARK 3 S21: 0.3960 S22: 0.1208 S23: 0.0500
REMARK 3 S31: 1.0366 S32: -0.1656 S33: -0.0111
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESID 43:99)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8067 -13.0138 7.4028
REMARK 3 T TENSOR
REMARK 3 T11: 0.2375 T22: 0.2746
REMARK 3 T33: 0.0997 T12: -0.0338
REMARK 3 T13: 0.0620 T23: 0.0280
REMARK 3 L TENSOR
REMARK 3 L11: 0.4458 L22: 0.4319
REMARK 3 L33: 1.2205 L12: -0.0550
REMARK 3 L13: -0.1423 L23: 0.2933
REMARK 3 S TENSOR
REMARK 3 S11: -0.1409 S12: -0.2320 S13: -0.1103
REMARK 3 S21: 0.3895 S22: -0.0573 S23: -0.0390
REMARK 3 S31: 0.9467 S32: 0.1787 S33: -0.0031
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN C AND RESID 1:10)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7756 10.2431 -15.1681
REMARK 3 T TENSOR
REMARK 3 T11: -0.1225 T22: 0.4148
REMARK 3 T33: 0.2795 T12: 0.0873
REMARK 3 T13: -0.0970 T23: 0.0831
REMARK 3 L TENSOR
REMARK 3 L11: 0.0610 L22: 0.5678
REMARK 3 L33: 0.4867 L12: -0.1407
REMARK 3 L13: 0.0019 L23: -0.3284
REMARK 3 S TENSOR
REMARK 3 S11: -0.1808 S12: 0.0030 S13: 0.0753
REMARK 3 S21: 0.1263 S22: -0.4469 S23: -0.2693
REMARK 3 S31: -0.0628 S32: 0.7529 S33: -0.0999
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN D AND RESID 3:109)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6400 30.7149 -31.7865
REMARK 3 T TENSOR
REMARK 3 T11: 0.5710 T22: -0.0099
REMARK 3 T33: 0.2892 T12: -0.0258
REMARK 3 T13: 0.1192 T23: 0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 0.1640 L22: 0.9805
REMARK 3 L33: 0.3704 L12: 0.1005
REMARK 3 L13: 0.2913 L23: -0.0634
REMARK 3 S TENSOR
REMARK 3 S11: -0.1341 S12: 0.0313 S13: -0.1326
REMARK 3 S21: -0.0588 S22: 0.1697 S23: -0.0584
REMARK 3 S31: -0.7797 S32: -0.2311 S33: 0.0519
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN D AND RESID 110:176)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.4775 38.1922 -62.8503
REMARK 3 T TENSOR
REMARK 3 T11: 2.1692 T22: 0.0600
REMARK 3 T33: 0.2997 T12: -0.3140
REMARK 3 T13: 0.0663 T23: -0.0713
REMARK 3 L TENSOR
REMARK 3 L11: 0.0783 L22: 0.4468
REMARK 3 L33: 1.4059 L12: -0.1946
REMARK 3 L13: -0.2456 L23: 0.4797
REMARK 3 S TENSOR
REMARK 3 S11: -0.1294 S12: 0.1209 S13: 0.0244
REMARK 3 S21: -0.9900 S22: 0.2288 S23: -0.0430
REMARK 3 S31: -0.2783 S32: 0.5057 S33: -0.0514
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN D AND RESID 177:199)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.4643 46.0918 -67.2639
REMARK 3 T TENSOR
REMARK 3 T11: 1.8903 T22: 0.1124
REMARK 3 T33: 0.6251 T12: -0.3032
REMARK 3 T13: -0.2894 T23: 0.0740
REMARK 3 L TENSOR
REMARK 3 L11: 1.4925 L22: 0.3009
REMARK 3 L33: 0.6165 L12: 0.0721
REMARK 3 L13: -0.2981 L23: 0.2428
REMARK 3 S TENSOR
REMARK 3 S11: 0.3723 S12: -0.3608 S13: 0.4321
REMARK 3 S21: -0.0919 S22: 0.3376 S23: 0.1673
REMARK 3 S31: -0.1512 S32: -0.1759 S33: 0.0037
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN E AND RESID 3:118)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.8340 9.5917 -38.9540
REMARK 3 T TENSOR
REMARK 3 T11: -0.1622 T22: 0.0079
REMARK 3 T33: 0.1960 T12: -0.1711
REMARK 3 T13: -0.0373 T23: 0.0276
REMARK 3 L TENSOR
REMARK 3 L11: 0.8288 L22: 0.1490
REMARK 3 L33: 1.7631 L12: 0.0341
REMARK 3 L13: -0.2505 L23: 0.1907
REMARK 3 S TENSOR
REMARK 3 S11: 0.1808 S12: 0.3369 S13: -0.1623
REMARK 3 S21: -0.1823 S22: 0.0007 S23: 0.1027
REMARK 3 S31: -0.6607 S32: -0.2079 S33: 0.0410
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN E AND RESID 119:201)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7902 26.9079 -64.1769
REMARK 3 T TENSOR
REMARK 3 T11: 1.2401 T22: 0.1421
REMARK 3 T33: 0.1461 T12: -0.1230
REMARK 3 T13: 0.2787 T23: 0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 0.5426 L22: 0.4590
REMARK 3 L33: 0.7372 L12: 0.3972
REMARK 3 L13: 0.2077 L23: 0.3514
REMARK 3 S TENSOR
REMARK 3 S11: 0.3623 S12: 0.1794 S13: 0.1492
REMARK 3 S21: -0.1977 S22: 0.1984 S23: 0.0178
REMARK 3 S31: -1.4041 S32: 0.1472 S33: 0.0445
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN E AND RESID 202:244)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5077 15.5320 -68.2193
REMARK 3 T TENSOR
