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HEADER LYASE 28-SEP-13 4MYS
TITLE 1.4 ANGSTROM CRYSTAL STRUCTURE OF 2-SUCCINYL-6-HYDROXY-2,4-
TITLE 2 CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE WITH SHCHC AND PYRUVATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE
COMPND 3 SYNTHASE;
COMPND 4 CHAIN: A, B, C;
COMPND 5 SYNONYM: SHCHC SYNTHASE;
COMPND 6 EC: 4.2.99.20;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: B2263, JW2258, MENH, YFBB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETM
KEYWDS ALPHA/BETA HYDROLASE FOLD, 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-
KEYWDS 2 CARBOXYLATE SYNTHASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.SUN,S.YIN,Y.FENG,J.LI,J.ZHOU,C.LIU,G.ZHU,Z.GUO
REVDAT 1 23-APR-14 4MYS 0
JRNL AUTH Y.SUN,S.YIN,Y.FENG,J.LI,J.ZHOU,C.LIU,G.ZHU,Z.GUO
JRNL TITL MOLECULAR BASIS OF THE GENERAL BASE CATALYSIS OF AN
JRNL TITL 2 ALPHA/BETA HYDROLASE CATALYTIC TRIAD
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 145825
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 7310
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 35.1001 - 4.4188 0.96 4463 222 0.1772 0.1931
REMARK 3 2 4.4188 - 3.5083 0.99 4579 247 0.1249 0.1427
REMARK 3 3 3.5083 - 3.0652 1.00 4663 207 0.1498 0.1784
REMARK 3 4 3.0652 - 2.7850 1.00 4598 251 0.1593 0.1809
REMARK 3 5 2.7850 - 2.5855 1.00 4631 270 0.1547 0.2001
REMARK 3 6 2.5855 - 2.4331 1.00 4665 230 0.1549 0.1794
REMARK 3 7 2.4331 - 2.3113 1.00 4693 223 0.1510 0.1633
REMARK 3 8 2.3113 - 2.2107 1.00 4593 262 0.1575 0.1825
REMARK 3 9 2.2107 - 2.1256 1.00 4629 258 0.1562 0.1789
REMARK 3 10 2.1256 - 2.0522 1.00 4629 242 0.1610 0.1768
REMARK 3 11 2.0522 - 1.9881 1.00 4645 271 0.1599 0.1743
REMARK 3 12 1.9881 - 1.9313 1.00 4628 242 0.1602 0.1992
REMARK 3 13 1.9313 - 1.8804 1.00 4587 234 0.1623 0.1757
REMARK 3 14 1.8804 - 1.8345 1.00 4659 239 0.1660 0.2083
REMARK 3 15 1.8345 - 1.7928 1.00 4619 253 0.1634 0.2033
REMARK 3 16 1.7928 - 1.7547 1.00 4702 257 0.1602 0.1856
REMARK 3 17 1.7547 - 1.7196 1.00 4614 244 0.1543 0.1658
REMARK 3 18 1.7196 - 1.6871 1.00 4665 253 0.1610 0.2009
REMARK 3 19 1.6871 - 1.6570 1.00 4603 245 0.1552 0.1799
REMARK 3 20 1.6570 - 1.6289 1.00 4632 255 0.1590 0.1839
REMARK 3 21 1.6289 - 1.6026 1.00 4625 244 0.1611 0.1705
REMARK 3 22 1.6026 - 1.5780 1.00 4627 248 0.1622 0.1842
REMARK 3 23 1.5780 - 1.5548 1.00 4629 240 0.1615 0.1949
REMARK 3 24 1.5548 - 1.5329 1.00 4717 241 0.1649 0.1828
REMARK 3 25 1.5329 - 1.5122 1.00 4549 255 0.1719 0.1859
REMARK 3 26 1.5122 - 1.4925 1.00 4691 264 0.1715 0.1946
REMARK 3 27 1.4925 - 1.4739 1.00 4624 234 0.1901 0.2304
REMARK 3 28 1.4739 - 1.4561 1.00 4615 220 0.2056 0.2552
REMARK 3 29 1.4561 - 1.4392 0.98 4668 221 0.2268 0.2496
REMARK 3 30 1.4392 - 1.4230 0.94 4273 238 0.2330 0.2503
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.120
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.87
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 : 0.006 7998
REMARK 3 ANGLE : 1.058 10881
REMARK 3 CHIRALITY : 0.044 1174
REMARK 3 PLANARITY : 0.005 1453
REMARK 3 DIHEDRAL : 14.336 2831
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 1:20)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.3100 52.2295 2.7605
REMARK 3 T TENSOR
REMARK 3 T11: 0.1579 T22: 0.1403
REMARK 3 T33: 0.1221 T12: -0.0246
REMARK 3 T13: -0.0541 T23: -0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 3.7376 L22: 1.1977
REMARK 3 L33: 1.5462 L12: 0.4659
REMARK 3 L13: 0.2484 L23: -0.2527
REMARK 3 S TENSOR
REMARK 3 S11: 0.0378 S12: -0.3080 S13: -0.0573
REMARK 3 S21: 0.2573 S22: 0.0244 S23: -0.2480
