HEADER HYDROLASE/HYDROLASE INHIBITOR 18-APR-17 5Q02
TITLE HUMAN LIVER FRUCTOSE-1,6-BISPHOSPHATASE 1 (FRUCTOSE 1,6-BISPHOSPHATE
TITLE 2 1-PHOSPHATASE, E.C.3.1.3.11) COMPLEXED WITH THE ALLOSTERIC INHIBITOR
TITLE 3 1-(5-BROMO-1,3-THIAZOL-2-YL)-3-[5-(1,2-OXAZOL-3-YL)THIOPHEN-2-
TITLE 4 YL]SULFONYLUREA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FRUCTOSE-1,6-BISPHOSPHATASE 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: GROWTH-INHIBITING PROTEIN 17,CDNA FLJ75786,HIGHLY SIMILAR TO
COMPND 5 HOMO SAPIENS FRUCTOSE-1,6-BISPHOSPHATASE 1 (FBP1),MRNA;
COMPND 6 EC: 3.1.3.11;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FBP1, HCG_1640493;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS D3R DOCKING, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.RUF,C.JOSEPH,A.ALKER,D.BANNER,T.TETAZ,J.BENZ,B.KUHN,M.G.RUDOLPH,
AUTHOR 2 H.YANG,C.SHAO,S.K.BURLEY
REVDAT 5 06-MAR-24 5Q02 1 REMARK
REVDAT 4 10-FEB-21 5Q02 1 AUTHOR
REVDAT 3 06-FEB-19 5Q02 1 AUTHOR JRNL
REVDAT 2 16-JAN-19 5Q02 1 REMARK
REVDAT 1 09-JAN-19 5Q02 0
JRNL AUTH A.RUF,C.JOSEPH,A.ALKER,D.BANNER,T.TETAZ,J.BENZ,B.KUHN,
JRNL AUTH 2 M.G.RUDOLPH
JRNL TITL HUMAN LIVER FRUCTOSE-1,6-BISPHOSPHATASE 1 (FRUCTOSE
JRNL TITL 2 1,6-BISPHOSPHATE 1-PHOSPHATASE, E.C.3.1.3.11) COMPLEXED WITH
JRNL TITL 3 THE ALLOSTERIC INHIBITOR
JRNL TITL 4 1-(5-BROMO-1,3-THIAZOL-2-YL)-3-[5-(1,2-OXAZOL-3-YL)
JRNL TITL 5 THIOPHEN-2-YL]SULFONYLUREA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 91565
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4584
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 19.9775 - 6.4386 1.00 3172 171 0.1720 0.2002
REMARK 3 2 6.4386 - 5.1392 1.00 3032 160 0.1678 0.1988
REMARK 3 3 5.1392 - 4.4980 1.00 3031 138 0.1260 0.1528
REMARK 3 4 4.4980 - 4.0906 1.00 2977 171 0.1288 0.1599
REMARK 3 5 4.0906 - 3.7995 1.00 2938 179 0.1348 0.1763
REMARK 3 6 3.7995 - 3.5769 1.00 2976 139 0.1359 0.1844
REMARK 3 7 3.5769 - 3.3987 1.00 2958 156 0.1359 0.1725
REMARK 3 8 3.3987 - 3.2514 1.00 2959 137 0.1420 0.1831
REMARK 3 9 3.2514 - 3.1267 1.00 2934 170 0.1394 0.1662
REMARK 3 10 3.1267 - 3.0192 1.00 2962 140 0.1464 0.1959
REMARK 3 11 3.0192 - 2.9251 1.00 2911 147 0.1484 0.1997
REMARK 3 12 2.9251 - 2.8417 1.00 2942 155 0.1436 0.2138
REMARK 3 13 2.8417 - 2.7671 1.00 2943 129 0.1428 0.2152
REMARK 3 14 2.7671 - 2.6997 1.00 2906 156 0.1422 0.1934
REMARK 3 15 2.6997 - 2.6385 1.00 2935 148 0.1433 0.2216
REMARK 3 16 2.6385 - 2.5825 1.00 2895 148 0.1476 0.2083
REMARK 3 17 2.5825 - 2.5309 1.00 2931 149 0.1572 0.2027
REMARK 3 18 2.5309 - 2.4832 1.00 2886 166 0.1533 0.1944
REMARK 3 19 2.4832 - 2.4390 1.00 2907 160 0.1529 0.2203
REMARK 3 20 2.4390 - 2.3977 1.00 2860 168 0.1562 0.2062
REMARK 3 21 2.3977 - 2.3591 1.00 2958 161 0.1554 0.2341
REMARK 3 22 2.3591 - 2.3228 1.00 2829 163 0.1530 0.2094
REMARK 3 23 2.3228 - 2.2887 1.00 2938 148 0.1535 0.1942
REMARK 3 24 2.2887 - 2.2565 1.00 2899 149 0.1646 0.2374
REMARK 3 25 2.2565 - 2.2261 1.00 2903 151 0.1789 0.2471
REMARK 3 26 2.2261 - 2.1972 1.00 2885 166 0.1821 0.2486
REMARK 3 27 2.1972 - 2.1698 1.00 2879 161 0.1804 0.2268
REMARK 3 28 2.1698 - 2.1437 1.00 2893 149 0.1862 0.2259
REMARK 3 29 2.1437 - 2.1188 0.98 2890 145 0.1831 0.2297
REMARK 3 30 2.1188 - 2.0950 0.65 1852 104 0.1935 0.2266
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.350
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 10022
REMARK 3 ANGLE : 0.923 13549
REMARK 3 CHIRALITY : 0.059 1531
REMARK 3 PLANARITY : 0.006 1733
REMARK 3 DIHEDRAL : 12.008 6081
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 9 THROUGH 122 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8570 43.0501 16.3922
REMARK 3 T TENSOR
REMARK 3 T11: 0.0974 T22: 0.0776
REMARK 3 T33: 0.0440 T12: 0.0073
REMARK 3 T13: 0.0091 T23: 0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 0.0308 L22: 0.0074
REMARK 3 L33: 0.0257 L12: -0.0065
REMARK 3 L13: -0.0015 L23: -0.0006
REMARK 3 S TENSOR
REMARK 3 S11: -0.0162 S12: 0.0417 S13: 0.0019
REMARK 3 S21: 0.0332 S22: 0.0138 S23: 0.0359
REMARK 3 S31: -0.0926 S32: -0.0656 S33: -0.0211