REMARK 3 T11: 0.6140 T22: 0.1722
REMARK 3 T33: 0.2518 T12: -0.1494
REMARK 3 T13: 0.2500 T23: -0.1346
REMARK 3 L TENSOR
REMARK 3 L11: 0.6312 L22: 0.7188
REMARK 3 L33: 1.2666 L12: -0.4468
REMARK 3 L13: 0.0519 L23: 0.2418
REMARK 3 S TENSOR
REMARK 3 S11: 0.1309 S12: 0.3413 S13: -0.3321
REMARK 3 S21: -0.3926 S22: 0.4428 S23: -0.2556
REMARK 3 S31: -1.3460 S32: 0.0314 S33: 0.0539
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN F AND RESID 1:181)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.1665 -20.5905 -54.7557
REMARK 3 T TENSOR
REMARK 3 T11: -0.3337 T22: 0.0362
REMARK 3 T33: 0.1321 T12: 0.1703
REMARK 3 T13: -0.0616 T23: 0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 0.6654 L22: 1.0649
REMARK 3 L33: 1.0244 L12: 0.6909
REMARK 3 L13: -0.2792 L23: -0.4773
REMARK 3 S TENSOR
REMARK 3 S11: -0.4104 S12: -0.0261 S13: -0.0858
REMARK 3 S21: -0.6732 S22: 0.1475 S23: -0.2311
REMARK 3 S31: 0.9677 S32: -0.0235 S33: -0.3315
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN F AND RESID 182:275)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.9000 -13.6209 -89.3465
REMARK 3 T TENSOR
REMARK 3 T11: 0.2388 T22: 0.3448
REMARK 3 T33: 0.1496 T12: 0.0409
REMARK 3 T13: 0.1002 T23: 0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 0.2497 L22: 0.2379
REMARK 3 L33: 0.7364 L12: -0.0537
REMARK 3 L13: 0.0467 L23: 0.2516
REMARK 3 S TENSOR
REMARK 3 S11: -0.1701 S12: -0.1073 S13: 0.2164
REMARK 3 S21: -0.3084 S22: 0.1998 S23: -0.1352
REMARK 3 S31: 0.3538 S32: 0.2673 S33: 0.0001
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN G AND RESID 0:37)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4930 -5.3309 -73.2019
REMARK 3 T TENSOR
REMARK 3 T11: 0.0185 T22: 0.1689
REMARK 3 T33: 0.1725 T12: 0.0103
REMARK 3 T13: -0.0231 T23: 0.0599
REMARK 3 L TENSOR
REMARK 3 L11: 0.6670 L22: 0.4426
REMARK 3 L33: 1.7117 L12: 0.0845
REMARK 3 L13: -0.0685 L23: 0.1911
REMARK 3 S TENSOR
REMARK 3 S11: 0.2151 S12: 0.1451 S13: -0.2115
REMARK 3 S21: -0.0493 S22: 0.1145 S23: 0.0030
REMARK 3 S31: -0.2072 S32: -0.1327 S33: 0.0212
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN G AND RESID 38:99)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5223 -1.9976 -73.4476
REMARK 3 T TENSOR
REMARK 3 T11: 0.1539 T22: 0.1430
REMARK 3 T33: 0.1160 T12: 0.0430
REMARK 3 T13: 0.0044 T23: 0.0458
REMARK 3 L TENSOR
REMARK 3 L11: 0.6216 L22: 0.5633
REMARK 3 L33: 0.7491 L12: -0.0035
REMARK 3 L13: 0.0488 L23: -0.1573
REMARK 3 S TENSOR
REMARK 3 S11: -0.1155 S12: 0.1760 S13: -0.0272
REMARK 3 S21: -0.0125 S22: -0.0352 S23: 0.0049
REMARK 3 S31: -0.3250 S32: -0.0544 S33: -0.0004
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN H AND RESID 1:10)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.1179 -23.3691 -47.4896
REMARK 3 T TENSOR
REMARK 3 T11: -0.0041 T22: 0.1639
REMARK 3 T33: 0.1854 T12: -0.2313
REMARK 3 T13: -0.1532 T23: -0.1291
REMARK 3 L TENSOR
REMARK 3 L11: 0.2079 L22: 4.7266
REMARK 3 L33: 0.2799 L12: 0.7297
REMARK 3 L13: -0.1614 L23: 0.0455
REMARK 3 S TENSOR
REMARK 3 S11: 0.0175 S12: -0.2900 S13: 0.1763
REMARK 3 S21: -0.1837 S22: -0.7717 S23: -0.0594
REMARK 3 S31: 0.0504 S32: -0.2666 S33: -0.2650
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN I AND RESID 3:109)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7804 -44.2500 -31.3694
REMARK 3 T TENSOR
REMARK 3 T11: 0.4997 T22: -0.2552
REMARK 3 T33: 0.1394 T12: -0.1150
REMARK 3 T13: -0.0192 T23: -0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 0.3751 L22: 0.9778
REMARK 3 L33: 1.4216 L12: -0.4037
REMARK 3 L13: -0.0733 L23: -0.3892
REMARK 3 S TENSOR
REMARK 3 S11: -0.5454 S12: -0.4147 S13: 0.0921
REMARK 3 S21: 0.1345 S22: 0.4009 S23: -0.0549
REMARK 3 S31: 0.9771 S32: -0.7028 S33: -0.0132
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN I AND RESID 110:170)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0275 -52.3791 -1.6814
REMARK 3 T TENSOR
REMARK 3 T11: 1.3889 T22: 0.4618
REMARK 3 T33: 0.5044 T12: 0.1494
REMARK 3 T13: 0.2384 T23: -0.1025
REMARK 3 L TENSOR
REMARK 3 L11: 0.1352 L22: 0.1705
REMARK 3 L33: 0.1127 L12: -0.1409
REMARK 3 L13: 0.0599 L23: -0.0292
REMARK 3 S TENSOR
