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HEADER HYDROLASE 24-APR-12 4ETW
TITLE STRUCTURE OF THE ENZYME-ACP SUBSTRATE GATEKEEPER COMPLEX REQUIRED FOR
TITLE 2 BIOTIN SYNTHESIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PIMELYL-[ACYL-CARRIER PROTEIN] METHYL ESTER ESTERASE;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: BIOTIN SYNTHESIS PROTEIN BIOH, CARBOXYLESTERASE BIOH;
COMPND 5 EC: 3.1.1.85;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: ACYL CARRIER PROTEIN;
COMPND 10 CHAIN: D, B;
COMPND 11 SYNONYM: ACP;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SHIGELLA FLEXNERI;
SOURCE 3 ORGANISM_TAXID: 623;
SOURCE 4 GENE: BIOH, SF3435, S4329;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: SHIGELLA FLEXNERI 5;
SOURCE 7 ORGANISM_TAXID: 373384;
SOURCE 8 STRAIN: SS046;
SOURCE 9 GENE: ACPP, SFV_1114, SSON_1114
KEYWDS ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.AGARWAL,S.K.NAIR
REVDAT 2 07-NOV-12 4ETW 1 JRNL
REVDAT 1 17-OCT-12 4ETW 0
JRNL AUTH V.AGARWAL,S.LIN,T.LUKK,S.K.NAIR,J.E.CRONAN
JRNL TITL STRUCTURE OF THE ENZYME-ACYL CARRIER PROTEIN (ACP) SUBSTRATE
JRNL TITL 2 GATEKEEPER COMPLEX REQUIRED FOR BIOTIN SYNTHESIS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 17406 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 23045647
JRNL DOI 10.1073/PNAS.1207028109
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.160
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 42538
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 2145
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 35.1350 - 5.0512 0.98 2694 155 0.1818 0.1967
REMARK 3 2 5.0512 - 4.0111 0.99 2723 150 0.1546 0.1894
REMARK 3 3 4.0111 - 3.5046 0.99 2725 135 0.1819 0.2315
REMARK 3 4 3.5046 - 3.1844 0.98 2646 183 0.1930 0.2436
REMARK 3 5 3.1844 - 2.9563 0.99 2724 147 0.2066 0.2419
REMARK 3 6 2.9563 - 2.7821 0.98 2721 129 0.2008 0.2748
REMARK 3 7 2.7821 - 2.6428 0.98 2681 143 0.2118 0.2663
REMARK 3 8 2.6428 - 2.5278 0.98 2691 142 0.2168 0.2714
REMARK 3 9 2.5278 - 2.4305 0.98 2729 131 0.1995 0.2692
REMARK 3 10 2.4305 - 2.3466 0.98 2696 141 0.2121 0.2760
REMARK 3 11 2.3466 - 2.2733 0.97 2653 133 0.2174 0.3208
REMARK 3 12 2.2733 - 2.2083 0.97 2696 128 0.2129 0.2664
REMARK 3 13 2.2083 - 2.1502 0.97 2720 142 0.2045 0.2689
REMARK 3 14 2.1502 - 2.0977 0.97 2634 146 0.2220 0.2446
REMARK 3 15 2.0977 - 2.0500 0.97 2655 140 0.2387 0.3030
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 50.22
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.550
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.28150
REMARK 3 B22 (A**2) : -0.52590
REMARK 3 B33 (A**2) : 0.80750
REMARK 3 B12 (A**2) : -0.20090
REMARK 3 B13 (A**2) : -0.99220
REMARK 3 B23 (A**2) : 0.52030
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 : 0.010 5320
REMARK 3 ANGLE : 1.195 7236
REMARK 3 CHIRALITY : 0.078 822