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 123 THROUGH 247 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.0319 43.3243 11.0328
REMARK 3 T TENSOR
REMARK 3 T11: 0.1400 T22: 0.1468
REMARK 3 T33: 0.0992 T12: -0.0444
REMARK 3 T13: 0.0114 T23: 0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 0.0226 L22: 0.0215
REMARK 3 L33: 0.0527 L12: -0.0106
REMARK 3 L13: -0.0087 L23: -0.0173
REMARK 3 S TENSOR
REMARK 3 S11: -0.0428 S12: 0.1101 S13: 0.0403
REMARK 3 S21: -0.0322 S22: 0.0222 S23: -0.0022
REMARK 3 S31: -0.1369 S32: 0.0916 S33: -0.0238
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 248 THROUGH 335 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.6274 45.5075 2.7835
REMARK 3 T TENSOR
REMARK 3 T11: 0.1346 T22: 0.1917
REMARK 3 T33: 0.0401 T12: -0.1238
REMARK 3 T13: 0.0561 T23: 0.0396
REMARK 3 L TENSOR
REMARK 3 L11: 0.0098 L22: 0.0598
REMARK 3 L33: 0.0040 L12: -0.0110
REMARK 3 L13: 0.0033 L23: -0.0086
REMARK 3 S TENSOR
REMARK 3 S11: 0.0241 S12: 0.0284 S13: 0.0265
REMARK 3 S21: -0.0402 S22: -0.0169 S23: -0.0511
REMARK 3 S31: -0.0358 S32: 0.0389 S33: 0.0135
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 9 THROUGH 122 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.2424 19.1472 37.1305
REMARK 3 T TENSOR
REMARK 3 T11: 0.0481 T22: 0.0876
REMARK 3 T33: 0.1249 T12: 0.0135
REMARK 3 T13: -0.0042 T23: -0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 0.0181 L22: 0.0062
REMARK 3 L33: 0.0208 L12: -0.0141
REMARK 3 L13: -0.0024 L23: -0.0014
REMARK 3 S TENSOR
REMARK 3 S11: 0.0014 S12: -0.0821 S13: -0.1001
REMARK 3 S21: 0.0069 S22: 0.0261 S23: 0.0359
REMARK 3 S31: -0.0055 S32: 0.0248 S33: 0.0202
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 123 THROUGH 247 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.2488 18.4175 18.9687
REMARK 3 T TENSOR
REMARK 3 T11: -0.0643 T22: 0.1101
REMARK 3 T33: 0.0422 T12: 0.0580
REMARK 3 T13: 0.0706 T23: -0.0730
REMARK 3 L TENSOR
REMARK 3 L11: 0.0673 L22: 0.0132
REMARK 3 L33: 0.0123 L12: -0.0147
REMARK 3 L13: -0.0094 L23: 0.0039
REMARK 3 S TENSOR
REMARK 3 S11: 0.0541 S12: 0.0894 S13: -0.0842
REMARK 3 S21: -0.0217 S22: 0.0383 S23: -0.0395
REMARK 3 S31: 0.0023 S32: 0.1169 S33: 0.1127
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 248 THROUGH 335 )
REMARK 3 ORIGIN FOR THE GROUP (A): 49.2326 16.1871 16.3408
REMARK 3 T TENSOR
REMARK 3 T11: 0.0199 T22: 0.2106
REMARK 3 T33: 0.0909 T12: 0.0694
REMARK 3 T13: 0.0000 T23: -0.0657
REMARK 3 L TENSOR
REMARK 3 L11: 0.0097 L22: 0.0145
REMARK 3 L33: 0.0035 L12: -0.0032
REMARK 3 L13: 0.0047 L23: 0.0008
REMARK 3 S TENSOR
REMARK 3 S11: -0.0013 S12: 0.0458 S13: -0.0319
REMARK 3 S21: 0.0004 S22: -0.0289 S23: -0.0181
REMARK 3 S31: -0.0003 S32: 0.0466 S33: -0.0383
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 9 THROUGH 106 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5028 48.7247 39.8221
REMARK 3 T TENSOR
REMARK 3 T11: 0.1302 T22: 0.0279
REMARK 3 T33: 0.0722 T12: 0.0159
REMARK 3 T13: 0.0195 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.0150 L22: 0.0085
REMARK 3 L33: 0.0208 L12: 0.0014
REMARK 3 L13: 0.0007 L23: 0.0071
REMARK 3 S TENSOR
REMARK 3 S11: 0.0211 S12: 0.0095 S13: 0.0484
REMARK 3 S21: -0.0538 S22: 0.0184 S23: -0.0299
REMARK 3 S31: -0.0942 S32: 0.0194 S33: 0.0174
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 107 THROUGH 148 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4326 53.5691 46.9530
REMARK 3 T TENSOR
REMARK 3 T11: 0.1458 T22: 0.0085
REMARK 3 T33: 0.0931 T12: 0.0243
REMARK 3 T13: 0.0530 T23: -0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 0.0221 L22: 0.0323
REMARK 3 L33: 0.0152 L12: -0.0039
REMARK 3 L13: -0.0071 L23: 0.0108
REMARK 3 S TENSOR
REMARK 3 S11: -0.0219 S12: -0.0283 S13: -0.0011
REMARK 3 S21: 0.0044 S22: 0.0012 S23: -0.0052
REMARK 3 S31: -0.0217 S32: 0.0214 S33: -0.0131
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 149 THROUGH 247 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4738 42.4474 47.0577
REMARK 3 T TENSOR
REMARK 3 T11: 0.0841 T22: 0.0795
REMARK 3 T33: 0.0932 T12: 0.0145
REMARK 3 T13: 0.0182 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.0181 L22: 0.0180
