HEADER OXIDOREDUCTASE 25-OCT-10 3PDU
TITLE CRYSTAL STRUCTURE OF GAMMA-HYDROXYBUTYRATE DEHYDROGENASE FROM
TITLE 2 GEOBACTER SULFURREDUCENS IN COMPLEX WITH NADP+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-HYDROXYISOBUTYRATE DEHYDROGENASE FAMILY PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACTER SULFURREDUCENS;
SOURCE 3 ORGANISM_TAXID: 35554;
SOURCE 4 GENE: GSU1372;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PLW01
KEYWDS GAMMA-HYDROXYBUTYRATE DEHYDROGENASE, SUCCINIC SEMIALDEHYDE REDUCTASE,
KEYWDS 2 GLYOXYLATE METABOLISM, GEOBACTER SULFURREDUCENS,
KEYWDS 3 DEHYDROGENASE/REDUCTASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHANG,R.M.GARAVITO
REVDAT 3 21-FEB-24 3PDU 1 REMARK SEQADV
REVDAT 2 01-JUN-16 3PDU 1 JRNL
REVDAT 1 11-JAN-12 3PDU 0
JRNL AUTH Y.ZHANG,Y.ZHENG,L.QIN,S.WANG,G.W.BUCHKO,R.M.GARAVITO
JRNL TITL STRUCTURAL CHARACTERIZATION OF A BETA-HYDROXYACID
JRNL TITL 2 DEHYDROGENASE FROM GEOBACTER SULFURREDUCENS AND GEOBACTER
JRNL TITL 3 METALLIREDUCENS WITH SUCCINIC SEMIALDEHYDE REDUCTASE
JRNL TITL 4 ACTIVITY.
JRNL REF BIOCHIMIE V. 104 61 2014
JRNL REFN ISSN 0300-9084
JRNL PMID 24878278
JRNL DOI 10.1016/J.BIOCHI.2014.05.002
REMARK 2
REMARK 2 RESOLUTION. 1.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2)
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) : 1.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 208482
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.151
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6262
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 28.8141 - 4.0684 1.00 21471 643 0.1403 0.1642
REMARK 3 2 4.0684 - 3.2306 1.00 20954 641 0.1347 0.1741
REMARK 3 3 3.2306 - 2.8227 1.00 20851 637 0.1494 0.1773
REMARK 3 4 2.8227 - 2.5648 1.00 20650 711 0.1528 0.1984
REMARK 3 5 2.5648 - 2.3810 1.00 20776 611 0.1460 0.1860
REMARK 3 6 2.3810 - 2.2407 1.00 20742 608 0.1442 0.1873
REMARK 3 7 2.2407 - 2.1285 1.00 20568 655 0.1456 0.1847
REMARK 3 8 2.1285 - 2.0359 0.99 20378 628 0.1603 0.2112
REMARK 3 9 2.0359 - 1.9575 0.92 19014 604 0.1904 0.2336
REMARK 3 10 1.9575 - 1.8900 0.81 16816 524 0.2108 0.2554
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 : 0.36
REMARK 3 B_SOL : 40.45
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.34360
REMARK 3 B22 (A**2) : -0.72190
REMARK 3 B33 (A**2) : -0.62170
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 17209
REMARK 3 ANGLE : 1.070 23292
REMARK 3 CHIRALITY : 0.065 2609
REMARK 3 PLANARITY : 0.005 3043
REMARK 3 DIHEDRAL : 20.321 6309
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 64
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 1:19)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.9045 35.5130 4.0168
REMARK 3 T TENSOR
REMARK 3 T11: 0.1745 T22: 0.1902
REMARK 3 T33: 0.1489 T12: -0.0317
REMARK 3 T13: 0.0160 T23: 0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 0.2305 L22: 0.6689
REMARK 3 L33: 1.0917 L12: 0.2131
REMARK 3 L13: 0.1130 L23: -0.3604
REMARK 3 S TENSOR
REMARK 3 S11: -0.0621 S12: 0.0551 S13: -0.0196
REMARK 3 S21: -0.0054 S22: -0.1011 S23: 0.1003
REMARK 3 S31: -0.1224 S32: 0.2039 S33: 0.1173
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 20:46)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.7029 41.7417 3.5499
REMARK 3 T TENSOR
REMARK 3 T11: 0.2320 T22: 0.2059
REMARK 3 T33: 0.1652 T12: -0.0551
REMARK 3 T13: -0.0129 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.7823 L22: 0.3635
REMARK 3 L33: 0.3320 L12: 0.1236
REMARK 3 L13: 0.3998 L23: 0.1567
REMARK 3 S TENSOR
REMARK 3 S11: -0.0906 S12: 0.0268 S13: 0.1731
REMARK 3 S21: 0.0831 S22: -0.0619 S23: -0.0965
REMARK 3 S31: -0.3687 S32: 0.1962 S33: 0.0882
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 47:111)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.1302 29.2384 -7.2175
REMARK 3 T TENSOR
REMARK 3 T11: 0.1544 T22: 0.2135
REMARK 3 T33: 0.1540 T12: -0.0342
REMARK 3 T13: 0.0349 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 0.1944 L22: 0.7563
REMARK 3 L33: 0.7707 L12: 0.0251
REMARK 3 L13: 0.3025 L23: 0.1477
REMARK 3 S TENSOR
REMARK 3 S11: -0.0116 S12: 0.1522 S13: -0.0097
REMARK 3 S21: -0.1451 S22: 0.0054 S23: -0.0678
REMARK 3 S31: -0.0995 S32: 0.2839 S33: 0.0023
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 112:157)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.0689 25.6536 4.1703
REMARK 3 T TENSOR
REMARK 3 T11: 0.1498 T22: 0.1511
REMARK 3 T33: 0.1476 T12: -0.0237
REMARK 3 T13: 0.0036 T23: 0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 0.4672 L22: 0.7615
REMARK 3 L33: 1.2790 L12: 0.1671
REMARK 3 L13: 0.6573 L23: -0.1142
REMARK 3 S TENSOR
REMARK 3 S11: 0.0206 S12: 0.0213 S13: -0.0784
REMARK 3 S21: 0.0302 S22: 0.0071 S23: -0.0533
REMARK 3 S31: -0.0240 S32: 0.1474 S33: -0.0204
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 158:198)
REMARK 3 ORIGIN FOR THE GROUP (A): -18.5835 26.5330 -4.6599
REMARK 3 T TENSOR
REMARK 3 T11: 0.2042 T22: 0.1234
REMARK 3 T33: 0.1569 T12: 0.0165
REMARK 3 T13: 0.0017 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.5505 L22: 0.0363
REMARK 3 L33: 0.2246 L12: -0.0079
REMARK 3 L13: 0.1962 L23: -0.0738
REMARK 3 S TENSOR
REMARK 3 S11: -0.1152 S12: -0.0680 S13: -0.0444
REMARK 3 S21: 0.1109 S22: 0.0706 S23: 0.0028
REMARK 3 S31: -0.1178 S32: -0.0316 S33: 0.0175
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 199:227)
REMARK 3 ORIGIN FOR THE GROUP (A): -28.1379 34.5280 2.8764
REMARK 3 T TENSOR
REMARK 3 T11: 0.2576 T22: 0.2062
REMARK 3 T33: 0.1571 T12: 0.0504
REMARK 3 T13: 0.0212 T23: -0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 1.1070 L22: 0.7857
REMARK 3 L33: 0.2669 L12: -0.2356
REMARK 3 L13: 0.4585 L23: -0.0733
REMARK 3 S TENSOR
REMARK 3 S11: 0.1068 S12: -0.4131 S13: 0.0405
REMARK 3 S21: 0.2036 S22: -0.0497 S23: 0.0211
REMARK 3 S31: -0.1171 S32: -0.1858 S33: -0.0512
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 228:268)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1066 28.7053 -13.4282
REMARK 3 T TENSOR
REMARK 3 T11: 0.1508 T22: 0.1100
REMARK 3 T33: 0.1105 T12: 0.0065
REMARK 3 T13: 0.0037 T23: -0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 0.2456 L22: 0.5433
REMARK 3 L33: 0.6619 L12: 0.0722
REMARK 3 L13: 0.3889 L23: 0.0588
REMARK 3 S TENSOR
REMARK 3 S11: 0.0260 S12: 0.0008 S13: -0.0769
REMARK 3 S21: -0.0983 S22: -0.0315 S23: -0.0491
REMARK 3 S31: -0.1129 S32: -0.0733 S33: 0.0009
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 269:287)
REMARK 3 ORIGIN FOR THE GROUP (A): -20.9136 40.5721 -10.7992
REMARK 3 T TENSOR
REMARK 3 T11: 0.2521 T22: 0.1122
REMARK 3 T33: 0.1442 T12: 0.0185
REMARK 3 T13: 0.0065 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.6094 L22: 0.3603
REMARK 3 L33: 0.7391 L12: 0.0976
REMARK 3 L13: -0.0788 L23: 0.1053
REMARK 3 S TENSOR
REMARK 3 S11: -0.0143 S12: -0.1499 S13: 0.2390
REMARK 3 S21: -0.0820 S22: 0.0769 S23: -0.0273
REMARK 3 S31: -0.3773 S32: -0.0242 S33: -0.0605
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 2:32)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4600 14.9853 -48.3665
REMARK 3 T TENSOR
REMARK 3 T11: 0.1837 T22: 0.2208
REMARK 3 T33: 0.1851 T12: 0.0346
REMARK 3 T13: 0.0312 T23: -0.0537
REMARK 3 L TENSOR
REMARK 3 L11: 0.7409 L22: 0.5229
REMARK 3 L33: 0.4943 L12: -0.0822
REMARK 3 L13: 0.3570 L23: 0.2753
REMARK 3 S TENSOR
REMARK 3 S11: -0.0345 S12: 0.2806 S13: -0.2608
REMARK 3 S21: -0.0782 S22: 0.0510 S23: -0.0203
REMARK 3 S31: 0.0082 S32: 0.1134 S33: -0.0260
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 33:58)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5409 10.5939 -45.8891
REMARK 3 T TENSOR
REMARK 3 T11: 0.1885 T22: 0.2530
REMARK 3 T33: 0.3682 T12: 0.0910
REMARK 3 T13: 0.0277 T23: -0.0766
REMARK 3 L TENSOR
REMARK 3 L11: 0.7718 L22: 1.7417
REMARK 3 L33: 2.0374 L12: 0.4262
REMARK 3 L13: -1.0165 L23: 0.1193
REMARK 3 S TENSOR
REMARK 3 S11: 0.0597 S12: 0.0404 S13: -0.4637
REMARK 3 S21: 0.0643 S22: -0.0767 S23: -0.3638
REMARK 3 S31: 0.2898 S32: 0.5158 S33: -0.0338
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN B AND RESID 59:109)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.6077 23.6161 -36.4323
REMARK 3 T TENSOR
REMARK 3 T11: 0.1765 T22: 0.2430
REMARK 3 T33: 0.2258 T12: -0.0121
REMARK 3 T13: 0.0195 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 0.5847 L22: 0.7027
REMARK 3 L33: 1.0470 L12: 0.2164
REMARK 3 L13: 0.0816 L23: 0.2086
REMARK 3 S TENSOR
REMARK 3 S11: 0.0807 S12: -0.0675 S13: 0.0071
REMARK 3 S21: 0.0273 S22: -0.0339 S23: -0.2174
REMARK 3 S31: -0.1315 S32: 0.3700 S33: -0.0499
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN B AND RESID 110:157)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.3230 26.3623 -46.9697
REMARK 3 T TENSOR
REMARK 3 T11: 0.2134 T22: 0.1929
REMARK 3 T33: 0.1552 T12: 0.0141
REMARK 3 T13: 0.0375 T23: -0.0180
REMARK 3 L TENSOR
REMARK 3 L11: 1.2975 L22: 1.0645
REMARK 3 L33: 0.9766 L12: -0.0240
REMARK 3 L13: -0.5901 L23: 0.2454
REMARK 3 S TENSOR
REMARK 3 S11: 0.1298 S12: 0.2991 S13: 0.0086
REMARK 3 S21: -0.2162 S22: -0.0631 S23: -0.1549
REMARK 3 S31: -0.1703 S32: 0.1555 S33: -0.0752
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN B AND RESID 158:196)
REMARK 3 ORIGIN FOR THE GROUP (A): -20.0317 24.5305 -35.8053
REMARK 3 T TENSOR
REMARK 3 T11: 0.2296 T22: 0.1210
REMARK 3 T33: 0.1625 T12: 0.0185
REMARK 3 T13: -0.0044 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 0.4330 L22: 0.1574
REMARK 3 L33: 0.1754 L12: -0.0642
REMARK 3 L13: -0.1083 L23: 0.1469
REMARK 3 S TENSOR
REMARK 3 S11: -0.0947 S12: 0.0732 S13: 0.0593
REMARK 3 S21: -0.2310 S22: 0.0579 S23: 0.0311
REMARK 3 S31: 0.0085 S32: -0.0110 S33: 0.0429
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN B AND RESID 197:227)
REMARK 3 ORIGIN FOR THE GROUP (A): -32.2592 15.2459 -41.8567
REMARK 3 T TENSOR
REMARK 3 T11: 0.2241 T22: 0.1677
REMARK 3 T33: 0.2138 T12: 0.0230
REMARK 3 T13: -0.0385 T23: -0.0617
REMARK 3 L TENSOR