REMARK 3 PLANARITY : 0.004 934
REMARK 3 DIHEDRAL : 17.069 1940
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 30
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 3:45 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0978 -18.9526 29.6338
REMARK 3 T TENSOR
REMARK 3 T11: 0.1152 T22: 0.1805
REMARK 3 T33: 0.2008 T12: -0.0455
REMARK 3 T13: -0.0210 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 0.4157 L22: 0.6690
REMARK 3 L33: 0.7154 L12: 0.1295
REMARK 3 L13: -0.2963 L23: -0.6556
REMARK 3 S TENSOR
REMARK 3 S11: 0.1169 S12: -0.2029 S13: -0.2744
REMARK 3 S21: 0.1232 S22: -0.0874 S23: 0.0240
REMARK 3 S31: -0.1422 S32: 0.2355 S33: 0.1428
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 46:60 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.2520 -9.5466 38.7247
REMARK 3 T TENSOR
REMARK 3 T11: 0.3941 T22: 0.1793
REMARK 3 T33: 0.1236 T12: -0.0460
REMARK 3 T13: 0.0835 T23: -0.0325
REMARK 3 L TENSOR
REMARK 3 L11: 1.1017 L22: 0.2635
REMARK 3 L33: 0.1211 L12: -0.0105
REMARK 3 L13: 0.3535 L23: 0.0427
REMARK 3 S TENSOR
REMARK 3 S11: 0.1694 S12: -0.2529 S13: 0.0393
REMARK 3 S21: 0.2341 S22: 0.0652 S23: 0.0318
REMARK 3 S31: -0.2254 S32: -0.0360 S33: 0.0864
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 61:75 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9188 -4.4701 33.6985
REMARK 3 T TENSOR
REMARK 3 T11: 0.5346 T22: 0.1707
REMARK 3 T33: 0.3543 T12: -0.2202
REMARK 3 T13: 0.1220 T23: -0.1491
REMARK 3 L TENSOR
REMARK 3 L11: 0.0873 L22: 0.0199
REMARK 3 L33: 0.0190 L12: -0.0404
REMARK 3 L13: 0.0420 L23: -0.0192
REMARK 3 S TENSOR
REMARK 3 S11: 0.1058 S12: -0.0394 S13: -0.0187
REMARK 3 S21: 0.0984 S22: 0.0044 S23: -0.1447
REMARK 3 S31: -0.0665 S32: 0.0537 S33: 0.1430
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 76:121 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5477 -4.9626 21.5637
REMARK 3 T TENSOR
REMARK 3 T11: 0.4807 T22: 0.0232
REMARK 3 T33: 0.2856 T12: -0.0093
REMARK 3 T13: 0.1661 T23: 0.0180
REMARK 3 L TENSOR
REMARK 3 L11: 0.7067 L22: 0.5857
REMARK 3 L33: 2.0081 L12: 0.0474
REMARK 3 L13: -1.1682 L23: 0.1533
REMARK 3 S TENSOR
REMARK 3 S11: 0.3057 S12: 0.2179 S13: 0.4156
REMARK 3 S21: -0.1080 S22: 0.0330 S23: 0.0009
REMARK 3 S31: -0.8783 S32: -0.3182 S33: 1.1054
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 122:148 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.5390 -13.2025 28.8479
REMARK 3 T TENSOR
REMARK 3 T11: 0.2969 T22: 0.4102
REMARK 3 T33: 0.2959 T12: 0.2177
REMARK 3 T13: 0.1345 T23: 0.0351
REMARK 3 L TENSOR
REMARK 3 L11: 0.1688 L22: 0.0707
REMARK 3 L33: 0.0996 L12: 0.0845
REMARK 3 L13: -0.0748 L23: 0.0089
REMARK 3 S TENSOR
REMARK 3 S11: -0.0697 S12: 0.0150 S13: -0.0690
REMARK 3 S21: 0.1466 S22: 0.1022 S23: 0.3022
REMARK 3 S31: -0.2036 S32: -0.3743 S33: 0.1505