REMARK 3 S11: -0.1648 S12: -0.1460 S13: -0.0435
REMARK 3 S21: 0.4665 S22: 0.3649 S23: 0.3719
REMARK 3 S31: -0.2003 S32: 0.3076 S33: -0.0001
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN I AND RESID 171:199)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7858 -59.2096 0.8830
REMARK 3 T TENSOR
REMARK 3 T11: 1.1379 T22: 0.3704
REMARK 3 T33: 0.7231 T12: 0.1098
REMARK 3 T13: 0.2203 T23: 0.0515
REMARK 3 L TENSOR
REMARK 3 L11: 0.0570 L22: 0.0442
REMARK 3 L33: 0.0249 L12: 0.0340
REMARK 3 L13: -0.0361 L23: -0.0424
REMARK 3 S TENSOR
REMARK 3 S11: -0.2889 S12: 0.3058 S13: -0.3515
REMARK 3 S21: -0.1884 S22: 0.5554 S23: -0.1308
REMARK 3 S31: 0.4206 S32: 0.1198 S33: -0.0003
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN J AND RESID 2:115)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5508 -25.0110 -27.9148
REMARK 3 T TENSOR
REMARK 3 T11: 0.0588 T22: 0.3465
REMARK 3 T33: 0.1427 T12: 0.0880
REMARK 3 T13: -0.0300 T23: -0.0237
REMARK 3 L TENSOR
REMARK 3 L11: 0.6141 L22: 0.3594
REMARK 3 L33: 1.6145 L12: 0.3274
REMARK 3 L13: -0.0954 L23: 0.3646
REMARK 3 S TENSOR
REMARK 3 S11: -0.0161 S12: -0.3702 S13: 0.2004
REMARK 3 S21: -0.0609 S22: -0.1722 S23: 0.1113
REMARK 3 S31: -0.2053 S32: -0.4689 S33: 0.0008
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN J AND RESID 116:204)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2241 -41.0261 -0.5981
REMARK 3 T TENSOR
REMARK 3 T11: 0.6570 T22: 0.3705
REMARK 3 T33: 0.1694 T12: 0.1705
REMARK 3 T13: 0.0444 T23: -0.0631
REMARK 3 L TENSOR
REMARK 3 L11: 0.5759 L22: 0.7443
REMARK 3 L33: 0.5764 L12: -0.6092
REMARK 3 L13: -0.3562 L23: 0.2592
REMARK 3 S TENSOR
REMARK 3 S11: 0.0649 S12: 0.1115 S13: -0.0510
REMARK 3 S21: 0.1783 S22: 0.0359 S23: 0.0145
REMARK 3 S31: 1.0740 S32: 0.1896 S33: 0.0011
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN J AND RESID 205:244)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.3728 -30.0551 1.4428
REMARK 3 T TENSOR
REMARK 3 T11: 0.3069 T22: 0.4838
REMARK 3 T33: 0.0741 T12: 0.1169
REMARK 3 T13: 0.0596 T23: -0.0534
REMARK 3 L TENSOR
REMARK 3 L11: 0.5126 L22: 0.9346
REMARK 3 L33: 1.4666 L12: -0.3067
REMARK 3 L13: 0.1006 L23: 0.3059
REMARK 3 S TENSOR
REMARK 3 S11: -0.3632 S12: -0.2505 S13: 0.2538
REMARK 3 S21: 0.4329 S22: 0.4941 S23: -0.1774
REMARK 3 S31: 0.9278 S32: -0.0622 S33: 0.0443
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 3UTT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-DEC-11.
REMARK 100 THE DEPOSITION ID IS D_1000069199.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 0.9778
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61204
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.579
REMARK 200 RESOLUTION RANGE LOW (A) : 47.925
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 2.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.73600
REMARK 200 R SYM FOR SHELL (I) : 0.73600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% W/V PEG3350, 0.2 M SODIUM CITRATE,
REMARK 280 0.1 M BIS-TRIS PROPANE, PH 6.5, VAPOR DIFFUSION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: PENTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G, H, 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 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 ALA E 2
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 ASP A 29 -109.50 53.89
REMARK 500 ASN A 86 76.20 47.02
REMARK 500 LEU A 110 -83.62 -85.91
REMARK 500 TYR A 123 -67.83 -101.33
REMARK 500 ARG A 131 -27.67 -142.72
REMARK 500 TRP A 133 -143.79 -138.99
REMARK 500 ASP A 137 -166.90 -167.08
REMARK 500 ALA A 193 79.86 -69.98
REMARK 500 SER A 195 -135.40 -151.77
REMARK 500 GLU A 212 109.79 -57.96
REMARK 500 LEU A 230 113.17 -167.48
REMARK 500 ASP A 238 17.53 -145.86
REMARK 500 LYS A 243 110.93 -178.41
REMARK 500 TRP A 274 -163.98 87.20
REMARK 500 HIS B 31 135.90 172.88
REMARK 500 SER B 57 -168.40 -116.12
REMARK 500 TRP B 60 -8.91 70.59
REMARK 500 PRO B 90 113.95 -39.43
REMARK 500 ASP B 98 33.91 -91.97
REMARK 500 ASP C 6 167.71 163.94
REMARK 500 ALA C 8 53.48 72.11
REMARK 500 LEU D 11 116.39 45.58
REMARK 500 ASN D 27 102.69 175.66
REMARK 500 SER D 28 -164.25 -59.49