REMARK 3 S31: 0.0185 S32: 0.1574 S33: -0.0369
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resid 21:117)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0248 55.0595 -4.0292
REMARK 3 T TENSOR
REMARK 3 T11: 0.1085 T22: 0.1019
REMARK 3 T33: 0.0678 T12: -0.0181
REMARK 3 T13: -0.0223 T23: -0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 1.4495 L22: 1.3813
REMARK 3 L33: 1.0275 L12: 0.3676
REMARK 3 L13: 0.1976 L23: 0.1996
REMARK 3 S TENSOR
REMARK 3 S11: 0.0013 S12: 0.0095 S13: 0.0678
REMARK 3 S21: 0.0715 S22: 0.0378 S23: -0.0843
REMARK 3 S31: -0.0636 S32: 0.0630 S33: -0.0301
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resid 118:182)
REMARK 3 ORIGIN FOR THE GROUP (A): -24.2083 46.3716 -9.0109
REMARK 3 T TENSOR
REMARK 3 T11: 0.1036 T22: 0.1206
REMARK 3 T33: 0.0434 T12: -0.0118
REMARK 3 T13: -0.0275 T23: 0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 1.4548 L22: 1.0548
REMARK 3 L33: 1.0150 L12: 0.1668
REMARK 3 L13: -0.3049 L23: 0.2928
REMARK 3 S TENSOR
REMARK 3 S11: -0.0123 S12: 0.1268 S13: 0.0819
REMARK 3 S21: -0.0622 S22: 0.0133 S23: 0.1122
REMARK 3 S31: -0.0171 S32: -0.0782 S33: 0.0009
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'A' and (resid 183:200)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.9848 63.0641 -16.0858
REMARK 3 T TENSOR
REMARK 3 T11: 0.1971 T22: 0.1471
REMARK 3 T33: 0.1565 T12: -0.0297
REMARK 3 T13: 0.0275 T23: 0.0493
REMARK 3 L TENSOR
REMARK 3 L11: 1.5831 L22: 1.5743
REMARK 3 L33: 1.9848 L12: -0.0359
REMARK 3 L13: -0.3946 L23: -0.3336
REMARK 3 S TENSOR
REMARK 3 S11: 0.0501 S12: 0.2111 S13: 0.3150
REMARK 3 S21: -0.2813 S22: -0.0228 S23: -0.1765
REMARK 3 S31: -0.2294 S32: 0.1259 S33: -0.0502
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'A' and (resid 201:227)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9522 49.8600 -21.2604
REMARK 3 T TENSOR
REMARK 3 T11: 0.2937 T22: 0.2934
REMARK 3 T33: 0.1270 T12: -0.0391
REMARK 3 T13: 0.0456 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 3.4795 L22: 1.7131
REMARK 3 L33: 1.8651 L12: -0.4379
REMARK 3 L13: 1.4837 L23: 0.8628
REMARK 3 S TENSOR
REMARK 3 S11: 0.0609 S12: 0.6531 S13: 0.1268
REMARK 3 S21: -0.7600 S22: -0.0028 S23: -0.1920
REMARK 3 S31: -0.3369 S32: 0.3292 S33: -0.0099
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'A' and (resid 228:252)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2725 42.4770 -13.6441
REMARK 3 T TENSOR
REMARK 3 T11: 0.1122 T22: 0.1976
REMARK 3 T33: 0.1182 T12: -0.0015
REMARK 3 T13: 0.0099 T23: -0.0383
REMARK 3 L TENSOR
REMARK 3 L11: 3.9075 L22: 2.0381
REMARK 3 L33: 1.8256 L12: -0.2395
REMARK 3 L13: 0.1220 L23: -0.2354
REMARK 3 S TENSOR
REMARK 3 S11: 0.0531 S12: 0.0844 S13: -0.1326
REMARK 3 S21: -0.1712 S22: 0.0237 S23: -0.3179
REMARK 3 S31: -0.0321 S32: 0.3377 S33: -0.0707
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain 'B' and (resid 1:20)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.0791 26.3665 -10.6397
REMARK 3 T TENSOR
REMARK 3 T11: 0.1634 T22: 0.1306
REMARK 3 T33: 0.1167 T12: -0.0173
REMARK 3 T13: -0.0163 T23: 0.0541
REMARK 3 L TENSOR
REMARK 3 L11: 1.4666 L22: 3.4569
REMARK 3 L33: 1.5071 L12: -0.8990
REMARK 3 L13: 0.2629 L23: -0.0915
REMARK 3 S TENSOR
REMARK 3 S11: 0.0667 S12: 0.2500 S13: 0.1715
REMARK 3 S21: -0.3184 S22: 0.0019 S23: 0.1723
REMARK 3 S31: -0.1049 S32: -0.0919 S33: -0.0622
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: chain 'B' and (resid 21:117)
REMARK 3 ORIGIN FOR THE GROUP (A): 51.0784 21.5186 -3.8518
REMARK 3 T TENSOR
REMARK 3 T11: 0.1170 T22: 0.0918
REMARK 3 T33: 0.0685 T12: -0.0114