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 149:166 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.4158 -26.3979 24.4331
REMARK 3 T TENSOR
REMARK 3 T11: 0.1191 T22: 0.2133
REMARK 3 T33: 0.2462 T12: -0.1062
REMARK 3 T13: 0.0163 T23: -0.0187
REMARK 3 L TENSOR
REMARK 3 L11: 0.2725 L22: 0.9982
REMARK 3 L33: 0.4968 L12: -0.4611
REMARK 3 L13: 0.0645 L23: 0.2156
REMARK 3 S TENSOR
REMARK 3 S11: -0.2292 S12: 0.1304 S13: -0.0730
REMARK 3 S21: 0.0561 S22: 0.0900 S23: -0.0423
REMARK 3 S31: 0.1049 S32: -0.0888 S33: -0.0443
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 167:211 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.3580 -6.5522 23.1677
REMARK 3 T TENSOR
REMARK 3 T11: 0.4330 T22: 0.1012
REMARK 3 T33: 0.1741 T12: 0.1409
REMARK 3 T13: 0.1268 T23: 0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 0.1892 L22: 0.0568
REMARK 3 L33: 0.7735 L12: 0.0746
REMARK 3 L13: -0.3380 L23: -0.1868
REMARK 3 S TENSOR
REMARK 3 S11: 0.2939 S12: 0.0600 S13: 0.4406
REMARK 3 S21: 0.2137 S22: 0.0029 S23: 0.0258
REMARK 3 S31: -0.7116 S32: -0.2350 S33: 0.3159
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 212:230 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.3014 -7.2325 9.0713
REMARK 3 T TENSOR
REMARK 3 T11: 0.4007 T22: 0.2787
REMARK 3 T33: 0.1463 T12: 0.1279
REMARK 3 T13: 0.1419 T23: 0.0814
REMARK 3 L TENSOR
REMARK 3 L11: 0.3651 L22: 0.4446
REMARK 3 L33: 0.9754 L12: -0.0469
REMARK 3 L13: 0.3370 L23: 0.1880
REMARK 3 S TENSOR
REMARK 3 S11: 0.1807 S12: 0.2449 S13: 0.2213
REMARK 3 S21: -0.0997 S22: 0.0136 S23: -0.0254
REMARK 3 S31: -0.2105 S32: -0.0495 S33: 0.6176
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN A AND RESID 231:257 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2845 -20.2821 16.0073
REMARK 3 T TENSOR
REMARK 3 T11: 0.1726 T22: 0.2044
REMARK 3 T33: 0.1608 T12: 0.0300
REMARK 3 T13: 0.0306 T23: -0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 0.0144 L22: 0.0117
REMARK 3 L33: 0.1049 L12: 0.0107
REMARK 3 L13: 0.0096 L23: -0.0229
REMARK 3 S TENSOR
REMARK 3 S11: 0.0282 S12: 0.3576 S13: -0.1051
REMARK 3 S21: -0.1737 S22: -0.0731 S23: -0.0371
REMARK 3 S31: 0.1487 S32: -0.0913 S33: 0.0011
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN C AND RESID 3:45 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1471 -22.5048 -2.3899
REMARK 3 T TENSOR
REMARK 3 T11: 0.0928 T22: 0.2464
REMARK 3 T33: 0.1369 T12: -0.0291
REMARK 3 T13: 0.0021 T23: -0.0261
REMARK 3 L TENSOR
REMARK 3 L11: 0.4621 L22: 0.1226
REMARK 3 L33: 0.4724 L12: -0.0911
REMARK 3 L13: 0.1171 L23: 0.1936
REMARK 3 S TENSOR
REMARK 3 S11: 0.0176 S12: -0.2345 S13: 0.1814
REMARK 3 S21: 0.1092 S22: -0.0110 S23: 0.1021
REMARK 3 S31: 0.1639 S32: -0.2147 S33: -0.1120
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN C AND RESID 46:60 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.6555 -34.8833 1.5412
REMARK 3 T TENSOR