REMARK 3 L11: 1.0862 L22: 0.1020
REMARK 3 L33: 0.4151 L12: 0.3299
REMARK 3 L13: -0.0462 L23: -0.0502
REMARK 3 S TENSOR
REMARK 3 S11: 0.0980 S12: 0.2520 S13: -0.3328
REMARK 3 S21: -0.0433 S22: -0.0385 S23: 0.0693
REMARK 3 S31: 0.0577 S32: -0.1588 S33: -0.0427
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN B AND RESID 228:266)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.7382 22.2607 -28.1467
REMARK 3 T TENSOR
REMARK 3 T11: 0.1612 T22: 0.1045
REMARK 3 T33: 0.1260 T12: 0.0148
REMARK 3 T13: -0.0060 T23: -0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 0.1829 L22: 0.0432
REMARK 3 L33: 0.0393 L12: -0.0455
REMARK 3 L13: -0.0440 L23: 0.0479
REMARK 3 S TENSOR
REMARK 3 S11: 0.0252 S12: -0.0434 S13: -0.0070
REMARK 3 S21: 0.0396 S22: -0.0312 S23: -0.0795
REMARK 3 S31: -0.0621 S32: -0.0058 S33: -0.0052
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN B AND RESID 267:287)
REMARK 3 ORIGIN FOR THE GROUP (A): -21.6649 10.0202 -29.1568
REMARK 3 T TENSOR
REMARK 3 T11: 0.2159 T22: 0.1214
REMARK 3 T33: 0.2239 T12: 0.0229
REMARK 3 T13: -0.0281 T23: -0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 0.4939 L22: 0.0338
REMARK 3 L33: 0.3485 L12: 0.0140
REMARK 3 L13: 0.3974 L23: 0.0112
REMARK 3 S TENSOR
REMARK 3 S11: 0.0847 S12: -0.0862 S13: -0.2407
REMARK 3 S21: 0.1525 S22: 0.0451 S23: -0.0513
REMARK 3 S31: 0.2597 S32: 0.0396 S33: -0.1340
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN C AND RESID 2:31)
REMARK 3 ORIGIN FOR THE GROUP (A): -53.4764 14.1664 9.5249
REMARK 3 T TENSOR
REMARK 3 T11: 0.2000 T22: 0.3995
REMARK 3 T33: 0.2929 T12: 0.0084
REMARK 3 T13: 0.0417 T23: 0.1145
REMARK 3 L TENSOR
REMARK 3 L11: 0.1705 L22: 0.3242
REMARK 3 L33: 0.5022 L12: 0.0382
REMARK 3 L13: 0.2502 L23: 0.0926
REMARK 3 S TENSOR
REMARK 3 S11: -0.0908 S12: -0.3771 S13: -0.2708
REMARK 3 S21: 0.0603 S22: -0.0089 S23: 0.2028
REMARK 3 S31: 0.0634 S32: -0.3164 S33: 0.0448
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN C AND RESID 32:46)
REMARK 3 ORIGIN FOR THE GROUP (A): -55.3597 5.6912 6.9502
REMARK 3 T TENSOR
REMARK 3 T11: 0.3596 T22: 0.3915
REMARK 3 T33: 0.5682 T12: -0.0583
REMARK 3 T13: 0.0763 T23: 0.1545
REMARK 3 L TENSOR
REMARK 3 L11: 1.3354 L22: 0.0109
REMARK 3 L33: 2.2557 L12: 0.0119
REMARK 3 L13: -0.7278 L23: -0.1495
REMARK 3 S TENSOR
REMARK 3 S11: -0.0246 S12: -0.0347 S13: -1.1888
REMARK 3 S21: 0.0609 S22: -0.0979 S23: 0.1599
REMARK 3 S31: 0.3109 S32: -0.5891 S33: 0.1076
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN C AND RESID 47:111)
REMARK 3 ORIGIN FOR THE GROUP (A): -58.5699 21.1309 -1.8632
REMARK 3 T TENSOR
REMARK 3 T11: 0.1485 T22: 0.3910
REMARK 3 T33: 0.2942 T12: 0.0390
REMARK 3 T13: 0.0214 T23: 0.0710
REMARK 3 L TENSOR
REMARK 3 L11: 0.4647 L22: 0.9115
REMARK 3 L33: 0.7905 L12: -0.5450
REMARK 3 L13: -0.0180 L23: -0.1936
REMARK 3 S TENSOR
REMARK 3 S11: 0.0616 S12: 0.0612 S13: -0.2494
REMARK 3 S21: -0.0521 S22: -0.0147 S23: 0.3250
REMARK 3 S31: -0.0838 S32: -0.5134 S33: -0.0693
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN C AND RESID 112:175)
REMARK 3 ORIGIN FOR THE GROUP (A): -47.2852 27.0663 5.4115
REMARK 3 T TENSOR
REMARK 3 T11: 0.2401 T22: 0.2840
REMARK 3 T33: 0.1910 T12: 0.0533
REMARK 3 T13: 0.0633 T23: 0.0396
REMARK 3 L TENSOR
REMARK 3 L11: 1.1314 L22: 1.2477
REMARK 3 L33: 0.9635 L12: 0.0874
REMARK 3 L13: -0.4009 L23: -0.1749
REMARK 3 S TENSOR
REMARK 3 S11: 0.0408 S12: -0.2312 S13: -0.0670
REMARK 3 S21: 0.2645 S22: -0.0005 S23: 0.1947
REMARK 3 S31: -0.1544 S32: -0.1524 S33: -0.0536
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN C AND RESID 176:196)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.1544 17.9510 -7.0396
REMARK 3 T TENSOR
REMARK 3 T11: 0.2046 T22: 0.1268
REMARK 3 T33: 0.1562 T12: 0.0039
REMARK 3 T13: -0.0156 T23: 0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 0.5188 L22: 0.3623
REMARK 3 L33: 0.3125 L12: 0.4189
REMARK 3 L13: -0.1091 L23: -0.0970
REMARK 3 S TENSOR
REMARK 3 S11: 0.0151 S12: -0.0782 S13: -0.2775
REMARK 3 S21: -0.0152 S22: 0.0296 S23: 0.0175
REMARK 3 S31: 0.0541 S32: -0.0327 S33: -0.0317
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN C AND RESID 197:227)
REMARK 3 ORIGIN FOR THE GROUP (A): -19.9618 15.4810 2.2370
REMARK 3 T TENSOR
REMARK 3 T11: 0.1863 T22: 0.1562
REMARK 3 T33: 0.2013 T12: 0.0102
REMARK 3 T13: -0.0098 T23: 0.0662
REMARK 3 L TENSOR
REMARK 3 L11: 0.8317 L22: 0.2070
REMARK 3 L33: 0.6835 L12: -0.3330
REMARK 3 L13: 0.0562 L23: 0.0706
REMARK 3 S TENSOR
REMARK 3 S11: 0.0965 S12: -0.3219 S13: -0.1902
REMARK 3 S21: 0.0070 S22: -0.0511 S23: -0.0284
REMARK 3 S31: -0.1049 S32: 0.0386 S33: -0.0186
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN C AND RESID 228:266)
REMARK 3 ORIGIN FOR THE GROUP (A): -36.7311 21.7906 -11.4588
REMARK 3 T TENSOR
REMARK 3 T11: 0.1356 T22: 0.1339
REMARK 3 T33: 0.1252 T12: 0.0295
REMARK 3 T13: 0.0090 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 0.8456 L22: 0.2068
REMARK 3 L33: 0.3634 L12: -0.0309
REMARK 3 L13: 0.1699 L23: 0.2260
REMARK 3 S TENSOR
REMARK 3 S11: -0.0076 S12: -0.0506 S13: -0.0669
REMARK 3 S21: -0.0383 S22: -0.0344 S23: 0.0666
REMARK 3 S31: -0.0250 S32: -0.1054 S33: 0.0252
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN C AND RESID 267:286)
REMARK 3 ORIGIN FOR THE GROUP (A): -30.5860 9.9262 -10.3026
REMARK 3 T TENSOR
REMARK 3 T11: 0.1719 T22: 0.1207
REMARK 3 T33: 0.2124 T12: -0.0003
REMARK 3 T13: -0.0299 T23: 0.0346
REMARK 3 L TENSOR
REMARK 3 L11: 0.8323 L22: 0.1053
REMARK 3 L33: 0.7678 L12: -0.0093
REMARK 3 L13: -0.0700 L23: -0.1016
REMARK 3 S TENSOR
REMARK 3 S11: -0.0527 S12: 0.0566 S13: -0.1454
REMARK 3 S21: -0.0917 S22: 0.1845 S23: 0.1030
REMARK 3 S31: 0.3208 S32: 0.0257 S33: -0.1091
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (CHAIN D AND RESID 1:19)
REMARK 3 ORIGIN FOR THE GROUP (A): -56.9659 34.3369 -43.4842
REMARK 3 T TENSOR
REMARK 3 T11: 0.1809 T22: 0.2863
REMARK 3 T33: 0.1640 T12: 0.0697
REMARK 3 T13: -0.0068 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.3168 L22: 0.3488
REMARK 3 L33: 0.7536 L12: 0.0477
REMARK 3 L13: 0.0063 L23: 0.1932
REMARK 3 S TENSOR
REMARK 3 S11: 0.0608 S12: 0.0965 S13: -0.0220
REMARK 3 S21: 0.1333 S22: -0.0330 S23: 0.0045
REMARK 3 S31: 0.0983 S32: -0.3717 S33: -0.0083
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: (CHAIN D AND RESID 20:54)
REMARK 3 ORIGIN FOR THE GROUP (A): -61.4933 39.8483 -41.4719
REMARK 3 T TENSOR
REMARK 3 T11: 0.2315 T22: 0.2606
REMARK 3 T33: 0.1699 T12: 0.1379
REMARK 3 T13: -0.0094 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.5896 L22: 0.7342
REMARK 3 L33: 0.5655 L12: -0.0513
REMARK 3 L13: 0.1282 L23: -0.0625
REMARK 3 S TENSOR
REMARK 3 S11: 0.0448 S12: 0.1536 S13: 0.1017
REMARK 3 S21: -0.1181 S22: -0.1255 S23: 0.2884
REMARK 3 S31: -0.3597 S32: -0.3370 S33: 0.0310
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: (CHAIN D AND RESID 55:111)
REMARK 3 ORIGIN FOR THE GROUP (A): -60.1355 26.7065 -31.8932
REMARK 3 T TENSOR
REMARK 3 T11: 0.1664 T22: 0.2707
REMARK 3 T33: 0.1978 T12: 0.0461
REMARK 3 T13: 0.0041 T23: 0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 0.3630 L22: 0.8754
REMARK 3 L33: 0.5328 L12: -0.1067
REMARK 3 L13: -0.1080 L23: 0.0190
REMARK 3 S TENSOR
REMARK 3 S11: 0.0068 S12: -0.0451 S13: -0.0968
REMARK 3 S21: 0.0891 S22: 0.0141 S23: 0.0966
REMARK 3 S31: -0.0682 S32: -0.3030 S33: -0.0200
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: (CHAIN D AND RESID 112:157)
REMARK 3 ORIGIN FOR THE GROUP (A): -52.6303 24.6630 -43.6937
REMARK 3 T TENSOR
REMARK 3 T11: 0.1846 T22: 0.2252
REMARK 3 T33: 0.1752 T12: 0.0529
REMARK 3 T13: -0.0378 T23: -0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 0.5473 L22: 0.4533
REMARK 3 L33: 0.7693 L12: -0.3844
REMARK 3 L13: 0.2009 L23: 0.2180
REMARK 3 S TENSOR
REMARK 3 S11: 0.0514 S12: 0.1927 S13: -0.1411
REMARK 3 S21: -0.0255 S22: -0.0033 S23: 0.0508
REMARK 3 S31: -0.0536 S32: -0.1736 S33: -0.0455
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: (CHAIN D AND RESID 158:193)
REMARK 3 ORIGIN FOR THE GROUP (A): -36.6595 24.5480 -34.9003
REMARK 3 T TENSOR
REMARK 3 T11: 0.1947 T22: 0.0927
REMARK 3 T33: 0.1212 T12: 0.0405
REMARK 3 T13: -0.0082 T23: -0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 0.6167 L22: 0.0744
REMARK 3 L33: 0.0280 L12: -0.2199
REMARK 3 L13: 0.1128 L23: -0.0467
REMARK 3 S TENSOR
REMARK 3 S11: -0.0967 S12: 0.0075 S13: -0.1217
REMARK 3 S21: -0.1892 S22: 0.0442 S23: -0.0404
REMARK 3 S31: -0.0668 S32: 0.0063 S33: 0.0388
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: (CHAIN D AND RESID 194:222)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.1551 33.9008 -42.0681
REMARK 3 T TENSOR
REMARK 3 T11: 0.2619 T22: 0.1695
REMARK 3 T33: 0.1558 T12: 0.0435
REMARK 3 T13: 0.0071 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 1.3656 L22: 0.5498
REMARK 3 L33: 0.1538 L12: 0.4514
REMARK 3 L13: 0.0006 L23: 0.0458
REMARK 3 S TENSOR
REMARK 3 S11: 0.1577 S12: 0.2754 S13: 0.1296
REMARK 3 S21: -0.1396 S22: -0.0554 S23: -0.0354
REMARK 3 S31: -0.1082 S32: 0.0890 S33: -0.0927
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: (CHAIN D AND RESID 223:268)
REMARK 3 ORIGIN FOR THE GROUP (A): -36.6210 29.7825 -27.3366
REMARK 3 T TENSOR
REMARK 3 T11: 0.1774 T22: 0.1335
REMARK 3 T33: 0.1343 T12: 0.0383
REMARK 3 T13: -0.0083 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 0.5967 L22: 0.5303
REMARK 3 L33: 0.4309 L12: -0.0408
REMARK 3 L13: -0.1088 L23: -0.0786
REMARK 3 S TENSOR
REMARK 3 S11: 0.0057 S12: -0.0515 S13: 0.0066
REMARK 3 S21: -0.0403 S22: -0.0358 S23: -0.0251
REMARK 3 S31: -0.0736 S32: -0.0614 S33: 0.0431
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: (CHAIN D AND RESID 269:287)
REMARK 3 ORIGIN FOR THE GROUP (A): -32.3257 40.3101 -28.7664
REMARK 3 T TENSOR
REMARK 3 T11: 0.2580 T22: 0.1204
REMARK 3 T33: 0.1442 T12: 0.0611
REMARK 3 T13: 0.0132 T23: -0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 0.7122 L22: 0.4824