REMARK 3 T13: -0.0082 T23: 0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 1.0884 L22: 1.6373
REMARK 3 L33: 1.0047 L12: 0.1574
REMARK 3 L13: -0.1269 L23: -0.2485
REMARK 3 S TENSOR
REMARK 3 S11: -0.0007 S12: 0.0698 S13: 0.1056
REMARK 3 S21: 0.0025 S22: 0.0404 S23: -0.0097
REMARK 3 S31: -0.0805 S32: 0.0179 S33: -0.0303
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: chain 'B' and (resid 118:135)
REMARK 3 ORIGIN FOR THE GROUP (A): 61.8141 2.7970 5.1482
REMARK 3 T TENSOR
REMARK 3 T11: 0.2311 T22: 0.1647
REMARK 3 T33: 0.1508 T12: 0.0187
REMARK 3 T13: -0.0779 T23: 0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 2.0236 L22: 1.9313
REMARK 3 L33: 2.4203 L12: 0.5244
REMARK 3 L13: 0.7719 L23: 1.3863
REMARK 3 S TENSOR
REMARK 3 S11: -0.0053 S12: -0.1430 S13: 0.0520
REMARK 3 S21: 0.5997 S22: 0.0825 S23: -0.4367
REMARK 3 S31: 0.2262 S32: 0.2790 S33: -0.1052
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: chain 'B' and (resid 136:182)
REMARK 3 ORIGIN FOR THE GROUP (A): 47.8558 1.6773 -0.8316
REMARK 3 T TENSOR
REMARK 3 T11: 0.1156 T22: 0.0928
REMARK 3 T33: 0.0466 T12: -0.0049
REMARK 3 T13: -0.0110 T23: 0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 0.7665 L22: 1.0980
REMARK 3 L33: 1.2209 L12: -0.2684
REMARK 3 L13: -0.1122 L23: 0.2413
REMARK 3 S TENSOR
REMARK 3 S11: -0.0151 S12: -0.0369 S13: -0.0700
REMARK 3 S21: 0.0203 S22: 0.0034 S23: 0.0228
REMARK 3 S31: 0.1013 S32: -0.0302 S33: 0.0199
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: chain 'B' and (resid 183:200)
REMARK 3 ORIGIN FOR THE GROUP (A): 59.9133 22.5254 8.0798
REMARK 3 T TENSOR
REMARK 3 T11: 0.1654 T22: 0.1515
REMARK 3 T33: 0.1501 T12: -0.0322
REMARK 3 T13: -0.0227 T23: -0.0405
REMARK 3 L TENSOR
REMARK 3 L11: 2.5182 L22: 2.0167
REMARK 3 L33: 2.8033 L12: -0.3776
REMARK 3 L13: 0.1900 L23: 1.0579
REMARK 3 S TENSOR
REMARK 3 S11: 0.0550 S12: -0.3001 S13: 0.3496
REMARK 3 S21: 0.2073 S22: -0.0439 S23: -0.1910
REMARK 3 S31: -0.1537 S32: 0.0272 S33: -0.0139
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: chain 'B' and (resid 201:227)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.8512 19.4613 13.4533
REMARK 3 T TENSOR
REMARK 3 T11: 0.3147 T22: 0.2637
REMARK 3 T33: 0.1136 T12: -0.0152
REMARK 3 T13: 0.0212 T23: -0.0280
REMARK 3 L TENSOR
REMARK 3 L11: 2.6745 L22: 2.4422
REMARK 3 L33: 0.7971 L12: -0.2529
REMARK 3 L13: -0.3687 L23: -1.3035
REMARK 3 S TENSOR
REMARK 3 S11: 0.0636 S12: -0.7672 S13: 0.1802
REMARK 3 S21: 0.5625 S22: -0.0007 S23: -0.0022
REMARK 3 S31: -0.4393 S32: 0.1329 S33: -0.0109
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: chain 'B' and (resid 228:252)
REMARK 3 ORIGIN FOR THE GROUP (A): 37.3400 20.5690 5.8352
REMARK 3 T TENSOR
REMARK 3 T11: 0.1868 T22: 0.1389
REMARK 3 T33: 0.1258 T12: 0.0390
REMARK 3 T13: 0.0375 T23: 0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 2.7772 L22: 2.9956
REMARK 3 L33: 1.6046 L12: -0.7921
REMARK 3 L13: 0.2058 L23: -0.0690
REMARK 3 S TENSOR
REMARK 3 S11: 0.0757 S12: -0.1738 S13: 0.2312
REMARK 3 S21: 0.1169 S22: 0.0113 S23: 0.3010
REMARK 3 S31: -0.3271 S32: -0.1379 S33: -0.0961
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: chain 'C' and (resid 2:60)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2807 28.1843 -3.9312
REMARK 3 T TENSOR
REMARK 3 T11: 0.0687 T22: 0.0768
REMARK 3 T33: 0.3694 T12: 0.0390
REMARK 3 T13: 0.0755 T23: -0.0374
REMARK 3 L TENSOR
REMARK 3 L11: 0.0308 L22: 0.0145
REMARK 3 L33: 0.0035 L12: -0.0213
REMARK 3 L13: 0.0058 L23: -0.0026
REMARK 3 S TENSOR
REMARK 3 S11: -0.0252 S12: 0.0106 S13: -0.0836
REMARK 3 S21: -0.0061 S22: -0.0221 S23: 0.0352