REMARK 3 T11: 0.4743 T22: 0.2828
REMARK 3 T33: 0.1544 T12: 0.0294
REMARK 3 T13: -0.0061 T23: 0.0666
REMARK 3 L TENSOR
REMARK 3 L11: 0.7552 L22: 0.3419
REMARK 3 L33: 0.0274 L12: 0.2693
REMARK 3 L13: 0.0444 L23: 0.0960
REMARK 3 S TENSOR
REMARK 3 S11: 0.0912 S12: -0.1591 S13: -0.0548
REMARK 3 S21: -0.0387 S22: -0.1257 S23: -0.0216
REMARK 3 S31: 0.4326 S32: 0.2572 S33: -0.0085
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN C AND RESID 61:75 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7700 -37.3101 -5.2453
REMARK 3 T TENSOR
REMARK 3 T11: 0.7024 T22: 0.2910
REMARK 3 T33: 0.3446 T12: -0.1759
REMARK 3 T13: 0.0387 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.3577 L22: 0.0828
REMARK 3 L33: 0.3548 L12: -0.0861
REMARK 3 L13: -0.0668 L23: -0.1294
REMARK 3 S TENSOR
REMARK 3 S11: 0.0901 S12: -0.1244 S13: -0.1159
REMARK 3 S21: 0.0553 S22: -0.1947 S23: 0.1770
REMARK 3 S31: 0.3978 S32: -0.1272 S33: -0.0138
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN C AND RESID 76:121 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3567 -31.3197 -15.8463
REMARK 3 T TENSOR
REMARK 3 T11: 0.3767 T22: 0.0898
REMARK 3 T33: 0.1121 T12: -0.0260
REMARK 3 T13: -0.0196 T23: -0.0464
REMARK 3 L TENSOR
REMARK 3 L11: 0.2110 L22: 1.3833
REMARK 3 L33: 1.1343 L12: -0.2243
REMARK 3 L13: 0.4827 L23: -0.3177
REMARK 3 S TENSOR
REMARK 3 S11: -0.0533 S12: 0.1295 S13: -0.0543
REMARK 3 S21: -0.4110 S22: -0.1197 S23: -0.0330
REMARK 3 S31: 0.6809 S32: -0.0492 S33: -0.2942
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN C AND RESID 122:148 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5646 -26.9480 -5.5950
REMARK 3 T TENSOR
REMARK 3 T11: 0.2171 T22: 0.5224
REMARK 3 T33: 0.1446 T12: 0.3326
REMARK 3 T13: -0.0707 T23: 0.0762
REMARK 3 L TENSOR
REMARK 3 L11: 0.4279 L22: 0.0616
REMARK 3 L33: 0.0581 L12: -0.1163
REMARK 3 L13: 0.1562 L23: -0.0347
REMARK 3 S TENSOR
REMARK 3 S11: -0.1000 S12: -0.0626 S13: 0.0836
REMARK 3 S21: 0.0386 S22: -0.0364 S23: -0.1047
REMARK 3 S31: 0.0786 S32: 0.2250 S33: -0.4245
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN C AND RESID 149:167 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.0701 -13.5786 -3.2796
REMARK 3 T TENSOR
REMARK 3 T11: 0.1745 T22: 0.3455
REMARK 3 T33: 0.1924 T12: -0.0707
REMARK 3 T13: -0.0669 T23: -0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 0.4949 L22: 0.4608
REMARK 3 L33: 0.1660 L12: -0.2341
REMARK 3 L13: -0.2869 L23: 0.1445
REMARK 3 S TENSOR
REMARK 3 S11: -0.1690 S12: -0.1099 S13: 0.1301
REMARK 3 S21: 0.1077 S22: -0.0866 S23: 0.0320
REMARK 3 S31: -0.1255 S32: 0.0725 S33: -0.1939
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN C AND RESID 168:185 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.5530 -34.5364 -3.0140
REMARK 3 T TENSOR
REMARK 3 T11: 0.6382 T22: 0.3790
REMARK 3 T33: 0.2354 T12: 0.3222
REMARK 3 T13: 0.0345 T23: 0.1793