REMARK 3 L33: 1.5367 L12: 0.0114
REMARK 3 L13: 0.0481 L23: 0.1126
REMARK 3 S TENSOR
REMARK 3 S11: -0.0944 S12: 0.0327 S13: 0.1099
REMARK 3 S21: 0.2557 S22: 0.1312 S23: 0.0897
REMARK 3 S31: -0.4784 S32: 0.0171 S33: -0.0507
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: (CHAIN E AND RESID 1:19)
REMARK 3 ORIGIN FOR THE GROUP (A): -65.1547 25.9700 -64.2401
REMARK 3 T TENSOR
REMARK 3 T11: 0.1353 T22: 0.2537
REMARK 3 T33: 0.1887 T12: 0.0506
REMARK 3 T13: -0.0240 T23: 0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 0.4183 L22: 0.5746
REMARK 3 L33: 0.4581 L12: -0.0897
REMARK 3 L13: 0.0530 L23: -0.2049
REMARK 3 S TENSOR
REMARK 3 S11: -0.1231 S12: 0.0022 S13: -0.1050
REMARK 3 S21: -0.0143 S22: 0.0478 S23: 0.1866
REMARK 3 S31: -0.1122 S32: -0.0861 S33: 0.0435
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: (CHAIN E AND RESID 20:46)
REMARK 3 ORIGIN FOR THE GROUP (A): -71.7470 27.5950 -64.0730
REMARK 3 T TENSOR
REMARK 3 T11: 0.1426 T22: 0.3767
REMARK 3 T33: 0.2660 T12: 0.0764
REMARK 3 T13: -0.0292 T23: -0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 0.5966 L22: 0.6684
REMARK 3 L33: 1.0180 L12: -0.1308
REMARK 3 L13: -0.4171 L23: 0.2856
REMARK 3 S TENSOR
REMARK 3 S11: -0.1675 S12: -0.0964 S13: 0.1233
REMARK 3 S21: 0.0782 S22: -0.0838 S23: 0.3819
REMARK 3 S31: -0.3582 S32: -0.7232 S33: 0.1523
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: (CHAIN E AND RESID 47:111)
REMARK 3 ORIGIN FOR THE GROUP (A): -60.5754 32.1250 -75.2217
REMARK 3 T TENSOR
REMARK 3 T11: 0.2853 T22: 0.2263
REMARK 3 T33: 0.2024 T12: 0.0505
REMARK 3 T13: -0.0472 T23: 0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 0.9722 L22: 0.5487
REMARK 3 L33: 0.9781 L12: -0.1227
REMARK 3 L13: -0.2565 L23: -0.2081
REMARK 3 S TENSOR
REMARK 3 S11: -0.0706 S12: 0.0820 S13: 0.1298
REMARK 3 S21: -0.2328 S22: 0.0960 S23: 0.0258
REMARK 3 S31: -0.4498 S32: -0.1701 S33: 0.0195
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: (CHAIN E AND RESID 112:157)
REMARK 3 ORIGIN FOR THE GROUP (A): -54.7753 23.8284 -64.7829
REMARK 3 T TENSOR
REMARK 3 T11: 0.1604 T22: 0.2243
REMARK 3 T33: 0.1902 T12: 0.0250
REMARK 3 T13: -0.0219 T23: -0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 0.5739 L22: 0.5409
REMARK 3 L33: 1.0341 L12: 0.1735
REMARK 3 L13: -0.2679 L23: 0.4278
REMARK 3 S TENSOR
REMARK 3 S11: -0.0558 S12: -0.0901 S13: 0.0275
REMARK 3 S21: -0.0120 S22: 0.0632 S23: 0.0386
REMARK 3 S31: -0.1122 S32: -0.0710 S33: 0.0072
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: (CHAIN E AND RESID 158:193)
REMARK 3 ORIGIN FOR THE GROUP (A): -51.3247 9.4393 -74.7978
REMARK 3 T TENSOR
REMARK 3 T11: 0.1042 T22: 0.1962
REMARK 3 T33: 0.1505 T12: -0.0213
REMARK 3 T13: 0.0002 T23: -0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 0.1923 L22: 0.5773
REMARK 3 L33: 0.1510 L12: -0.3257
REMARK 3 L13: 0.0019 L23: 0.0846
REMARK 3 S TENSOR
REMARK 3 S11: -0.0353 S12: -0.0523 S13: -0.0730
REMARK 3 S21: -0.0325 S22: 0.0414 S23: -0.0719
REMARK 3 S31: -0.0271 S32: -0.0745 S33: 0.0072
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: (CHAIN E AND RESID 194:227)
REMARK 3 ORIGIN FOR THE GROUP (A): -58.8414 -7.2830 -69.1101
REMARK 3 T TENSOR
REMARK 3 T11: 0.1143 T22: 0.2670
REMARK 3 T33: 0.2452 T12: -0.0241
REMARK 3 T13: 0.0169 T23: 0.0187
REMARK 3 L TENSOR
REMARK 3 L11: 0.2407 L22: 0.6697
REMARK 3 L33: 0.5430 L12: -0.2024
REMARK 3 L13: 0.3506 L23: -0.1478
REMARK 3 S TENSOR
REMARK 3 S11: -0.1021 S12: -0.0678 S13: -0.1126
REMARK 3 S21: 0.1462 S22: 0.1337 S23: 0.2687
REMARK 3 S31: 0.1073 S32: -0.1612 S33: -0.0414
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: (CHAIN E AND RESID 228:268)
REMARK 3 ORIGIN FOR THE GROUP (A): -55.6600 9.8070 -83.3088
REMARK 3 T TENSOR
REMARK 3 T11: 0.1198 T22: 0.1976
REMARK 3 T33: 0.1287 T12: -0.0195
REMARK 3 T13: -0.0070 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 0.2702 L22: 1.2720
REMARK 3 L33: 0.6261 L12: -0.2613
REMARK 3 L13: 0.2840 L23: 0.1047
REMARK 3 S TENSOR
REMARK 3 S11: -0.0286 S12: 0.0851 S13: -0.0528
REMARK 3 S21: -0.2379 S22: -0.0331 S23: 0.1387
REMARK 3 S31: -0.1035 S32: -0.1403 S33: 0.0536
REMARK 3 TLS GROUP : 40
REMARK 3 SELECTION: (CHAIN E AND RESID 269:287)
REMARK 3 ORIGIN FOR THE GROUP (A): -66.1536 1.7672 -81.0348
REMARK 3 T TENSOR
REMARK 3 T11: 0.0860 T22: 0.2862
REMARK 3 T33: 0.2059 T12: -0.0398
REMARK 3 T13: -0.0361 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.0613 L22: 0.7312
REMARK 3 L33: 1.3514 L12: 0.1072
REMARK 3 L13: -0.1492 L23: 0.0325
REMARK 3 S TENSOR
REMARK 3 S11: 0.0274 S12: 0.0940 S13: -0.1116
REMARK 3 S21: -0.0461 S22: -0.1033 S23: 0.3274
REMARK 3 S31: 0.0736 S32: -0.5658 S33: 0.0931
REMARK 3 TLS GROUP : 41
REMARK 3 SELECTION: (CHAIN F AND RESID 2:30)
REMARK 3 ORIGIN FOR THE GROUP (A): -36.5590 62.7388 -23.8403
REMARK 3 T TENSOR
REMARK 3 T11: 0.1373 T22: 0.1362
REMARK 3 T33: 0.1187 T12: 0.0496
REMARK 3 T13: -0.0079 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.2963 L22: 0.1899
REMARK 3 L33: 1.0304 L12: -0.0420
REMARK 3 L13: -0.2270 L23: 0.4338
REMARK 3 S TENSOR
REMARK 3 S11: -0.0351 S12: -0.0327 S13: 0.0615
REMARK 3 S21: 0.1307 S22: -0.0198 S23: -0.0782
REMARK 3 S31: 0.2026 S32: 0.0656 S33: 0.0268
REMARK 3 TLS GROUP : 42
REMARK 3 SELECTION: (CHAIN F AND RESID 31:46)
REMARK 3 ORIGIN FOR THE GROUP (A): -28.0674 61.8865 -27.6879
REMARK 3 T TENSOR
REMARK 3 T11: 0.1486 T22: 0.2671
REMARK 3 T33: 0.2397 T12: 0.0870
REMARK 3 T13: -0.0339 T23: 0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.1999 L22: 0.7685
REMARK 3 L33: 1.0841 L12: 0.1417
REMARK 3 L13: 0.3464 L23: -0.2063
REMARK 3 S TENSOR
REMARK 3 S11: -0.0114 S12: 0.1773 S13: -0.0495
REMARK 3 S21: 0.0287 S22: -0.0588 S23: -0.4890
REMARK 3 S31: 0.1998 S32: 0.4536 S33: 0.0671
REMARK 3 TLS GROUP : 43
REMARK 3 SELECTION: (CHAIN F AND RESID 47:111)
REMARK 3 ORIGIN FOR THE GROUP (A): -43.4207 58.0816 -35.8439
REMARK 3 T TENSOR
REMARK 3 T11: 0.1867 T22: 0.1324
REMARK 3 T33: 0.1598 T12: 0.0732
REMARK 3 T13: 0.0035 T23: -0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 1.0780 L22: 0.4516
REMARK 3 L33: 0.4325 L12: -0.1413
REMARK 3 L13: 0.2026 L23: 0.2647
REMARK 3 S TENSOR
REMARK 3 S11: 0.0491 S12: 0.0936 S13: -0.1084
REMARK 3 S21: -0.0929 S22: -0.0011 S23: 0.0232
REMARK 3 S31: 0.1865 S32: 0.0562 S33: -0.0364
REMARK 3 TLS GROUP : 44
REMARK 3 SELECTION: (CHAIN F AND RESID 112:157)
REMARK 3 ORIGIN FOR THE GROUP (A): -47.8381 66.7870 -25.1237
REMARK 3 T TENSOR
REMARK 3 T11: 0.1688 T22: 0.1349
REMARK 3 T33: 0.1672 T12: 0.0410
REMARK 3 T13: -0.0010 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 0.5472 L22: 0.2749
REMARK 3 L33: 0.5804 L12: -0.1497
REMARK 3 L13: 0.1035 L23: -0.3497
REMARK 3 S TENSOR
REMARK 3 S11: -0.0077 S12: -0.0439 S13: -0.0031
REMARK 3 S21: 0.0188 S22: -0.0360 S23: 0.0423
REMARK 3 S31: 0.0175 S32: 0.0191 S33: 0.0386
REMARK 3 TLS GROUP : 45
REMARK 3 SELECTION: (CHAIN F AND RESID 158:193)
REMARK 3 ORIGIN FOR THE GROUP (A): -49.5380 81.6931 -34.9317
REMARK 3 T TENSOR
REMARK 3 T11: 0.1104 T22: 0.1543
REMARK 3 T33: 0.1504 T12: 0.0385
REMARK 3 T13: -0.0016 T23: -0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 0.0429 L22: 0.4275
REMARK 3 L33: -0.0053 L12: -0.1404
REMARK 3 L13: -0.0031 L23: 0.0271
REMARK 3 S TENSOR
REMARK 3 S11: 0.0288 S12: -0.0441 S13: -0.0491
REMARK 3 S21: 0.0579 S22: -0.0830 S23: -0.0990
REMARK 3 S31: -0.0146 S32: 0.0302 S33: 0.0526
REMARK 3 TLS GROUP : 46
REMARK 3 SELECTION: (CHAIN F AND RESID 194:227)
REMARK 3 ORIGIN FOR THE GROUP (A): -40.4223 97.2875 -29.4881
REMARK 3 T TENSOR
REMARK 3 T11: 0.1137 T22: 0.1451
REMARK 3 T33: 0.1909 T12: 0.0181
REMARK 3 T13: -0.0378 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 0.1724 L22: 1.0585
REMARK 3 L33: 0.7237 L12: -0.0883
REMARK 3 L13: -0.2315 L23: -0.2540
REMARK 3 S TENSOR
REMARK 3 S11: 0.0308 S12: -0.0545 S13: -0.0030
REMARK 3 S21: 0.2446 S22: -0.0281 S23: -0.2388
REMARK 3 S31: -0.0970 S32: 0.0870 S33: -0.0062
REMARK 3 TLS GROUP : 47
REMARK 3 SELECTION: (CHAIN F AND RESID 228:282)
REMARK 3 ORIGIN FOR THE GROUP (A): -42.7826 81.7333 -43.0318
REMARK 3 T TENSOR
REMARK 3 T11: 0.0984 T22: 0.1366
REMARK 3 T33: 0.1387 T12: 0.0396
REMARK 3 T13: -0.0032 T23: 0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 0.0768 L22: 0.2812
REMARK 3 L33: 0.4547 L12: -0.0953
REMARK 3 L13: 0.1472 L23: 0.0175
REMARK 3 S TENSOR
REMARK 3 S11: -0.0051 S12: 0.1019 S13: -0.0082
REMARK 3 S21: -0.1005 S22: -0.0305 S23: -0.1059
REMARK 3 S31: 0.0143 S32: 0.1163 S33: 0.0336
REMARK 3 TLS GROUP : 48
REMARK 3 SELECTION: (CHAIN F AND RESID 283:287)
REMARK 3 ORIGIN FOR THE GROUP (A): -34.3396 94.2745 -43.2452
REMARK 3 T TENSOR
REMARK 3 T11: 0.1475 T22: 0.2484
REMARK 3 T33: 0.2189 T12: 0.0077
REMARK 3 T13: 0.0353 T23: 0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 0.8166 L22: 2.7767
REMARK 3 L33: 7.4080 L12: 0.9809
REMARK 3 L13: -1.0057 L23: -0.0452
REMARK 3 S TENSOR
REMARK 3 S11: 0.2016 S12: -0.1835 S13: -0.1110
REMARK 3 S21: -0.0361 S22: 0.2194 S23: -0.0787
REMARK 3 S31: -0.5132 S32: 0.9944 S33: -0.2700
REMARK 3 TLS GROUP : 49
REMARK 3 SELECTION: (CHAIN G AND RESID 3:24)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3786 62.6264 -28.8567
REMARK 3 T TENSOR
REMARK 3 T11: 0.8508 T22: 0.3510
REMARK 3 T33: 0.4011 T12: -0.0218
REMARK 3 T13: -0.3220 T23: 0.1817
REMARK 3 L TENSOR
REMARK 3 L11: 0.2045 L22: 0.8764
REMARK 3 L33: 0.6574 L12: 0.4180
REMARK 3 L13: 0.1914 L23: 0.3623
REMARK 3 S TENSOR
REMARK 3 S11: 0.6518 S12: -0.0488 S13: -0.6453
REMARK 3 S21: 1.1024 S22: -0.1283 S23: -0.6941
REMARK 3 S31: 0.6365 S32: -0.0693 S33: -0.4846
REMARK 3 TLS GROUP : 50
REMARK 3 SELECTION: (CHAIN G AND RESID 25:60)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0341 54.4063 -32.3728
REMARK 3 T TENSOR
REMARK 3 T11: 0.9222 T22: 0.3008
REMARK 3 T33: 0.5741 T12: 0.1868
REMARK 3 T13: -0.3028 T23: 0.1434
REMARK 3 L TENSOR
REMARK 3 L11: 2.8636 L22: 0.7657
REMARK 3 L33: 3.6330 L12: 0.1586