REMARK 500 ALA D 29 -42.23 76.76
REMARK 500 PHE D 30 108.18 -46.99
REMARK 500 SER D 40 -104.93 43.04
REMARK 500 LEU D 47 -66.90 -108.75
REMARK 500 SER D 52 -179.31 -175.02
REMARK 500 SER D 53 141.72 -39.51
REMARK 500 SER D 82 -120.15 -52.98
REMARK 500 ASP D 83 -46.07 57.33
REMARK 500 ALA D 85 177.82 173.64
REMARK 500 ARG D 92 -163.40 -172.91
REMARK 500 ASP D 94 -92.98 51.69
REMARK 500 LYS D 98 106.24 -46.99
REMARK 500 ASN D 115 79.99 -150.16
REMARK 500 ARG D 124 106.43 -49.86
REMARK 500 SER D 141 41.01 -76.43
REMARK 500 GLN D 147 -150.46 -73.44
REMARK 500 LYS D 149 -75.76 -70.76
REMARK 500 ASP D 152 23.32 -76.74
REMARK 500 ARG D 164 -169.58 56.56
REMARK 500 SER D 165 -90.36 42.46
REMARK 500 MET D 166 92.51 -64.22
REMARK 500 ASP D 167 64.22 -63.00
REMARK 500 SER D 177 151.02 175.62
REMARK 500 PHE D 188 62.59 -109.68
REMARK 500 ILE D 192 71.87 -68.92
REMARK 500 ASN E 51 62.08 63.20
REMARK 500
REMARK 500 THIS ENTRY HAS 119 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UTP RELATED DB: PDB
REMARK 900 1E6 TCR SPECIFIC FOR HLA-A*0201-ALWGPDPAAA
REMARK 900 RELATED ID: 3UTQ RELATED DB: PDB
REMARK 900 HUMAN HLA-A*0201-ALWGPDPAAA
REMARK 900 RELATED ID: 3UTS RELATED DB: PDB
REMARK 900 1E6-A*0201-ALWGPDPAAA COMPLEX, MONOCLINIC
DBREF 3UTT A 1 275 UNP P01892 1A02_HUMAN 25 299
DBREF 3UTT B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 3UTT C 1 10 UNP P01308 INS_HUMAN 15 24
DBREF 3UTT F 1 275 UNP P01892 1A02_HUMAN 25 299
DBREF 3UTT G 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 3UTT H 1 10 UNP P01308 INS_HUMAN 15 24
DBREF 3UTT D 3 201 PDB 3UTT 3UTT 3 201
DBREF 3UTT I 3 201 PDB 3UTT 3UTT 3 201
DBREF 3UTT E 2 246 PDB 3UTT 3UTT 2 246
DBREF 3UTT J 2 246 PDB 3UTT 3UTT 2 246
SEQADV 3UTT MET B 0 UNP P61769 INITIATING METHIONINE
SEQADV 3UTT MET G 0 UNP P61769 INITIATING METHIONINE
SEQRES 1 A 275 GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SER
SEQRES 2 A 275 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY
SEQRES 3 A 275 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 A 275 ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE
SEQRES 5 A 275 GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR ARG
SEQRES 6 A 275 LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP LEU
SEQRES 7 A 275 GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY
SEQRES 8 A 275 SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL GLY
SEQRES 9 A 275 SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR ALA
SEQRES 10 A 275 TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP LEU
SEQRES 11 A 275 ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR THR
SEQRES 12 A 275 LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN LEU
SEQRES 13 A 275 ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG
SEQRES 14 A 275 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR
SEQRES 15 A 275 ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SER
SEQRES 16 A 275 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER PHE
SEQRES 17 A 275 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY
SEQRES 18 A 275 GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG
SEQRES 19 A 275 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 A 275 VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS HIS
SEQRES 21 A 275 VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG
SEQRES 22 A 275 TRP GLU
SEQRES 1 B 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 B 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 B 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 B 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 B 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 B 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 B 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 B 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 C 10 ALA LEU TRP GLY PRO ASP PRO ALA ALA ALA
SEQRES 1 D 199 GLU VAL GLU GLN ASP PRO GLY PRO LEU SER VAL PRO GLU
SEQRES 2 D 199 GLY ALA ILE VAL SER LEU ASN CYS THR TYR SER ASN SER
SEQRES 3 D 199 ALA PHE GLN TYR PHE MET TRP TYR ARG GLN TYR SER ARG
SEQRES 4 D 199 LYS GLY PRO GLU LEU LEU MET TYR THR TYR SER SER GLY
