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HEADER HYDROLASE/HYDROLASE INHIBITOR 07-MAY-12 4F21
TITLE CRYSTAL STRUCTURE OF CARBOXYLESTERASE/PHOSPHOLIPASE FAMILY PROTEIN
TITLE 2 FROM FRANCISELLA TULARENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE/PHOSPHOLIPASE FAMILY PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FRANCISELLA TULARENSIS SUBSP. TULARENSIS;
SOURCE 3 ORGANISM_TAXID: 177416;
SOURCE 4 STRAIN: SCHU S4 / SCHU 4;
SOURCE 5 GENE: FTT_0258;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, NIAID, NATIONAL INSTITUTE OF ALLERGY AND
KEYWDS 2 INFECTIOUS DISEASES, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
KEYWDS 3 DISEASES, CSGID, CARBOXYLESTERASE, PHOSPHOLIPASE, HYDROLASE-
KEYWDS 4 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.V.FILIPPOVA,G.MINASOV,KUHN M.,Z.WAWRZAK,SHUVALOVA L.,I.DUBROVSKA,
AUTHOR 2 J.R.WINSOR,O.KIRYUKHINA,D.P.BECKER,N.ARMOUSH,W.F.ANDERSON,CENTER FOR
AUTHOR 3 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 1 29-AUG-12 4F21 0
JRNL AUTH L.A.WESTON,M.KUHN,A.M.GEHRING,E.V.FILIPPOVA,G.MINASOV,
JRNL AUTH 2 Z.WAWRZAK,L.SHUVALOVA,I.DUBROVSKA,J.R.WINSOR,O.KIRYUKHINA,
JRNL AUTH 3 L.D.LAVIS,C.T.ADKINS,N.ARMOUSH,J.R.JOHNSON,D.P.BECKER,
JRNL AUTH 4 W.F.ANDERSON
JRNL TITL CRYSTAL STRUCTURE OF CARBOXYLESTERASE/PHOSPHOLIPASE FAMILY
JRNL TITL 2 PROTEIN FROM FRANCISELLA TULARENSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.46
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 3 NUMBER OF REFLECTIONS : 57489
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.170
REMARK 3 FREE R VALUE TEST SET COUNT : 2972
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 25.5195 - 6.7474 0.94 2889 144 0.1865 0.2418
REMARK 3 2 6.7474 - 5.3720 0.95 2861 138 0.2104 0.2539
REMARK 3 3 5.3720 - 4.6977 0.94 2904 148 0.1816 0.2233
REMARK 3 4 4.6977 - 4.2704 0.93 2789 162 0.1459 0.1923
REMARK 3 5 4.2704 - 3.9655 0.93 2862 150 0.1605 0.2078
REMARK 3 6 3.9655 - 3.7325 0.75 2273 134 0.1569 0.2232
REMARK 3 7 3.7325 - 3.5461 0.38 1143 62 0.1489 0.2938
REMARK 3 8 3.5461 - 3.3921 0.92 2781 157 0.1787 0.2818
REMARK 3 9 3.3921 - 3.2618 0.93 2881 167 0.1942 0.2684
REMARK 3 10 3.2618 - 3.1494 0.94 2852 128 0.2102 0.2933
REMARK 3 11 3.1494 - 3.0511 0.93 2848 150 0.2139 0.3011
REMARK 3 12 3.0511 - 2.9640 0.93 2817 162 0.2279 0.2569
REMARK 3 13 2.9640 - 2.8861 0.93 2864 159 0.2300 0.3152
REMARK 3 14 2.8861 - 2.8158 0.93 2761 157 0.2546 0.3023
REMARK 3 15 2.8158 - 2.7518 0.93 2902 150 0.2761 0.3644
REMARK 3 16 2.7518 - 2.6933 0.92 2757 164 0.2600 0.2922
REMARK 3 17 2.6933 - 2.6395 0.93 2890 140 0.2595 0.3358
REMARK 3 18 2.6395 - 2.5898 0.92 2812 160 0.2818 0.3525
REMARK 3 19 2.5898 - 2.5436 0.93 2814 133 0.2815 0.3447
REMARK 3 20 2.5436 - 2.5000 0.93 2832 140 0.2826 0.3273
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 : 0.31
REMARK 3 B_SOL : 38.63
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.740
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.40180
REMARK 3 B22 (A**2) : -17.29510
REMARK 3 B33 (A**2) : 14.89320
REMARK 3 B12 (A**2) : 0.79930
REMARK 3 B13 (A**2) : -0.96680
REMARK 3 B23 (A**2) : -1.67650
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 13560
REMARK 3 ANGLE : 0.802 18322
REMARK 3 CHIRALITY : 0.052 2080
REMARK 3 PLANARITY : 0.003 2322
REMARK 3 DIHEDRAL : 14.794 4879
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 47
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resseq -1:42)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.7900 7.2822 -0.4596
REMARK 3 T TENSOR
REMARK 3 T11: 0.1611 T22: 0.2368
REMARK 3 T33: 0.1036 T12: -0.0245
REMARK 3 T13: -0.0519 T23: -0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 0.6590 L22: 1.0355
REMARK 3 L33: 2.6640 L12: -0.3266
REMARK 3 L13: 1.0156 L23: 0.4773
REMARK 3 S TENSOR
REMARK 3 S11: -0.0621 S12: 0.1353 S13: 0.1896
REMARK 3 S21: 0.1074 S22: -0.0196 S23: -0.0475
REMARK 3 S31: -0.1553 S32: 0.0587 S33: 0.0850
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resseq 43:82)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8953 2.2896 -6.6420
REMARK 3 T TENSOR
REMARK 3 T11: 0.1267 T22: 0.3313
REMARK 3 T33: 0.0908 T12: -0.0097
REMARK 3 T13: 0.0577 T23: -0.0250
REMARK 3 L TENSOR
REMARK 3 L11: 1.2710 L22: 0.3189
REMARK 3 L33: 1.4088 L12: -0.3444
REMARK 3 L13: -1.3065 L23: 0.4758
REMARK 3 S TENSOR
REMARK 3 S11: 0.2148 S12: -0.1081 S13: 0.2706
REMARK 3 S21: -0.0195 S22: 0.1062 S23: -0.1222
REMARK 3 S31: -0.2826 S32: 0.2618 S33: -0.1519
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resseq 83:103)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.9706 9.8484 8.5108
REMARK 3 T TENSOR
REMARK 3 T11: 0.2055 T22: 0.2458
REMARK 3 T33: 0.2194 T12: 0.0049
REMARK 3 T13: -0.1078 T23: -0.1563
REMARK 3 L TENSOR
REMARK 3 L11: 6.6833 L22: 2.9207
REMARK 3 L33: 6.2335 L12: -3.2569
REMARK 3 L13: -5.5930 L23: 3.0129
REMARK 3 S TENSOR
REMARK 3 S11: 0.1585 S12: -0.0023 S13: 0.1427
REMARK 3 S21: -0.2423 S22: 0.1531 S23: -0.1693
REMARK 3 S31: -0.3289 S32: 0.5151 S33: -0.1659
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'A' and (resseq 105:174)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8238 -2.6343 3.3698
REMARK 3 T TENSOR
REMARK 3 T11: 0.0672 T22: 0.3388
REMARK 3 T33: 0.0333 T12: 0.0963
REMARK 3 T13: 0.0160 T23: -0.0615
REMARK 3 L TENSOR
REMARK 3 L11: 0.3276 L22: 0.3365
REMARK 3 L33: 0.8920 L12: -0.0407
REMARK 3 L13: -0.5362 L23: 0.1052
REMARK 3 S TENSOR
REMARK 3 S11: -0.0271 S12: -0.2231 S13: 0.0079
REMARK 3 S21: 0.1448 S22: 0.1000 S23: -0.0807
REMARK 3 S31: -0.0080 S32: 0.3240 S33: -0.0637
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'A' and (resseq 175:222)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0791 -9.0410 -2.6911
REMARK 3 T TENSOR
REMARK 3 T11: 0.0169 T22: 0.1965
REMARK 3 T33: 0.0655 T12: -0.0120
REMARK 3 T13: -0.0410 T23: -0.0391
REMARK 3 L TENSOR
REMARK 3 L11: 0.1430 L22: 0.7111
REMARK 3 L33: 1.2415 L12: 0.2650
REMARK 3 L13: -0.0667 L23: 0.3832
REMARK 3 S TENSOR
REMARK 3 S11: -0.0131 S12: -0.0657 S13: -0.1325
REMARK 3 S21: 0.1186 S22: 0.0569 S23: -0.1870
REMARK 3 S31: 0.1744 S32: 0.1659 S33: -0.1029
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'B' and (resseq -1:57)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3211 -30.1502 68.4920
REMARK 3 T TENSOR
REMARK 3 T11: 0.0907 T22: 0.1530
REMARK 3 T33: 0.0179 T12: -0.0526
REMARK 3 T13: -0.0251 T23: 0.0347
REMARK 3 L TENSOR
REMARK 3 L11: 2.0231 L22: 1.9627
REMARK 3 L33: 2.3098 L12: -0.7572
REMARK 3 L13: 0.1988 L23: 0.5175
REMARK 3 S TENSOR
REMARK 3 S11: 0.0950 S12: -0.0146 S13: 0.2128
REMARK 3 S21: -0.1512 S22: -0.0391 S23: -0.2331
REMARK 3 S31: -0.1982 S32: 0.1274 S33: 0.0687
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain 'B' and (resseq 58:82)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.5766 -41.0124 59.1749
REMARK 3 T TENSOR
REMARK 3 T11: 0.2203 T22: 0.3713
REMARK 3 T33: 0.1791 T12: -0.0890
REMARK 3 T13: -0.1213 T23: -0.0916
REMARK 3 L TENSOR
REMARK 3 L11: 0.6910 L22: 2.3853
REMARK 3 L33: 3.1511 L12: 0.9328
REMARK 3 L13: 0.8236 L23: 1.6933
REMARK 3 S TENSOR
REMARK 3 S11: -0.0266 S12: -0.4218 S13: 0.1915
REMARK 3 S21: 0.3542 S22: -0.1274 S23: -0.0571
REMARK 3 S31: -0.1669 S32: -0.1769 S33: -0.0525
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: chain 'B' and (resseq 83:174)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.2079 -37.7818 73.7774
REMARK 3 T TENSOR
REMARK 3 T11: 0.0197 T22: 0.2177