REMARK 3 L TENSOR
REMARK 3 L11: -0.0011 L22: 0.0095
REMARK 3 L33: 0.0004 L12: -0.0003
REMARK 3 L13: -0.0005 L23: 0.0031
REMARK 3 S TENSOR
REMARK 3 S11: 0.0389 S12: -0.0125 S13: -0.0498
REMARK 3 S21: -0.0647 S22: -0.0507 S23: -0.0424
REMARK 3 S31: 0.1221 S32: 0.0618 S33: 0.0563
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN C AND RESID 186:221 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4620 -27.3602 -22.9736
REMARK 3 T TENSOR
REMARK 3 T11: 0.3401 T22: 0.1866
REMARK 3 T33: 0.0703 T12: 0.0378
REMARK 3 T13: -0.0282 T23: -0.0406
REMARK 3 L TENSOR
REMARK 3 L11: 0.9188 L22: 0.6925
REMARK 3 L33: 0.2209 L12: -0.2269
REMARK 3 L13: 0.2321 L23: 0.2629
REMARK 3 S TENSOR
REMARK 3 S11: 0.0098 S12: 0.2102 S13: -0.0494
REMARK 3 S21: -0.3460 S22: -0.0376 S23: -0.0246
REMARK 3 S31: 0.3827 S32: 0.0038 S33: -0.0843
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN C AND RESID 222:241 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.6262 -18.3543 -18.3490
REMARK 3 T TENSOR
REMARK 3 T11: 0.1468 T22: 0.1963
REMARK 3 T33: 0.1571 T12: 0.0163
REMARK 3 T13: -0.0417 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.0127 L22: 0.0592
REMARK 3 L33: 0.0872 L12: 0.0029
REMARK 3 L13: -0.0083 L23: -0.0306
REMARK 3 S TENSOR
REMARK 3 S11: 0.0124 S12: 0.1770 S13: 0.1499
REMARK 3 S21: -0.1195 S22: -0.0754 S23: 0.1539
REMARK 3 S31: 0.0255 S32: -0.1341 S33: 0.0126
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN C AND RESID 242:257 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.6286 -15.7286 -14.9139
REMARK 3 T TENSOR
REMARK 3 T11: 0.1344 T22: 0.3147
REMARK 3 T33: 0.1992 T12: 0.0702
REMARK 3 T13: -0.0484 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 0.1550 L22: 0.0856
REMARK 3 L33: 0.1697 L12: -0.1154
REMARK 3 L13: 0.1611 L23: -0.1194
REMARK 3 S TENSOR
REMARK 3 S11: 0.0738 S12: 0.1410 S13: 0.1050
REMARK 3 S21: -0.0684 S22: -0.0565 S23: 0.0451
REMARK 3 S31: -0.0539 S32: -0.1121 S33: 0.1102
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN D AND RESID 500:514 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5228 -9.5817 5.8993
REMARK 3 T TENSOR
REMARK 3 T11: 0.2423 T22: 0.7632
REMARK 3 T33: 0.3966 T12: -0.0522
REMARK 3 T13: -0.0242 T23: -0.1046
REMARK 3 L TENSOR
REMARK 3 L11: 0.0081 L22: 0.0002
REMARK 3 L33: 0.0004 L12: 0.0004
REMARK 3 L13: -0.0018 L23: 0.0001
REMARK 3 S TENSOR
REMARK 3 S11: 0.0487 S12: -0.0790 S13: 0.1892
REMARK 3 S21: 0.1349 S22: -0.0718 S23: -0.0634
REMARK 3 S31: 0.0126 S32: 0.1117 S33: 0.0004
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN D AND RESID 515:520 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.9485 -16.2186 4.5734
REMARK 3 T TENSOR
REMARK 3 T11: 0.7522 T22: 0.9676
REMARK 3 T33: 0.6454 T12: 0.1082
REMARK 3 T13: -0.2512 T23: 0.0472
REMARK 3 L TENSOR
REMARK 3 L11: 0.0147 L22: 0.0131
REMARK 3 L33: 0.0065 L12: -0.0027