REMARK 3 L13: 0.5343 L23: 1.6109
REMARK 3 S TENSOR
REMARK 3 S11: 0.4699 S12: -0.0185 S13: -0.9380
REMARK 3 S21: 1.0528 S22: 0.1035 S23: -0.4892
REMARK 3 S31: 1.5443 S32: 0.2754 S33: -0.7730
REMARK 3 TLS GROUP : 51
REMARK 3 SELECTION: (CHAIN G AND RESID 61:79)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2175 59.8147 -44.1453
REMARK 3 T TENSOR
REMARK 3 T11: 0.5817 T22: 0.3472
REMARK 3 T33: 0.3854 T12: 0.0872
REMARK 3 T13: -0.0896 T23: 0.0354
REMARK 3 L TENSOR
REMARK 3 L11: 1.3141 L22: 2.0188
REMARK 3 L33: 0.3034 L12: -0.0969
REMARK 3 L13: -0.3419 L23: 0.6307
REMARK 3 S TENSOR
REMARK 3 S11: 0.0396 S12: 0.1552 S13: -0.5886
REMARK 3 S21: 0.2483 S22: -0.0469 S23: -0.5051
REMARK 3 S31: 0.5753 S32: 0.4109 S33: 0.0001
REMARK 3 TLS GROUP : 52
REMARK 3 SELECTION: (CHAIN G AND RESID 80:163)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1535 64.8775 -34.8409
REMARK 3 T TENSOR
REMARK 3 T11: 0.6016 T22: 0.3698
REMARK 3 T33: 0.2657 T12: -0.0902
REMARK 3 T13: -0.0316 T23: 0.1019
REMARK 3 L TENSOR
REMARK 3 L11: 0.9978 L22: 1.4999
REMARK 3 L33: 0.3749 L12: 0.3058
REMARK 3 L13: 0.2895 L23: 0.0204
REMARK 3 S TENSOR
REMARK 3 S11: 0.2207 S12: -0.2905 S13: -0.3971
REMARK 3 S21: 0.5823 S22: -0.1521 S23: -0.1060
REMARK 3 S31: 0.5377 S32: -0.1188 S33: -0.0656
REMARK 3 TLS GROUP : 53
REMARK 3 SELECTION: (CHAIN G AND RESID 164:197)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0875 86.7665 -42.7592
REMARK 3 T TENSOR
REMARK 3 T11: 0.2686 T22: 0.3305
REMARK 3 T33: 0.1363 T12: 0.0103
REMARK 3 T13: -0.0265 T23: 0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 0.0527 L22: 0.4028
REMARK 3 L33: 0.0938 L12: 0.0469
REMARK 3 L13: -0.0328 L23: 0.1283
REMARK 3 S TENSOR
REMARK 3 S11: 0.0927 S12: -0.1278 S13: -0.0105
REMARK 3 S21: 0.3719 S22: -0.0265 S23: -0.0109
REMARK 3 S31: 0.0489 S32: 0.0612 S33: -0.0685
REMARK 3 TLS GROUP : 54
REMARK 3 SELECTION: (CHAIN G AND RESID 198:227)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4206 92.8746 -34.0796
REMARK 3 T TENSOR
REMARK 3 T11: 0.3395 T22: 0.4176
REMARK 3 T33: 0.1367 T12: -0.0277
REMARK 3 T13: -0.1125 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 0.6526 L22: 2.7365
REMARK 3 L33: 0.4849 L12: 0.5819
REMARK 3 L13: 0.2694 L23: -0.6687
REMARK 3 S TENSOR
REMARK 3 S11: 0.0870 S12: -0.3272 S13: 0.0105
REMARK 3 S21: 0.9027 S22: 0.0130 S23: -0.1623
REMARK 3 S31: -0.0787 S32: 0.0114 S33: -0.0142
REMARK 3 TLS GROUP : 55
REMARK 3 SELECTION: (CHAIN G AND RESID 228:267)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.9423 79.7384 -49.3053
REMARK 3 T TENSOR
REMARK 3 T11: 0.2356 T22: 0.2663
REMARK 3 T33: 0.1552 T12: 0.0394
REMARK 3 T13: -0.0336 T23: 0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 0.3837 L22: 0.4643
REMARK 3 L33: 0.6965 L12: 0.1168
REMARK 3 L13: -0.1924 L23: 0.0609
REMARK 3 S TENSOR
REMARK 3 S11: -0.0087 S12: -0.0599 S13: -0.0424
REMARK 3 S21: 0.2040 S22: -0.0503 S23: -0.0415
REMARK 3 S31: 0.2132 S32: 0.0132 S33: 0.0376
REMARK 3 TLS GROUP : 56
REMARK 3 SELECTION: (CHAIN G AND RESID 268:286)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8024 82.4832 -47.2109
REMARK 3 T TENSOR
REMARK 3 T11: 0.2103 T22: 0.3976
REMARK 3 T33: 0.2229 T12: 0.0762
REMARK 3 T13: -0.0817 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.1766 L22: 1.5970
REMARK 3 L33: 1.4547 L12: -0.1531
REMARK 3 L13: -0.3973 L23: -0.4230
REMARK 3 S TENSOR
REMARK 3 S11: 0.3233 S12: 0.0778 S13: -0.0772
REMARK 3 S21: 0.2109 S22: -0.1851 S23: -0.4690
REMARK 3 S31: 0.0097 S32: 0.8169 S33: -0.0162
REMARK 3 TLS GROUP : 57
REMARK 3 SELECTION: (CHAIN H AND RESID 2:30)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9371 30.1163 -68.7225
REMARK 3 T TENSOR
REMARK 3 T11: 0.3724 T22: 0.1586
REMARK 3 T33: 0.1719 T12: -0.0069
REMARK 3 T13: 0.0633 T23: -0.0360
REMARK 3 L TENSOR
REMARK 3 L11: 0.1533 L22: 0.5606
REMARK 3 L33: 0.6547 L12: -0.2617
REMARK 3 L13: 0.0119 L23: -0.2989
REMARK 3 S TENSOR
REMARK 3 S11: -0.0232 S12: -0.0418 S13: -0.0233
REMARK 3 S21: 0.3259 S22: -0.0071 S23: 0.1924
REMARK 3 S31: -0.3984 S32: 0.0724 S33: 0.0022
REMARK 3 TLS GROUP : 58
REMARK 3 SELECTION: (CHAIN H AND RESID 31:46)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.3006 32.4893 -72.3263
REMARK 3 T TENSOR
REMARK 3 T11: 0.3859 T22: 0.2445
REMARK 3 T33: 0.2974 T12: 0.0655
REMARK 3 T13: 0.0975 T23: -0.0275
REMARK 3 L TENSOR
REMARK 3 L11: 0.2062 L22: 0.2053
REMARK 3 L33: 1.3295 L12: -0.2056
REMARK 3 L13: -0.3079 L23: 0.3001
REMARK 3 S TENSOR
REMARK 3 S11: -0.1048 S12: -0.1224 S13: 0.0395
REMARK 3 S21: 0.1591 S22: 0.0440 S23: 0.4958
REMARK 3 S31: -0.5598 S32: 0.1204 S33: -0.1182
REMARK 3 TLS GROUP : 59
REMARK 3 SELECTION: (CHAIN H AND RESID 47:106)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.4229 33.4862 -80.6786
REMARK 3 T TENSOR
REMARK 3 T11: 0.3856 T22: 0.1468
REMARK 3 T33: 0.1730 T12: -0.0460
REMARK 3 T13: 0.0350 T23: -0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 0.8110 L22: 0.2611
REMARK 3 L33: 0.9018 L12: -0.1935
REMARK 3 L13: -0.2725 L23: -0.0883
REMARK 3 S TENSOR
REMARK 3 S11: -0.0190 S12: -0.0177 S13: 0.1197
REMARK 3 S21: -0.0703 S22: 0.0611 S23: -0.0133
REMARK 3 S31: -0.4306 S32: 0.0800 S33: -0.0356
REMARK 3 TLS GROUP : 60
REMARK 3 SELECTION: (CHAIN H AND RESID 107:157)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8605 25.3411 -71.3437
REMARK 3 T TENSOR
REMARK 3 T11: 0.2965 T22: 0.2142
REMARK 3 T33: 0.1623 T12: -0.0736
REMARK 3 T13: 0.0138 T23: -0.0563
REMARK 3 L TENSOR
REMARK 3 L11: 0.3506 L22: 0.9900
REMARK 3 L33: 0.6842 L12: -0.3034
REMARK 3 L13: -0.3553 L23: 0.5351
REMARK 3 S TENSOR
REMARK 3 S11: -0.0687 S12: -0.1583 S13: 0.0666
REMARK 3 S21: 0.1450 S22: 0.1349 S23: -0.0119
REMARK 3 S31: -0.1269 S32: 0.1914 S33: -0.0547
REMARK 3 TLS GROUP : 61
REMARK 3 SELECTION: (CHAIN H AND RESID 158:193)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.2021 9.1119 -80.3803
REMARK 3 T TENSOR
REMARK 3 T11: 0.1822 T22: 0.2025
REMARK 3 T33: 0.1542 T12: -0.0308
REMARK 3 T13: 0.0080 T23: -0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 0.0113 L22: 0.3651
REMARK 3 L33: 0.6676 L12: 0.0644
REMARK 3 L13: 0.0688 L23: 0.2506
REMARK 3 S TENSOR
REMARK 3 S11: -0.0197 S12: -0.0934 S13: -0.0264
REMARK 3 S21: 0.0751 S22: 0.0177 S23: -0.0613
REMARK 3 S31: -0.0690 S32: 0.0025 S33: 0.0032
REMARK 3 TLS GROUP : 62
REMARK 3 SELECTION: (CHAIN H AND RESID 194:227)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.5604 -4.3633 -74.7422
REMARK 3 T TENSOR
REMARK 3 T11: 0.2067 T22: 0.2456
REMARK 3 T33: 0.1861 T12: -0.0430
REMARK 3 T13: 0.0547 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 0.4221 L22: 1.5148
REMARK 3 L33: 0.4895 L12: 0.2441
REMARK 3 L13: -0.0584 L23: -0.0772
REMARK 3 S TENSOR
REMARK 3 S11: 0.0284 S12: -0.0850 S13: 0.0302
REMARK 3 S21: 0.4088 S22: 0.0625 S23: 0.2161
REMARK 3 S31: 0.1270 S32: -0.1347 S33: -0.0638
REMARK 3 TLS GROUP : 63
REMARK 3 SELECTION: (CHAIN H AND RESID 228:266)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.9923 11.3123 -88.6889
REMARK 3 T TENSOR
REMARK 3 T11: 0.1625 T22: 0.1601
REMARK 3 T33: 0.1458 T12: -0.0346
REMARK 3 T13: 0.0157 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.2145 L22: 0.5091
REMARK 3 L33: 0.2542 L12: -0.1264
REMARK 3 L13: -0.1443 L23: 0.1310
REMARK 3 S TENSOR
REMARK 3 S11: -0.0626 S12: -0.1296 S13: 0.0597
REMARK 3 S21: 0.0929 S22: 0.0114 S23: -0.0035
REMARK 3 S31: -0.0574 S32: 0.0713 S33: 0.0269
REMARK 3 TLS GROUP : 64
REMARK 3 SELECTION: (CHAIN H AND RESID 267:287)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.5623 6.3088 -87.2971
REMARK 3 T TENSOR
REMARK 3 T11: 0.1328 T22: 0.2172
REMARK 3 T33: 0.1689 T12: -0.0276
REMARK 3 T13: 0.0301 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 0.2427 L22: 0.7712
REMARK 3 L33: 0.4150 L12: 0.0848
REMARK 3 L13: -0.0809 L23: 0.1148
REMARK 3 S TENSOR
REMARK 3 S11: 0.0909 S12: 0.1295 S13: 0.0699
REMARK 3 S21: -0.1148 S22: -0.1587 S23: 0.2064
REMARK 3 S31: 0.0554 S32: -0.3081 S33: 0.0671
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 3PDU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-10.
REMARK 100 THE DEPOSITION ID IS D_1000062257.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-DEC-09
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 : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 208482
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.890
REMARK 200 RESOLUTION RANGE LOW (A) : 28.811
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, 12%, SODIUM CACODYLATE 100
REMARK 280 MM, SODIUM ACETATE 200 MM, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 50.01700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 91.03500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.01700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 91.03500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 19620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -127.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 19310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -123.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 BIOMT1 2 -1.000000 0.000000 0.000000 -100.03400
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 -50.01700
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 -91.03500
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 -147.17200
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 -50.01700
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 91.03500
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 -147.17200
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 19580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -128.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -50.01700
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 91.03500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -147.17200
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C1196 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C1231 LIES ON A SPECIAL POSITION.