REMARK 3 T33: -0.0358 T12: 0.0152
REMARK 3 T13: -0.1611 T23: -0.1161
REMARK 3 L TENSOR
REMARK 3 L11: 0.1980 L22: 0.2751
REMARK 3 L33: 0.4994 L12: 0.0423
REMARK 3 L13: 0.2157 L23: 0.2103
REMARK 3 S TENSOR
REMARK 3 S11: -0.0309 S12: -0.0690 S13: 0.0783
REMARK 3 S21: 0.1131 S22: 0.0229 S23: -0.0991
REMARK 3 S31: -0.0695 S32: 0.1894 S33: 0.0250
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: chain 'B' and (resseq 175:222)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6276 -47.2849 66.7567
REMARK 3 T TENSOR
REMARK 3 T11: 0.0184 T22: 0.2589
REMARK 3 T33: 0.0376 T12: 0.0473
REMARK 3 T13: -0.0140 T23: -0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 0.0703 L22: 0.3837
REMARK 3 L33: 1.5688 L12: -0.0090
REMARK 3 L13: 0.2262 L23: 0.0925
REMARK 3 S TENSOR
REMARK 3 S11: -0.0655 S12: 0.0033 S13: -0.0186
REMARK 3 S21: 0.0494 S22: 0.0771 S23: -0.0064
REMARK 3 S31: 0.1282 S32: 0.0647 S33: -0.0094
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: chain 'C' and (resseq -1:42)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.9217 -15.2657 -31.3589
REMARK 3 T TENSOR
REMARK 3 T11: 0.0099 T22: 0.1357
REMARK 3 T33: -0.0260 T12: -0.1510
REMARK 3 T13: -0.0143 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 0.6057 L22: 0.5285
REMARK 3 L33: 1.6844 L12: 0.0098
REMARK 3 L13: 0.6269 L23: 0.0954
REMARK 3 S TENSOR
REMARK 3 S11: -0.0187 S12: 0.1165 S13: -0.0188
REMARK 3 S21: 0.0264 S22: -0.0346 S23: -0.0192
REMARK 3 S31: -0.0150 S32: 0.0399 S33: -0.0726
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: chain 'C' and (resseq 43:58)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4948 -17.2321 -30.0908
REMARK 3 T TENSOR
REMARK 3 T11: 0.0760 T22: 0.1763
REMARK 3 T33: 0.0317 T12: -0.0406
REMARK 3 T13: 0.0030 T23: 0.0420
REMARK 3 L TENSOR
REMARK 3 L11: 1.8353 L22: 0.9759
REMARK 3 L33: 2.0039 L12: 0.1866
REMARK 3 L13: -0.6365 L23: -0.7806
REMARK 3 S TENSOR
REMARK 3 S11: 0.0270 S12: -0.2419 S13: -0.0488
REMARK 3 S21: 0.0985 S22: -0.1118 S23: -0.1503
REMARK 3 S31: -0.1080 S32: 0.3678 S33: 0.1169
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: chain 'C' and (resseq 59:82)
REMARK 3 ORIGIN FOR THE GROUP (A): 42.9551 -4.6150 -21.6410
REMARK 3 T TENSOR
REMARK 3 T11: 0.0796 T22: 0.2283
REMARK 3 T33: 0.1295 T12: 0.0233
REMARK 3 T13: -0.1064 T23: -0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 0.3830 L22: 1.3844
REMARK 3 L33: 2.7457 L12: 0.4786
REMARK 3 L13: 0.2720 L23: 1.4476
REMARK 3 S TENSOR
REMARK 3 S11: 0.0736 S12: 0.2569 S13: -0.1448
REMARK 3 S21: -0.1562 S22: 0.0159 S23: 0.1142
REMARK 3 S31: 0.0910 S32: -0.0929 S33: -0.0828
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: chain 'C' and (resseq 83:149)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.1196 -10.8229 -37.8437
REMARK 3 T TENSOR
REMARK 3 T11: -0.0250 T22: 0.2259
REMARK 3 T33: 0.0223 T12: 0.0061
REMARK 3 T13: -0.0038 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 1.0027 L22: 0.5123
REMARK 3 L33: 0.1971 L12: -0.2333
REMARK 3 L13: 0.0431 L23: 0.0943
REMARK 3 S TENSOR
REMARK 3 S11: 0.0085 S12: 0.2394 S13: 0.0400
REMARK 3 S21: -0.0690 S22: 0.0421 S23: -0.0649
REMARK 3 S31: 0.0248 S32: 0.1343 S33: -0.0234
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: chain 'C' and (resseq 150:160)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.3435 -2.7401 -44.7860
REMARK 3 T TENSOR
REMARK 3 T11: 0.3357 T22: 0.3268
REMARK 3 T33: 0.1381 T12: -0.0290
REMARK 3 T13: 0.1050 T23: 0.0432
REMARK 3 L TENSOR
REMARK 3 L11: 1.6927 L22: 0.1068
REMARK 3 L33: 0.7016 L12: -0.0873
REMARK 3 L13: -0.8954 L23: 0.1988
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: 0.0665 S13: 0.0982
REMARK 3 S21: 0.0187 S22: -0.0165 S23: -0.0643
REMARK 3 S31: -0.0136 S32: 0.3805 S33: 0.0689
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: chain 'C' and (resseq 161:222)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6816 1.0039 -28.0727
REMARK 3 T TENSOR
REMARK 3 T11: -0.0384 T22: 0.2347
REMARK 3 T33: 0.0507 T12: -0.0769
REMARK 3 T13: -0.0026 T23: 0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 0.5972 L22: 0.3746
REMARK 3 L33: 0.6759 L12: 0.3635
REMARK 3 L13: 0.6314 L23: 0.3857
REMARK 3 S TENSOR
REMARK 3 S11: -0.1367 S12: 0.0424 S13: 0.2413
REMARK 3 S21: -0.1037 S22: 0.0391 S23: 0.0695
REMARK 3 S31: -0.1042 S32: -0.0215 S33: -0.1106
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: chain 'D' and (resseq -1:64)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.5881 -53.1878 39.4035
REMARK 3 T TENSOR
REMARK 3 T11: 0.0188 T22: 0.2306
REMARK 3 T33: -0.0017 T12: -0.1213
REMARK 3 T13: -0.0001 T23: 0.0782
REMARK 3 L TENSOR
REMARK 3 L11: 0.3548 L22: 0.6023
REMARK 3 L33: 0.8477 L12: -0.0531
REMARK 3 L13: 0.1048 L23: -0.3372
REMARK 3 S TENSOR
REMARK 3 S11: 0.0019 S12: -0.0025 S13: -0.0043
REMARK 3 S21: 0.0911 S22: -0.0937 S23: -0.1038
REMARK 3 S31: -0.0293 S32: 0.0747 S33: 0.0221
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: chain 'D' and (resseq 65:82)
REMARK 3 ORIGIN FOR THE GROUP (A): 61.8368 -40.7851 46.7480
REMARK 3 T TENSOR
REMARK 3 T11: 0.1093 T22: 0.2214
REMARK 3 T33: 0.1401 T12: -0.0232
REMARK 3 T13: -0.0846 T23: 0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 2.5242 L22: 1.6641
REMARK 3 L33: 4.4287 L12: 1.7154
REMARK 3 L13: 2.4763 L23: 1.5139
REMARK 3 S TENSOR
REMARK 3 S11: 0.0562 S12: 0.4396 S13: -0.2672
REMARK 3 S21: -0.0705 S22: 0.1633 S23: -0.2045
REMARK 3 S31: 0.1200 S32: 0.2848 S33: -0.4211
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: chain 'D' and (resseq 83:139)
REMARK 3 ORIGIN FOR THE GROUP (A): 44.7846 -50.3721 30.3904
REMARK 3 T TENSOR
REMARK 3 T11: -0.0098 T22: 0.1474
REMARK 3 T33: -0.0588 T12: 0.0251
REMARK 3 T13: 0.0139 T23: -0.0489
REMARK 3 L TENSOR
REMARK 3 L11: 0.5298 L22: 0.2755
REMARK 3 L33: 0.9450 L12: -0.0824
REMARK 3 L13: 0.0632 L23: -0.2184
REMARK 3 S TENSOR
REMARK 3 S11: 0.0148 S12: 0.1978 S13: -0.0712
REMARK 3 S21: -0.0950 S22: -0.0067 S23: 0.0147
REMARK 3 S31: 0.1159 S32: 0.0500 S33: -0.0342
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: chain 'D' and (resseq 140:148)
REMARK 3 ORIGIN FOR THE GROUP (A): 55.5365 -41.8122 37.3072
REMARK 3 T TENSOR
REMARK 3 T11: 0.1208 T22: 0.1657
REMARK 3 T33: 0.2701 T12: 0.0420
REMARK 3 T13: 0.0773 T23: 0.0278
REMARK 3 L TENSOR
REMARK 3 L11: 4.1357 L22: 0.5509
REMARK 3 L33: 4.8235 L12: 1.1080
REMARK 3 L13: -2.6126 L23: 0.1982
REMARK 3 S TENSOR
REMARK 3 S11: -0.4317 S12: -0.0321 S13: -0.5497
REMARK 3 S21: -0.2056 S22: 0.1047 S23: -0.6414
REMARK 3 S31: 0.5878 S32: 0.7133 S33: 0.4265
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: chain 'D' and (resseq 149:188)
REMARK 3 ORIGIN FOR THE GROUP (A): 48.7559 -37.3837 36.9247
REMARK 3 T TENSOR
REMARK 3 T11: 0.0523 T22: 0.1524
REMARK 3 T33: -0.0320 T12: -0.0761
REMARK 3 T13: -0.0037 T23: -0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.2229 L22: 0.4147
REMARK 3 L33: 0.4933 L12: -0.1946
REMARK 3 L13: 0.1863 L23: 0.1196
REMARK 3 S TENSOR
REMARK 3 S11: -0.0196 S12: 0.0942 S13: 0.0267
REMARK 3 S21: -0.1350 S22: -0.0213 S23: -0.0245
REMARK 3 S31: -0.1046 S32: 0.0573 S33: -0.2443
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: chain 'D' and (resseq 189:222)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.0667 -38.2754 40.7293
REMARK 3 T TENSOR
REMARK 3 T11: 0.0189 T22: 0.1995
REMARK 3 T33: 0.0919 T12: -0.0091
REMARK 3 T13: -0.0476 T23: 0.0222
REMARK 3 L TENSOR
REMARK 3 L11: 1.7226 L22: 1.4648
REMARK 3 L33: 0.4372 L12: 0.2371