REMARK 3 L13: 0.0008 L23: -0.0078
REMARK 3 S TENSOR
REMARK 3 S11: 0.0063 S12: 0.0153 S13: -0.0139
REMARK 3 S21: 0.0273 S22: 0.0276 S23: 0.0074
REMARK 3 S31: -0.0382 S32: 0.0202 S33: -0.0005
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN D AND RESID 521:534 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.1652 -12.1121 -5.9627
REMARK 3 T TENSOR
REMARK 3 T11: 0.1532 T22: 0.6681
REMARK 3 T33: 0.3314 T12: -0.0751
REMARK 3 T13: -0.0535 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.1362 L22: 0.1352
REMARK 3 L33: 0.1443 L12: -0.0283
REMARK 3 L13: 0.1365 L23: -0.0012
REMARK 3 S TENSOR
REMARK 3 S11: 0.0773 S12: 0.2811 S13: -0.0379
REMARK 3 S21: -0.0630 S22: -0.0776 S23: 0.0369
REMARK 3 S31: 0.0150 S32: 0.0413 S33: -0.0311
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN D AND RESID 535:554 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0208 -8.3052 -0.6831
REMARK 3 T TENSOR
REMARK 3 T11: 0.1441 T22: 0.6406
REMARK 3 T33: 0.5074 T12: -0.0591
REMARK 3 T13: 0.0005 T23: -0.1126
REMARK 3 L TENSOR
REMARK 3 L11: 0.1239 L22: 0.0367
REMARK 3 L33: 0.0519 L12: 0.0599
REMARK 3 L13: 0.0363 L23: -0.0011
REMARK 3 S TENSOR
REMARK 3 S11: -0.0096 S12: 0.1277 S13: -0.0791
REMARK 3 S21: -0.0305 S22: -0.0166 S23: 0.0258
REMARK 3 S31: 0.0128 S32: -0.0065 S33: 0.0867
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN D AND RESID 555:563 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0947 -2.6889 -8.9287
REMARK 3 T TENSOR
REMARK 3 T11: 0.5845 T22: 0.5079
REMARK 3 T33: 0.5124 T12: -0.0450
REMARK 3 T13: -0.0684 T23: 0.0815
REMARK 3 L TENSOR
REMARK 3 L11: 0.1170 L22: 0.0114
REMARK 3 L33: 0.0381 L12: 0.0069
REMARK 3 L13: 0.0493 L23: -0.0111
REMARK 3 S TENSOR
REMARK 3 S11: -0.1086 S12: -0.0164 S13: 0.0347
REMARK 3 S21: -0.0661 S22: -0.1459 S23: 0.0657
REMARK 3 S31: -0.0275 S32: -0.0130 S33: -0.0022
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (CHAIN D AND RESID 564:574 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4689 0.3074 0.3905
REMARK 3 T TENSOR
REMARK 3 T11: 0.3253 T22: 0.4821
REMARK 3 T33: 1.0417 T12: -0.0601
REMARK 3 T13: 0.1187 T23: -0.1346
REMARK 3 L TENSOR
REMARK 3 L11: 0.0121 L22: 0.0579
REMARK 3 L33: 0.2224 L12: -0.0264
REMARK 3 L13: 0.0062 L23: -0.0024
REMARK 3 S TENSOR
REMARK 3 S11: -0.0035 S12: -0.0622 S13: -0.0030
REMARK 3 S21: -0.0083 S22: 0.0025 S23: -0.0389
REMARK 3 S31: -0.1296 S32: -0.0402 S33: -0.0044
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: (CHAIN B AND RESID 500:520 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.2916 -31.7384 32.4262
REMARK 3 T TENSOR
REMARK 3 T11: 0.3232 T22: 0.5045
REMARK 3 T33: 0.7802 T12: -0.0177
REMARK 3 T13: 0.1051 T23: 0.2318
REMARK 3 L TENSOR
REMARK 3 L11: 0.0798 L22: 0.0001
REMARK 3 L33: 0.7511 L12: 0.0049
REMARK 3 L13: 0.2447 L23: 0.0135
REMARK 3 S TENSOR
REMARK 3 S11: -0.2263 S12: -0.0266 S13: -0.2144