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 B 1
REMARK 465 MET C 1
REMARK 465 MET F 1
REMARK 465 MET G 1
REMARK 465 THR G 2
REMARK 465 ALA G 287
REMARK 465 MET H 1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 40 CA - CB - CG ANGL. DEV. = -16.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 9 68.68 -107.86
REMARK 500 ALA A 119 63.01 -152.26
REMARK 500 THR A 124 -156.25 -103.57
REMARK 500 LEU A 136 77.51 -106.94
REMARK 500 LEU B 9 64.57 -107.64
REMARK 500 ALA B 119 60.33 -152.97
REMARK 500 THR B 124 -150.02 -103.56
REMARK 500 LEU B 136 76.20 -113.02
REMARK 500 LEU C 9 60.51 -105.37
REMARK 500 ALA C 119 64.74 -155.35
REMARK 500 THR C 124 -153.95 -102.50
REMARK 500 LEU C 136 78.60 -106.37
REMARK 500 LEU D 9 55.38 -108.36
REMARK 500 ALA D 119 58.63 -152.73
REMARK 500 THR D 124 -152.23 -103.61
REMARK 500 LEU D 136 76.91 -108.23
REMARK 500 LEU E 9 67.24 -111.11
REMARK 500 ALA E 119 61.86 -152.93
REMARK 500 THR E 124 -153.69 -104.83
REMARK 500 LEU E 136 78.17 -108.37
REMARK 500 LEU F 9 64.61 -108.67
REMARK 500 ALA F 119 64.57 -151.68
REMARK 500 THR F 124 -154.35 -98.10
REMARK 500 LEU G 9 59.42 -104.63
REMARK 500 ALA G 119 61.99 -155.59
REMARK 500 THR G 124 -157.14 -99.96
REMARK 500 LEU H 9 61.92 -104.32
REMARK 500 ALA H 119 57.35 -155.11
REMARK 500 THR H 124 -152.64 -101.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 288
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP F 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 288
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP G 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP H 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PEF RELATED DB: PDB
DBREF 3PDU A 1 286 UNP Q74DE4 Q74DE4_GEOSL 1 286
DBREF 3PDU B 1 286 UNP Q74DE4 Q74DE4_GEOSL 1 286
DBREF 3PDU C 1 286 UNP Q74DE4 Q74DE4_GEOSL 1 286
DBREF 3PDU D 1 286 UNP Q74DE4 Q74DE4_GEOSL 1 286
DBREF 3PDU E 1 286 UNP Q74DE4 Q74DE4_GEOSL 1 286
DBREF 3PDU F 1 286 UNP Q74DE4 Q74DE4_GEOSL 1 286
DBREF 3PDU G 1 286 UNP Q74DE4 Q74DE4_GEOSL 1 286
DBREF 3PDU H 1 286 UNP Q74DE4 Q74DE4_GEOSL 1 286
SEQADV 3PDU ALA A 287 UNP Q74DE4 EXPRESSION TAG
SEQADV 3PDU ALA B 287 UNP Q74DE4 EXPRESSION TAG
SEQADV 3PDU ALA C 287 UNP Q74DE4 EXPRESSION TAG
SEQADV 3PDU ALA D 287 UNP Q74DE4 EXPRESSION TAG
SEQADV 3PDU ALA E 287 UNP Q74DE4 EXPRESSION TAG
SEQADV 3PDU ALA F 287 UNP Q74DE4 EXPRESSION TAG
SEQADV 3PDU ALA G 287 UNP Q74DE4 EXPRESSION TAG
SEQADV 3PDU ALA H 287 UNP Q74DE4 EXPRESSION TAG
SEQRES 1 A 287 MET THR THR TYR GLY PHE LEU GLY LEU GLY ILE MET GLY
SEQRES 2 A 287 GLY PRO MET ALA ALA ASN LEU VAL ARG ALA GLY PHE ASP
SEQRES 3 A 287 VAL THR VAL TRP ASN ARG ASN PRO ALA LYS CYS ALA PRO
SEQRES 4 A 287 LEU VAL ALA LEU GLY ALA ARG GLN ALA SER SER PRO ALA
SEQRES 5 A 287 GLU VAL CYS ALA ALA CYS ASP ILE THR ILE ALA MET LEU
SEQRES 6 A 287 ALA ASP PRO ALA ALA ALA ARG GLU VAL CYS PHE GLY ALA
SEQRES 7 A 287 ASN GLY VAL LEU GLU GLY ILE GLY GLY GLY ARG GLY TYR
SEQRES 8 A 287 ILE ASP MET SER THR VAL ASP ASP GLU THR SER THR ALA
SEQRES 9 A 287 ILE GLY ALA ALA VAL THR ALA ARG GLY GLY ARG PHE LEU
SEQRES 10 A 287 GLU ALA PRO VAL SER GLY THR LYS LYS PRO ALA GLU ASP
SEQRES 11 A 287 GLY THR LEU ILE ILE LEU ALA ALA GLY ASP GLN SER LEU
SEQRES 12 A 287 PHE THR ASP ALA GLY PRO ALA PHE ALA ALA LEU GLY LYS
SEQRES 13 A 287 LYS CYS LEU HIS LEU GLY GLU VAL GLY GLN GLY ALA ARG
SEQRES 14 A 287 MET LYS LEU VAL VAL ASN MET ILE MET GLY GLN MET MET
SEQRES 15 A 287 THR ALA LEU GLY GLU GLY MET ALA LEU GLY ARG ASN CYS
SEQRES 16 A 287 GLY LEU ASP GLY GLY GLN LEU LEU GLU VAL LEU ASP ALA
SEQRES 17 A 287 GLY ALA MET ALA ASN PRO MET PHE LYS GLY LYS GLY GLN
SEQRES 18 A 287 MET LEU LEU SER GLY GLU PHE PRO THR SER PHE PRO LEU
SEQRES 19 A 287 LYS HIS MET GLN LYS ASP LEU ARG LEU ALA VAL GLU LEU
SEQRES 20 A 287 GLY ASP ARG LEU GLY GLN PRO LEU HIS GLY ALA ALA THR
SEQRES 21 A 287 ALA ASN GLU SER PHE LYS ARG ALA ARG ALA ALA GLY HIS
SEQRES 22 A 287 ALA ASP GLU ASP PHE ALA ALA VAL PHE ARG VAL LEU GLU
SEQRES 23 A 287 ALA
SEQRES 1 B 287 MET THR THR TYR GLY PHE LEU GLY LEU GLY ILE MET GLY
SEQRES 2 B 287 GLY PRO MET ALA ALA ASN LEU VAL ARG ALA GLY PHE ASP
SEQRES 3 B 287 VAL THR VAL TRP ASN ARG ASN PRO ALA LYS CYS ALA PRO
SEQRES 4 B 287 LEU VAL ALA LEU GLY ALA ARG GLN ALA SER SER PRO ALA
SEQRES 5 B 287 GLU VAL CYS ALA ALA CYS ASP ILE THR ILE ALA MET LEU
SEQRES 6 B 287 ALA ASP PRO ALA ALA ALA ARG GLU VAL CYS PHE GLY ALA
SEQRES 7 B 287 ASN GLY VAL LEU GLU GLY ILE GLY GLY GLY ARG GLY TYR
SEQRES 8 B 287 ILE ASP MET SER THR VAL ASP ASP GLU THR SER THR ALA
SEQRES 9 B 287 ILE GLY ALA ALA VAL THR ALA ARG GLY GLY ARG PHE LEU
SEQRES 10 B 287 GLU ALA PRO VAL SER GLY THR LYS LYS PRO ALA GLU ASP
SEQRES 11 B 287 GLY THR LEU ILE ILE LEU ALA ALA GLY ASP GLN SER LEU
SEQRES 12 B 287 PHE THR ASP ALA GLY PRO ALA PHE ALA ALA LEU GLY LYS
SEQRES 13 B 287 LYS CYS LEU HIS LEU GLY GLU VAL GLY GLN GLY ALA ARG
SEQRES 14 B 287 MET LYS LEU VAL VAL ASN MET ILE MET GLY GLN MET MET
SEQRES 15 B 287 THR ALA LEU GLY GLU GLY MET ALA LEU GLY ARG ASN CYS
SEQRES 16 B 287 GLY LEU ASP GLY GLY GLN LEU LEU GLU VAL LEU ASP ALA
SEQRES 17 B 287 GLY ALA MET ALA ASN PRO MET PHE LYS GLY LYS GLY GLN
SEQRES 18 B 287 MET LEU LEU SER GLY GLU PHE PRO THR SER PHE PRO LEU
SEQRES 19 B 287 LYS HIS MET GLN LYS ASP LEU ARG LEU ALA VAL GLU LEU
SEQRES 20 B 287 GLY ASP ARG LEU GLY GLN PRO LEU HIS GLY ALA ALA THR
SEQRES 21 B 287 ALA ASN GLU SER PHE LYS ARG ALA ARG ALA ALA GLY HIS
SEQRES 22 B 287 ALA ASP GLU ASP PHE ALA ALA VAL PHE ARG VAL LEU GLU
SEQRES 23 B 287 ALA
SEQRES 1 C 287 MET THR THR TYR GLY PHE LEU GLY LEU GLY ILE MET GLY
SEQRES 2 C 287 GLY PRO MET ALA ALA ASN LEU VAL ARG ALA GLY PHE ASP
SEQRES 3 C 287 VAL THR VAL TRP ASN ARG ASN PRO ALA LYS CYS ALA PRO
SEQRES 4 C 287 LEU VAL ALA LEU GLY ALA ARG GLN ALA SER SER PRO ALA
SEQRES 5 C 287 GLU VAL CYS ALA ALA CYS ASP ILE THR ILE ALA MET LEU
SEQRES 6 C 287 ALA ASP PRO ALA ALA ALA ARG GLU VAL CYS PHE GLY ALA
SEQRES 7 C 287 ASN GLY VAL LEU GLU GLY ILE GLY GLY GLY ARG GLY TYR
SEQRES 8 C 287 ILE ASP MET SER THR VAL ASP ASP GLU THR SER THR ALA
SEQRES 9 C 287 ILE GLY ALA ALA VAL THR ALA ARG GLY GLY ARG PHE LEU
SEQRES 10 C 287 GLU ALA PRO VAL SER GLY THR LYS LYS PRO ALA GLU ASP
SEQRES 11 C 287 GLY THR LEU ILE ILE LEU ALA ALA GLY ASP GLN SER LEU
SEQRES 12 C 287 PHE THR ASP ALA GLY PRO ALA PHE ALA ALA LEU GLY LYS
SEQRES 13 C 287 LYS CYS LEU HIS LEU GLY GLU VAL GLY GLN GLY ALA ARG
SEQRES 14 C 287 MET LYS LEU VAL VAL ASN MET ILE MET GLY GLN MET MET
SEQRES 15 C 287 THR ALA LEU GLY GLU GLY MET ALA LEU GLY ARG ASN CYS
SEQRES 16 C 287 GLY LEU ASP GLY GLY GLN LEU LEU GLU VAL LEU ASP ALA
SEQRES 17 C 287 GLY ALA MET ALA ASN PRO MET PHE LYS GLY LYS GLY GLN
SEQRES 18 C 287 MET LEU LEU SER GLY GLU PHE PRO THR SER PHE PRO LEU
SEQRES 19 C 287 LYS HIS MET GLN LYS ASP LEU ARG LEU ALA VAL GLU LEU
SEQRES 20 C 287 GLY ASP ARG LEU GLY GLN PRO LEU HIS GLY ALA ALA THR
SEQRES 21 C 287 ALA ASN GLU SER PHE LYS ARG ALA ARG ALA ALA GLY HIS
SEQRES 22 C 287 ALA ASP GLU ASP PHE ALA ALA VAL PHE ARG VAL LEU GLU
SEQRES 23 C 287 ALA
SEQRES 1 D 287 MET THR THR TYR GLY PHE LEU GLY LEU GLY ILE MET GLY
SEQRES 2 D 287 GLY PRO MET ALA ALA ASN LEU VAL ARG ALA GLY PHE ASP
SEQRES 3 D 287 VAL THR VAL TRP ASN ARG ASN PRO ALA LYS CYS ALA PRO
SEQRES 4 D 287 LEU VAL ALA LEU GLY ALA ARG GLN ALA SER SER PRO ALA
SEQRES 5 D 287 GLU VAL CYS ALA ALA CYS ASP ILE THR ILE ALA MET LEU
SEQRES 6 D 287 ALA ASP PRO ALA ALA ALA ARG GLU VAL CYS PHE GLY ALA
SEQRES 7 D 287 ASN GLY VAL LEU GLU GLY ILE GLY GLY GLY ARG GLY TYR
SEQRES 8 D 287 ILE ASP MET SER THR VAL ASP ASP GLU THR SER THR ALA
SEQRES 9 D 287 ILE GLY ALA ALA VAL THR ALA ARG GLY GLY ARG PHE LEU
SEQRES 10 D 287 GLU ALA PRO VAL SER GLY THR LYS LYS PRO ALA GLU ASP
SEQRES 11 D 287 GLY THR LEU ILE ILE LEU ALA ALA GLY ASP GLN SER LEU
SEQRES 12 D 287 PHE THR ASP ALA GLY PRO ALA PHE ALA ALA LEU GLY LYS
SEQRES 13 D 287 LYS CYS LEU HIS LEU GLY GLU VAL GLY GLN GLY ALA ARG