REMARK 3 L13: 0.1898 L23: 0.3818
REMARK 3 S TENSOR
REMARK 3 S11: -0.1684 S12: 0.0155 S13: 0.1511
REMARK 3 S21: -0.1164 S22: -0.0781 S23: 0.0684
REMARK 3 S31: -0.1083 S32: -0.0871 S33: 0.0193
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: chain 'E' and (resseq -2:39)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4050 30.3840 -31.5200
REMARK 3 T TENSOR
REMARK 3 T11: -0.0060 T22: 0.1834
REMARK 3 T33: 0.0092 T12: -0.0083
REMARK 3 T13: 0.0219 T23: -0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 0.5457 L22: 1.0419
REMARK 3 L33: 1.4441 L12: -0.0544
REMARK 3 L13: 0.0520 L23: -0.4323
REMARK 3 S TENSOR
REMARK 3 S11: 0.0635 S12: 0.0754 S13: -0.0006
REMARK 3 S21: -0.1042 S22: -0.0410 S23: -0.1591
REMARK 3 S31: 0.1113 S32: 0.3654 S33: 0.0894
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: chain 'E' and (resseq 40:84)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2120 34.1871 -25.8934
REMARK 3 T TENSOR
REMARK 3 T11: 0.0435 T22: 0.0542
REMARK 3 T33: 0.0102 T12: -0.0191
REMARK 3 T13: -0.0297 T23: -0.0461
REMARK 3 L TENSOR
REMARK 3 L11: 3.1286 L22: 0.4627
REMARK 3 L33: 1.7504 L12: 0.4181
REMARK 3 L13: -0.9287 L23: -0.3930
REMARK 3 S TENSOR
REMARK 3 S11: 0.0583 S12: -0.2527 S13: 0.3009
REMARK 3 S21: 0.0877 S22: 0.0535 S23: 0.1487
REMARK 3 S31: -0.1657 S32: -0.1917 S33: -0.0532
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: chain 'E' and (resseq 85:127)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.1739 28.6035 -38.1227
REMARK 3 T TENSOR
REMARK 3 T11: 0.1450 T22: 0.2665
REMARK 3 T33: 0.1017 T12: 0.0652
REMARK 3 T13: -0.1469 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.1775 L22: 0.2146
REMARK 3 L33: 0.4704 L12: -0.0559
REMARK 3 L13: 0.1764 L23: -0.1878
REMARK 3 S TENSOR
REMARK 3 S11: -0.0244 S12: 0.1341 S13: 0.0629
REMARK 3 S21: -0.0795 S22: 0.0387 S23: 0.0667
REMARK 3 S31: -0.0177 S32: -0.1053 S33: 0.0780
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: chain 'E' and (resseq 128:174)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7770 18.6435 -33.8844
REMARK 3 T TENSOR
REMARK 3 T11: 0.0935 T22: 0.0941
REMARK 3 T33: 0.2020 T12: 0.0016
REMARK 3 T13: -0.1673 T23: -0.0352
REMARK 3 L TENSOR
REMARK 3 L11: 1.1804 L22: 0.2937
REMARK 3 L33: 1.0722 L12: -0.1376
REMARK 3 L13: 0.3871 L23: -0.2912
REMARK 3 S TENSOR
REMARK 3 S11: 0.0020 S12: 0.0433 S13: -0.0463
REMARK 3 S21: -0.1002 S22: 0.0522 S23: 0.1360
REMARK 3 S31: 0.0215 S32: -0.2374 S33: 0.0274
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: chain 'E' and (resseq 175:186)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.3498 11.1221 -29.3109
REMARK 3 T TENSOR
REMARK 3 T11: 0.1794 T22: 0.3265
REMARK 3 T33: 0.6773 T12: -0.0336
REMARK 3 T13: -0.0762 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 0.0541 L22: 0.4340
REMARK 3 L33: 0.8325 L12: -0.0884
REMARK 3 L13: 0.1891 L23: -0.0896
REMARK 3 S TENSOR
REMARK 3 S11: 0.1874 S12: -0.0588 S13: -1.0443
REMARK 3 S21: -0.0021 S22: 0.0231 S23: -0.0505
REMARK 3 S31: 0.3665 S32: -0.2848 S33: -0.2358
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: chain 'E' and (resseq 187:222)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2269 14.7860 -28.9783
REMARK 3 T TENSOR
REMARK 3 T11: 0.0647 T22: 0.1152
REMARK 3 T33: 0.2248 T12: -0.0359
REMARK 3 T13: -0.0199 T23: -0.0632
REMARK 3 L TENSOR
REMARK 3 L11: 0.4012 L22: 1.0976
REMARK 3 L33: 1.7005 L12: -0.1052
REMARK 3 L13: -0.2514 L23: -0.6728
REMARK 3 S TENSOR
REMARK 3 S11: 0.0734 S12: -0.0304 S13: -0.2734
REMARK 3 S21: -0.1989 S22: -0.1192 S23: -0.1358
REMARK 3 S31: 0.2307 S32: 0.0454 S33: -0.0517
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: chain 'F' and (resseq -2:39)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.7483 -7.5439 37.7569
REMARK 3 T TENSOR
REMARK 3 T11: 0.0844 T22: 0.1337
REMARK 3 T33: 0.0137 T12: -0.0339
REMARK 3 T13: 0.0069 T23: 0.0346
REMARK 3 L TENSOR
REMARK 3 L11: 1.0988 L22: 1.7552
REMARK 3 L33: 3.2672 L12: 0.4439
REMARK 3 L13: -0.3550 L23: -1.1734
REMARK 3 S TENSOR
REMARK 3 S11: 0.0291 S12: 0.0288 S13: -0.1013
REMARK 3 S21: -0.2352 S22: -0.0602 S23: -0.1327
REMARK 3 S31: 0.3165 S32: 0.2455 S33: 0.0807
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: chain 'F' and (resseq 40:145)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.7854 -8.8332 35.8722
REMARK 3 T TENSOR
REMARK 3 T11: 0.0469 T22: 0.1644
REMARK 3 T33: 0.1398 T12: 0.1131
REMARK 3 T13: -0.0797 T23: 0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 0.7218 L22: 0.4268
REMARK 3 L33: 0.4991 L12: 0.0983
REMARK 3 L13: 0.2235 L23: -0.0500
REMARK 3 S TENSOR
REMARK 3 S11: 0.0631 S12: 0.1373 S13: 0.0460
REMARK 3 S21: -0.0804 S22: 0.0380 S23: 0.1669
REMARK 3 S31: -0.1030 S32: -0.1717 S33: -0.0002
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: chain 'F' and (resseq 146:174)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.2755 -21.1078 36.5973
REMARK 3 T TENSOR
REMARK 3 T11: 0.1017 T22: 0.1689
REMARK 3 T33: 0.2860 T12: 0.0401
REMARK 3 T13: -0.1169 T23: -0.0324
REMARK 3 L TENSOR
REMARK 3 L11: 0.7414 L22: 0.6826
REMARK 3 L33: 2.8718 L12: -0.2279
REMARK 3 L13: -0.2321 L23: -0.3727
REMARK 3 S TENSOR
REMARK 3 S11: -0.0062 S12: -0.0189 S13: -0.0305
REMARK 3 S21: -0.2045 S22: 0.0514 S23: 0.4049
REMARK 3 S31: -0.0775 S32: -0.4519 S33: -0.2277
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: chain 'F' and (resseq 175:186)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8156 -27.0432 39.9424
REMARK 3 T TENSOR
REMARK 3 T11: 0.3518 T22: 0.1456
REMARK 3 T33: 0.5557 T12: -0.0530
REMARK 3 T13: -0.1050 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 0.7221 L22: 0.1152
REMARK 3 L33: 0.4206 L12: 0.1659
REMARK 3 L13: -0.4326 L23: 0.0035
REMARK 3 S TENSOR
REMARK 3 S11: -0.1326 S12: 0.1085 S13: -0.0191
REMARK 3 S21: -0.3000 S22: -0.0336 S23: 0.7490
REMARK 3 S31: 0.4993 S32: -0.3308 S33: 0.1795
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: chain 'F' and (resseq 187:222)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.7497 -23.3531 40.3186
REMARK 3 T TENSOR
REMARK 3 T11: 0.1064 T22: 0.1018
REMARK 3 T33: 0.4470 T12: -0.0073
REMARK 3 T13: 0.0178 T23: -0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 0.5281 L22: 2.3190
REMARK 3 L33: 0.7174 L12: 0.3510
REMARK 3 L13: 0.1858 L23: 0.1819
REMARK 3 S TENSOR
REMARK 3 S11: -0.0490 S12: 0.0918 S13: -0.3033
REMARK 3 S21: -0.3072 S22: 0.1282 S23: -0.3562
REMARK 3 S31: 0.0715 S32: 0.0748 S33: -0.0206
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: chain 'G' and (resseq -2:13)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.860 -43.700 4.610
REMARK 3 T TENSOR
REMARK 3 T11: 0.3501 T22: 0.1989
REMARK 3 T33: 0.5430 T12: 0.0044
REMARK 3 T13: -0.1637 T23: 0.0678
REMARK 3 L TENSOR
REMARK 3 L11: 2.3680 L22: 1.6417
REMARK 3 L33: 0.9816 L12: 1.4262
REMARK 3 L13: -0.4678 L23: 0.5527
REMARK 3 S TENSOR
REMARK 3 S11: 0.1059 S12: -0.1595 S13: -0.9396
REMARK 3 S21: 0.3300 S22: -0.0788 S23: -0.1325
REMARK 3 S31: 0.1687 S32: 0.1505 S33: -0.0423
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: chain 'G' and (resseq 14:42)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1331 -34.6670 -2.1911
REMARK 3 T TENSOR
REMARK 3 T11: 0.3009 T22: 0.0925
REMARK 3 T33: 0.3718 T12: 0.0219
REMARK 3 T13: -0.0287 T23: 0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 1.6995 L22: 4.9341
REMARK 3 L33: 3.2142 L12: -1.9957
REMARK 3 L13: 0.0072 L23: -1.0761
REMARK 3 S TENSOR