REMARK 3 L33: 0.0136 L12: -0.0091
REMARK 3 L13: 0.0125 L23: 0.0051
REMARK 3 S TENSOR
REMARK 3 S11: 0.0236 S12: 0.0010 S13: 0.0577
REMARK 3 S21: -0.0259 S22: -0.0043 S23: 0.0713
REMARK 3 S31: -0.0575 S32: -0.0630 S33: 0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 248 THROUGH 335 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7462 48.6185 53.6283
REMARK 3 T TENSOR
REMARK 3 T11: -0.0045 T22: -0.0566
REMARK 3 T33: 0.0443 T12: 0.1525
REMARK 3 T13: 0.0655 T23: -0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 0.0017 L22: 0.0266
REMARK 3 L33: -0.0009 L12: -0.0081
REMARK 3 L13: 0.0002 L23: -0.0024
REMARK 3 S TENSOR
REMARK 3 S11: 0.0211 S12: -0.0246 S13: 0.0338
REMARK 3 S21: 0.0511 S22: 0.0177 S23: 0.0166
REMARK 3 S31: -0.0442 S32: -0.0442 S33: 0.0398
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 9 THROUGH 28 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.2796 9.3872 47.2067
REMARK 3 T TENSOR
REMARK 3 T11: 0.1374 T22: 0.1776
REMARK 3 T33: 0.3151 T12: 0.0225
REMARK 3 T13: -0.0383 T23: 0.0217
REMARK 3 L TENSOR
REMARK 3 L11: 0.0026 L22: 0.0008
REMARK 3 L33: 0.0001 L12: -0.0005
REMARK 3 L13: 0.0005 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0008 S12: -0.0090 S13: -0.0176
REMARK 3 S21: -0.0018 S22: 0.0026 S23: -0.0068
REMARK 3 S31: 0.0172 S32: 0.0098 S33: -0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 29 THROUGH 88 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.7297 19.0622 33.1640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0318 T22: 0.0536
REMARK 3 T33: 0.0474 T12: -0.0008
REMARK 3 T13: 0.0055 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.0035 L22: 0.0062
REMARK 3 L33: 0.0063 L12: 0.0045
REMARK 3 L13: 0.0023 L23: 0.0013
REMARK 3 S TENSOR
REMARK 3 S11: 0.0020 S12: 0.0262 S13: -0.0314
REMARK 3 S21: -0.0209 S22: 0.0154 S23: -0.0082
REMARK 3 S31: 0.0237 S32: -0.0041 S33: 0.0060
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 89 THROUGH 122 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.4169 5.6773 36.9314
REMARK 3 T TENSOR
REMARK 3 T11: 0.0923 T22: 0.0360
REMARK 3 T33: 0.1165 T12: 0.0020
REMARK 3 T13: -0.0067 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.0039 L22: 0.0081
REMARK 3 L33: 0.0049 L12: 0.0005
REMARK 3 L13: -0.0048 L23: 0.0010
REMARK 3 S TENSOR
REMARK 3 S11: 0.0160 S12: 0.0108 S13: -0.0241
REMARK 3 S21: -0.0215 S22: 0.0101 S23: 0.0081
REMARK 3 S31: 0.0192 S32: -0.0013 S33: 0.0054
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 123 THROUGH 155 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.7185 8.5115 43.3057
REMARK 3 T TENSOR
REMARK 3 T11: 0.0843 T22: 0.0041
REMARK 3 T33: 0.1098 T12: 0.0040
REMARK 3 T13: 0.0148 T23: 0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 0.0062 L22: 0.0247
REMARK 3 L33: 0.0172 L12: 0.0051
REMARK 3 L13: -0.0048 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0029 S12: 0.0006 S13: 0.0116
REMARK 3 S21: -0.0013 S22: 0.0033 S23: 0.0132
REMARK 3 S31: -0.0186 S32: -0.0282 S33: 0.0020
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 156 THROUGH 179 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4176 14.7947 49.6157
REMARK 3 T TENSOR
REMARK 3 T11: 0.0687 T22: 0.0075
REMARK 3 T33: 0.0852 T12: 0.0323
REMARK 3 T13: 0.0082 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 0.0026 L22: 0.0106
REMARK 3 L33: 0.0138 L12: -0.0021
REMARK 3 L13: -0.0052 L23: 0.0019
REMARK 3 S TENSOR
REMARK 3 S11: 0.0119 S12: -0.0073 S13: -0.0306
REMARK 3 S21: 0.0001 S22: 0.0084 S23: -0.0050
REMARK 3 S31: -0.0028 S32: 0.0080 S33: 0.0068
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 180 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.9276 22.5144 54.0190
REMARK 3 T TENSOR
REMARK 3 T11: 0.1118 T22: 0.1163
REMARK 3 T33: 0.0916 T12: 0.0011
REMARK 3 T13: 0.0046 T23: 0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 0.0077 L22: 0.0029
REMARK 3 L33: 0.0022 L12: 0.0071
REMARK 3 L13: 0.0049 L23: 0.0053
REMARK 3 S TENSOR
REMARK 3 S11: 0.0213 S12: -0.0044 S13: -0.0190
REMARK 3 S21: 0.0452 S22: 0.0007 S23: -0.0420
REMARK 3 S31: 0.0195 S32: 0.0099 S33: 0.0000