REMARK 3 S31: 0.0196 S32: -0.0054 S33: -0.0305
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: chain 'C' and (resid 61:128)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9744 24.1923 -3.9417
REMARK 3 T TENSOR
REMARK 3 T11: -0.0152 T22: 0.0564
REMARK 3 T33: 0.5786 T12: 0.0999
REMARK 3 T13: -0.0072 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 0.0544 L22: 0.0274
REMARK 3 L33: 0.0391 L12: 0.0056
REMARK 3 L13: 0.0025 L23: -0.0195
REMARK 3 S TENSOR
REMARK 3 S11: -0.0320 S12: -0.0125 S13: -0.0308
REMARK 3 S21: -0.0203 S22: -0.0347 S23: -0.0233
REMARK 3 S31: 0.0758 S32: -0.0342 S33: -0.0400
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: chain 'C' and (resid 129:157)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3749 7.5650 -3.9353
REMARK 3 T TENSOR
REMARK 3 T11: 0.1639 T22: 0.1138
REMARK 3 T33: 0.7068 T12: -0.0447
REMARK 3 T13: 0.0367 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.0103 L22: 0.0122
REMARK 3 L33: 0.0037 L12: 0.0022
REMARK 3 L13: 0.0093 L23: -0.0019
REMARK 3 S TENSOR
REMARK 3 S11: -0.0088 S12: 0.0039 S13: -0.0616
REMARK 3 S21: 0.0111 S22: -0.0022 S23: 0.0460
REMARK 3 S31: 0.0249 S32: -0.0224 S33: -0.0011
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: chain 'C' and (resid 158:182)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3653 12.7581 -3.9382
REMARK 3 T TENSOR
REMARK 3 T11: 0.1463 T22: 0.1592
REMARK 3 T33: 0.4984 T12: 0.0221
REMARK 3 T13: 0.0436 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.0080 L22: 0.0177
REMARK 3 L33: 0.0192 L12: 0.0169
REMARK 3 L13: -0.0027 L23: 0.0015
REMARK 3 S TENSOR
REMARK 3 S11: 0.0142 S12: -0.0331 S13: -0.1298
REMARK 3 S21: -0.0209 S22: -0.0235 S23: 0.0588
REMARK 3 S31: 0.1088 S32: -0.0525 S33: 0.0003
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: chain 'C' and (resid 183:210)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1402 22.7535 -3.9621
REMARK 3 T TENSOR
REMARK 3 T11: 0.1731 T22: 0.2331
REMARK 3 T33: 0.5807 T12: 0.0675
REMARK 3 T13: -0.0204 T23: 0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 0.0190 L22: 0.0153
REMARK 3 L33: 0.0346 L12: 0.0099
REMARK 3 L13: -0.0178 L23: 0.0044
REMARK 3 S TENSOR
REMARK 3 S11: -0.0038 S12: 0.0207 S13: -0.0413
REMARK 3 S21: 0.0324 S22: 0.0364 S23: 0.0178
REMARK 3 S31: 0.0374 S32: -0.0262 S33: -0.0009
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: chain 'C' and (resid 211:227)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3910 21.4779 -3.9493
REMARK 3 T TENSOR
REMARK 3 T11: 0.2037 T22: 0.2497
REMARK 3 T33: 0.3335 T12: 0.0295
REMARK 3 T13: -0.0524 T23: 0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 0.0066 L22: 0.0032
REMARK 3 L33: -0.0000 L12: -0.0053
REMARK 3 L13: -0.0009 L23: 0.0006
REMARK 3 S TENSOR
REMARK 3 S11: 0.0551 S12: 0.0060 S13: -0.0513
REMARK 3 S21: 0.0286 S22: 0.0767 S23: 0.0394
REMARK 3 S31: -0.0187 S32: 0.0044 S33: 0.0000
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: chain 'C' and (resid 228:252)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.3067 26.5137 -3.9391
REMARK 3 T TENSOR
REMARK 3 T11: 0.0973 T22: 0.1083
REMARK 3 T33: 0.2735 T12: 0.0075
REMARK 3 T13: -0.0026 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 0.0122 L22: 0.0063
REMARK 3 L33: 0.0007 L12: -0.0131
REMARK 3 L13: 0.0087 L23: -0.0051
REMARK 3 S TENSOR
REMARK 3 S11: -0.0297 S12: 0.0108 S13: -0.0406
REMARK 3 S21: 0.0335 S22: 0.0159 S23: 0.0377
REMARK 3 S31: -0.0170 S32: 0.0011 S33: -0.0082
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 4MYS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-OCT-13.