REMARK 3 S11: 0.0585 S12: 0.0778 S13: -0.0305
REMARK 3 S21: 0.0918 S22: -0.2596 S23: -0.1980
REMARK 3 S31: -0.1697 S32: 0.1736 S33: 0.1928
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: chain 'G' and (resseq 43:84)
REMARK 3 ORIGIN FOR THE GROUP (A): -26.1911 -44.3947 -7.0535
REMARK 3 T TENSOR
REMARK 3 T11: 0.1461 T22: 0.3073
REMARK 3 T33: 0.0836 T12: -0.0541
REMARK 3 T13: -0.0295 T23: 0.0458
REMARK 3 L TENSOR
REMARK 3 L11: 0.7360 L22: 0.5400
REMARK 3 L33: 1.2512 L12: -0.6132
REMARK 3 L13: 0.5966 L23: -0.6452
REMARK 3 S TENSOR
REMARK 3 S11: 0.0500 S12: -0.0087 S13: -0.0883
REMARK 3 S21: -0.1005 S22: 0.1187 S23: 0.1343
REMARK 3 S31: 0.3876 S32: -0.1814 S33: -0.0750
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: chain 'G' and (resseq 85:106)
REMARK 3 ORIGIN FOR THE GROUP (A): -18.1476 -40.9668 9.3997
REMARK 3 T TENSOR
REMARK 3 T11: 0.3612 T22: 0.1619
REMARK 3 T33: 0.1200 T12: -0.0399
REMARK 3 T13: 0.0505 T23: 0.0636
REMARK 3 L TENSOR
REMARK 3 L11: 6.6471 L22: 0.8811
REMARK 3 L33: 1.1235 L12: 0.7268
REMARK 3 L13: 1.2371 L23: 0.1100
REMARK 3 S TENSOR
REMARK 3 S11: -0.1539 S12: -0.4370 S13: -0.4972
REMARK 3 S21: 0.1535 S22: 0.1251 S23: -0.0860
REMARK 3 S31: 0.0641 S32: -0.3661 S33: -0.0223
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: chain 'G' and (resseq 107:175)
REMARK 3 ORIGIN FOR THE GROUP (A): -21.3408 -28.0193 2.3074
REMARK 3 T TENSOR
REMARK 3 T11: 0.1090 T22: 0.1197
REMARK 3 T33: 0.1140 T12: 0.0722
REMARK 3 T13: -0.0201 T23: -0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 1.7139 L22: 2.8150
REMARK 3 L33: 2.6887 L12: -0.0473
REMARK 3 L13: 0.3815 L23: -0.8325
REMARK 3 S TENSOR
REMARK 3 S11: 0.0028 S12: -0.1722 S13: 0.1248
REMARK 3 S21: 0.3796 S22: 0.0886 S23: 0.3412
REMARK 3 S31: -0.1399 S32: -0.4776 S33: -0.0717
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: chain 'G' and (resseq 176:222)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.4396 -21.9452 -2.5032
REMARK 3 T TENSOR
REMARK 3 T11: 0.2127 T22: 0.0907
REMARK 3 T33: 0.2993 T12: -0.0025
REMARK 3 T13: -0.0375 T23: -0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 0.9906 L22: 1.6307
REMARK 3 L33: 0.8696 L12: -0.9602
REMARK 3 L13: 0.2539 L23: -0.8320
REMARK 3 S TENSOR
REMARK 3 S11: -0.1225 S12: -0.1104 S13: 0.4415
REMARK 3 S21: 0.2000 S22: -0.1411 S23: -0.0533
REMARK 3 S31: -0.1479 S32: 0.0635 S33: 0.1567
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: chain 'H' and (resseq -2:13)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.763 -81.768 73.952
REMARK 3 T TENSOR
REMARK 3 T11: 0.3610 T22: 0.2000
REMARK 3 T33: 0.3430 T12: 0.0602
REMARK 3 T13: -0.2189 T23: 0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 5.1762 L22: 2.0269
REMARK 3 L33: 3.8968 L12: 2.4086
REMARK 3 L13: 4.4770 L23: 2.0638
REMARK 3 S TENSOR
REMARK 3 S11: 0.2855 S12: -0.1778 S13: -0.1308
REMARK 3 S21: 0.0570 S22: -0.3344 S23: -0.0150
REMARK 3 S31: 0.1037 S32: -0.0949 S33: -0.1962
REMARK 3 TLS GROUP : 40
REMARK 3 SELECTION: chain 'H' and (resseq 14:42)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0906 -72.9907 66.9640
REMARK 3 T TENSOR
REMARK 3 T11: 0.2458 T22: 0.1995
REMARK 3 T33: 0.5600 T12: 0.0576
REMARK 3 T13: -0.2096 T23: -0.0495
REMARK 3 L TENSOR
REMARK 3 L11: 0.4634 L22: 0.4668
REMARK 3 L33: 0.3394 L12: -0.3252
REMARK 3 L13: -0.1065 L23: -0.0540
REMARK 3 S TENSOR
REMARK 3 S11: -0.0429 S12: -0.0208 S13: -0.1354
REMARK 3 S21: -0.0195 S22: -0.0784 S23: 0.0448
REMARK 3 S31: -0.0190 S32: 0.0288 S33: -0.0145
REMARK 3 TLS GROUP : 41
REMARK 3 SELECTION: chain 'H' and (resseq 43:84)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1114 -81.6707 62.9285
REMARK 3 T TENSOR
REMARK 3 T11: 0.1536 T22: 0.4686
REMARK 3 T33: 0.1495 T12: -0.1410
REMARK 3 T13: -0.0008 T23: 0.0389
REMARK 3 L TENSOR
REMARK 3 L11: 1.0807 L22: 0.6798
REMARK 3 L33: 0.7247 L12: -0.7377
REMARK 3 L13: 0.8575 L23: -0.6736
REMARK 3 S TENSOR
REMARK 3 S11: 0.0149 S12: -0.2172 S13: 0.0127
REMARK 3 S21: 0.0894 S22: -0.1255 S23: 0.0279
REMARK 3 S31: 0.0880 S32: -0.1571 S33: 0.0871
REMARK 3 TLS GROUP : 42
REMARK 3 SELECTION: chain 'H' and (resseq 85:126)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2002 -75.0887 75.5635
REMARK 3 T TENSOR
REMARK 3 T11: 0.1382 T22: 0.1190
REMARK 3 T33: 0.1463 T12: 0.0733
REMARK 3 T13: -0.0537 T23: 0.0708
REMARK 3 L TENSOR
REMARK 3 L11: 1.3693 L22: 1.0876
REMARK 3 L33: 1.9196 L12: -0.3857
REMARK 3 L13: 0.9403 L23: -0.8762
REMARK 3 S TENSOR
REMARK 3 S11: 0.0338 S12: -0.2317 S13: -0.1436
REMARK 3 S21: 0.1577 S22: 0.0073 S23: -0.0188
REMARK 3 S31: 0.1670 S32: 0.0257 S33: -0.0571
REMARK 3 TLS GROUP : 43
REMARK 3 SELECTION: chain 'H' and (resseq 127:139)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2614 -68.4330 77.9090
REMARK 3 T TENSOR
REMARK 3 T11: 0.5055 T22: 0.2836
REMARK 3 T33: 0.1992 T12: -0.0973
REMARK 3 T13: -0.0087 T23: 0.0239
REMARK 3 L TENSOR
REMARK 3 L11: 6.8712 L22: 1.4310
REMARK 3 L33: 4.0783 L12: -2.3592
REMARK 3 L13: 0.2248 L23: 0.1874
REMARK 3 S TENSOR
REMARK 3 S11: -0.1186 S12: -1.3010 S13: -0.5808
REMARK 3 S21: 1.0537 S22: 0.0233 S23: 0.0296
REMARK 3 S31: 0.3585 S32: 0.1056 S33: 0.1137
REMARK 3 TLS GROUP : 44
REMARK 3 SELECTION: chain 'H' and (resseq 140:160)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.0932 -64.9912 75.2943
REMARK 3 T TENSOR
REMARK 3 T11: 0.4433 T22: 0.5568
REMARK 3 T33: 0.3207 T12: 0.1211
REMARK 3 T13: 0.1301 T23: -0.0318
REMARK 3 L TENSOR
REMARK 3 L11: 0.6234 L22: 0.7530
REMARK 3 L33: 7.3482 L12: 0.6274
REMARK 3 L13: 1.3066 L23: 2.0643
REMARK 3 S TENSOR
REMARK 3 S11: 0.1212 S12: -0.5449 S13: 0.4407
REMARK 3 S21: 0.4804 S22: -0.2804 S23: 0.5825
REMARK 3 S31: -0.0357 S32: -1.7337 S33: 0.2198
REMARK 3 TLS GROUP : 45
REMARK 3 SELECTION: chain 'H' and (resseq 161:186)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7544 -59.1855 63.6898
REMARK 3 T TENSOR
REMARK 3 T11: 0.0807 T22: 0.0914
REMARK 3 T33: 0.3188 T12: 0.0200
REMARK 3 T13: -0.0674 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 3.8154 L22: 2.5095
REMARK 3 L33: 4.7203 L12: -0.0772
REMARK 3 L13: 3.1974 L23: 1.6979
REMARK 3 S TENSOR
REMARK 3 S11: -0.2059 S12: -0.0890 S13: 0.5401
REMARK 3 S21: 0.0855 S22: -0.0004 S23: 0.0320
REMARK 3 S31: -0.2172 S32: -0.0872 S33: 0.2405
REMARK 3 TLS GROUP : 46
REMARK 3 SELECTION: chain 'H' and (resseq 187:205)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4997 -59.1218 63.9253
REMARK 3 T TENSOR
REMARK 3 T11: 0.2045 T22: 0.1120
REMARK 3 T33: 0.2219 T12: 0.0438
REMARK 3 T13: -0.1718 T23: -0.0422
REMARK 3 L TENSOR
REMARK 3 L11: 0.8259 L22: 1.3458
REMARK 3 L33: 4.5065 L12: 0.7509
REMARK 3 L13: 0.7844 L23: -0.8666
REMARK 3 S TENSOR
REMARK 3 S11: -0.0479 S12: -0.1320 S13: 0.1789
REMARK 3 S21: 0.1512 S22: -0.0999 S23: -0.0519
REMARK 3 S31: -0.4394 S32: -0.4048 S33: 0.1340
REMARK 3 TLS GROUP : 47
REMARK 3 SELECTION: chain 'H' and (resseq 206:222)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3028 -62.7897 69.3167
REMARK 3 T TENSOR
REMARK 3 T11: 0.1504 T22: 0.1639
REMARK 3 T33: 0.4158 T12: -0.0459
REMARK 3 T13: -0.1113 T23: 0.0380
REMARK 3 L TENSOR
REMARK 3 L11: 5.9498 L22: 4.5167
REMARK 3 L33: 1.5386 L12: 2.0790
REMARK 3 L13: 1.5551 L23: -0.4696
REMARK 3 S TENSOR
REMARK 3 S11: 0.1044 S12: -0.4386 S13: 0.2912
REMARK 3 S21: 0.2635 S22: -0.1982 S23: 0.1044
REMARK 3 S31: -0.1176 S32: -0.3160 S33: 0.0928
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 4F21 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-12.