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 213 THROUGH 231 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.7736 24.7175 64.5480
REMARK 3 T TENSOR
REMARK 3 T11: 0.1208 T22: 0.1067
REMARK 3 T33: 0.1062 T12: -0.0264
REMARK 3 T13: 0.0411 T23: 0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 0.0018 L22: 0.0010
REMARK 3 L33: 0.0002 L12: 0.0006
REMARK 3 L13: -0.0000 L23: -0.0009
REMARK 3 S TENSOR
REMARK 3 S11: -0.0026 S12: 0.0130 S13: 0.0039
REMARK 3 S21: 0.0021 S22: 0.0051 S23: 0.0101
REMARK 3 S31: 0.0067 S32: -0.0100 S33: -0.0006
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 232 THROUGH 247 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1124 30.4679 66.3818
REMARK 3 T TENSOR
REMARK 3 T11: 0.1401 T22: 0.0896
REMARK 3 T33: 0.0625 T12: -0.0094
REMARK 3 T13: 0.0344 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 0.0020 L22: 0.0033
REMARK 3 L33: 0.0012 L12: 0.0003
REMARK 3 L13: -0.0002 L23: -0.0011
REMARK 3 S TENSOR
REMARK 3 S11: 0.0015 S12: 0.0086 S13: -0.0026
REMARK 3 S21: -0.0046 S22: -0.0010 S23: -0.0016
REMARK 3 S31: 0.0033 S32: -0.0000 S33: -0.0007
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 248 THROUGH 274 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.7388 20.4663 56.1816
REMARK 3 T TENSOR
REMARK 3 T11: 0.0941 T22: 0.0739
REMARK 3 T33: 0.0811 T12: -0.0164
REMARK 3 T13: 0.0119 T23: -0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 0.0010 L22: 0.0004
REMARK 3 L33: 0.0024 L12: -0.0014
REMARK 3 L13: -0.0013 L23: 0.0017
REMARK 3 S TENSOR
REMARK 3 S11: -0.0089 S12: 0.0040 S13: -0.0034
REMARK 3 S21: 0.0054 S22: -0.0076 S23: 0.0101
REMARK 3 S31: -0.0059 S32: 0.0005 S33: -0.0000
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 275 THROUGH 335 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8940 11.7632 58.9718
REMARK 3 T TENSOR
REMARK 3 T11: 0.0933 T22: 0.0738
REMARK 3 T33: 0.0786 T12: -0.0060
REMARK 3 T13: 0.0077 T23: 0.0280
REMARK 3 L TENSOR
REMARK 3 L11: 0.0081 L22: 0.0087
REMARK 3 L33: 0.0038 L12: 0.0008
REMARK 3 L13: -0.0033 L23: 0.0039
REMARK 3 S TENSOR
REMARK 3 S11: 0.0269 S12: 0.0004 S13: -0.0239
REMARK 3 S21: 0.0478 S22: -0.0211 S23: 0.0472
REMARK 3 S31: 0.0082 S32: -0.0075 S33: -0.0026
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 9 THROUGH 37 OR RESID
REMARK 3 39 THROUGH 61 OR RESID 72 THROUGH 335))
REMARK 3 SELECTION : (CHAIN B AND (RESID 9 THROUGH 37 OR RESID
REMARK 3 39 THROUGH 335))
REMARK 3 ATOM PAIRS NUMBER : 6090
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 9 THROUGH 37 OR RESID
REMARK 3 39 THROUGH 61 OR RESID 72 THROUGH 335))
REMARK 3 SELECTION : (CHAIN C AND (RESID 9 THROUGH 37 OR RESID
REMARK 3 39 THROUGH 61 OR RESID 72 THROUGH 335))
REMARK 3 ATOM PAIRS NUMBER : 6090
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 9 THROUGH 37 OR RESID
REMARK 3 39 THROUGH 61 OR RESID 72 THROUGH 335))
REMARK 3 SELECTION : (CHAIN D AND (RESID 9 THROUGH 37 OR RESID
REMARK 3 39 THROUGH 335))
REMARK 3 ATOM PAIRS NUMBER : 6090
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5Q02 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1001401328.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 91565
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.095
REMARK 200 RESOLUTION RANGE LOW (A) : 19.977
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.0, 0.1M AMMONIUM
REMARK 280 ACETATE, 12% PEG 3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 33.60150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 139.00300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.65550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 139.00300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.60150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.65550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 0
REMARK 465 ALA A 1
REMARK 465 ASP A 2
REMARK 465 GLN A 3
REMARK 465 ALA A 4
REMARK 465 PRO A 5
REMARK 465 PHE A 6
REMARK 465 ASP A 7
REMARK 465 THR A 8
REMARK 465 SER A 62
REMARK 465 THR A 63
REMARK 465 ASN A 64
REMARK 465 VAL A 65
REMARK 465 THR A 66
REMARK 465 GLY A 67
REMARK 465 ASP A 68
REMARK 465 GLN A 69
REMARK 465 ALA A 336