REMARK 3 S21: 0.1001 S22: -0.0112 S23: 0.0971
REMARK 3 S31: -0.0979 S32: -0.0510 S33: -0.0587
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: (CHAIN B AND RESID 521:534 )
REMARK 3 ORIGIN FOR THE GROUP (A): -40.2771 -26.6928 21.9875
REMARK 3 T TENSOR
REMARK 3 T11: 0.1995 T22: 0.5688
REMARK 3 T33: 0.4062 T12: -0.0924
REMARK 3 T13: 0.0185 T23: -0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 0.0198 L22: 0.0078
REMARK 3 L33: 0.0122 L12: -0.0042
REMARK 3 L13: -0.0075 L23: 0.0103
REMARK 3 S TENSOR
REMARK 3 S11: 0.0744 S12: 0.1641 S13: -0.1323
REMARK 3 S21: -0.0651 S22: -0.0685 S23: 0.0225
REMARK 3 S31: 0.0637 S32: -0.0015 S33: -0.0000
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: (CHAIN B AND RESID 535:549 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.2168 -29.8074 26.1684
REMARK 3 T TENSOR
REMARK 3 T11: 0.1655 T22: 0.3808
REMARK 3 T33: 0.5562 T12: -0.0895
REMARK 3 T13: 0.0467 T23: -0.0450
REMARK 3 L TENSOR
REMARK 3 L11: 0.0378 L22: 0.0756
REMARK 3 L33: 0.0397 L12: -0.0454
REMARK 3 L13: 0.0032 L23: -0.0331
REMARK 3 S TENSOR
REMARK 3 S11: -0.0194 S12: 0.0845 S13: -0.0918
REMARK 3 S21: 0.0233 S22: -0.0054 S23: -0.0198
REMARK 3 S31: -0.0239 S32: -0.0365 S33: -0.0033
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: (CHAIN B AND RESID 550:563 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.4924 -35.8139 18.8193
REMARK 3 T TENSOR
REMARK 3 T11: 0.3415 T22: 0.7685
REMARK 3 T33: 0.7184 T12: -0.0101
REMARK 3 T13: 0.0797 T23: -0.3933
REMARK 3 L TENSOR
REMARK 3 L11: 0.0005 L22: 0.1940
REMARK 3 L33: 0.0996 L12: -0.0071
REMARK 3 L13: 0.0047 L23: -0.1389
REMARK 3 S TENSOR
REMARK 3 S11: -0.1295 S12: -0.0212 S13: -0.0804
REMARK 3 S21: -0.0612 S22: -0.0277 S23: -0.0947
REMARK 3 S31: 0.0888 S32: 0.0856 S33: -0.0353
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: (CHAIN B AND RESID 564:574 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.4353 -40.5054 23.4050
REMARK 3 T TENSOR
REMARK 3 T11: 0.3859 T22: 0.2775
REMARK 3 T33: 0.9322 T12: -0.1236
REMARK 3 T13: 0.0985 T23: -0.2122
REMARK 3 L TENSOR
REMARK 3 L11: 0.0481 L22: 0.1485
REMARK 3 L33: 0.0531 L12: 0.0841
REMARK 3 L13: 0.0095 L23: 0.0254
REMARK 3 S TENSOR
REMARK 3 S11: -0.0294 S12: 0.0087 S13: -0.0416
REMARK 3 S21: -0.0181 S22: -0.0084 S23: -0.0428
REMARK 3 S31: 0.0602 S32: -0.0197 S33: -0.1211
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: chain A and (resseq 3:257 )
REMARK 3 SELECTION : chain C and (resseq 3:257 )
REMARK 3 ATOM PAIRS NUMBER : 1998
REMARK 3 RMSD : 0.055
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: chain D and (resseq 500:574 )
REMARK 3 SELECTION : chain B and (resseq 500:574 )
REMARK 3 ATOM PAIRS NUMBER : 573
REMARK 3 RMSD : 0.118
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4ETW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-12.