REMARK 100 THE RCSB ID CODE IS RCSB072355.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
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-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : DIAMOND(111)
REMARK 200 OPTICS : BERYLLIUM LENSES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58087
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1FJ2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M AMMONIUM ACETATE, 0.1 M BIS-
REMARK 280 TRIS, 17% PEG10000, PH 5.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
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, 3, 4, 5, 6, 7, 8
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 GLY A -14
REMARK 465 VAL A -13
REMARK 465 ASP A -12
REMARK 465 LEU A -11
REMARK 465 GLY A -10
REMARK 465 THR A -9
REMARK 465 GLU A -8
REMARK 465 ASN A -7
REMARK 465 LEU A -6
REMARK 465 TYR A -5
REMARK 465 PHE A -4
REMARK 465 GLN A -3
REMARK 465 SER A -2
REMARK 465 LEU A 22
REMARK 465 GLY A 23
REMARK 465 ASP A 73
REMARK 465 ALA A 74
REMARK 465 ASN A 75
REMARK 465 GLY A 85
REMARK 465 GLY A 104
REMARK 465 MET B -23
REMARK 465 HIS B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 SER B -16
REMARK 465 SER B -15
REMARK 465 GLY B -14
REMARK 465 VAL B -13
REMARK 465 ASP B -12
REMARK 465 LEU B -11
REMARK 465 GLY B -10
REMARK 465 THR B -9
REMARK 465 GLU B -8
REMARK 465 ASN B -7
REMARK 465 LEU B -6
REMARK 465 TYR B -5
REMARK 465 PHE B -4
REMARK 465 GLN B -3
REMARK 465 SER B -2
REMARK 465 LEU B 22
REMARK 465 GLY B 23
REMARK 465 ALA B 74
REMARK 465 ASN B 75
REMARK 465 MET C -23
REMARK 465 HIS C -22
REMARK 465 HIS C -21
REMARK 465 HIS C -20
REMARK 465 HIS C -19
REMARK 465 HIS C -18
REMARK 465 HIS C -17
REMARK 465 SER C -16
REMARK 465 SER C -15
REMARK 465 GLY C -14
REMARK 465 VAL C -13
REMARK 465 ASP C -12
REMARK 465 LEU C -11
REMARK 465 GLY C -10
REMARK 465 THR C -9
REMARK 465 GLU C -8
REMARK 465 ASN C -7
REMARK 465 LEU C -6
REMARK 465 TYR C -5
REMARK 465 PHE C -4
REMARK 465 GLN C -3
REMARK 465 SER C -2
REMARK 465 LEU C 22
REMARK 465 GLY C 23
REMARK 465 ALA C 74
REMARK 465 ASN C 75
REMARK 465 MET D -23
REMARK 465 HIS D -22
REMARK 465 HIS D -21
REMARK 465 HIS D -20
REMARK 465 HIS D -19
REMARK 465 HIS D -18
REMARK 465 HIS D -17
REMARK 465 SER D -16
REMARK 465 SER D -15
REMARK 465 GLY D -14
REMARK 465 VAL D -13
REMARK 465 ASP D -12
REMARK 465 LEU D -11
REMARK 465 GLY D -10
REMARK 465 THR D -9
REMARK 465 GLU D -8
REMARK 465 ASN D -7
REMARK 465 LEU D -6
REMARK 465 TYR D -5
REMARK 465 PHE D -4
REMARK 465 GLN D -3
REMARK 465 SER D -2
REMARK 465 LEU D 22
REMARK 465 GLY D 23
REMARK 465 ALA D 74
REMARK 465 ASN D 75
REMARK 465 MET E -23
REMARK 465 HIS E -22
REMARK 465 HIS E -21
REMARK 465 HIS E -20
REMARK 465 HIS E -19
REMARK 465 HIS E -18
REMARK 465 HIS E -17
REMARK 465 SER E -16
REMARK 465 SER E -15
REMARK 465 GLY E -14
REMARK 465 VAL E -13
REMARK 465 ASP E -12
REMARK 465 LEU E -11
REMARK 465 GLY E -10
REMARK 465 THR E -9
REMARK 465 GLU E -8
REMARK 465 ASN E -7
REMARK 465 LEU E -6
REMARK 465 TYR E -5
REMARK 465 PHE E -4
REMARK 465 GLN E -3
REMARK 465 GLY E 23
REMARK 465 ALA E 24
REMARK 465 ASP E 25
REMARK 465 ILE E 53
REMARK 465 PRO E 54
REMARK 465 VAL E 55
REMARK 465 THR E 56
REMARK 465 ILE E 57
REMARK 465 ASN E 58
REMARK 465 MET E 59
REMARK 465 LEU E 72
REMARK 465 ASP E 73
REMARK 465 ALA E 74
REMARK 465 ASN E 75
REMARK 465 SER E 76
REMARK 465 LEU E 77
REMARK 465 ASN E 78
REMARK 465 ARG E 79
REMARK 465 VAL E 80
REMARK 465 MET F -23
REMARK 465 HIS F -22
REMARK 465 HIS F -21
REMARK 465 HIS F -20
REMARK 465 HIS F -19
REMARK 465 HIS F -18
REMARK 465 HIS F -17
REMARK 465 SER F -16
REMARK 465 SER F -15
REMARK 465 GLY F -14
REMARK 465 VAL F -13
REMARK 465 ASP F -12
REMARK 465 LEU F -11
REMARK 465 GLY F -10
REMARK 465 THR F -9
REMARK 465 GLU F -8
REMARK 465 ASN F -7
REMARK 465 LEU F -6
REMARK 465 TYR F -5
REMARK 465 PHE F -4
REMARK 465 GLN F -3
REMARK 465 GLY F 23
REMARK 465 ALA F 24
REMARK 465 ASP F 25
REMARK 465 ILE F 53
REMARK 465 PRO F 54
REMARK 465 VAL F 55
REMARK 465 THR F 56
REMARK 465 ILE F 57
REMARK 465 ASN F 58
REMARK 465 LEU F 72
REMARK 465 ASP F 73
REMARK 465 ALA F 74
REMARK 465 ASN F 75
REMARK 465 SER F 76
REMARK 465 LEU F 77
REMARK 465 ASN F 78
REMARK 465 ARG F 79
REMARK 465 VAL F 80
REMARK 465 VAL F 81
REMARK 465 ASP F 82
REMARK 465 MET G -23
REMARK 465 HIS G -22
REMARK 465 HIS G -21
REMARK 465 HIS G -20
REMARK 465 HIS G -19
REMARK 465 HIS G -18
REMARK 465 HIS G -17
REMARK 465 SER G -16
REMARK 465 SER G -15
REMARK 465 GLY G -14
REMARK 465 VAL G -13
REMARK 465 ASP G -12
REMARK 465 LEU G -11
REMARK 465 GLY G -10
REMARK 465 THR G -9
REMARK 465 GLU G -8
REMARK 465 ASN G -7
REMARK 465 LEU G -6
REMARK 465 TYR G -5
REMARK 465 PHE G -4
REMARK 465 GLN G -3
REMARK 465 GLY G 21
REMARK 465 LEU G 22
REMARK 465 GLY G 23
REMARK 465 ALA G 24
REMARK 465 ASP G 25
REMARK 465 GLY G 26
REMARK 465 ASP G 51
REMARK 465 ILE G 52
REMARK 465 ASN G 58
REMARK 465 MET G 59
REMARK 465 SER G 71
REMARK 465 LEU G 72
REMARK 465 ASP G 73
REMARK 465 ALA G 74
REMARK 465 ASN G 75
REMARK 465 SER G 76
REMARK 465 LEU G 77
REMARK 465 ASN G 78
REMARK 465 ARG G 79
REMARK 465 ALA G 91
REMARK 465 PHE G 149
REMARK 465 MET H -23
REMARK 465 HIS H -22
REMARK 465 HIS H -21
REMARK 465 HIS H -20
REMARK 465 HIS H -19
REMARK 465 HIS H -18
REMARK 465 HIS H -17
REMARK 465 SER H -16
REMARK 465 SER H -15
REMARK 465 GLY H -14
REMARK 465 VAL H -13
REMARK 465 ASP H -12
REMARK 465 LEU H -11
REMARK 465 GLY H -10
REMARK 465 THR H -9
REMARK 465 GLU H -8
REMARK 465 ASN H -7
REMARK 465 LEU H -6
REMARK 465 TYR H -5
REMARK 465 PHE H -4
REMARK 465 GLN H -3
REMARK 465 LEU H 22
REMARK 465 GLY H 23
REMARK 465 ALA H 24
REMARK 465 ASP H 25
REMARK 465 GLY H 26
REMARK 465 ASP H 51
REMARK 465 ILE H 52
REMARK 465 ASN H 58
REMARK 465 MET H 59
REMARK 465 GLY H 60
REMARK 465 MET H 61
REMARK 465 GLN H 62
REMARK 465 SER H 71
REMARK 465 LEU H 72
REMARK 465 ASP H 73
REMARK 465 ALA H 74
REMARK 465 ASN H 75
REMARK 465 SER H 76
REMARK 465 LEU H 77
REMARK 465 ASN H 78
REMARK 465 ARG H 79
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 MET A 63 SD CE
REMARK 470 ILE A 105 CD1
REMARK 470 ILE A 156 CD1
REMARK 470 LYS A 218 NZ
REMARK 470 LYS B 150 CE NZ
REMARK 470 LYS B 218 NZ
REMARK 470 LYS C 150 CE NZ
REMARK 470 LYS C 184 CE NZ
REMARK 470 LYS D 150 CE NZ
REMARK 470 SER E -2 OG
REMARK 470 MET E 61 SD CE
REMARK 470 LYS E 132 NZ
REMARK 470 LYS E 150 CE NZ
REMARK 470 LYS E 218 NZ
REMARK 470 MET F 61 SD CE
REMARK 470 VAL F 83 CG1 CG2
REMARK 470 GLU F 84 CG CD OE1 OE2
REMARK 470 LYS F 150 CE NZ
REMARK 470 LYS F 218 NZ
REMARK 470 MET G 61 SD CE
REMARK 470 LYS G 150 CE NZ
REMARK 470 LEU G 160 CD1
REMARK 470 LYS G 218 NZ
REMARK 470 LYS H 150 CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLN B 201 C HIS B 202 N 0.170
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PHE E 115 O - C - N ANGL. DEV. = -10.0 DEGREES
REMARK 500 GLY E 119 O - C - N ANGL. DEV. = 11.1 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 THR A 56 6.93 -63.88
REMARK 500 ILE A 57 -63.30 -91.82
REMARK 500 GLN A 62 44.84 -100.46
REMARK 500 ASP A 82 81.59 -69.56
REMARK 500 SER A 116 -115.67 54.74
REMARK 500 LYS A 158 92.99 -63.54
REMARK 500 PRO A 161 108.10 -56.56
REMARK 500 GLN A 201 -129.99 -103.80
REMARK 500 SER A 203 -168.91 -163.79
REMARK 500 GLN B 62 37.70 -97.30
REMARK 500 SER B 116 -121.09 52.63
REMARK 500 LEU B 133 -169.16 -100.13
REMARK 500 PRO B 174 150.49 -46.59
REMARK 500 GLN B 201 -127.12 -101.93
REMARK 500 ALA C 0 91.97 -62.75
REMARK 500 ASP C 25 36.32 -82.65
REMARK 500 THR C 56 32.27 -93.28
REMARK 500 ILE C 69 132.67 -37.61
REMARK 500 SER C 116 -120.62 58.29
REMARK 500 LYS C 158 96.99 -62.27
REMARK 500 GLN C 201 -155.02 -112.56
REMARK 500 HIS C 202 66.87 -67.91
REMARK 500 ASP D 51 5.09 -62.70
REMARK 500 ILE D 69 125.36 -33.00
REMARK 500 VAL D 80 48.51 -107.48
REMARK 500 SER D 116 -116.69 51.97
REMARK 500 THR D 154 -155.28 -121.99
REMARK 500 LYS D 158 99.06 -67.76
REMARK 500 GLN D 201 -135.47 -106.88
REMARK 500 ALA E 9 -73.18 -54.34
REMARK 500 ARG E 64 -68.24 -143.78
REMARK 500 ILE E 69 16.11 -69.56
REMARK 500 SER E 116 -128.53 53.08
REMARK 500 GLN E 201 -116.82 -102.49
REMARK 500 HIS E 202 62.36 -107.36
REMARK 500 ASN F -1 -1.69 -149.60
REMARK 500 ALA F 0 94.07 -68.26
REMARK 500 VAL F 38 -179.07 -66.12
REMARK 500 GLN F 62 -8.20 -56.82
REMARK 500 ARG F 64 -72.91 -130.78
REMARK 500 ILE F 69 -15.56 -48.05
REMARK 500 SER F 116 -118.21 49.17
REMARK 500 THR F 141 -160.84 -103.45
REMARK 500 VAL F 198 98.01 -65.27
REMARK 500 GLN F 201 -142.07 -94.37
REMARK 500 LYS G 10 -158.37 -90.93
REMARK 500 HIS G 49 -167.07 -101.49
REMARK 500 ARG G 64 -74.37 -108.79
REMARK 500 SER G 116 -103.08 52.08
REMARK 500 PRO G 161 109.13 -56.52
REMARK 500
REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH F 305 DISTANCE = 6.99 ANGSTROMS
REMARK 525 HOH F 333 DISTANCE = 11.22 ANGSTROMS
REMARK 525 HOH F 334 DISTANCE = 9.08 ANGSTROMS
REMARK 525 HOH F 335 DISTANCE = 8.52 ANGSTROMS
REMARK 525 HOH F 336 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH F 337 DISTANCE = 7.45 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 0S1 E 301
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 HOH H 322
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0S1 E 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CSGID-IDP01809 RELATED DB: TARGETTRACK
DBREF 4F21 A 1 222 UNP Q5NI32 Q5NI32_FRATT 1 222
DBREF 4F21 B 1 222 UNP Q5NI32 Q5NI32_FRATT 1 222
DBREF 4F21 C 1 222 UNP Q5NI32 Q5NI32_FRATT 1 222
DBREF 4F21 D 1 222 UNP Q5NI32 Q5NI32_FRATT 1 222
DBREF 4F21 E 1 222 UNP Q5NI32 Q5NI32_FRATT 1 222
DBREF 4F21 F 1 222 UNP Q5NI32 Q5NI32_FRATT 1 222