SEQRES 5 D 199 ASN LYS GLU ASP GLY ARG PHE THR ALA GLN VAL ASP LYS
SEQRES 6 D 199 SER SER LYS TYR ILE SER LEU PHE ILE ARG ASP SER GLN
SEQRES 7 D 199 PRO SER ASP SER ALA THR TYR LEU CYS ALA MET ARG GLY
SEQRES 8 D 199 ASP SER SER TYR LYS LEU ILE PHE GLY SER GLY THR ARG
SEQRES 9 D 199 LEU LEU VAL ARG PRO ASP ILE GLN ASN PRO ASP PRO ALA
SEQRES 10 D 199 VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS SER
SEQRES 11 D 199 VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN VAL
SEQRES 12 D 199 SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP LYS
SEQRES 13 D 199 CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER ASN
SEQRES 14 D 199 SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA CYS
SEQRES 15 D 199 ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP THR
SEQRES 16 D 199 PHE PHE PRO SER
SEQRES 1 E 245 ALA GLY VAL ILE GLN SER PRO ARG HIS GLU VAL THR GLU
SEQRES 2 E 245 MET GLY GLN GLN VAL THR LEU ARG CYS LYS PRO ILE SER
SEQRES 3 E 245 GLY HIS ASP TYR LEU PHE TRP TYR ARG GLN THR MET MET
SEQRES 4 E 245 ARG GLY LEU GLU LEU LEU ILE TYR PHE ASN ASN ASN VAL
SEQRES 5 E 245 PRO ILE ASP ASP SER GLY MET PRO GLU ASP ARG PHE SER
SEQRES 6 E 245 ALA LYS MET PRO ASN ALA SER PHE SER THR LEU LYS ILE
SEQRES 7 E 245 GLN PRO SER GLU PRO ARG ASP SER ALA VAL TYR PHE CYS
SEQRES 8 E 245 ALA SER SER LEU TRP GLU LYS LEU ALA LYS ASN ILE GLN
SEQRES 9 E 245 TYR PHE GLY ALA GLY THR ARG LEU SER VAL LEU GLU ASP
SEQRES 10 E 245 LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU
SEQRES 11 E 245 PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR
SEQRES 12 E 245 LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL
SEQRES 13 E 245 GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER
SEQRES 14 E 245 GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO
SEQRES 15 E 245 ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU
SEQRES 16 E 245 ARG VAL SER ALA THR PHE TRP GLN ASP PRO ARG ASN HIS
SEQRES 17 E 245 PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN
SEQRES 18 E 245 ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN
SEQRES 19 E 245 ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP
SEQRES 1 F 275 GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SER
SEQRES 2 F 275 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY
SEQRES 3 F 275 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 F 275 ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE
SEQRES 5 F 275 GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR ARG
SEQRES 6 F 275 LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP LEU
SEQRES 7 F 275 GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY
SEQRES 8 F 275 SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL GLY
SEQRES 9 F 275 SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR ALA
SEQRES 10 F 275 TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP LEU
SEQRES 11 F 275 ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR THR
SEQRES 12 F 275 LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN LEU
SEQRES 13 F 275 ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG
SEQRES 14 F 275 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR
SEQRES 15 F 275 ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SER
SEQRES 16 F 275 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER PHE
SEQRES 17 F 275 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY
SEQRES 18 F 275 GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG
SEQRES 19 F 275 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 F 275 VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS HIS
SEQRES 21 F 275 VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG
SEQRES 22 F 275 TRP GLU
SEQRES 1 G 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 G 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 G 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 G 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 G 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 G 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 G 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 G 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 H 10 ALA LEU TRP GLY PRO ASP PRO ALA ALA ALA