REMARK 465 GLN A 337
REMARK 465 MET B 0
REMARK 465 ALA B 1
REMARK 465 ASP B 2
REMARK 465 GLN B 3
REMARK 465 ALA B 4
REMARK 465 PRO B 5
REMARK 465 PHE B 6
REMARK 465 ASP B 7
REMARK 465 THR B 8
REMARK 465 SER B 62
REMARK 465 THR B 63
REMARK 465 ASN B 64
REMARK 465 VAL B 65
REMARK 465 THR B 66
REMARK 465 GLY B 67
REMARK 465 ASP B 68
REMARK 465 GLN B 69
REMARK 465 VAL B 70
REMARK 465 LYS B 71
REMARK 465 ALA B 336
REMARK 465 GLN B 337
REMARK 465 MET C 0
REMARK 465 ALA C 1
REMARK 465 ASP C 2
REMARK 465 GLN C 3
REMARK 465 ALA C 4
REMARK 465 PRO C 5
REMARK 465 PHE C 6
REMARK 465 ASP C 7
REMARK 465 THR C 8
REMARK 465 SER C 62
REMARK 465 THR C 63
REMARK 465 ASN C 64
REMARK 465 VAL C 65
REMARK 465 THR C 66
REMARK 465 GLY C 67
REMARK 465 ASP C 68
REMARK 465 GLN C 69
REMARK 465 VAL C 70
REMARK 465 ALA C 336
REMARK 465 GLN C 337
REMARK 465 MET D 0
REMARK 465 ALA D 1
REMARK 465 ASP D 2
REMARK 465 GLN D 3
REMARK 465 ALA D 4
REMARK 465 PRO D 5
REMARK 465 PHE D 6
REMARK 465 ASP D 7
REMARK 465 THR D 8
REMARK 465 SER D 62
REMARK 465 THR D 63
REMARK 465 ASN D 64
REMARK 465 VAL D 65
REMARK 465 THR D 66
REMARK 465 GLY D 67
REMARK 465 ASP D 68
REMARK 465 GLN D 69
REMARK 465 VAL D 70
REMARK 465 LYS D 71
REMARK 465 ALA D 336
REMARK 465 GLN D 337
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 108 CD
REMARK 480 ARG B 140 CZ
REMARK 480 GLU C 332 CD
REMARK 480 GLU D 19 CD
REMARK 480 ARG D 140 CZ
REMARK 480 LYS D 274 CE
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH1 ARG B 22 OE1 GLN D 32 2.12
REMARK 500 O PRO B 271 O HOH B 501 2.16
REMARK 500 O HOH A 728 O HOH D 567 2.17
REMARK 500 O HOH D 753 O HOH D 784 2.17
REMARK 500 O HOH B 532 O HOH B 705 2.18
REMARK 500 NH2 ARG D 157 O HOH D 501 2.19
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 LEU A 33 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 LEU B 33 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
REMARK 500 ARG C 254 NE - CZ - NH2 ANGL. DEV. = -3.2 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 GLU A 280 -58.70 -121.96
REMARK 500 GLU B 280 -58.07 -121.86
REMARK 500 LEU C 153 54.59 -91.16
REMARK 500 GLU C 280 -59.76 -122.75
REMARK 500 ASP D 235 -147.01 -91.81
REMARK 500 GLU D 280 -59.39 -124.23
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 A 736 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH B 750 DISTANCE = 6.90 ANGSTROMS
REMARK 525 HOH D 816 DISTANCE = 7.23 ANGSTROMS
REMARK 525 HOH D 817 DISTANCE = 7.85 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 95J A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 95J B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 95J C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 95J D 401
DBREF 5Q02 A 0 337 UNP Q2TU34 Q2TU34_HUMAN 1 338
DBREF 5Q02 B 0 337 UNP Q2TU34 Q2TU34_HUMAN 1 338
DBREF 5Q02 C 0 337 UNP Q2TU34 Q2TU34_HUMAN 1 338
DBREF 5Q02 D 0 337 UNP Q2TU34 Q2TU34_HUMAN 1 338
SEQRES 1 A 338 MET ALA ASP GLN ALA PRO PHE ASP THR ASP VAL ASN THR
SEQRES 2 A 338 LEU THR ARG PHE VAL MET GLU GLU GLY ARG LYS ALA ARG
SEQRES 3 A 338 GLY THR GLY GLU LEU THR GLN LEU LEU ASN SER LEU CYS
SEQRES 4 A 338 THR ALA VAL LYS ALA ILE SER SER ALA VAL ARG LYS ALA
SEQRES 5 A 338 GLY ILE ALA HIS LEU TYR GLY ILE ALA GLY SER THR ASN
SEQRES 6 A 338 VAL THR GLY ASP GLN VAL LYS LYS LEU ASP VAL LEU SER
SEQRES 7 A 338 ASN ASP LEU VAL MET ASN MET LEU LYS SER SER PHE ALA
SEQRES 8 A 338 THR CYS VAL LEU VAL SER GLU GLU ASP LYS HIS ALA ILE
SEQRES 9 A 338 ILE VAL GLU PRO GLU LYS ARG GLY LYS TYR VAL VAL CYS
SEQRES 10 A 338 PHE ASP PRO LEU ASP GLY SER SER ASN ILE ASP CYS LEU
SEQRES 11 A 338 VAL SER VAL GLY THR ILE PHE GLY ILE TYR ARG LYS LYS
SEQRES 12 A 338 SER THR ASP GLU PRO SER GLU LYS ASP ALA LEU GLN PRO
SEQRES 13 A 338 GLY ARG ASN LEU VAL ALA ALA GLY TYR ALA LEU TYR GLY
SEQRES 14 A 338 SER ALA THR MET LEU VAL LEU ALA MET ASP CYS GLY VAL
SEQRES 15 A 338 ASN CYS PHE MET LEU ASP PRO ALA ILE GLY GLU PHE ILE
SEQRES 16 A 338 LEU VAL ASP LYS ASP VAL LYS ILE LYS LYS LYS GLY LYS
SEQRES 17 A 338 ILE TYR SER LEU ASN GLU GLY TYR ALA LYS ASP PHE ASP
SEQRES 18 A 338 PRO ALA VAL THR GLU TYR ILE GLN ARG LYS LYS PHE PRO