REMARK 100 THE RCSB ID CODE IS RCSB082535.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 145860
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.420
REMARK 200 RESOLUTION RANGE LOW (A) : 37.201
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.42
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M K/NA PHOSPHATE, PH 6.8, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 15.64667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 31.29333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 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 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 C 1
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 ARG A 129 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 162 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 212 CG CD CE NZ
REMARK 470 PHE A 252 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 198 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 119 CG CD OE1 OE2
REMARK 470 GLU C 123 CG CD OE1 OE2
REMARK 470 ARG C 126 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 149 CG CD OE1 NE2
REMARK 470 GLU C 219 CG CD OE1 OE2
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 O HOH B 557 O HOH B 652 2.05
REMARK 500 OD2 ASP B 79 O HOH B 467 2.12
REMARK 500 O LEU C 216 O HOH C 338 2.13
REMARK 500 O HOH B 520 O HOH C 345 2.13
REMARK 500 O HOH B 712 O HOH B 733 2.14
REMARK 500 O HOH A 619 O HOH A 734 2.14
REMARK 500 OD1 ASP B 158 O HOH B 775 2.14
REMARK 500 O GLN C 188 O HOH C 319 2.14
REMARK 500 OD2 ASP A 79 O HOH A 468 2.15
REMARK 500 O HOH C 323 O HOH C 324 2.15
REMARK 500 NE2 GLN A 130 O HOH A 652 2.15
REMARK 500 O HOH B 687 O HOH B 719 2.15
REMARK 500 O HOH A 488 O HOH A 693 2.15
REMARK 500 O GLN C 188 O HOH C 315 2.16
REMARK 500 O HOH B 734 O HOH B 765 2.16
REMARK 500 O HOH B 602 O HOH B 775 2.16
REMARK 500 O HOH B 592 O HOH B 726 2.17
REMARK 500 O HOH B 639 O HOH B 650 2.17
REMARK 500 O LEU C 216 O HOH C 331 2.17
REMARK 500 O HOH B 485 O HOH B 686 2.17
REMARK 500 O HOH B 500 O HOH B 746 2.17
REMARK 500 O HOH C 313 O HOH C 322 2.18
REMARK 500 O HOH B 461 O HOH B 602 2.18
REMARK 500 O HOH B 651 O HOH B 655 2.18
REMARK 500 O GLU C 35 O HOH C 322 2.18
REMARK 500 O HOH A 683 O HOH A 686 2.19
REMARK 500 O HOH A 684 O HOH A 686 2.19
REMARK 500 OE2 GLU B 35 O HOH B 636 2.19
REMARK 500 O HOH B 708 O HOH B 764 2.19
REMARK 500 OE2 GLU B 119 O HOH B 751 2.19
REMARK 500 O HOH C 312 O HOH C 343 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 734 O HOH B 727 2554 2.15
REMARK 500 O HOH A 721 NE2 GLN B 130 2554 2.18
REMARK 500 O HOH A 660 O HOH A 497 2665 2.19
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 SER A 24 -0.70 74.19
REMARK 500 PHE A 37 57.46 -99.46
REMARK 500 SER A 86 -119.29 58.11
REMARK 500 ALA A 221 57.43 -90.44
REMARK 500 PHE B 37 56.99 -99.44
REMARK 500 SER B 86 -118.50 58.87
REMARK 500 ALA B 221 13.50 54.77