SEQRES 1 I 199 GLU VAL GLU GLN ASP PRO GLY PRO LEU SER VAL PRO GLU
SEQRES 2 I 199 GLY ALA ILE VAL SER LEU ASN CYS THR TYR SER ASN SER
SEQRES 3 I 199 ALA PHE GLN TYR PHE MET TRP TYR ARG GLN TYR SER ARG
SEQRES 4 I 199 LYS GLY PRO GLU LEU LEU MET TYR THR TYR SER SER GLY
SEQRES 5 I 199 ASN LYS GLU ASP GLY ARG PHE THR ALA GLN VAL ASP LYS
SEQRES 6 I 199 SER SER LYS TYR ILE SER LEU PHE ILE ARG ASP SER GLN
SEQRES 7 I 199 PRO SER ASP SER ALA THR TYR LEU CYS ALA MET ARG GLY
SEQRES 8 I 199 ASP SER SER TYR LYS LEU ILE PHE GLY SER GLY THR ARG
SEQRES 9 I 199 LEU LEU VAL ARG PRO ASP ILE GLN ASN PRO ASP PRO ALA
SEQRES 10 I 199 VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS SER
SEQRES 11 I 199 VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN VAL
SEQRES 12 I 199 SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP LYS
SEQRES 13 I 199 CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER ASN
SEQRES 14 I 199 SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA CYS
SEQRES 15 I 199 ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP THR
SEQRES 16 I 199 PHE PHE PRO SER
SEQRES 1 J 245 ALA GLY VAL ILE GLN SER PRO ARG HIS GLU VAL THR GLU
SEQRES 2 J 245 MET GLY GLN GLN VAL THR LEU ARG CYS LYS PRO ILE SER
SEQRES 3 J 245 GLY HIS ASP TYR LEU PHE TRP TYR ARG GLN THR MET MET
SEQRES 4 J 245 ARG GLY LEU GLU LEU LEU ILE TYR PHE ASN ASN ASN VAL
SEQRES 5 J 245 PRO ILE ASP ASP SER GLY MET PRO GLU ASP ARG PHE SER
SEQRES 6 J 245 ALA LYS MET PRO ASN ALA SER PHE SER THR LEU LYS ILE
SEQRES 7 J 245 GLN PRO SER GLU PRO ARG ASP SER ALA VAL TYR PHE CYS
SEQRES 8 J 245 ALA SER SER LEU TRP GLU LYS LEU ALA LYS ASN ILE GLN
SEQRES 9 J 245 TYR PHE GLY ALA GLY THR ARG LEU SER VAL LEU GLU ASP
SEQRES 10 J 245 LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU
SEQRES 11 J 245 PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR
SEQRES 12 J 245 LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL
SEQRES 13 J 245 GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER
SEQRES 14 J 245 GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO
SEQRES 15 J 245 ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU
SEQRES 16 J 245 ARG VAL SER ALA THR PHE TRP GLN ASP PRO ARG ASN HIS
SEQRES 17 J 245 PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN
SEQRES 18 J 245 ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN
SEQRES 19 J 245 ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP
FORMUL 11 HOH *151(H2 O)
HELIX 1 1 GLY A 56 TYR A 85 1 30
HELIX 2 2 ASP A 137 ALA A 149 1 13
HELIX 3 3 HIS A 151 GLY A 162 1 12
HELIX 4 4 GLY A 162 GLY A 175 1 14
HELIX 5 5 GLY A 175 GLN A 180 1 6
HELIX 6 6 GLN A 253 GLN A 255 5 3
HELIX 7 7 GLU E 83 SER E 87 5 5
HELIX 8 8 LEU E 96 LYS E 102 1 7
HELIX 9 9 ASP E 118 VAL E 122 5 5
HELIX 10 10 SER E 133 THR E 140 1 8
HELIX 11 11 ALA E 200 GLN E 204 1 5
HELIX 12 12 TRP F 51 GLU F 55 5 5
HELIX 13 13 GLY F 56 TYR F 85 1 30
HELIX 14 14 ASP F 137 ALA F 150 1 14
HELIX 15 15 HIS F 151 GLY F 162 1 12
HELIX 16 16 GLY F 162 GLY F 175 1 14
HELIX 17 17 GLY F 175 GLN F 180 1 6
HELIX 18 18 GLN F 253 GLN F 255 5 3
HELIX 19 19 GLN I 80 SER I 84 5 5
HELIX 20 20 ALA I 183 ALA I 187 5 5
HELIX 21 21 GLU J 83 SER J 87 5 5
HELIX 22 22 LEU J 96 ALA J 101 1 6
HELIX 23 23 ASP J 118 VAL J 122 5 5
HELIX 24 24 SER J 133 THR J 140 1 8
HELIX 25 25 ALA J 200 GLN J 204 1 5
SHEET 1 A 7 GLU A 46 PRO A 47 0
SHEET 2 A 7 THR A 31 ASP A 37 -1 N ARG A 35 O GLU A 46
SHEET 3 A 7 ARG A 21 VAL A 28 -1 N GLY A 26 O VAL A 34
SHEET 4 A 7 HIS A 3 VAL A 12 -1 N THR A 10 O ILE A 23
SHEET 5 A 7 THR A 94 VAL A 103 -1 O VAL A 95 N SER A 11
SHEET 6 A 7 PHE A 109 TYR A 118 -1 O ARG A 111 N ASP A 102
SHEET 7 A 7 LYS A 121 ALA A 125 -1 O TYR A 123 N TYR A 116
SHEET 1 B 3 LYS A 186 HIS A 192 0
SHEET 2 B 3 GLU A 198 LEU A 206 -1 O THR A 200 N HIS A 192
SHEET 3 B 3 ALA A 245 PRO A 250 -1 O ALA A 245 N CYS A 203
SHEET 1 C 4 GLU A 222 GLN A 224 0
SHEET 2 C 4 THR A 214 ARG A 219 -1 N ARG A 219 O GLU A 222
SHEET 3 C 4 TYR A 257 HIS A 263 -1 O THR A 258 N GLN A 218
SHEET 4 C 4 LEU A 266 LEU A 272 -1 O LEU A 272 N CYS A 259