SEQRES 19 A 338 PRO ASP ASN SER ALA PRO TYR GLY ALA ARG TYR VAL GLY
SEQRES 20 A 338 SER MET VAL ALA ASP VAL HIS ARG THR LEU VAL TYR GLY
SEQRES 21 A 338 GLY ILE PHE LEU TYR PRO ALA ASN LYS LYS SER PRO ASN
SEQRES 22 A 338 GLY LYS LEU ARG LEU LEU TYR GLU CYS ASN PRO MET ALA
SEQRES 23 A 338 TYR VAL MET GLU LYS ALA GLY GLY MET ALA THR THR GLY
SEQRES 24 A 338 LYS GLU ALA VAL LEU ASP VAL ILE PRO THR ASP ILE HIS
SEQRES 25 A 338 GLN ARG ALA PRO VAL ILE LEU GLY SER PRO ASP ASP VAL
SEQRES 26 A 338 LEU GLU PHE LEU LYS VAL TYR GLU LYS HIS SER ALA GLN
SEQRES 1 B 338 MET ALA ASP GLN ALA PRO PHE ASP THR ASP VAL ASN THR
SEQRES 2 B 338 LEU THR ARG PHE VAL MET GLU GLU GLY ARG LYS ALA ARG
SEQRES 3 B 338 GLY THR GLY GLU LEU THR GLN LEU LEU ASN SER LEU CYS
SEQRES 4 B 338 THR ALA VAL LYS ALA ILE SER SER ALA VAL ARG LYS ALA
SEQRES 5 B 338 GLY ILE ALA HIS LEU TYR GLY ILE ALA GLY SER THR ASN
SEQRES 6 B 338 VAL THR GLY ASP GLN VAL LYS LYS LEU ASP VAL LEU SER
SEQRES 7 B 338 ASN ASP LEU VAL MET ASN MET LEU LYS SER SER PHE ALA
SEQRES 8 B 338 THR CYS VAL LEU VAL SER GLU GLU ASP LYS HIS ALA ILE
SEQRES 9 B 338 ILE VAL GLU PRO GLU LYS ARG GLY LYS TYR VAL VAL CYS
SEQRES 10 B 338 PHE ASP PRO LEU ASP GLY SER SER ASN ILE ASP CYS LEU
SEQRES 11 B 338 VAL SER VAL GLY THR ILE PHE GLY ILE TYR ARG LYS LYS
SEQRES 12 B 338 SER THR ASP GLU PRO SER GLU LYS ASP ALA LEU GLN PRO
SEQRES 13 B 338 GLY ARG ASN LEU VAL ALA ALA GLY TYR ALA LEU TYR GLY
SEQRES 14 B 338 SER ALA THR MET LEU VAL LEU ALA MET ASP CYS GLY VAL
SEQRES 15 B 338 ASN CYS PHE MET LEU ASP PRO ALA ILE GLY GLU PHE ILE
SEQRES 16 B 338 LEU VAL ASP LYS ASP VAL LYS ILE LYS LYS LYS GLY LYS
SEQRES 17 B 338 ILE TYR SER LEU ASN GLU GLY TYR ALA LYS ASP PHE ASP
SEQRES 18 B 338 PRO ALA VAL THR GLU TYR ILE GLN ARG LYS LYS PHE PRO
SEQRES 19 B 338 PRO ASP ASN SER ALA PRO TYR GLY ALA ARG TYR VAL GLY
SEQRES 20 B 338 SER MET VAL ALA ASP VAL HIS ARG THR LEU VAL TYR GLY
SEQRES 21 B 338 GLY ILE PHE LEU TYR PRO ALA ASN LYS LYS SER PRO ASN
SEQRES 22 B 338 GLY LYS LEU ARG LEU LEU TYR GLU CYS ASN PRO MET ALA
SEQRES 23 B 338 TYR VAL MET GLU LYS ALA GLY GLY MET ALA THR THR GLY
SEQRES 24 B 338 LYS GLU ALA VAL LEU ASP VAL ILE PRO THR ASP ILE HIS
SEQRES 25 B 338 GLN ARG ALA PRO VAL ILE LEU GLY SER PRO ASP ASP VAL
SEQRES 26 B 338 LEU GLU PHE LEU LYS VAL TYR GLU LYS HIS SER ALA GLN
SEQRES 1 C 338 MET ALA ASP GLN ALA PRO PHE ASP THR ASP VAL ASN THR
SEQRES 2 C 338 LEU THR ARG PHE VAL MET GLU GLU GLY ARG LYS ALA ARG
SEQRES 3 C 338 GLY THR GLY GLU LEU THR GLN LEU LEU ASN SER LEU CYS
SEQRES 4 C 338 THR ALA VAL LYS ALA ILE SER SER ALA VAL ARG LYS ALA
SEQRES 5 C 338 GLY ILE ALA HIS LEU TYR GLY ILE ALA GLY SER THR ASN
SEQRES 6 C 338 VAL THR GLY ASP GLN VAL LYS LYS LEU ASP VAL LEU SER
SEQRES 7 C 338 ASN ASP LEU VAL MET ASN MET LEU LYS SER SER PHE ALA
SEQRES 8 C 338 THR CYS VAL LEU VAL SER GLU GLU ASP LYS HIS ALA ILE
SEQRES 9 C 338 ILE VAL GLU PRO GLU LYS ARG GLY LYS TYR VAL VAL CYS
SEQRES 10 C 338 PHE ASP PRO LEU ASP GLY SER SER ASN ILE ASP CYS LEU
SEQRES 11 C 338 VAL SER VAL GLY THR ILE PHE GLY ILE TYR ARG LYS LYS
SEQRES 12 C 338 SER THR ASP GLU PRO SER GLU LYS ASP ALA LEU GLN PRO
SEQRES 13 C 338 GLY ARG ASN LEU VAL ALA ALA GLY TYR ALA LEU TYR GLY
SEQRES 14 C 338 SER ALA THR MET LEU VAL LEU ALA MET ASP CYS GLY VAL
SEQRES 15 C 338 ASN CYS PHE MET LEU ASP PRO ALA ILE GLY GLU PHE ILE
SEQRES 16 C 338 LEU VAL ASP LYS ASP VAL LYS ILE LYS LYS LYS GLY LYS
SEQRES 17 C 338 ILE TYR SER LEU ASN GLU GLY TYR ALA LYS ASP PHE ASP
SEQRES 18 C 338 PRO ALA VAL THR GLU TYR ILE GLN ARG LYS LYS PHE PRO
SEQRES 19 C 338 PRO ASP ASN SER ALA PRO TYR GLY ALA ARG TYR VAL GLY
SEQRES 20 C 338 SER MET VAL ALA ASP VAL HIS ARG THR LEU VAL TYR GLY
SEQRES 21 C 338 GLY ILE PHE LEU TYR PRO ALA ASN LYS LYS SER PRO ASN
SEQRES 22 C 338 GLY LYS LEU ARG LEU LEU TYR GLU CYS ASN PRO MET ALA
SEQRES 23 C 338 TYR VAL MET GLU LYS ALA GLY GLY MET ALA THR THR GLY
SEQRES 24 C 338 LYS GLU ALA VAL LEU ASP VAL ILE PRO THR ASP ILE HIS
SEQRES 25 C 338 GLN ARG ALA PRO VAL ILE LEU GLY SER PRO ASP ASP VAL
SEQRES 26 C 338 LEU GLU PHE LEU LYS VAL TYR GLU LYS HIS SER ALA GLN