REMARK 500 ASP B 223 108.21 -56.75
REMARK 500 SER C 86 -118.12 60.91
REMARK 500 ARG C 126 -3.79 -155.39
REMARK 500 ASP C 128 -114.22 -137.55
REMARK 500 ARG C 129 -54.85 3.05
REMARK 500 ASP C 210 75.35 -101.42
REMARK 500 ALA C 222 68.32 -53.52
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 704 DISTANCE = 6.54 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 164 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 164 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4MXD RELATED DB: PDB
REMARK 900 RELATED ID: 4MYD RELATED DB: PDB
DBREF 4MYS A 1 252 UNP P37355 MENH_ECOLI 1 252
DBREF 4MYS B 1 252 UNP P37355 MENH_ECOLI 1 252
DBREF 4MYS C 1 252 UNP P37355 MENH_ECOLI 1 252
SEQRES 1 A 252 MET ILE LEU HIS ALA GLN ALA LYS HIS GLY LYS PRO GLY
SEQRES 2 A 252 LEU PRO TRP LEU VAL PHE LEU HIS GLY PHE SER GLY ASP
SEQRES 3 A 252 CYS HIS GLU TRP GLN GLU VAL GLY GLU ALA PHE ALA ASP
SEQRES 4 A 252 TYR SER ARG LEU TYR VAL ASP LEU PRO GLY HIS GLY GLY
SEQRES 5 A 252 SER ALA ALA ILE SER VAL ASP GLY PHE ASP ASP VAL THR
SEQRES 6 A 252 ASP LEU LEU ARG LYS THR LEU VAL SER TYR ASN ILE LEU
SEQRES 7 A 252 ASP PHE TRP LEU VAL GLY TYR SER LEU GLY GLY ARG VAL
SEQRES 8 A 252 ALA MET MET ALA ALA CYS GLN GLY LEU ALA GLY LEU CYS
SEQRES 9 A 252 GLY VAL ILE VAL GLU GLY GLY HIS PRO GLY LEU GLN ASN
SEQRES 10 A 252 ALA GLU GLN ARG ALA GLU ARG GLN ARG SER ASP ARG GLN
SEQRES 11 A 252 TRP VAL GLN ARG PHE LEU THR GLU PRO LEU THR ALA VAL
SEQRES 12 A 252 PHE ALA ASP TRP TYR GLN GLN PRO VAL PHE ALA SER LEU
SEQRES 13 A 252 ASN ASP ASP GLN ARG ARG GLU LEU VAL ALA LEU ARG SER
SEQRES 14 A 252 ASN ASN ASN GLY ALA THR LEU ALA ALA MET LEU GLU ALA
SEQRES 15 A 252 THR SER LEU ALA VAL GLN PRO ASP LEU ARG ALA ASN LEU
SEQRES 16 A 252 SER ALA ARG THR PHE ALA PHE TYR TYR LEU CYS GLY GLU
SEQRES 17 A 252 ARG ASP SER LYS PHE ARG ALA LEU ALA ALA GLU LEU ALA
SEQRES 18 A 252 ALA ASP CYS HIS VAL ILE PRO ARG ALA GLY HIS ASN ALA
SEQRES 19 A 252 HIS ARG GLU ASN PRO ALA GLY VAL ILE ALA SER LEU ALA
SEQRES 20 A 252 GLN ILE LEU ARG PHE
SEQRES 1 B 252 MET ILE LEU HIS ALA GLN ALA LYS HIS GLY LYS PRO GLY
SEQRES 2 B 252 LEU PRO TRP LEU VAL PHE LEU HIS GLY PHE SER GLY ASP
SEQRES 3 B 252 CYS HIS GLU TRP GLN GLU VAL GLY GLU ALA PHE ALA ASP
SEQRES 4 B 252 TYR SER ARG LEU TYR VAL ASP LEU PRO GLY HIS GLY GLY
SEQRES 5 B 252 SER ALA ALA ILE SER VAL ASP GLY PHE ASP ASP VAL THR
SEQRES 6 B 252 ASP LEU LEU ARG LYS THR LEU VAL SER TYR ASN ILE LEU
SEQRES 7 B 252 ASP PHE TRP LEU VAL GLY TYR SER LEU GLY GLY ARG VAL
SEQRES 8 B 252 ALA MET MET ALA ALA CYS GLN GLY LEU ALA GLY LEU CYS
SEQRES 9 B 252 GLY VAL ILE VAL GLU GLY GLY HIS PRO GLY LEU GLN ASN
SEQRES 10 B 252 ALA GLU GLN ARG ALA GLU ARG GLN ARG SER ASP ARG GLN
SEQRES 11 B 252 TRP VAL GLN ARG PHE LEU THR GLU PRO LEU THR ALA VAL
SEQRES 12 B 252 PHE ALA ASP TRP TYR GLN GLN PRO VAL PHE ALA SER LEU