SHEET 1 D 2 ARG A 234 PRO A 235 0
SHEET 2 D 2 PHE A 241 GLN A 242 -1 O GLN A 242 N ARG A 234
SHEET 1 E 4 LYS B 6 SER B 11 0
SHEET 2 E 4 ASN B 21 PHE B 30 -1 O SER B 28 N LYS B 6
SHEET 3 E 4 PHE B 62 PHE B 70 -1 O LEU B 64 N VAL B 27
SHEET 4 E 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67
SHEET 1 F 4 LYS B 6 SER B 11 0
SHEET 2 F 4 ASN B 21 PHE B 30 -1 O SER B 28 N LYS B 6
SHEET 3 F 4 PHE B 62 PHE B 70 -1 O LEU B 64 N VAL B 27
SHEET 4 F 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 G 4 GLU B 44 ARG B 45 0
SHEET 2 G 4 ILE B 35 LYS B 41 -1 N LYS B 41 O GLU B 44
SHEET 3 G 4 TYR B 78 HIS B 84 -1 O ASN B 83 N GLU B 36
SHEET 4 G 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82
SHEET 1 H 5 VAL D 4 GLN D 6 0
SHEET 2 H 5 VAL D 19 TYR D 25 -1 O THR D 24 N GLU D 5
SHEET 3 H 5 TYR D 71 ILE D 76 -1 O LEU D 74 N LEU D 21
SHEET 4 H 5 PHE D 61 ASP D 66 -1 N GLN D 64 O SER D 73
SHEET 5 H 5 GLY D 54 ASP D 58 -1 N ASP D 58 O PHE D 61
SHEET 1 I 5 SER D 12 PRO D 14 0
SHEET 2 I 5 THR D 105 ARG D 110 1 O LEU D 108 N VAL D 13
SHEET 3 I 5 ALA D 85 GLY D 93 -1 N TYR D 87 O THR D 105
SHEET 4 I 5 TYR D 32 GLN D 38 -1 N TYR D 36 O LEU D 88
SHEET 5 I 5 GLU D 45 THR D 50 -1 O LEU D 47 N TRP D 35
SHEET 1 J 4 SER D 12 PRO D 14 0
SHEET 2 J 4 THR D 105 ARG D 110 1 O LEU D 108 N VAL D 13
SHEET 3 J 4 ALA D 85 GLY D 93 -1 N TYR D 87 O THR D 105
SHEET 4 J 4 SER D 96 PHE D 101 -1 O ILE D 100 N MET D 91
SHEET 1 K 4 ALA D 119 LEU D 123 0
SHEET 2 K 4 VAL D 133 PHE D 139 -1 O LEU D 135 N TYR D 121
SHEET 3 K 4 LYS D 169 TRP D 176 -1 O ALA D 175 N CYS D 134
SHEET 4 K 4 TYR D 154 ILE D 155 -1 N TYR D 154 O TRP D 176
SHEET 1 L 4 ALA D 119 LEU D 123 0
SHEET 2 L 4 VAL D 133 PHE D 139 -1 O LEU D 135 N TYR D 121
SHEET 3 L 4 LYS D 169 TRP D 176 -1 O ALA D 175 N CYS D 134
SHEET 4 L 4 CYS D 159 ASP D 162 -1 N CYS D 159 O SER D 172
SHEET 1 M 4 ILE E 5 SER E 7 0
SHEET 2 M 4 VAL E 19 LYS E 24 -1 O ARG E 22 N SER E 7
SHEET 3 M 4 PHE E 74 ILE E 79 -1 O SER E 75 N CYS E 23
SHEET 4 M 4 PHE E 65 ASN E 71 -1 N LYS E 68 O THR E 76
SHEET 1 N 6 HIS E 10 GLU E 14 0
SHEET 2 N 6 THR E 111 LEU E 116 1 O SER E 114 N GLU E 11
SHEET 3 N 6 ALA E 88 SER E 95 -1 N ALA E 88 O LEU E 113
SHEET 4 N 6 TYR E 31 GLN E 37 -1 N TYR E 35 O PHE E 91
SHEET 5 N 6 GLU E 44 ASN E 50 -1 O LEU E 46 N TRP E 34
SHEET 6 N 6 VAL E 53 ASP E 56 -1 O VAL E 53 N ASN E 50
SHEET 1 O 4 HIS E 10 GLU E 14 0
SHEET 2 O 4 THR E 111 LEU E 116 1 O SER E 114 N GLU E 11
SHEET 3 O 4 ALA E 88 SER E 95 -1 N ALA E 88 O LEU E 113
SHEET 4 O 4 TYR E 106 PHE E 107 -1 O TYR E 106 N SER E 94
SHEET 1 P 3 LYS E 142 VAL E 146 0
SHEET 2 P 3 SER E 194 SER E 199 -1 O VAL E 198 N ALA E 143
SHEET 3 P 3 VAL E 172 THR E 174 -1 N CYS E 173 O ARG E 195
SHEET 1 Q 4 LYS E 166 GLU E 167 0
SHEET 2 Q 4 VAL E 157 VAL E 163 -1 N VAL E 163 O LYS E 166
SHEET 3 Q 4 HIS E 209 PHE E 216 -1 O ARG E 211 N TRP E 162
SHEET 4 Q 4 GLN E 235 TRP E 242 -1 O ALA E 239 N CYS E 212
SHEET 1 R 2 LEU E 179 LYS E 180 0
SHEET 2 R 2 TYR E 190 ALA E 191 -1 O ALA E 191 N LEU E 179
SHEET 1 S 8 GLU F 46 PRO F 47 0
SHEET 2 S 8 THR F 31 ASP F 37 -1 N ARG F 35 O GLU F 46
SHEET 3 S 8 ARG F 21 VAL F 28 -1 N GLY F 26 O VAL F 34
SHEET 4 S 8 HIS F 3 VAL F 12 -1 N ARG F 6 O TYR F 27
SHEET 5 S 8 THR F 94 VAL F 103 -1 O ARG F 97 N PHE F 9
SHEET 6 S 8 PHE F 109 TYR F 118 -1 O GLN F 115 N MET F 98
SHEET 7 S 8 LYS F 121 LEU F 126 -1 O LEU F 126 N HIS F 114
SHEET 8 S 8 TRP F 133 ALA F 135 -1 O THR F 134 N ALA F 125
SHEET 1 T 4 LYS F 186 ALA F 193 0
SHEET 2 T 4 GLU F 198 PHE F 208 -1 O TRP F 204 N HIS F 188
SHEET 3 T 4 PHE F 241 PRO F 250 -1 O VAL F 249 N ALA F 199
SHEET 4 T 4 ARG F 234 PRO F 235 -1 N ARG F 234 O GLN F 242
SHEET 1 U 4 GLU F 222 ASP F 223 0
SHEET 2 U 4 THR F 214 ARG F 219 -1 N ARG F 219 O GLU F 222
SHEET 3 U 4 TYR F 257 GLN F 262 -1 O THR F 258 N GLN F 218
SHEET 4 U 4 LEU F 270 LEU F 272 -1 O LEU F 272 N CYS F 259
SHEET 1 V 4 VAL G 9 SER G 11 0
SHEET 2 V 4 ASN G 21 PHE G 30 -1 O ASN G 24 N TYR G 10
SHEET 3 V 4 PHE G 62 PHE G 70 -1 O TYR G 66 N CYS G 25
SHEET 4 V 4 GLU G 50 HIS G 51 -1 N GLU G 50 O TYR G 67
SHEET 1 W 4 VAL G 9 SER G 11 0