SEQRES 14 D 287 MET LYS LEU VAL VAL ASN MET ILE MET GLY GLN MET MET
SEQRES 15 D 287 THR ALA LEU GLY GLU GLY MET ALA LEU GLY ARG ASN CYS
SEQRES 16 D 287 GLY LEU ASP GLY GLY GLN LEU LEU GLU VAL LEU ASP ALA
SEQRES 17 D 287 GLY ALA MET ALA ASN PRO MET PHE LYS GLY LYS GLY GLN
SEQRES 18 D 287 MET LEU LEU SER GLY GLU PHE PRO THR SER PHE PRO LEU
SEQRES 19 D 287 LYS HIS MET GLN LYS ASP LEU ARG LEU ALA VAL GLU LEU
SEQRES 20 D 287 GLY ASP ARG LEU GLY GLN PRO LEU HIS GLY ALA ALA THR
SEQRES 21 D 287 ALA ASN GLU SER PHE LYS ARG ALA ARG ALA ALA GLY HIS
SEQRES 22 D 287 ALA ASP GLU ASP PHE ALA ALA VAL PHE ARG VAL LEU GLU
SEQRES 23 D 287 ALA
SEQRES 1 E 287 MET THR THR TYR GLY PHE LEU GLY LEU GLY ILE MET GLY
SEQRES 2 E 287 GLY PRO MET ALA ALA ASN LEU VAL ARG ALA GLY PHE ASP
SEQRES 3 E 287 VAL THR VAL TRP ASN ARG ASN PRO ALA LYS CYS ALA PRO
SEQRES 4 E 287 LEU VAL ALA LEU GLY ALA ARG GLN ALA SER SER PRO ALA
SEQRES 5 E 287 GLU VAL CYS ALA ALA CYS ASP ILE THR ILE ALA MET LEU
SEQRES 6 E 287 ALA ASP PRO ALA ALA ALA ARG GLU VAL CYS PHE GLY ALA
SEQRES 7 E 287 ASN GLY VAL LEU GLU GLY ILE GLY GLY GLY ARG GLY TYR
SEQRES 8 E 287 ILE ASP MET SER THR VAL ASP ASP GLU THR SER THR ALA
SEQRES 9 E 287 ILE GLY ALA ALA VAL THR ALA ARG GLY GLY ARG PHE LEU
SEQRES 10 E 287 GLU ALA PRO VAL SER GLY THR LYS LYS PRO ALA GLU ASP
SEQRES 11 E 287 GLY THR LEU ILE ILE LEU ALA ALA GLY ASP GLN SER LEU
SEQRES 12 E 287 PHE THR ASP ALA GLY PRO ALA PHE ALA ALA LEU GLY LYS
SEQRES 13 E 287 LYS CYS LEU HIS LEU GLY GLU VAL GLY GLN GLY ALA ARG
SEQRES 14 E 287 MET LYS LEU VAL VAL ASN MET ILE MET GLY GLN MET MET
SEQRES 15 E 287 THR ALA LEU GLY GLU GLY MET ALA LEU GLY ARG ASN CYS
SEQRES 16 E 287 GLY LEU ASP GLY GLY GLN LEU LEU GLU VAL LEU ASP ALA
SEQRES 17 E 287 GLY ALA MET ALA ASN PRO MET PHE LYS GLY LYS GLY GLN
SEQRES 18 E 287 MET LEU LEU SER GLY GLU PHE PRO THR SER PHE PRO LEU
SEQRES 19 E 287 LYS HIS MET GLN LYS ASP LEU ARG LEU ALA VAL GLU LEU
SEQRES 20 E 287 GLY ASP ARG LEU GLY GLN PRO LEU HIS GLY ALA ALA THR
SEQRES 21 E 287 ALA ASN GLU SER PHE LYS ARG ALA ARG ALA ALA GLY HIS
SEQRES 22 E 287 ALA ASP GLU ASP PHE ALA ALA VAL PHE ARG VAL LEU GLU
SEQRES 23 E 287 ALA
SEQRES 1 F 287 MET THR THR TYR GLY PHE LEU GLY LEU GLY ILE MET GLY
SEQRES 2 F 287 GLY PRO MET ALA ALA ASN LEU VAL ARG ALA GLY PHE ASP
SEQRES 3 F 287 VAL THR VAL TRP ASN ARG ASN PRO ALA LYS CYS ALA PRO
SEQRES 4 F 287 LEU VAL ALA LEU GLY ALA ARG GLN ALA SER SER PRO ALA
SEQRES 5 F 287 GLU VAL CYS ALA ALA CYS ASP ILE THR ILE ALA MET LEU
SEQRES 6 F 287 ALA ASP PRO ALA ALA ALA ARG GLU VAL CYS PHE GLY ALA
SEQRES 7 F 287 ASN GLY VAL LEU GLU GLY ILE GLY GLY GLY ARG GLY TYR
SEQRES 8 F 287 ILE ASP MET SER THR VAL ASP ASP GLU THR SER THR ALA
SEQRES 9 F 287 ILE GLY ALA ALA VAL THR ALA ARG GLY GLY ARG PHE LEU
SEQRES 10 F 287 GLU ALA PRO VAL SER GLY THR LYS LYS PRO ALA GLU ASP
SEQRES 11 F 287 GLY THR LEU ILE ILE LEU ALA ALA GLY ASP GLN SER LEU
SEQRES 12 F 287 PHE THR ASP ALA GLY PRO ALA PHE ALA ALA LEU GLY LYS
SEQRES 13 F 287 LYS CYS LEU HIS LEU GLY GLU VAL GLY GLN GLY ALA ARG
SEQRES 14 F 287 MET LYS LEU VAL VAL ASN MET ILE MET GLY GLN MET MET
SEQRES 15 F 287 THR ALA LEU GLY GLU GLY MET ALA LEU GLY ARG ASN CYS
SEQRES 16 F 287 GLY LEU ASP GLY GLY GLN LEU LEU GLU VAL LEU ASP ALA
SEQRES 17 F 287 GLY ALA MET ALA ASN PRO MET PHE LYS GLY LYS GLY GLN
SEQRES 18 F 287 MET LEU LEU SER GLY GLU PHE PRO THR SER PHE PRO LEU
SEQRES 19 F 287 LYS HIS MET GLN LYS ASP LEU ARG LEU ALA VAL GLU LEU
SEQRES 20 F 287 GLY ASP ARG LEU GLY GLN PRO LEU HIS GLY ALA ALA THR
SEQRES 21 F 287 ALA ASN GLU SER PHE LYS ARG ALA ARG ALA ALA GLY HIS
SEQRES 22 F 287 ALA ASP GLU ASP PHE ALA ALA VAL PHE ARG VAL LEU GLU
SEQRES 23 F 287 ALA
SEQRES 1 G 287 MET THR THR TYR GLY PHE LEU GLY LEU GLY ILE MET GLY
SEQRES 2 G 287 GLY PRO MET ALA ALA ASN LEU VAL ARG ALA GLY PHE ASP
SEQRES 3 G 287 VAL THR VAL TRP ASN ARG ASN PRO ALA LYS CYS ALA PRO
SEQRES 4 G 287 LEU VAL ALA LEU GLY ALA ARG GLN ALA SER SER PRO ALA
SEQRES 5 G 287 GLU VAL CYS ALA ALA CYS ASP ILE THR ILE ALA MET LEU
SEQRES 6 G 287 ALA ASP PRO ALA ALA ALA ARG GLU VAL CYS PHE GLY ALA
SEQRES 7 G 287 ASN GLY VAL LEU GLU GLY ILE GLY GLY GLY ARG GLY TYR
SEQRES 8 G 287 ILE ASP MET SER THR VAL ASP ASP GLU THR SER THR ALA
SEQRES 9 G 287 ILE GLY ALA ALA VAL THR ALA ARG GLY GLY ARG PHE LEU
SEQRES 10 G 287 GLU ALA PRO VAL SER GLY THR LYS LYS PRO ALA GLU ASP
SEQRES 11 G 287 GLY THR LEU ILE ILE LEU ALA ALA GLY ASP GLN SER LEU
SEQRES 12 G 287 PHE THR ASP ALA GLY PRO ALA PHE ALA ALA LEU GLY LYS
SEQRES 13 G 287 LYS CYS LEU HIS LEU GLY GLU VAL GLY GLN GLY ALA ARG
SEQRES 14 G 287 MET LYS LEU VAL VAL ASN MET ILE MET GLY GLN MET MET
SEQRES 15 G 287 THR ALA LEU GLY GLU GLY MET ALA LEU GLY ARG ASN CYS
SEQRES 16 G 287 GLY LEU ASP GLY GLY GLN LEU LEU GLU VAL LEU ASP ALA
SEQRES 17 G 287 GLY ALA MET ALA ASN PRO MET PHE LYS GLY LYS GLY GLN
SEQRES 18 G 287 MET LEU LEU SER GLY GLU PHE PRO THR SER PHE PRO LEU
SEQRES 19 G 287 LYS HIS MET GLN LYS ASP LEU ARG LEU ALA VAL GLU LEU
SEQRES 20 G 287 GLY ASP ARG LEU GLY GLN PRO LEU HIS GLY ALA ALA THR
SEQRES 21 G 287 ALA ASN GLU SER PHE LYS ARG ALA ARG ALA ALA GLY HIS
SEQRES 22 G 287 ALA ASP GLU ASP PHE ALA ALA VAL PHE ARG VAL LEU GLU
SEQRES 23 G 287 ALA
SEQRES 1 H 287 MET THR THR TYR GLY PHE LEU GLY LEU GLY ILE MET GLY
SEQRES 2 H 287 GLY PRO MET ALA ALA ASN LEU VAL ARG ALA GLY PHE ASP
SEQRES 3 H 287 VAL THR VAL TRP ASN ARG ASN PRO ALA LYS CYS ALA PRO
SEQRES 4 H 287 LEU VAL ALA LEU GLY ALA ARG GLN ALA SER SER PRO ALA
SEQRES 5 H 287 GLU VAL CYS ALA ALA CYS ASP ILE THR ILE ALA MET LEU
SEQRES 6 H 287 ALA ASP PRO ALA ALA ALA ARG GLU VAL CYS PHE GLY ALA
SEQRES 7 H 287 ASN GLY VAL LEU GLU GLY ILE GLY GLY GLY ARG GLY TYR
SEQRES 8 H 287 ILE ASP MET SER THR VAL ASP ASP GLU THR SER THR ALA
SEQRES 9 H 287 ILE GLY ALA ALA VAL THR ALA ARG GLY GLY ARG PHE LEU
SEQRES 10 H 287 GLU ALA PRO VAL SER GLY THR LYS LYS PRO ALA GLU ASP
SEQRES 11 H 287 GLY THR LEU ILE ILE LEU ALA ALA GLY ASP GLN SER LEU
SEQRES 12 H 287 PHE THR ASP ALA GLY PRO ALA PHE ALA ALA LEU GLY LYS
SEQRES 13 H 287 LYS CYS LEU HIS LEU GLY GLU VAL GLY GLN GLY ALA ARG
SEQRES 14 H 287 MET LYS LEU VAL VAL ASN MET ILE MET GLY GLN MET MET
SEQRES 15 H 287 THR ALA LEU GLY GLU GLY MET ALA LEU GLY ARG ASN CYS
SEQRES 16 H 287 GLY LEU ASP GLY GLY GLN LEU LEU GLU VAL LEU ASP ALA
SEQRES 17 H 287 GLY ALA MET ALA ASN PRO MET PHE LYS GLY LYS GLY GLN
SEQRES 18 H 287 MET LEU LEU SER GLY GLU PHE PRO THR SER PHE PRO LEU
SEQRES 19 H 287 LYS HIS MET GLN LYS ASP LEU ARG LEU ALA VAL GLU LEU
SEQRES 20 H 287 GLY ASP ARG LEU GLY GLN PRO LEU HIS GLY ALA ALA THR
SEQRES 21 H 287 ALA ASN GLU SER PHE LYS ARG ALA ARG ALA ALA GLY HIS
SEQRES 22 H 287 ALA ASP GLU ASP PHE ALA ALA VAL PHE ARG VAL LEU GLU
SEQRES 23 H 287 ALA
HET NAP A 301 48
HET GOL A 304 6
HET GOL B 304 6
HET NAP B 301 48
HET GOL B 305 6
HET NAP C 301 48
HET GOL C 304 6
HET GOL C 288 6
HET NAP D 301 48
HET GOL D 305 6
HET NAP E 301 48
HET GOL E 304 6
HET NAP F 301 48
HET GOL F 304 6
HET GOL F 288 6
HET NAP G 301 48
HET GOL G 304 6
HET GOL H 305 6
HET NAP H 301 48
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM GOL GLYCEROL
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 9 NAP 8(C21 H28 N7 O17 P3)
FORMUL 10 GOL 11(C3 H8 O3)
FORMUL 28 HOH *1809(H2 O)
HELIX 1 1 MET A 12 GLY A 24 1 13
HELIX 2 2 ASN A 33 LYS A 36 5 4
HELIX 3 3 CYS A 37 GLY A 44 1 8
HELIX 4 4 SER A 50 CYS A 58 1 9
HELIX 5 5 ASP A 67 GLY A 77 1 11
HELIX 6 6 GLY A 80 GLY A 84 5 5
HELIX 7 7 ASP A 98 ARG A 112 1 15
HELIX 8 8 THR A 124 GLY A 131 1 8
HELIX 9 9 ASP A 140 ALA A 147 1 8
HELIX 10 10 ALA A 147 LEU A 154 1 8
HELIX 11 11 GLY A 165 CYS A 195 1 31
HELIX 12 12 ASP A 198 GLY A 209 1 12
HELIX 13 13 ASN A 213 GLY A 226 1 14
HELIX 14 14 PRO A 233 GLY A 252 1 20
HELIX 15 15 LEU A 255 ALA A 271 1 17
HELIX 16 16 ASP A 277 ALA A 280 5 4
HELIX 17 17 VAL A 281 GLU A 286 1 6
HELIX 18 18 MET B 12 ALA B 23 1 12