SEQRES 1 D 338 MET ALA ASP GLN ALA PRO PHE ASP THR ASP VAL ASN THR
SEQRES 2 D 338 LEU THR ARG PHE VAL MET GLU GLU GLY ARG LYS ALA ARG
SEQRES 3 D 338 GLY THR GLY GLU LEU THR GLN LEU LEU ASN SER LEU CYS
SEQRES 4 D 338 THR ALA VAL LYS ALA ILE SER SER ALA VAL ARG LYS ALA
SEQRES 5 D 338 GLY ILE ALA HIS LEU TYR GLY ILE ALA GLY SER THR ASN
SEQRES 6 D 338 VAL THR GLY ASP GLN VAL LYS LYS LEU ASP VAL LEU SER
SEQRES 7 D 338 ASN ASP LEU VAL MET ASN MET LEU LYS SER SER PHE ALA
SEQRES 8 D 338 THR CYS VAL LEU VAL SER GLU GLU ASP LYS HIS ALA ILE
SEQRES 9 D 338 ILE VAL GLU PRO GLU LYS ARG GLY LYS TYR VAL VAL CYS
SEQRES 10 D 338 PHE ASP PRO LEU ASP GLY SER SER ASN ILE ASP CYS LEU
SEQRES 11 D 338 VAL SER VAL GLY THR ILE PHE GLY ILE TYR ARG LYS LYS
SEQRES 12 D 338 SER THR ASP GLU PRO SER GLU LYS ASP ALA LEU GLN PRO
SEQRES 13 D 338 GLY ARG ASN LEU VAL ALA ALA GLY TYR ALA LEU TYR GLY
SEQRES 14 D 338 SER ALA THR MET LEU VAL LEU ALA MET ASP CYS GLY VAL
SEQRES 15 D 338 ASN CYS PHE MET LEU ASP PRO ALA ILE GLY GLU PHE ILE
SEQRES 16 D 338 LEU VAL ASP LYS ASP VAL LYS ILE LYS LYS LYS GLY LYS
SEQRES 17 D 338 ILE TYR SER LEU ASN GLU GLY TYR ALA LYS ASP PHE ASP
SEQRES 18 D 338 PRO ALA VAL THR GLU TYR ILE GLN ARG LYS LYS PHE PRO
SEQRES 19 D 338 PRO ASP ASN SER ALA PRO TYR GLY ALA ARG TYR VAL GLY
SEQRES 20 D 338 SER MET VAL ALA ASP VAL HIS ARG THR LEU VAL TYR GLY
SEQRES 21 D 338 GLY ILE PHE LEU TYR PRO ALA ASN LYS LYS SER PRO ASN
SEQRES 22 D 338 GLY LYS LEU ARG LEU LEU TYR GLU CYS ASN PRO MET ALA
SEQRES 23 D 338 TYR VAL MET GLU LYS ALA GLY GLY MET ALA THR THR GLY
SEQRES 24 D 338 LYS GLU ALA VAL LEU ASP VAL ILE PRO THR ASP ILE HIS
SEQRES 25 D 338 GLN ARG ALA PRO VAL ILE LEU GLY SER PRO ASP ASP VAL
SEQRES 26 D 338 LEU GLU PHE LEU LYS VAL TYR GLU LYS HIS SER ALA GLN
HET 95J A 401 23
HET 95J B 401 23
HET 95J C 401 23
HET 95J D 401 23
HETNAM 95J N-[(5-BROMO-1,3-THIAZOL-2-YL)CARBAMOYL]-5-(1,2-OXAZOL-
HETNAM 2 95J 3-YL)THIOPHENE-2-SULFONAMIDE
FORMUL 5 95J 4(C11 H7 BR N4 O4 S3)
FORMUL 9 HOH *1094(H2 O)
HELIX 1 AA1 THR A 12 ARG A 25 1 14
HELIX 2 AA2 GLY A 28 ARG A 49 1 22
HELIX 3 AA3 GLY A 52 TYR A 57 1 6
HELIX 4 AA4 LYS A 72 SER A 87 1 16
HELIX 5 AA5 GLU A 106 GLU A 108 5 3
HELIX 6 AA6 GLY A 122 LEU A 129 5 8
HELIX 7 AA7 SER A 148 LEU A 153 5 6
HELIX 8 AA8 PRO A 155 LEU A 159 5 5
HELIX 9 AA9 ASN A 212 PHE A 219 5 8
HELIX 10 AB1 ASP A 220 PHE A 232 1 13
HELIX 11 AB2 SER A 247 GLY A 259 1 13
HELIX 12 AB3 GLU A 280 ALA A 291 1 12
HELIX 13 AB4 ALA A 301 VAL A 305 5 5
HELIX 14 AB5 SER A 320 HIS A 334 1 15
HELIX 15 AB6 THR B 12 ARG B 25 1 14
HELIX 16 AB7 GLY B 28 ARG B 49 1 22
HELIX 17 AB8 GLY B 52 TYR B 57 1 6
HELIX 18 AB9 LEU B 73 SER B 88 1 16
HELIX 19 AC1 GLU B 106 GLU B 108 5 3
HELIX 20 AC2 GLY B 122 LEU B 129 5 8
HELIX 21 AC3 SER B 148 LEU B 153 5 6
HELIX 22 AC4 PRO B 155 ARG B 157 5 3
HELIX 23 AC5 ASN B 212 PHE B 219 5 8
HELIX 24 AC6 ASP B 220 PHE B 232 1 13
HELIX 25 AC7 SER B 247 GLY B 259 1 13
HELIX 26 AC8 GLU B 280 ALA B 291 1 12
HELIX 27 AC9 ALA B 301 VAL B 305 5 5
HELIX 28 AD1 SER B 320 HIS B 334 1 15
HELIX 29 AD2 THR C 12 ARG C 25 1 14
HELIX 30 AD3 GLY C 28 ARG C 49 1 22
HELIX 31 AD4 GLY C 52 TYR C 57 1 6
HELIX 32 AD5 LYS C 72 SER C 88 1 17
HELIX 33 AD6 GLU C 106 GLU C 108 5 3
HELIX 34 AD7 GLY C 122 LEU C 129 5 8
HELIX 35 AD8 SER C 148 LEU C 153 5 6
HELIX 36 AD9 PRO C 155 LEU C 159 5 5
HELIX 37 AE1 ASN C 212 PHE C 219 5 8
HELIX 38 AE2 ASP C 220 PHE C 232 1 13
HELIX 39 AE3 SER C 247 GLY C 259 1 13
HELIX 40 AE4 GLU C 280 ALA C 291 1 12
HELIX 41 AE5 ALA C 301 VAL C 305 5 5
HELIX 42 AE6 SER C 320 HIS C 334 1 15
HELIX 43 AE7 THR D 12 ARG D 25 1 14
HELIX 44 AE8 GLY D 28 ARG D 49 1 22
HELIX 45 AE9 GLY D 52 TYR D 57 1 6
HELIX 46 AF1 LEU D 73 SER D 87 1 15
HELIX 47 AF2 GLU D 106 GLU D 108 5 3
HELIX 48 AF3 GLY D 122 LEU D 129 5 8
HELIX 49 AF4 SER D 148 LEU D 153 5 6
HELIX 50 AF5 PRO D 155 ARG D 157 5 3
HELIX 51 AF6 ASN D 212 PHE D 219 5 8
HELIX 52 AF7 ASP D 220 PHE D 232 1 13
HELIX 53 AF8 SER D 247 GLY D 259 1 13
HELIX 54 AF9 GLU D 280 ALA D 291 1 12
HELIX 55 AG1 ALA D 301 VAL D 305 5 5
HELIX 56 AG2 SER D 320 HIS D 334 1 15
SHEET 1 AA1 8 ILE A 103 ILE A 104 0