SHEET 2 W 4 ASN G 21 PHE G 30 -1 O ASN G 24 N TYR G 10
SHEET 3 W 4 PHE G 62 PHE G 70 -1 O TYR G 66 N CYS G 25
SHEET 4 W 4 SER G 55 PHE G 56 -1 N SER G 55 O TYR G 63
SHEET 1 X 4 GLU G 44 ARG G 45 0
SHEET 2 X 4 ILE G 35 LYS G 41 -1 N LYS G 41 O GLU G 44
SHEET 3 X 4 TYR G 78 HIS G 84 -1 O ALA G 79 N LEU G 40
SHEET 4 X 4 LYS G 91 LYS G 94 -1 O LYS G 91 N VAL G 82
SHEET 1 Y 5 VAL I 4 GLN I 6 0
SHEET 2 Y 5 VAL I 19 TYR I 25 -1 O THR I 24 N GLU I 5
SHEET 3 Y 5 TYR I 71 ILE I 76 -1 O ILE I 72 N CYS I 23
SHEET 4 Y 5 PHE I 61 ASP I 66 -1 N GLN I 64 O SER I 73
SHEET 5 Y 5 ASN I 55 ASP I 58 -1 N ASP I 58 O PHE I 61
SHEET 1 Z 5 SER I 12 PRO I 14 0
SHEET 2 Z 5 THR I 105 ARG I 110 1 O LEU I 108 N VAL I 13
SHEET 3 Z 5 ALA I 85 ARG I 92 -1 N ALA I 85 O LEU I 107
SHEET 4 Z 5 TYR I 32 GLN I 38 -1 N MET I 34 O ALA I 90
SHEET 5 Z 5 GLU I 45 THR I 50 -1 O THR I 50 N PHE I 33
SHEET 1 AA 4 SER I 12 PRO I 14 0
SHEET 2 AA 4 THR I 105 ARG I 110 1 O LEU I 108 N VAL I 13
SHEET 3 AA 4 ALA I 85 ARG I 92 -1 N ALA I 85 O LEU I 107
SHEET 4 AA 4 LEU I 99 PHE I 101 -1 O ILE I 100 N MET I 91
SHEET 1 AB 4 ALA I 119 VAL I 120 0
SHEET 2 AB 4 CYS I 134 PHE I 139 -1 O THR I 137 N ALA I 119
SHEET 3 AB 4 ASN I 171 TRP I 176 -1 O ALA I 173 N PHE I 136
SHEET 4 AB 4 TYR I 154 THR I 156 -1 N TYR I 154 O TRP I 176
SHEET 1 AC 2 ARG I 124 ASP I 125 0
SHEET 2 AC 2 PHE J 130 GLU J 131 -1 O GLU J 131 N ARG I 124
SHEET 1 AD 4 ILE J 5 SER J 7 0
SHEET 2 AD 4 LEU J 21 LYS J 24 -1 O ARG J 22 N SER J 7
SHEET 3 AD 4 PHE J 74 ILE J 79 -1 O LEU J 77 N LEU J 21
SHEET 4 AD 4 PHE J 65 ASN J 71 -1 N SER J 66 O LYS J 78
SHEET 1 AE 6 HIS J 10 GLU J 14 0
SHEET 2 AE 6 THR J 111 LEU J 116 1 O SER J 114 N GLU J 11
SHEET 3 AE 6 ALA J 88 SER J 95 -1 N TYR J 90 O THR J 111
SHEET 4 AE 6 TYR J 31 GLN J 37 -1 N PHE J 33 O ALA J 93
SHEET 5 AE 6 LEU J 43 ASN J 50 -1 O GLU J 44 N ARG J 36
SHEET 6 AE 6 VAL J 53 ASP J 56 -1 O VAL J 53 N ASN J 50
SHEET 1 AF 4 HIS J 10 GLU J 14 0
SHEET 2 AF 4 THR J 111 LEU J 116 1 O SER J 114 N GLU J 11
SHEET 3 AF 4 ALA J 88 SER J 95 -1 N TYR J 90 O THR J 111
SHEET 4 AF 4 TYR J 106 PHE J 107 -1 O TYR J 106 N SER J 94
SHEET 1 AG 3 LYS J 142 PHE J 152 0
SHEET 2 AG 3 TYR J 190 SER J 199 -1 O VAL J 198 N ALA J 143
SHEET 3 AG 3 VAL J 172 THR J 174 -1 N CYS J 173 O ARG J 195
SHEET 1 AH 3 LYS J 142 PHE J 152 0
SHEET 2 AH 3 TYR J 190 SER J 199 -1 O VAL J 198 N ALA J 143
SHEET 3 AH 3 LEU J 179 LYS J 180 -1 N LEU J 179 O ALA J 191
SHEET 1 AI 4 LYS J 166 VAL J 168 0
SHEET 2 AI 4 VAL J 157 VAL J 163 -1 N VAL J 163 O LYS J 166
SHEET 3 AI 4 HIS J 209 PHE J 216 -1 O GLN J 213 N SER J 160
SHEET 4 AI 4 GLN J 235 TRP J 242 -1 O GLN J 235 N PHE J 216
SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.03
SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.04
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.03
SSBOND 4 CYS D 23 CYS D 89 1555 1555 2.03
SSBOND 5 CYS D 134 CYS D 184 1555 1555 2.03
SSBOND 6 CYS D 159 CYS E 173 1555 1555 2.03
SSBOND 7 CYS E 23 CYS E 92 1555 1555 2.02
SSBOND 8 CYS E 147 CYS E 212 1555 1555 2.03
SSBOND 9 CYS F 101 CYS F 164 1555 1555 2.03
SSBOND 10 CYS F 203 CYS F 259 1555 1555 2.04
SSBOND 11 CYS G 25 CYS G 80 1555 1555 2.03
SSBOND 12 CYS I 23 CYS I 89 1555 1555 2.03
SSBOND 13 CYS I 134 CYS I 184 1555 1555 2.03
SSBOND 14 CYS I 159 CYS J 173 1555 1555 2.03
SSBOND 15 CYS J 23 CYS J 92 1555 1555 2.03
SSBOND 16 CYS J 147 CYS J 212 1555 1555 2.03
CISPEP 1 TYR A 209 PRO A 210 0 -0.10
CISPEP 2 HIS B 31 PRO B 32 0 2.79
CISPEP 3 GLY C 4 PRO C 5 0 -0.07
CISPEP 4 PRO C 7 ALA C 8 0 13.88
CISPEP 5 SER E 7 PRO E 8 0 -2.24
CISPEP 6 TYR E 153 PRO E 154 0 2.58
CISPEP 7 TYR F 209 PRO F 210 0 3.32
CISPEP 8 HIS G 31 PRO G 32 0 2.09
CISPEP 9 GLY H 4 PRO H 5 0 -4.69
CISPEP 10 PRO H 7 ALA H 8 0 13.87
CISPEP 11 PRO I 8 GLY I 9 0 0.05
CISPEP 12 ASP I 94 SER I 95 0 6.28
CISPEP 13 SER J 7 PRO J 8 0 0.27
CISPEP 14 TYR J 153 PRO J 154 0 -1.23
CRYST1 41.480 98.440 121.300 97.27 98.16 93.38 P 1 2
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 0.024108 0.001422 0.003684 0.00000
SCALE2 0.000000 0.010176 0.001402 0.00000
SCALE3 0.000000 0.000000 0.008407 0.00000
(ATOM LINES ARE NOT SHOWN.)
END