HELIX 19 19 ASN B 33 LYS B 36 5 4
HELIX 20 20 CYS B 37 GLY B 44 1 8
HELIX 21 21 SER B 50 CYS B 58 1 9
HELIX 22 22 ASP B 67 GLY B 77 1 11
HELIX 23 23 GLY B 80 GLY B 84 5 5
HELIX 24 24 ASP B 98 ARG B 112 1 15
HELIX 25 25 THR B 124 GLY B 131 1 8
HELIX 26 26 ASP B 140 ALA B 147 1 8
HELIX 27 27 ALA B 147 LEU B 154 1 8
HELIX 28 28 GLY B 165 CYS B 195 1 31
HELIX 29 29 ASP B 198 GLY B 209 1 12
HELIX 30 30 ASN B 213 GLY B 226 1 14
HELIX 31 31 PRO B 233 GLY B 252 1 20
HELIX 32 32 LEU B 255 ALA B 271 1 17
HELIX 33 33 ASP B 277 ALA B 280 5 4
HELIX 34 34 VAL B 281 GLU B 286 1 6
HELIX 35 35 MET C 12 ALA C 23 1 12
HELIX 36 36 ASN C 33 LYS C 36 5 4
HELIX 37 37 CYS C 37 GLY C 44 1 8
HELIX 38 38 SER C 50 CYS C 58 1 9
HELIX 39 39 ASP C 67 GLY C 77 1 11
HELIX 40 40 GLY C 80 GLY C 84 5 5
HELIX 41 41 ASP C 98 ARG C 112 1 15
HELIX 42 42 THR C 124 GLY C 131 1 8
HELIX 43 43 ASP C 140 ALA C 147 1 8
HELIX 44 44 ALA C 147 LEU C 154 1 8
HELIX 45 45 GLY C 165 CYS C 195 1 31
HELIX 46 46 ASP C 198 GLY C 209 1 12
HELIX 47 47 ASN C 213 GLY C 226 1 14
HELIX 48 48 PRO C 233 GLY C 252 1 20
HELIX 49 49 LEU C 255 ALA C 271 1 17
HELIX 50 50 ASP C 277 ALA C 280 5 4
HELIX 51 51 VAL C 281 GLU C 286 1 6
HELIX 52 52 MET D 12 GLY D 24 1 13
HELIX 53 53 ASN D 33 LYS D 36 5 4
HELIX 54 54 CYS D 37 GLY D 44 1 8
HELIX 55 55 SER D 50 CYS D 58 1 9
HELIX 56 56 ASP D 67 GLY D 77 1 11
HELIX 57 57 GLY D 80 GLY D 84 5 5
HELIX 58 58 ASP D 98 ARG D 112 1 15
HELIX 59 59 THR D 124 GLY D 131 1 8
HELIX 60 60 ASP D 140 ALA D 147 1 8
HELIX 61 61 ALA D 147 LEU D 154 1 8
HELIX 62 62 GLY D 165 CYS D 195 1 31
HELIX 63 63 ASP D 198 GLY D 209 1 12
HELIX 64 64 ASN D 213 GLY D 226 1 14
HELIX 65 65 PRO D 233 GLY D 252 1 20
HELIX 66 66 LEU D 255 ALA D 271 1 17
HELIX 67 67 ASP D 277 ALA D 280 5 4
HELIX 68 68 VAL D 281 GLU D 286 1 6
HELIX 69 69 MET E 12 GLY E 24 1 13
HELIX 70 70 ASN E 33 LYS E 36 5 4
HELIX 71 71 CYS E 37 GLY E 44 1 8
HELIX 72 72 SER E 50 CYS E 58 1 9
HELIX 73 73 ASP E 67 GLY E 77 1 11
HELIX 74 74 GLY E 80 GLY E 84 5 5
HELIX 75 75 ASP E 98 ARG E 112 1 15
HELIX 76 76 THR E 124 GLY E 131 1 8
HELIX 77 77 ASP E 140 ALA E 147 1 8
HELIX 78 78 ALA E 147 LEU E 154 1 8
HELIX 79 79 GLY E 165 CYS E 195 1 31
HELIX 80 80 ASP E 198 GLY E 209 1 12
HELIX 81 81 ASN E 213 GLY E 226 1 14
HELIX 82 82 PRO E 233 GLY E 252 1 20
HELIX 83 83 LEU E 255 ALA E 271 1 17
HELIX 84 84 ASP E 277 ALA E 280 5 4
HELIX 85 85 VAL E 281 GLU E 286 1 6
HELIX 86 86 MET F 12 ALA F 23 1 12
HELIX 87 87 ASN F 33 LYS F 36 5 4
HELIX 88 88 CYS F 37 GLY F 44 1 8
HELIX 89 89 SER F 50 CYS F 58 1 9
HELIX 90 90 ASP F 67 GLY F 77 1 11
HELIX 91 91 GLY F 80 ILE F 85 1 6
HELIX 92 92 ASP F 98 ARG F 112 1 15
HELIX 93 93 THR F 124 GLY F 131 1 8
HELIX 94 94 ASP F 140 ALA F 147 1 8
HELIX 95 95 ALA F 147 LEU F 154 1 8
HELIX 96 96 GLY F 165 CYS F 195 1 31
HELIX 97 97 ASP F 198 GLY F 209 1 12
HELIX 98 98 ASN F 213 GLY F 226 1 14
HELIX 99 99 PRO F 233 GLY F 252 1 20
HELIX 100 100 LEU F 255 ALA F 271 1 17
HELIX 101 101 ASP F 277 ALA F 280 5 4
HELIX 102 102 VAL F 281 GLU F 286 1 6
HELIX 103 103 MET G 12 ALA G 23 1 12
HELIX 104 104 ASN G 33 LYS G 36 5 4
HELIX 105 105 CYS G 37 GLY G 44 1 8
HELIX 106 106 SER G 50 CYS G 58 1 9
HELIX 107 107 ASP G 67 GLY G 77 1 11
HELIX 108 108 GLY G 80 ILE G 85 1 6
HELIX 109 109 ASP G 98 ARG G 112 1 15
HELIX 110 110 THR G 124 GLY G 131 1 8
HELIX 111 111 ASP G 140 ALA G 147 1 8
HELIX 112 112 ALA G 147 LEU G 154 1 8
HELIX 113 113 GLY G 165 CYS G 195 1 31
HELIX 114 114 ASP G 198 GLY G 209 1 12
HELIX 115 115 ASN G 213 GLY G 226 1 14
HELIX 116 116 PRO G 233 GLY G 252 1 20
HELIX 117 117 LEU G 255 ALA G 271 1 17
HELIX 118 118 ASP G 277 ALA G 280 5 4
HELIX 119 119 VAL G 281 GLU G 286 1 6
HELIX 120 120 MET H 12 ALA H 23 1 12
HELIX 121 121 ASN H 33 LYS H 36 5 4
HELIX 122 122 CYS H 37 GLY H 44 1 8
HELIX 123 123 SER H 50 CYS H 58 1 9
HELIX 124 124 ASP H 67 GLY H 77 1 11
HELIX 125 125 GLY H 80 ILE H 85 1 6
HELIX 126 126 ASP H 98 ARG H 112 1 15
HELIX 127 127 THR H 124 GLY H 131 1 8
HELIX 128 128 ASP H 140 ALA H 147 1 8
HELIX 129 129 ALA H 147 LEU H 154 1 8
HELIX 130 130 GLY H 165 CYS H 195 1 31
HELIX 131 131 ASP H 198 ALA H 208 1 11
HELIX 132 132 ASN H 213 GLY H 226 1 14
HELIX 133 133 PRO H 233 GLY H 252 1 20
HELIX 134 134 LEU H 255 ALA H 271 1 17
HELIX 135 135 ASP H 277 ALA H 280 5 4
HELIX 136 136 VAL H 281 GLU H 286 1 6
SHEET 1 A 8 ARG A 46 GLN A 47 0
SHEET 2 A 8 VAL A 27 TRP A 30 1 N VAL A 29 O ARG A 46
SHEET 3 A 8 TYR A 4 LEU A 7 1 N TYR A 4 O THR A 28
SHEET 4 A 8 ILE A 60 ALA A 63 1 O ILE A 62 N LEU A 7
SHEET 5 A 8 GLY A 90 ASP A 93 1 O ILE A 92 N THR A 61
SHEET 6 A 8 ARG A 115 GLU A 118 1 O ARG A 115 N TYR A 91
SHEET 7 A 8 LEU A 133 GLY A 139 -1 O ALA A 138 N GLU A 118
SHEET 8 A 8 VAL A 121 SER A 122 -1 N SER A 122 O ILE A 134
SHEET 1 B 8 ARG A 46 GLN A 47 0
SHEET 2 B 8 VAL A 27 TRP A 30 1 N VAL A 29 O ARG A 46
SHEET 3 B 8 TYR A 4 LEU A 7 1 N TYR A 4 O THR A 28
SHEET 4 B 8 ILE A 60 ALA A 63 1 O ILE A 62 N LEU A 7
SHEET 5 B 8 GLY A 90 ASP A 93 1 O ILE A 92 N THR A 61
SHEET 6 B 8 ARG A 115 GLU A 118 1 O ARG A 115 N TYR A 91
SHEET 7 B 8 LEU A 133 GLY A 139 -1 O ALA A 138 N GLU A 118
SHEET 8 B 8 GLY A 155 HIS A 160 1 O LYS A 157 N ILE A 135
SHEET 1 C 8 ARG B 46 GLN B 47 0
SHEET 2 C 8 ASP B 26 TRP B 30 1 N VAL B 27 O ARG B 46
SHEET 3 C 8 THR B 3 LEU B 7 1 N TYR B 4 O ASP B 26
SHEET 4 C 8 ILE B 60 ALA B 63 1 O ILE B 62 N LEU B 7
SHEET 5 C 8 GLY B 90 ASP B 93 1 O ILE B 92 N THR B 61
SHEET 6 C 8 ARG B 115 GLU B 118 1 O ARG B 115 N TYR B 91
SHEET 7 C 8 LEU B 133 GLY B 139 -1 O ALA B 138 N GLU B 118
SHEET 8 C 8 VAL B 121 SER B 122 -1 N SER B 122 O ILE B 134
SHEET 1 D 8 ARG B 46 GLN B 47 0
SHEET 2 D 8 ASP B 26 TRP B 30 1 N VAL B 27 O ARG B 46
SHEET 3 D 8 THR B 3 LEU B 7 1 N TYR B 4 O ASP B 26
SHEET 4 D 8 ILE B 60 ALA B 63 1 O ILE B 62 N LEU B 7
SHEET 5 D 8 GLY B 90 ASP B 93 1 O ILE B 92 N THR B 61
SHEET 6 D 8 ARG B 115 GLU B 118 1 O ARG B 115 N TYR B 91
SHEET 7 D 8 LEU B 133 GLY B 139 -1 O ALA B 138 N GLU B 118
SHEET 8 D 8 GLY B 155 HIS B 160 1 O LYS B 157 N ILE B 135
SHEET 1 E 8 ARG C 46 GLN C 47 0
SHEET 2 E 8 ASP C 26 TRP C 30 1 N VAL C 29 O ARG C 46
SHEET 3 E 8 THR C 3 LEU C 7 1 N TYR C 4 O ASP C 26
SHEET 4 E 8 ILE C 60 ALA C 63 1 O ILE C 62 N GLY C 5
SHEET 5 E 8 GLY C 90 ASP C 93 1 O ILE C 92 N THR C 61
SHEET 6 E 8 ARG C 115 GLU C 118 1 O ARG C 115 N TYR C 91
SHEET 7 E 8 LEU C 133 GLY C 139 -1 O ALA C 138 N GLU C 118
SHEET 8 E 8 VAL C 121 SER C 122 -1 N SER C 122 O ILE C 134
SHEET 1 F 8 ARG C 46 GLN C 47 0
SHEET 2 F 8 ASP C 26 TRP C 30 1 N VAL C 29 O ARG C 46
SHEET 3 F 8 THR C 3 LEU C 7 1 N TYR C 4 O ASP C 26
SHEET 4 F 8 ILE C 60 ALA C 63 1 O ILE C 62 N GLY C 5
SHEET 5 F 8 GLY C 90 ASP C 93 1 O ILE C 92 N THR C 61
SHEET 6 F 8 ARG C 115 GLU C 118 1 O ARG C 115 N TYR C 91
SHEET 7 F 8 LEU C 133 GLY C 139 -1 O ALA C 138 N GLU C 118
SHEET 8 F 8 GLY C 155 HIS C 160 1 O LYS C 157 N ILE C 135
SHEET 1 G 8 ARG D 46 GLN D 47 0
SHEET 2 G 8 VAL D 27 TRP D 30 1 N VAL D 29 O ARG D 46
SHEET 3 G 8 TYR D 4 LEU D 7 1 N TYR D 4 O THR D 28
SHEET 4 G 8 ILE D 60 ALA D 63 1 O ILE D 62 N LEU D 7
SHEET 5 G 8 GLY D 90 ASP D 93 1 O ILE D 92 N THR D 61
SHEET 6 G 8 ARG D 115 GLU D 118 1 O ARG D 115 N TYR D 91
SHEET 7 G 8 LEU D 133 GLY D 139 -1 O ALA D 138 N GLU D 118
SHEET 8 G 8 VAL D 121 SER D 122 -1 N SER D 122 O ILE D 134
SHEET 1 H 8 ARG D 46 GLN D 47 0
SHEET 2 H 8 VAL D 27 TRP D 30 1 N VAL D 29 O ARG D 46
SHEET 3 H 8 TYR D 4 LEU D 7 1 N TYR D 4 O THR D 28
SHEET 4 H 8 ILE D 60 ALA D 63 1 O ILE D 62 N LEU D 7
SHEET 5 H 8 GLY D 90 ASP D 93 1 O ILE D 92 N THR D 61
SHEET 6 H 8 ARG D 115 GLU D 118 1 O ARG D 115 N TYR D 91
SHEET 7 H 8 LEU D 133 GLY D 139 -1 O ALA D 138 N GLU D 118
SHEET 8 H 8 GLY D 155 HIS D 160 1 O LYS D 157 N ILE D 135
SHEET 1 I 8 ARG E 46 GLN E 47 0
SHEET 2 I 8 VAL E 27 TRP E 30 1 N VAL E 29 O ARG E 46
SHEET 3 I 8 TYR E 4 LEU E 7 1 N TYR E 4 O THR E 28
SHEET 4 I 8 ILE E 60 ALA E 63 1 O ILE E 62 N LEU E 7