SEQRES 13 B 252 ASN ASP ASP GLN ARG ARG GLU LEU VAL ALA LEU ARG SER
SEQRES 14 B 252 ASN ASN ASN GLY ALA THR LEU ALA ALA MET LEU GLU ALA
SEQRES 15 B 252 THR SER LEU ALA VAL GLN PRO ASP LEU ARG ALA ASN LEU
SEQRES 16 B 252 SER ALA ARG THR PHE ALA PHE TYR TYR LEU CYS GLY GLU
SEQRES 17 B 252 ARG ASP SER LYS PHE ARG ALA LEU ALA ALA GLU LEU ALA
SEQRES 18 B 252 ALA ASP CYS HIS VAL ILE PRO ARG ALA GLY HIS ASN ALA
SEQRES 19 B 252 HIS ARG GLU ASN PRO ALA GLY VAL ILE ALA SER LEU ALA
SEQRES 20 B 252 GLN ILE LEU ARG PHE
SEQRES 1 C 252 MET ILE LEU HIS ALA GLN ALA LYS HIS GLY LYS PRO GLY
SEQRES 2 C 252 LEU PRO TRP LEU VAL PHE LEU HIS GLY PHE SER GLY ASP
SEQRES 3 C 252 CYS HIS GLU TRP GLN GLU VAL GLY GLU ALA PHE ALA ASP
SEQRES 4 C 252 TYR SER ARG LEU TYR VAL ASP LEU PRO GLY HIS GLY GLY
SEQRES 5 C 252 SER ALA ALA ILE SER VAL ASP GLY PHE ASP ASP VAL THR
SEQRES 6 C 252 ASP LEU LEU ARG LYS THR LEU VAL SER TYR ASN ILE LEU
SEQRES 7 C 252 ASP PHE TRP LEU VAL GLY TYR SER LEU GLY GLY ARG VAL
SEQRES 8 C 252 ALA MET MET ALA ALA CYS GLN GLY LEU ALA GLY LEU CYS
SEQRES 9 C 252 GLY VAL ILE VAL GLU GLY GLY HIS PRO GLY LEU GLN ASN
SEQRES 10 C 252 ALA GLU GLN ARG ALA GLU ARG GLN ARG SER ASP ARG GLN
SEQRES 11 C 252 TRP VAL GLN ARG PHE LEU THR GLU PRO LEU THR ALA VAL
SEQRES 12 C 252 PHE ALA ASP TRP TYR GLN GLN PRO VAL PHE ALA SER LEU
SEQRES 13 C 252 ASN ASP ASP GLN ARG ARG GLU LEU VAL ALA LEU ARG SER
SEQRES 14 C 252 ASN ASN ASN GLY ALA THR LEU ALA ALA MET LEU GLU ALA
SEQRES 15 C 252 THR SER LEU ALA VAL GLN PRO ASP LEU ARG ALA ASN LEU
SEQRES 16 C 252 SER ALA ARG THR PHE ALA PHE TYR TYR LEU CYS GLY GLU
SEQRES 17 C 252 ARG ASP SER LYS PHE ARG ALA LEU ALA ALA GLU LEU ALA
SEQRES 18 C 252 ALA ASP CYS HIS VAL ILE PRO ARG ALA GLY HIS ASN ALA
SEQRES 19 C 252 HIS ARG GLU ASN PRO ALA GLY VAL ILE ALA SER LEU ALA
SEQRES 20 C 252 GLN ILE LEU ARG PHE
HET 164 A 301 17
HET GOL A 302 6
HET 164 B 301 17
HET PYR B 302 6
HETNAM 164 2-(3-CARBOXYPROPIONYL)-6-HYDROXY-CYCLOHEXA-2,4-DIENE
HETNAM 2 164 CARBOXYLIC ACID
HETNAM GOL GLYCEROL
HETNAM PYR PYRUVIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 164 2(C11 H12 O6)
FORMUL 5 GOL C3 H8 O3
FORMUL 7 PYR C3 H4 O3
FORMUL 8 HOH *827(H2 O)
HELIX 1 1 TRP A 30 GLU A 35 1 6
HELIX 2 2 HIS A 50 ALA A 54 5 5
HELIX 3 3 GLY A 60 TYR A 75 1 16
HELIX 4 4 SER A 86 GLY A 99 1 14
HELIX 5 5 ASN A 117 GLU A 138 1 22
HELIX 6 6 PRO A 139 TYR A 148 1 10
HELIX 7 7 GLN A 149 ALA A 154 5 6
HELIX 8 8 ASN A 157 SER A 169 1 13
HELIX 9 9 ASN A 172 THR A 183 1 12
HELIX 10 10 SER A 184 GLN A 188 5 5
HELIX 11 11 LEU A 191 ALA A 197 1 7
HELIX 12 12 ASP A 210 LEU A 220 1 11
HELIX 13 13 ASN A 233 ASN A 238 1 6
HELIX 14 14 ASN A 238 ARG A 251 1 14
HELIX 15 15 TRP B 30 GLU B 35 1 6
HELIX 16 16 HIS B 50 ALA B 54 5 5
HELIX 17 17 GLY B 60 TYR B 75 1 16
HELIX 18 18 SER B 86 GLY B 99 1 14
HELIX 19 19 ASN B 117 GLU B 138 1 22
HELIX 20 20 PRO B 139 TYR B 148 1 10