DBREF 4F21 G 1 222 UNP Q5NI32 Q5NI32_FRATT 1 222
DBREF 4F21 H 1 222 UNP Q5NI32 Q5NI32_FRATT 1 222
SEQADV 4F21 MET A -23 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS A -22 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS A -21 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS A -20 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS A -19 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS A -18 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS A -17 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER A -16 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER A -15 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLY A -14 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 VAL A -13 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASP A -12 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 LEU A -11 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLY A -10 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 THR A -9 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLU A -8 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASN A -7 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 LEU A -6 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 TYR A -5 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 PHE A -4 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLN A -3 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER A -2 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASN A -1 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ALA A 0 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 MET B -23 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS B -22 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS B -21 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS B -20 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS B -19 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS B -18 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS B -17 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER B -16 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER B -15 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLY B -14 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 VAL B -13 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASP B -12 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 LEU B -11 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLY B -10 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 THR B -9 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLU B -8 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASN B -7 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 LEU B -6 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 TYR B -5 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 PHE B -4 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLN B -3 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER B -2 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASN B -1 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ALA B 0 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 MET C -23 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS C -22 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS C -21 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS C -20 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS C -19 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS C -18 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS C -17 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER C -16 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER C -15 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLY C -14 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 VAL C -13 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASP C -12 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 LEU C -11 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLY C -10 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 THR C -9 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLU C -8 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASN C -7 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 LEU C -6 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 TYR C -5 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 PHE C -4 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLN C -3 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER C -2 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASN C -1 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ALA C 0 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 MET D -23 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS D -22 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS D -21 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS D -20 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS D -19 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS D -18 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS D -17 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER D -16 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER D -15 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLY D -14 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 VAL D -13 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASP D -12 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 LEU D -11 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLY D -10 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 THR D -9 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLU D -8 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASN D -7 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 LEU D -6 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 TYR D -5 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 PHE D -4 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLN D -3 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER D -2 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASN D -1 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ALA D 0 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 MET E -23 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS E -22 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS E -21 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS E -20 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS E -19 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS E -18 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS E -17 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER E -16 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER E -15 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLY E -14 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 VAL E -13 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASP E -12 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 LEU E -11 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLY E -10 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 THR E -9 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLU E -8 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASN E -7 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 LEU E -6 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 TYR E -5 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 PHE E -4 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLN E -3 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER E -2 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASN E -1 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ALA E 0 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 MET F -23 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS F -22 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS F -21 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS F -20 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS F -19 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS F -18 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS F -17 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER F -16 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER F -15 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLY F -14 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 VAL F -13 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASP F -12 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 LEU F -11 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLY F -10 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 THR F -9 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLU F -8 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASN F -7 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 LEU F -6 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 TYR F -5 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 PHE F -4 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLN F -3 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER F -2 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASN F -1 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ALA F 0 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 MET G -23 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS G -22 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS G -21 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS G -20 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS G -19 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS G -18 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS G -17 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER G -16 