SHEET 2 AA1 8 THR A 91 SER A 96 -1 N LEU A 94 O ILE A 103
SHEET 3 AA1 8 ARG A 110 ASP A 121 1 O PHE A 117 N VAL A 95
SHEET 4 AA1 8 VAL A 132 ARG A 140 -1 O TYR A 139 N VAL A 114
SHEET 5 AA1 8 ALA A 161 TYR A 167 -1 O ALA A 161 N ILE A 138
SHEET 6 AA1 8 THR A 171 MET A 177 -1 O VAL A 174 N TYR A 164
SHEET 7 AA1 8 GLY A 180 ASP A 187 -1 O PHE A 184 N LEU A 173
SHEET 8 AA1 8 GLU A 192 ASP A 197 -1 O ILE A 194 N MET A 185
SHEET 1 AA2 5 GLY A 241 ALA A 242 0
SHEET 2 AA2 5 ILE A 208 SER A 210 1 N TYR A 209 O GLY A 241
SHEET 3 AA2 5 ILE A 261 TYR A 264 1 O LEU A 263 N SER A 210
SHEET 4 AA2 5 VAL A 316 GLY A 319 -1 O VAL A 316 N TYR A 264
SHEET 5 AA2 5 MET A 294 THR A 296 -1 N THR A 296 O ILE A 317
SHEET 1 AA3 8 ILE B 103 ILE B 104 0
SHEET 2 AA3 8 THR B 91 SER B 96 -1 N LEU B 94 O ILE B 103
SHEET 3 AA3 8 ARG B 110 ASP B 121 1 O VAL B 115 N VAL B 95
SHEET 4 AA3 8 VAL B 132 ARG B 140 -1 O TYR B 139 N VAL B 114
SHEET 5 AA3 8 LEU B 159 TYR B 167 -1 O ALA B 161 N ILE B 138
SHEET 6 AA3 8 THR B 171 MET B 177 -1 O VAL B 174 N TYR B 164
SHEET 7 AA3 8 GLY B 180 LEU B 186 -1 O LEU B 186 N THR B 171
SHEET 8 AA3 8 PHE B 193 ASP B 197 -1 O ILE B 194 N MET B 185
SHEET 1 AA4 5 GLY B 241 ALA B 242 0
SHEET 2 AA4 5 ILE B 208 SER B 210 1 N TYR B 209 O GLY B 241
SHEET 3 AA4 5 ILE B 261 TYR B 264 1 O LEU B 263 N SER B 210
SHEET 4 AA4 5 VAL B 316 GLY B 319 -1 O VAL B 316 N TYR B 264
SHEET 5 AA4 5 MET B 294 THR B 296 -1 N THR B 296 O ILE B 317
SHEET 1 AA5 8 ILE C 103 ILE C 104 0
SHEET 2 AA5 8 THR C 91 SER C 96 -1 N LEU C 94 O ILE C 103
SHEET 3 AA5 8 ARG C 110 ASP C 121 1 O VAL C 115 N VAL C 95
SHEET 4 AA5 8 VAL C 132 ARG C 140 -1 O TYR C 139 N VAL C 114
SHEET 5 AA5 8 ALA C 161 TYR C 167 -1 O ALA C 161 N ILE C 138
SHEET 6 AA5 8 THR C 171 MET C 177 -1 O VAL C 174 N TYR C 164
SHEET 7 AA5 8 GLY C 180 LEU C 186 -1 O PHE C 184 N LEU C 173
SHEET 8 AA5 8 PHE C 193 ASP C 197 -1 O ILE C 194 N MET C 185
SHEET 1 AA6 5 GLY C 241 ALA C 242 0
SHEET 2 AA6 5 ILE C 208 SER C 210 1 N TYR C 209 O GLY C 241
SHEET 3 AA6 5 ILE C 261 TYR C 264 1 O LEU C 263 N SER C 210
SHEET 4 AA6 5 VAL C 316 GLY C 319 -1 O LEU C 318 N PHE C 262
SHEET 5 AA6 5 MET C 294 THR C 296 -1 N THR C 296 O ILE C 317
SHEET 1 AA7 8 ILE D 103 ILE D 104 0
SHEET 2 AA7 8 THR D 91 SER D 96 -1 N LEU D 94 O ILE D 103
SHEET 3 AA7 8 ARG D 110 ASP D 121 1 O PHE D 117 N VAL D 95
SHEET 4 AA7 8 VAL D 132 ARG D 140 -1 O TYR D 139 N VAL D 114
SHEET 5 AA7 8 LEU D 159 TYR D 167 -1 O ALA D 161 N ILE D 138
SHEET 6 AA7 8 THR D 171 MET D 177 -1 O ALA D 176 N ALA D 162
SHEET 7 AA7 8 GLY D 180 LEU D 186 -1 O LEU D 186 N THR D 171
SHEET 8 AA7 8 PHE D 193 ASP D 197 -1 O ILE D 194 N MET D 185
SHEET 1 AA8 5 GLY D 241 ALA D 242 0
SHEET 2 AA8 5 ILE D 208 SER D 210 1 N TYR D 209 O GLY D 241
SHEET 3 AA8 5 ILE D 261 TYR D 264 1 O LEU D 263 N SER D 210
SHEET 4 AA8 5 VAL D 316 GLY D 319 -1 O VAL D 316 N TYR D 264
SHEET 5 AA8 5 MET D 294 THR D 296 -1 N THR D 296 O ILE D 317
SITE 1 AC1 17 VAL A 17 MET A 18 GLU A 20 GLY A 21
SITE 2 AC1 17 ARG A 22 GLY A 26 THR A 27 GLY A 28
SITE 3 AC1 17 GLU A 29 LEU A 30 THR A 31 MET A 177
SITE 4 AC1 17 CYS A 179 HOH A 557 THR C 27 GLY C 28
SITE 5 AC1 17 95J C 401
SITE 1 AC2 17 VAL B 17 MET B 18 GLU B 20 GLY B 21
SITE 2 AC2 17 ARG B 22 GLY B 26 THR B 27 GLY B 28
SITE 3 AC2 17 GLU B 29 LEU B 30 THR B 31 MET B 177
SITE 4 AC2 17 CYS B 179 HOH B 550 THR D 27 GLY D 28
SITE 5 AC2 17 95J D 401
SITE 1 AC3 16 THR A 27 95J A 401 MET C 18 GLU C 20
SITE 2 AC3 16 GLY C 21 ARG C 22 GLY C 26 THR C 27
SITE 3 AC3 16 GLY C 28 GLU C 29 LEU C 30 THR C 31
SITE 4 AC3 16 MET C 177 CYS C 179 HOH C 614 HOH C 660
SITE 1 AC4 17 THR B 27 GLY B 28 95J B 401 VAL D 17
SITE 2 AC4 17 MET D 18 GLU D 20 GLY D 21 ARG D 22
SITE 3 AC4 17 GLY D 26 THR D 27 GLY D 28 GLU D 29
SITE 4 AC4 17 LEU D 30 THR D 31 MET D 177 HOH D 549
SITE 5 AC4 17 HOH D 715
CRYST1 67.203 83.311 278.006 90.00 90.00 90.00 P 21 21 21 16
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 0.014880 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012003 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003597 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