SHEET 5 I 8 GLY E 90 ASP E 93 1 O ILE E 92 N THR E 61
SHEET 6 I 8 ARG E 115 GLU E 118 1 O ARG E 115 N TYR E 91
SHEET 7 I 8 LEU E 133 GLY E 139 -1 O ALA E 138 N GLU E 118
SHEET 8 I 8 VAL E 121 SER E 122 -1 N SER E 122 O ILE E 134
SHEET 1 J 8 ARG E 46 GLN E 47 0
SHEET 2 J 8 VAL E 27 TRP E 30 1 N VAL E 29 O ARG E 46
SHEET 3 J 8 TYR E 4 LEU E 7 1 N TYR E 4 O THR E 28
SHEET 4 J 8 ILE E 60 ALA E 63 1 O ILE E 62 N LEU E 7
SHEET 5 J 8 GLY E 90 ASP E 93 1 O ILE E 92 N THR E 61
SHEET 6 J 8 ARG E 115 GLU E 118 1 O ARG E 115 N TYR E 91
SHEET 7 J 8 LEU E 133 GLY E 139 -1 O ALA E 138 N GLU E 118
SHEET 8 J 8 GLY E 155 HIS E 160 1 O LYS E 157 N ILE E 135
SHEET 1 K 8 ARG F 46 GLN F 47 0
SHEET 2 K 8 VAL F 27 TRP F 30 1 N VAL F 29 O ARG F 46
SHEET 3 K 8 TYR F 4 LEU F 7 1 N TYR F 4 O THR F 28
SHEET 4 K 8 ILE F 60 ALA F 63 1 O ILE F 62 N LEU F 7
SHEET 5 K 8 GLY F 90 ASP F 93 1 O ILE F 92 N THR F 61
SHEET 6 K 8 ARG F 115 GLU F 118 1 O ARG F 115 N TYR F 91
SHEET 7 K 8 LEU F 133 GLY F 139 -1 O ALA F 138 N GLU F 118
SHEET 8 K 8 VAL F 121 SER F 122 -1 N SER F 122 O ILE F 134
SHEET 1 L 8 ARG F 46 GLN F 47 0
SHEET 2 L 8 VAL F 27 TRP F 30 1 N VAL F 29 O ARG F 46
SHEET 3 L 8 TYR F 4 LEU F 7 1 N TYR F 4 O THR F 28
SHEET 4 L 8 ILE F 60 ALA F 63 1 O ILE F 62 N LEU F 7
SHEET 5 L 8 GLY F 90 ASP F 93 1 O ILE F 92 N THR F 61
SHEET 6 L 8 ARG F 115 GLU F 118 1 O ARG F 115 N TYR F 91
SHEET 7 L 8 LEU F 133 GLY F 139 -1 O ALA F 138 N GLU F 118
SHEET 8 L 8 GLY F 155 HIS F 160 1 O LYS F 157 N ILE F 135
SHEET 1 M 8 ARG G 46 GLN G 47 0
SHEET 2 M 8 VAL G 27 TRP G 30 1 N VAL G 29 O ARG G 46
SHEET 3 M 8 TYR G 4 LEU G 7 1 N PHE G 6 O THR G 28
SHEET 4 M 8 ILE G 60 ALA G 63 1 O ILE G 62 N GLY G 5
SHEET 5 M 8 GLY G 90 ASP G 93 1 O ILE G 92 N THR G 61
SHEET 6 M 8 ARG G 115 GLU G 118 1 O ARG G 115 N TYR G 91
SHEET 7 M 8 LEU G 133 GLY G 139 -1 O ALA G 138 N GLU G 118
SHEET 8 M 8 VAL G 121 SER G 122 -1 N SER G 122 O ILE G 134
SHEET 1 N 8 ARG G 46 GLN G 47 0
SHEET 2 N 8 VAL G 27 TRP G 30 1 N VAL G 29 O ARG G 46
SHEET 3 N 8 TYR G 4 LEU G 7 1 N PHE G 6 O THR G 28
SHEET 4 N 8 ILE G 60 ALA G 63 1 O ILE G 62 N GLY G 5
SHEET 5 N 8 GLY G 90 ASP G 93 1 O ILE G 92 N THR G 61
SHEET 6 N 8 ARG G 115 GLU G 118 1 O ARG G 115 N TYR G 91
SHEET 7 N 8 LEU G 133 GLY G 139 -1 O ALA G 138 N GLU G 118
SHEET 8 N 8 GLY G 155 HIS G 160 1 O LYS G 157 N ILE G 135
SHEET 1 O 8 ARG H 46 GLN H 47 0
SHEET 2 O 8 ASP H 26 TRP H 30 1 N VAL H 29 O ARG H 46
SHEET 3 O 8 THR H 3 LEU H 7 1 N TYR H 4 O ASP H 26
SHEET 4 O 8 ILE H 60 ALA H 63 1 O ILE H 62 N LEU H 7
SHEET 5 O 8 GLY H 90 ASP H 93 1 O ILE H 92 N THR H 61
SHEET 6 O 8 ARG H 115 GLU H 118 1 O ARG H 115 N TYR H 91
SHEET 7 O 8 LEU H 133 GLY H 139 -1 O ALA H 138 N GLU H 118
SHEET 8 O 8 VAL H 121 SER H 122 -1 N SER H 122 O ILE H 134
SHEET 1 P 8 ARG H 46 GLN H 47 0
SHEET 2 P 8 ASP H 26 TRP H 30 1 N VAL H 29 O ARG H 46
SHEET 3 P 8 THR H 3 LEU H 7 1 N TYR H 4 O ASP H 26
SHEET 4 P 8 ILE H 60 ALA H 63 1 O ILE H 62 N LEU H 7
SHEET 5 P 8 GLY H 90 ASP H 93 1 O ILE H 92 N THR H 61
SHEET 6 P 8 ARG H 115 GLU H 118 1 O ARG H 115 N TYR H 91
SHEET 7 P 8 LEU H 133 GLY H 139 -1 O ALA H 138 N GLU H 118
SHEET 8 P 8 GLY H 155 HIS H 160 1 O LYS H 157 N ILE H 135
SITE 1 AC1 36 GLY A 8 LEU A 9 GLY A 10 ILE A 11
SITE 2 AC1 36 MET A 12 ASN A 31 ARG A 32 ASN A 33
SITE 3 AC1 36 MET A 64 LEU A 65 ALA A 66 ALA A 70
SITE 4 AC1 36 GLU A 73 VAL A 74 THR A 96 VAL A 121
SITE 5 AC1 36 GLY A 123 THR A 124 LYS A 125 LYS A 171
SITE 6 AC1 36 SER A 231 PHE A 232 PRO A 233 HIS A 236
SITE 7 AC1 36 LYS A 239 HOH A 308 HOH A 310 HOH A 325
SITE 8 AC1 36 HOH A 362 HOH A 437 HOH A 560 HOH A 630
SITE 9 AC1 36 HOH A 740 HOH A1011 HOH A1186 HOH A1423
SITE 1 AC2 4 ARG A 250 HOH A 410 ARG B 242 GLU B 246
SITE 1 AC3 6 ARG A 242 GLU A 246 HOH A 754 ARG B 250
SITE 2 AC3 6 HOH B1791 HOH B1797
SITE 1 AC4 33 GLY B 8 LEU B 9 GLY B 10 ILE B 11
SITE 2 AC4 33 MET B 12 ASN B 31 ARG B 32 ASN B 33
SITE 3 AC4 33 MET B 64 LEU B 65 ALA B 66 ALA B 70
SITE 4 AC4 33 GLU B 73 VAL B 74 THR B 96 VAL B 121
SITE 5 AC4 33 GLY B 123 THR B 124 SER B 231 PHE B 232
SITE 6 AC4 33 HIS B 236 LYS B 239 HOH B 292 HOH B 296
SITE 7 AC4 33 HOH B 317 HOH B 555 HOH B 564 HOH B 603
SITE 8 AC4 33 HOH B 918 HOH B 925 HOH B1116 HOH B1534
SITE 9 AC4 33 HOH B1589
SITE 1 AC5 8 GLY B 131 GLY B 155 LYS B 156 HOH B 303
SITE 2 AC5 8 HOH B 312 HOH B 539 HOH B 541 HOH B 760
SITE 1 AC6 32 GLY C 8 LEU C 9 GLY C 10 ILE C 11
SITE 2 AC6 32 MET C 12 ASN C 31 ARG C 32 ASN C 33
SITE 3 AC6 32 MET C 64 LEU C 65 ALA C 66 ALA C 70
SITE 4 AC6 32 GLU C 73 VAL C 74 THR C 96 VAL C 121
SITE 5 AC6 32 GLY C 123 THR C 124 LYS C 171 SER C 231
SITE 6 AC6 32 PHE C 232 HIS C 236 LYS C 239 HOH C 297
SITE 7 AC6 32 HOH C 314 HOH C 818 HOH C 971 HOH C1099
SITE 8 AC6 32 HOH C1102 HOH C1510 HOH C1557 HOH C1567
SITE 1 AC7 4 ARG C 242 GLU C 246 HOH C 474 ARG D 250
SITE 1 AC8 4 ARG C 250 HOH C 581 ARG D 242 GLU D 246
SITE 1 AC9 34 GLY D 8 LEU D 9 GLY D 10 ILE D 11
SITE 2 AC9 34 MET D 12 ASN D 31 ARG D 32 ASN D 33
SITE 3 AC9 34 LYS D 36 MET D 64 LEU D 65 ALA D 66
SITE 4 AC9 34 ALA D 70 GLU D 73 VAL D 74 THR D 96
SITE 5 AC9 34 VAL D 121 GLY D 123 THR D 124 LYS D 171
SITE 6 AC9 34 SER D 231 PHE D 232 PRO D 233 HIS D 236
SITE 7 AC9 34 LYS D 239 HOH D 296 HOH D 312 HOH D 316
SITE 8 AC9 34 HOH D 339 HOH D 554 HOH D 800 HOH D 938
SITE 9 AC9 34 HOH D1097 HOH D1439
SITE 1 BC1 7 GLU D 227 PHE D 228 PRO D 229 GLU D 276
SITE 2 BC1 7 HOH D 656 ALA F 52 ASN F 79
SITE 1 BC2 33 GLY E 8 LEU E 9 GLY E 10 ILE E 11
SITE 2 BC2 33 MET E 12 ASN E 31 ARG E 32 ASN E 33
SITE 3 BC2 33 MET E 64 LEU E 65 ALA E 66 ALA E 70
SITE 4 BC2 33 GLU E 73 VAL E 74 THR E 96 VAL E 121
SITE 5 BC2 33 GLY E 123 THR E 124 SER E 231 PHE E 232
SITE 6 BC2 33 PRO E 233 HIS E 236 LYS E 239 HOH E 317
SITE 7 BC2 33 HOH E 451 HOH E 913 HOH E1016 HOH E1081
SITE 8 BC2 33 HOH E1109 HOH E1132 HOH E1284 HOH E1498
SITE 9 BC2 33 HOH E1598
SITE 1 BC3 6 ARG E 242 GLU E 246 HOH E1345 GLU G 246
SITE 2 BC3 6 ARG G 250 HOH G 717
SITE 1 BC4 35 GLY F 8 LEU F 9 GLY F 10 ILE F 11
SITE 2 BC4 35 MET F 12 ASN F 31 ARG F 32 ASN F 33
SITE 3 BC4 35 MET F 64 LEU F 65 ALA F 66 ALA F 70
SITE 4 BC4 35 GLU F 73 VAL F 74 THR F 96 VAL F 121
SITE 5 BC4 35 GLY F 123 THR F 124 SER F 231 PHE F 232
SITE 6 BC4 35 PRO F 233 HIS F 236 LYS F 239 HOH F 292
SITE 7 BC4 35 HOH F 293 HOH F 339 HOH F 348 HOH F 350
SITE 8 BC4 35 HOH F 456 HOH F 466 HOH F 478 HOH F 617
SITE 9 BC4 35 HOH F 779 HOH F1009 HOH F1021
SITE 1 BC5 4 ARG F 242 GLU F 246 HOH F 766 ARG H 250
SITE 1 BC6 6 GLU F 246 ARG F 250 HOH F1104 ARG H 242
SITE 2 BC6 6 GLU H 246 HOH H 330
SITE 1 BC7 28 GLY G 8 LEU G 9 GLY G 10 ILE G 11
SITE 2 BC7 28 MET G 12 ASN G 31 ARG G 32 ASN G 33
SITE 3 BC7 28 MET G 64 LEU G 65 ALA G 66 ALA G 70
SITE 4 BC7 28 GLU G 73 VAL G 74 THR G 96 VAL G 121
SITE 5 BC7 28 GLY G 123 THR G 124 LYS G 171 SER G 231
SITE 6 BC7 28 PHE G 232 PRO G 233 HIS G 236 LYS G 239
SITE 7 BC7 28 HOH G 294 HOH G 593 HOH G 857 HOH G1495
SITE 1 BC8 4 ARG E 250 HOH E1178 ARG G 242 GLU G 246
SITE 1 BC9 9 HOH B 541 HOH B 773 ASN H 19 ASP H 130
SITE 2 BC9 9 ALA H 152 ALA H 153 HOH H 477 HOH H 540
SITE 3 BC9 9 HOH H1018
SITE 1 CC1 35 GLY H 8 LEU H 9 GLY H 10 ILE H 11
SITE 2 CC1 35 MET H 12 ASN H 31 ARG H 32 ASN H 33
SITE 3 CC1 35 MET H 64 LEU H 65 ALA H 66 ALA H 70
SITE 4 CC1 35 GLU H 73 VAL H 74 THR H 96 VAL H 121
SITE 5 CC1 35 GLY H 123 THR H 124 SER H 231 PHE H 232
SITE 6 CC1 35 PRO H 233 HIS H 236 LYS H 239 HOH H 314
SITE 7 CC1 35 HOH H 319 HOH H 321 HOH H 322 HOH H 325
SITE 8 CC1 35 HOH H 331 HOH H 395 HOH H 484 HOH H 759
SITE 9 CC1 35 HOH H 876 HOH H1064 HOH H1206
CRYST1 100.034 182.070 147.172 90.00 90.00 90.00 P 21 21 2 32
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 0.009997 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005492 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006795 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