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER G -15 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLY G -14 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 VAL G -13 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASP G -12 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 LEU G -11 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLY G -10 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 THR G -9 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLU G -8 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASN G -7 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 LEU G -6 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 TYR G -5 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 PHE G -4 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLN G -3 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER G -2 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASN G -1 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ALA G 0 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 MET H -23 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS H -22 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS H -21 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS H -20 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS H -19 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS H -18 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 HIS H -17 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER H -16 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER H -15 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLY H -14 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 VAL H -13 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASP H -12 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 LEU H -11 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLY H -10 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 THR H -9 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLU H -8 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASN H -7 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 LEU H -6 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 TYR H -5 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 PHE H -4 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 GLN H -3 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 SER H -2 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ASN H -1 UNP Q5NI32 EXPRESSION TAG
SEQADV 4F21 ALA H 0 UNP Q5NI32 EXPRESSION TAG
SEQRES 1 A 246 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 246 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET ASN
SEQRES 3 A 246 TYR GLU LEU MET GLU PRO ALA LYS GLN ALA ARG PHE CYS
SEQRES 4 A 246 VAL ILE TRP LEU HIS GLY LEU GLY ALA ASP GLY HIS ASP
SEQRES 5 A 246 PHE VAL ASP ILE VAL ASN TYR PHE ASP VAL SER LEU ASP
SEQRES 6 A 246 GLU ILE ARG PHE ILE PHE PRO HIS ALA ASP ILE ILE PRO
SEQRES 7 A 246 VAL THR ILE ASN MET GLY MET GLN MET ARG ALA TRP TYR
SEQRES 8 A 246 ASP ILE LYS SER LEU ASP ALA ASN SER LEU ASN ARG VAL
SEQRES 9 A 246 VAL ASP VAL GLU GLY ILE ASN SER SER ILE ALA LYS VAL
SEQRES 10 A 246 ASN LYS LEU ILE ASP SER GLN VAL ASN GLN GLY ILE ALA
SEQRES 11 A 246 SER GLU ASN ILE ILE LEU ALA GLY PHE SER GLN GLY GLY
SEQRES 12 A 246 ILE ILE ALA THR TYR THR ALA ILE THR SER GLN ARG LYS
SEQRES 13 A 246 LEU GLY GLY ILE MET ALA LEU SER THR TYR LEU PRO ALA
SEQRES 14 A 246 TRP ASP ASN PHE LYS GLY LYS ILE THR SER ILE ASN LYS
SEQRES 15 A 246 GLY LEU PRO ILE LEU VAL CYS HIS GLY THR ASP ASP GLN
SEQRES 16 A 246 VAL LEU PRO GLU VAL LEU GLY HIS ASP LEU SER ASP LYS
SEQRES 17 A 246 LEU LYS VAL SER GLY PHE ALA ASN GLU TYR LYS HIS TYR
SEQRES 18 A 246 VAL GLY MET GLN HIS SER VAL CYS MET GLU GLU ILE LYS
SEQRES 19 A 246 ASP ILE SER ASN PHE ILE ALA LYS THR PHE LYS ILE
SEQRES 1 B 246 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 246 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET ASN
SEQRES 3 B 246 TYR GLU LEU MET GLU PRO ALA LYS GLN ALA ARG PHE CYS
SEQRES 4 B 246 VAL ILE TRP LEU HIS GLY LEU GLY ALA ASP GLY HIS ASP
SEQRES 5 B 246 PHE VAL ASP ILE VAL ASN TYR PHE ASP VAL SER LEU ASP
SEQRES 6 B 246 GLU ILE ARG PHE ILE PHE PRO HIS ALA ASP ILE ILE PRO
SEQRES 7 B 246 VAL THR ILE ASN MET GLY MET GLN MET ARG ALA TRP TYR
SEQRES 8 B 246 ASP ILE LYS SER LEU ASP ALA ASN SER LEU ASN ARG VAL
SEQRES 9 B 246 VAL ASP VAL GLU GLY ILE ASN SER SER ILE ALA LYS VAL
SEQRES 10 B 246 ASN LYS LEU ILE ASP SER GLN VAL ASN GLN GLY ILE ALA
SEQRES 11 B 246 SER GLU ASN ILE ILE LEU ALA GLY PHE SER GLN GLY GLY
SEQRES 12 B 246 ILE ILE ALA THR TYR THR ALA ILE THR SER GLN ARG LYS
SEQRES 13 B 246 LEU GLY GLY ILE MET ALA LEU SER THR TYR LEU PRO ALA
SEQRES 14 B 246 TRP ASP ASN PHE LYS GLY LYS ILE THR SER ILE ASN LYS
SEQRES 15 B 246 GLY LEU PRO ILE LEU VAL CYS HIS GLY THR ASP ASP GLN
SEQRES 16 B 246 VAL LEU PRO GLU VAL LEU GLY HIS ASP LEU SER ASP LYS
SEQRES 17 B 246 LEU LYS VAL SER GLY PHE ALA ASN GLU TYR LYS HIS TYR
SEQRES 18 B 246 VAL GLY MET GLN HIS SER VAL CYS MET GLU GLU ILE LYS
SEQRES 19 B 246 ASP ILE SER ASN PHE ILE ALA LYS THR PHE LYS ILE
SEQRES 1 C 246 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 C 246 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET ASN
SEQRES 3 C 246 TYR GLU LEU MET GLU PRO ALA LYS GLN ALA ARG PHE CYS
SEQRES 4 C 246 VAL ILE TRP LEU HIS GLY LEU GLY ALA ASP GLY HIS ASP
SEQRES 5 C 246 PHE VAL ASP ILE VAL ASN TYR PHE ASP VAL SER LEU ASP
SEQRES 6 C 246 GLU ILE ARG PHE ILE PHE PRO HIS ALA ASP ILE ILE PRO
SEQRES 7 C 246 VAL THR ILE ASN MET GLY MET GLN MET ARG ALA TRP TYR
SEQRES 8 C 246 ASP ILE LYS SER LEU ASP ALA ASN SER LEU ASN ARG VAL
SEQRES 9 C 246 VAL ASP VAL GLU GLY ILE ASN SER SER ILE ALA LYS VAL
SEQRES 10 C 246 ASN LYS LEU ILE ASP SER GLN VAL ASN GLN GLY ILE ALA
SEQRES 11 C 246 SER GLU ASN ILE ILE LEU ALA GLY PHE SER GLN GLY GLY
SEQRES 12 C 246 ILE ILE ALA THR TYR THR ALA ILE THR SER GLN ARG LYS
SEQRES 13 C 246 LEU GLY GLY ILE MET ALA LEU SER THR TYR LEU PRO ALA
SEQRES 14 C 246 TRP ASP ASN PHE LYS GLY LYS ILE THR SER ILE ASN LYS
SEQRES 15 C 246 GLY LEU PRO ILE LEU VAL CYS HIS GLY THR ASP ASP GLN
SEQRES 16 C 246 VAL LEU PRO GLU VAL LEU GLY HIS ASP LEU SER ASP LYS
SEQRES 17 C 246 LEU LYS VAL SER GLY PHE ALA ASN GLU TYR LYS HIS TYR
SEQRES 18 C 246 VAL GLY MET GLN HIS SER VAL CYS MET GLU GLU ILE LYS
SEQRES 19 C 246 ASP ILE SER ASN PHE ILE ALA LYS THR PHE LYS ILE
SEQRES 1 D 246 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 D 246 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET ASN
SEQRES 3 D 246 TYR GLU LEU MET GLU PRO ALA LYS GLN ALA ARG PHE CYS
SEQRES 4 D 246 VAL ILE TRP LEU HIS GLY LEU GLY ALA ASP GLY HIS ASP
SEQRES 5 D 246 PHE VAL ASP ILE VAL ASN TYR PHE ASP VAL SER LEU ASP
SEQRES 6 D 246 GLU ILE ARG PHE ILE PHE PRO HIS ALA ASP ILE ILE PRO
SEQRES 7 D 246 VAL THR ILE ASN MET GLY MET GLN MET ARG ALA TRP TYR
SEQRES 8 D 246 ASP ILE LYS SER LEU ASP ALA ASN SER LEU ASN ARG VAL
SEQRES 9 D 246 VAL ASP VAL GLU GLY ILE ASN SER SER ILE ALA LYS VAL
SEQRES 10 D 246 ASN LYS LEU ILE ASP SER GLN VAL ASN GLN GLY ILE ALA
SEQRES 11 D 246 SER GLU ASN ILE ILE LEU ALA GLY PHE SER GLN GLY GLY
SEQRES 12 D 246 ILE ILE ALA THR TYR THR ALA ILE THR SER GLN ARG LYS
SEQRES 13 D 246 LEU GLY GLY ILE MET ALA LEU SER THR TYR LEU PRO ALA
SEQRES 14 D 246 TRP ASP ASN PHE LYS GLY LYS ILE THR SER ILE ASN LYS
SEQRES 15 D 246 GLY LEU PRO ILE LEU VAL CYS HIS GLY THR ASP ASP GLN
SEQRES 16 D 246 VAL LEU PRO GLU VAL LEU GLY HIS ASP LEU SER ASP LYS
SEQRES 17 D 246 LEU LYS VAL SER GLY PHE ALA ASN GLU TYR LYS HIS TYR
SEQRES 18 D 246 VAL GLY MET GLN HIS SER VAL CYS MET GLU GLU ILE LYS
SEQRES 19 D 246 ASP ILE SER ASN PHE ILE ALA LYS THR PHE LYS ILE
SEQRES 1 E 246 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 E 246 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET ASN
SEQRES 3 E 246 TYR GLU LEU MET GLU PRO ALA LYS GLN ALA ARG PHE CYS
SEQRES 4 E 246 VAL ILE TRP LEU HIS GLY LEU GLY ALA ASP GLY HIS ASP
SEQRES 5 E 246 PHE VAL ASP ILE VAL ASN TYR PHE ASP VAL SER LEU ASP
SEQRES 6 E 246 GLU ILE ARG PHE ILE PHE PRO HIS ALA ASP ILE ILE PRO
SEQRES 7 E 246 VAL THR ILE ASN MET GLY MET GLN MET ARG ALA TRP TYR
SEQRES 8 E 246 ASP ILE LYS SER LEU ASP ALA ASN SER LEU ASN ARG VAL
SEQRES 9 E 246 VAL ASP VAL GLU GLY ILE ASN SER SER ILE ALA LYS VAL
SEQRES 10 E 246 ASN LYS LEU ILE ASP SER GLN VAL ASN GLN GLY ILE ALA
SEQRES 11 E 246 SER GLU ASN ILE ILE LEU ALA GLY PHE SER GLN GLY GLY
SEQRES 12 E 246 ILE ILE ALA THR TYR THR ALA ILE THR SER GLN ARG LYS
SEQRES 13 E 246 LEU GLY GLY ILE MET ALA LEU SER THR TYR LEU PRO ALA
SEQRES 14 E 246 TRP ASP ASN PHE LYS GLY LYS ILE THR SER ILE ASN LYS
SEQRES 15 E 246 GLY LEU PRO ILE LEU VAL CYS HIS GLY THR ASP ASP GLN
SEQRES 16 E 246 VAL LEU PRO GLU VAL LEU GLY HIS ASP LEU SER ASP LYS
SEQRES 17 E 246 LEU LYS VAL SER GLY PHE ALA ASN GLU TYR LYS HIS TYR
SEQRES 18 E 246 VAL GLY MET GLN HIS SER VAL CYS MET GLU GLU ILE LYS
SEQRES 19 E 246 ASP ILE SER ASN PHE ILE ALA LYS THR PHE LYS ILE
SEQRES 1 F 246 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 F 246 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET ASN
SEQRES 3 F 246 TYR GLU LEU MET GLU PRO ALA LYS GLN ALA ARG PHE CYS
SEQRES 4 F 246 VAL ILE TRP LEU HIS GLY LEU GLY ALA ASP GLY HIS ASP
SEQRES 5 F 246 PHE VAL ASP ILE VAL ASN TYR PHE ASP VAL SER LEU ASP
SEQRES 6 F 246 GLU ILE ARG PHE ILE PHE PRO HIS ALA ASP ILE ILE PRO
SEQRES 7 F 246 VAL THR ILE ASN MET GLY MET GLN MET ARG ALA TRP TYR
SEQRES 8 F 246 ASP ILE LYS SER LEU ASP ALA ASN SER LEU ASN ARG VAL
SEQRES 9 F 246 VAL ASP VAL GLU GLY ILE ASN SER SER ILE ALA LYS VAL