HELIX 21 21 GLN B 149 ALA B 154 5 6
HELIX 22 22 ASN B 157 SER B 169 1 13
HELIX 23 23 ASN B 172 THR B 183 1 12
HELIX 24 24 SER B 184 GLN B 188 5 5
HELIX 25 25 LEU B 191 ALA B 197 1 7
HELIX 26 26 ASP B 210 ALA B 221 1 12
HELIX 27 27 ASN B 233 ASN B 238 1 6
HELIX 28 28 ASN B 238 ARG B 251 1 14
HELIX 29 29 TRP C 30 GLU C 35 1 6
HELIX 30 30 HIS C 50 ALA C 54 5 5
HELIX 31 31 GLY C 60 TYR C 75 1 16
HELIX 32 32 SER C 86 GLY C 99 1 14
HELIX 33 33 ASN C 117 ARG C 124 1 8
HELIX 34 34 ARG C 129 GLU C 138 1 10
HELIX 35 35 PRO C 139 TYR C 148 1 10
HELIX 36 36 GLN C 149 ALA C 154 5 6
HELIX 37 37 ASN C 157 SER C 169 1 13
HELIX 38 38 ASN C 172 THR C 183 1 12
HELIX 39 39 SER C 184 GLN C 188 5 5
HELIX 40 40 LEU C 191 ALA C 197 1 7
HELIX 41 41 ASP C 210 GLU C 219 1 10
HELIX 42 42 ASN C 233 ASN C 238 1 6
HELIX 43 43 ASN C 238 PHE C 252 1 15
SHEET 1 A 7 ALA A 5 LYS A 8 0
SHEET 2 A 7 SER A 41 VAL A 45 -1 O TYR A 44 N GLN A 6
SHEET 3 A 7 TRP A 16 LEU A 20 1 N PHE A 19 O LEU A 43
SHEET 4 A 7 PHE A 80 TYR A 85 1 O VAL A 83 N VAL A 18
SHEET 5 A 7 LEU A 103 GLU A 109 1 O CYS A 104 N PHE A 80
SHEET 6 A 7 ALA A 201 GLY A 207 1 O LEU A 205 N VAL A 108
SHEET 7 A 7 ASP A 223 ILE A 227 1 O HIS A 225 N TYR A 204
SHEET 1 B 7 ALA B 5 LYS B 8 0
SHEET 2 B 7 SER B 41 VAL B 45 -1 O TYR B 44 N GLN B 6
SHEET 3 B 7 TRP B 16 LEU B 20 1 N LEU B 17 O SER B 41
SHEET 4 B 7 PHE B 80 TYR B 85 1 O VAL B 83 N LEU B 20
SHEET 5 B 7 LEU B 103 GLU B 109 1 O CYS B 104 N PHE B 80
SHEET 6 B 7 ALA B 201 GLY B 207 1 O LEU B 205 N VAL B 108
SHEET 7 B 7 ASP B 223 ILE B 227 1 O HIS B 225 N TYR B 204
SHEET 1 C 7 ALA C 5 LYS C 8 0
SHEET 2 C 7 SER C 41 VAL C 45 -1 O TYR C 44 N GLN C 6
SHEET 3 C 7 TRP C 16 LEU C 20 1 N LEU C 17 O LEU C 43
SHEET 4 C 7 PHE C 80 TYR C 85 1 O VAL C 83 N LEU C 20
SHEET 5 C 7 LEU C 103 GLU C 109 1 O CYS C 104 N PHE C 80
SHEET 6 C 7 PHE C 202 GLY C 207 1 O LEU C 205 N VAL C 108
SHEET 7 C 7 CYS C 224 ILE C 227 1 O HIS C 225 N TYR C 204
SITE 1 AC1 15 GLY A 22 PHE A 23 TYR A 85 SER A 86
SITE 2 AC1 15 LEU A 87 ARG A 90 TRP A 147 TYR A 148
SITE 3 AC1 15 PHE A 153 GOL A 302 HOH A 408 HOH A 409
SITE 4 AC1 15 HOH A 411 HOH A 428 HOH A 482
SITE 1 AC2 8 ARG A 124 SER A 127 ASP A 128 TRP A 131
SITE 2 AC2 8 TRP A 147 GLN A 150 164 A 301 HOH A 508
SITE 1 AC3 15 GLY B 22 PHE B 23 TYR B 85 SER B 86
SITE 2 AC3 15 LEU B 87 ARG B 90 TRP B 147 TYR B 148
SITE 3 AC3 15 PHE B 153 PYR B 302 HOH B 408 HOH B 414
SITE 4 AC3 15 HOH B 417 HOH B 434 HOH B 471
SITE 1 AC4 7 ARG B 124 SER B 127 ASP B 128 TRP B 131
SITE 2 AC4 7 TRP B 147 GLN B 150 164 B 301
CRYST1 122.000 122.000 46.940 90.00 90.00 120.00 P 31 9
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 0.008197 0.004732 0.000000 0.00000
SCALE2 0.000000 0.009465 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021304 0.00000
TER 1935 PHE A 252
TER 3919 PHE B 252
TER 7766 PHE C 252
MASTER 683 0 4 43 21 0 12 6 6674 3 46 60
END |