SEQRES 10 F 246 ASN LYS LEU ILE ASP SER GLN VAL ASN GLN GLY ILE ALA
SEQRES 11 F 246 SER GLU ASN ILE ILE LEU ALA GLY PHE SER GLN GLY GLY
SEQRES 12 F 246 ILE ILE ALA THR TYR THR ALA ILE THR SER GLN ARG LYS
SEQRES 13 F 246 LEU GLY GLY ILE MET ALA LEU SER THR TYR LEU PRO ALA
SEQRES 14 F 246 TRP ASP ASN PHE LYS GLY LYS ILE THR SER ILE ASN LYS
SEQRES 15 F 246 GLY LEU PRO ILE LEU VAL CYS HIS GLY THR ASP ASP GLN
SEQRES 16 F 246 VAL LEU PRO GLU VAL LEU GLY HIS ASP LEU SER ASP LYS
SEQRES 17 F 246 LEU LYS VAL SER GLY PHE ALA ASN GLU TYR LYS HIS TYR
SEQRES 18 F 246 VAL GLY MET GLN HIS SER VAL CYS MET GLU GLU ILE LYS
SEQRES 19 F 246 ASP ILE SER ASN PHE ILE ALA LYS THR PHE LYS ILE
SEQRES 1 G 246 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 G 246 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET ASN
SEQRES 3 G 246 TYR GLU LEU MET GLU PRO ALA LYS GLN ALA ARG PHE CYS
SEQRES 4 G 246 VAL ILE TRP LEU HIS GLY LEU GLY ALA ASP GLY HIS ASP
SEQRES 5 G 246 PHE VAL ASP ILE VAL ASN TYR PHE ASP VAL SER LEU ASP
SEQRES 6 G 246 GLU ILE ARG PHE ILE PHE PRO HIS ALA ASP ILE ILE PRO
SEQRES 7 G 246 VAL THR ILE ASN MET GLY MET GLN MET ARG ALA TRP TYR
SEQRES 8 G 246 ASP ILE LYS SER LEU ASP ALA ASN SER LEU ASN ARG VAL
SEQRES 9 G 246 VAL ASP VAL GLU GLY ILE ASN SER SER ILE ALA LYS VAL
SEQRES 10 G 246 ASN LYS LEU ILE ASP SER GLN VAL ASN GLN GLY ILE ALA
SEQRES 11 G 246 SER GLU ASN ILE ILE LEU ALA GLY PHE SER GLN GLY GLY
SEQRES 12 G 246 ILE ILE ALA THR TYR THR ALA ILE THR SER GLN ARG LYS
SEQRES 13 G 246 LEU GLY GLY ILE MET ALA LEU SER THR TYR LEU PRO ALA
SEQRES 14 G 246 TRP ASP ASN PHE LYS GLY LYS ILE THR SER ILE ASN LYS
SEQRES 15 G 246 GLY LEU PRO ILE LEU VAL CYS HIS GLY THR ASP ASP GLN
SEQRES 16 G 246 VAL LEU PRO GLU VAL LEU GLY HIS ASP LEU SER ASP LYS
SEQRES 17 G 246 LEU LYS VAL SER GLY PHE ALA ASN GLU TYR LYS HIS TYR
SEQRES 18 G 246 VAL GLY MET GLN HIS SER VAL CYS MET GLU GLU ILE LYS
SEQRES 19 G 246 ASP ILE SER ASN PHE ILE ALA LYS THR PHE LYS ILE
SEQRES 1 H 246 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 H 246 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET ASN
SEQRES 3 H 246 TYR GLU LEU MET GLU PRO ALA LYS GLN ALA ARG PHE CYS
SEQRES 4 H 246 VAL ILE TRP LEU HIS GLY LEU GLY ALA ASP GLY HIS ASP
SEQRES 5 H 246 PHE VAL ASP ILE VAL ASN TYR PHE ASP VAL SER LEU ASP
SEQRES 6 H 246 GLU ILE ARG PHE ILE PHE PRO HIS ALA ASP ILE ILE PRO
SEQRES 7 H 246 VAL THR ILE ASN MET GLY MET GLN MET ARG ALA TRP TYR
SEQRES 8 H 246 ASP ILE LYS SER LEU ASP ALA ASN SER LEU ASN ARG VAL
SEQRES 9 H 246 VAL ASP VAL GLU GLY ILE ASN SER SER ILE ALA LYS VAL
SEQRES 10 H 246 ASN LYS LEU ILE ASP SER GLN VAL ASN GLN GLY ILE ALA
SEQRES 11 H 246 SER GLU ASN ILE ILE LEU ALA GLY PHE SER GLN GLY GLY
SEQRES 12 H 246 ILE ILE ALA THR TYR THR ALA ILE THR SER GLN ARG LYS
SEQRES 13 H 246 LEU GLY GLY ILE MET ALA LEU SER THR TYR LEU PRO ALA
SEQRES 14 H 246 TRP ASP ASN PHE LYS GLY LYS ILE THR SER ILE ASN LYS
SEQRES 15 H 246 GLY LEU PRO ILE LEU VAL CYS HIS GLY THR ASP ASP GLN
SEQRES 16 H 246 VAL LEU PRO GLU VAL LEU GLY HIS ASP LEU SER ASP LYS
SEQRES 17 H 246 LEU LYS VAL SER GLY PHE ALA ASN GLU TYR LYS HIS TYR
SEQRES 18 H 246 VAL GLY MET GLN HIS SER VAL CYS MET GLU GLU ILE LYS
SEQRES 19 H 246 ASP ILE SER ASN PHE ILE ALA LYS THR PHE LYS ILE
HET 0S1 E 301 5
HETNAM 0S1 N-((1R,2S)-2-ALLYL-4-OXOCYCLOBUTYL)-4-
HETNAM 2 0S1 METHYLBENZENESULFONAMIDE, BOUND FORM
FORMUL 9 0S1 C14 H19 N O3 S
FORMUL 10 HOH *458(H2 O)
HELIX 1 1 ASP A 28 PHE A 36 5 9
HELIX 2 2 ALA A 50 ILE A 53 5 4
HELIX 3 3 ILE A 57 ALA A 65 1 9
HELIX 4 4 SER A 76 VAL A 81 5 6
HELIX 5 5 VAL A 83 GLU A 84 5 2
HELIX 6 6 ILE A 86 ILE A 86 5 1
HELIX 7 7 ASN A 87 GLN A 103 1 17
HELIX 8 8 ALA A 106 GLU A 108 5 3
HELIX 9 9 GLY A 119 ILE A 127 1 9
HELIX 10 10 ALA A 145 LYS A 150 1 6
HELIX 11 11 THR A 154 LYS A 158 5 5
HELIX 12 12 PRO A 174 VAL A 187 1 14
HELIX 13 13 CYS A 205 PHE A 220 1 16
HELIX 14 14 ASP B 28 PHE B 36 5 9
HELIX 15 15 VAL B 55 GLY B 60 1 6
HELIX 16 16 GLY B 60 ALA B 65 1 6
HELIX 17 17 SER B 76 VAL B 80 5 5
HELIX 18 18 ASP B 82 GLN B 103 1 22
HELIX 19 19 ALA B 106 GLU B 108 5 3
HELIX 20 20 SER B 116 THR B 128 1 13
HELIX 21 21 ALA B 145 ILE B 153 5 9
HELIX 22 22 THR B 154 LYS B 158 5 5
HELIX 23 23 PRO B 174 SER B 188 1 15
HELIX 24 24 CYS B 205 LYS B 221 1 17
HELIX 25 25 VAL C 30 TYR C 35 5 6
HELIX 26 26 ALA C 50 ILE C 53 5 4
HELIX 27 27 ASN C 58 ALA C 65 1 8
HELIX 28 28 LEU C 77 VAL C 81 5 5
HELIX 29 29 ASP C 82 GLN C 103 1 22
HELIX 30 30 ALA C 106 GLU C 108 5 3
HELIX 31 31 SER C 116 THR C 128 1 13
HELIX 32 32 ALA C 145 LYS C 150 1 6
HELIX 33 33 PRO C 174 GLY C 189 1 16
HELIX 34 34 CYS C 205 PHE C 220 1 16
HELIX 35 35 ASP D 28 PHE D 36 5 9
HELIX 36 36 ALA D 50 ILE D 53 5 4
HELIX 37 37 VAL D 55 MET D 63 1 9
HELIX 38 38 LEU D 77 VAL D 81 5 5
HELIX 39 39 ASP D 82 GLN D 103 1 22
HELIX 40 40 ALA D 106 GLU D 108 5 3
HELIX 41 41 SER D 116 THR D 128 1 13
HELIX 42 42 ALA D 145 LYS D 150 1 6
HELIX 43 43 GLU D 175 GLY D 189 1 15
HELIX 44 44 CYS D 205 LYS D 221 1 17
HELIX 45 45 PHE E 29 PHE E 36 5 8
HELIX 46 46 SER E 39 ASP E 41 5 3
HELIX 47 48 ASP E 82 ASN E 102 1 21
HELIX 48 49 ALA E 106 GLU E 108 5 3
HELIX 49 50 SER E 116 ILE E 127 1 12
HELIX 50 51 ALA E 145 LYS E 150 1 6
HELIX 51 52 PRO E 174 GLY E 189 1 16
HELIX 52 53 CYS E 205 LYS E 221 1 17
HELIX 53 54 ASP F 28 PHE F 36 5 9
HELIX 54 55 GLY F 60 ARG F 64 5 5
HELIX 55 56 GLY F 85 GLN F 103 1 19
HELIX 56 57 ALA F 106 GLU F 108 5 3
HELIX 57 58 SER F 116 ILE F 127 1 12
HELIX 58 59 TRP F 146 GLY F 151 1 6
HELIX 59 60 PRO F 174 GLY F 189 1 16
HELIX 60 61 CYS F 205 PHE F 220 1 16
HELIX 61 62 PHE G 29 PHE G 36 5 8
HELIX 62 63 ASP G 82 SER G 88 1 7
HELIX 63 64 VAL G 93 GLY G 104 1 12
HELIX 64 65 SER G 116 SER G 129 1 14
HELIX 65 66 GLU G 175 SER G 188 1 14
HELIX 66 67 CYS G 205 PHE G 220 1 16
HELIX 67 68 VAL H 30 TYR H 35 5 6
HELIX 68 69 TRP H 66 LYS H 70 5 5
HELIX 69 70 ASP H 82 GLY H 104 1 23
HELIX 70 71 ALA H 106 GLU H 108 5 3
HELIX 71 72 SER H 116 THR H 125 1 10
HELIX 72 73 ALA H 145 GLY H 151 1 7
HELIX 73 74 GLU H 175 LYS H 186 1 12
HELIX 74 75 CYS H 205 PHE H 220 1 16
SHEET 1 A 7 TYR A 3 MET A 6 0
SHEET 2 A 7 ILE A 43 PRO A 48 -1 O PHE A 47 N GLU A 4
SHEET 3 A 7 PHE A 14 HIS A 20 1 N PHE A 14 O ARG A 44
SHEET 4 A 7 ILE A 110 PHE A 115 1 O ILE A 111 N ILE A 17
SHEET 5 A 7 GLY A 135 LEU A 139 1 O GLY A 135 N LEU A 112
SHEET 6 A 7 ILE A 162 GLY A 167 1 O LEU A 163 N ILE A 136
SHEET 7 A 7 ASN A 192 TYR A 197 1 O LYS A 195 N VAL A 164
SHEET 1 B 7 TYR B 3 MET B 6 0
SHEET 2 B 7 ILE B 43 PRO B 48 -1 O PHE B 47 N GLU B 4
SHEET 3 B 7 PHE B 14 HIS B 20 1 N VAL B 16 O ILE B 46
SHEET 4 B 7 ILE B 110 PHE B 115 1 O ILE B 111 N ILE B 17
SHEET 5 B 7 GLY B 135 LEU B 139 1 O MET B 137 N LEU B 112
SHEET 6 B 7 ILE B 162 GLY B 167 1 O LEU B 163 N ILE B 136
SHEET 7 B 7 GLU B 193 TYR B 197 1 O GLU B 193 N VAL B 164
SHEET 1 C 7 TYR C 3 MET C 6 0
SHEET 2 C 7 ILE C 43 PRO C 48 -1 O PHE C 47 N GLU C 4
SHEET 3 C 7 PHE C 14 LEU C 19 1 N TRP C 18 O ILE C 46
SHEET 4 C 7 ILE C 110 GLY C 114 1 O ILE C 111 N CYS C 15
SHEET 5 C 7 GLY C 135 LEU C 139 1 O LEU C 139 N GLY C 114
SHEET 6 C 7 ILE C 162 GLY C 167 1 O CYS C 165 N ALA C 138
SHEET 7 C 7 GLU C 193 TYR C 197 1 O GLU C 193 N ILE C 162
SHEET 1 D 7 TYR D 3 MET D 6 0
SHEET 2 D 7 ILE D 43 PRO D 48 -1 O PHE D 47 N GLU D 4
SHEET 3 D 7 PHE D 14 LEU D 19 1 N TRP D 18 O ILE D 46
SHEET 4 D 7 ILE D 110 PHE D 115 1 O ALA D 113 N LEU D 19
SHEET 5 D 7 GLY D 135 LEU D 139 1 O LEU D 139 N GLY D 114
SHEET 6 D 7 ILE D 162 GLY D 167 1 O LEU D 163 N ILE D 136
SHEET 7 D 7 GLU D 193 TYR D 197 1 O GLU D 193 N ILE D 162
SHEET 1 E 7 TYR E 3 MET E 6 0
SHEET 2 E 7 ILE E 43 PRO E 48 -1 O PHE E 47 N GLU E 4
SHEET 3 E 7 PHE E 14 LEU E 19 1 N VAL E 16 O ARG E 44
SHEET 4 E 7 ILE E 110 PHE E 115 1 O ILE E 111 N CYS E 15
SHEET 5 E 7 GLY E 135 LEU E 139 1 O GLY E 135 N LEU E 112
SHEET 6 E 7 ILE E 162 GLY E 167 1 O LEU E 163 N ILE E 136
SHEET 7 E 7 GLU E 193 TYR E 197 1 O GLU E 193 N ILE E 162
SHEET 1 F 7 TYR F 3 MET F 6 0
SHEET 2 F 7 ILE F 43 PRO F 48 -1 O PHE F 47 N GLU F 4
SHEET 3 F 7 PHE F 14 LEU F 19 1 N VAL F 16 O ILE F 46
SHEET 4 F 7 ILE F 110 PHE F 115 1 O ILE F 111 N ILE F 17
SHEET 5 F 7 GLY F 135 LEU F 139 1 O LEU F 139 N GLY F 114
SHEET 6 F 7 ILE F 162 GLY F 167 1 O LEU F 163 N ILE F 136
SHEET 7 F 7 GLU F 193 TYR F 197 1 O LYS F 195 N VAL F 164
SHEET 1 G 7 TYR G 3 MET G 6 0
SHEET 2 G 7 ILE G 43 PRO G 48 -1 O PHE G 45 N MET G 6
SHEET 3 G 7 PHE G 14 LEU G 19 1 N VAL G 16 O ARG G 44
SHEET 4 G 7 ILE G 110 PHE G 115 1 O ILE G 111 N CYS G 15
SHEET 5 G 7 ILE G 136 LEU G 139 1 O LEU G 139 N GLY G 114
SHEET 6 G 7 ILE G 162 GLY G 167 1 O CYS G 165 N ALA G 138
SHEET 7 G 7 ASN G 192 TYR G 197 1 O LYS G 195 N VAL G 164
SHEET 1 H 7 TYR H 3 MET H 6 0
SHEET 2 H 7 ILE H 43 PRO H 48 -1 O PHE H 45 N MET H 6
SHEET 3 H 7 PHE H 14 TRP H 18 1 N VAL H 16 O ARG H 44
SHEET 4 H 7 ILE H 110 PHE H 115 1 O ILE H 111 N CYS H 15
SHEET 5 H 7 GLY H 135 LEU H 139 1 O MET H 137 N GLY H 114
SHEET 6 H 7 ILE H 162 GLY H 167 1 O CYS H 165 N ALA H 138
SHEET 7 H 7 GLU H 193 TYR H 197 1 O GLU H 193 N ILE H 162
LINK OG SER E 116 C1 0S1 E 301 1555 1555 1.40
SITE 1 AC1 3 SER E 116 GLN E 117 HIS E 202
CRYST1 50.997 64.416 139.039 94.89 90.12 89.96 P 1 8
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 0.019609 -0.000014 0.000040 0.00000
SCALE2 0.000000 0.015524 0.001328 0.00000
SCALE3 0.000000 0.000000 0.007219 0.00000
TER 1702 ILE A 222
TER 3421 ILE B 222
TER 5140 ILE C 222
TER 6861 ILE D 222
TER 8469 ILE E 222
TER 10075 ILE F 222
TER 11674 ILE G 222
TER 13276 ILE H 222
MASTER 1424 0 1 74 56 0 1 613722 8 6 152
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