REMARK 100 THE RCSB ID CODE IS RCSB072063.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42538
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 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 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 (%): 47.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 1
REMARK 465 ASN A 2
REMARK 465 GLU A 258
REMARK 465 HIS A 259
REMARK 465 HIS A 260
REMARK 465 HIS A 261
REMARK 465 HIS A 262
REMARK 465 HIS A 263
REMARK 465 HIS A 264
REMARK 465 MET C 1
REMARK 465 ASN C 2
REMARK 465 GLU C 258
REMARK 465 HIS C 259
REMARK 465 HIS C 260
REMARK 465 HIS C 261
REMARK 465 HIS C 262
REMARK 465 HIS C 263
REMARK 465 HIS C 264
REMARK 465 GLN D 575
REMARK 465 ALA D 576
REMARK 465 GLN B 575
REMARK 465 ALA B 576
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 LYS D 517 CG CD CE NZ
REMARK 470 GLU D 519 CG CD OE1 OE2
REMARK 470 SER D 535 OG
REMARK 470 LYS B 517 CG CD CE NZ
REMARK 470 GLU B 519 CG CD OE1 OE2
REMARK 470 SER B 535 OG
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 NH2 ARG A 159 OE1 GLU B 546 1.78
REMARK 500 NH1 ARG A 54 O HOH A 396 1.80
REMARK 500 NZ LYS A 220 O HOH A 385 1.89
REMARK 500 OG SER A 196 O HOH A 318 1.90
REMARK 500 OH TYR C 228 OE1 GLU C 244 1.91
REMARK 500 OH TYR A 228 OE1 GLU A 244 1.93
REMARK 500 O LEU A 42 O HOH A 388 2.06
REMARK 500 OD2 ASP A 63 O HOH A 340 2.07
REMARK 500 O HOH C 383 O HOH C 392 2.09
REMARK 500 NH1 ARG C 155 OE2 GLU D 546 2.10
REMARK 500 O HOH C 379 O HOH C 407 2.15
REMARK 500 O HOH A 349 O HOH A 392 2.16
REMARK 500 CA SER B 535 OAK ZMK B 600 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 ASN D 572 CB ASN D 572 CG -0.146
REMARK 500 ASN D 572 CG ASN D 572 OD1 -0.153
REMARK 500 ASN B 572 CG ASN B 572 OD1 -0.151
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 24 -154.79 -114.78
REMARK 500 ALA A 82 -115.96 52.85
REMARK 500 ASP A 134 -109.84 -72.34
REMARK 500 ALA A 234 -122.17 -104.17
REMARK 500 LEU C 24 -156.28 -115.54
REMARK 500 ALA C 82 -116.33 55.06
REMARK 500 ASP C 134 -110.63 -72.58
REMARK 500 PHE C 136 -64.82 -28.41
REMARK 500 ALA C 234 -124.00 -104.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASN B 572 22.4 L L OUTSIDE RANGE
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 334 DISTANCE = 5.45 ANGSTROMS
REMARK 525 HOH A 384 DISTANCE = 5.18 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZMK D 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZMK B 600
DBREF 4ETW A 1 257 UNP Q83PW0 BIOH_SHIFL 1 257
DBREF 4ETW C 1 257 UNP Q83PW0 BIOH_SHIFL 1 257
DBREF 4ETW D 500 576 UNP Q0T5U2 ACP_SHIF8 2 78
DBREF 4ETW B 500 576 UNP Q0T5U2 ACP_SHIF8 2 78
SEQADV 4ETW ALA A 82 UNP Q83PW0 SER 82 ENGINEERED MUTATION
SEQADV 4ETW ALA A 243 UNP Q83PW0 VAL 243 ENGINEERED MUTATION
SEQADV 4ETW GLU A 258 UNP Q83PW0 EXPRESSION TAG
SEQADV 4ETW HIS A 259 UNP Q83PW0 EXPRESSION TAG
SEQADV 4ETW HIS A 260 UNP Q83PW0 EXPRESSION TAG
SEQADV 4ETW HIS A 261 UNP Q83PW0 EXPRESSION TAG
SEQADV 4ETW HIS A 262 UNP Q83PW0 EXPRESSION TAG
SEQADV 4ETW HIS A 263 UNP Q83PW0 EXPRESSION TAG
SEQADV 4ETW HIS A 264 UNP Q83PW0 EXPRESSION TAG
SEQADV 4ETW ALA C 82 UNP Q83PW0 SER 82 ENGINEERED MUTATION
SEQADV 4ETW ALA C 243 UNP Q83PW0 VAL 243 ENGINEERED MUTATION
SEQADV 4ETW GLU C 258 UNP Q83PW0 EXPRESSION TAG
SEQADV 4ETW HIS C 259 UNP Q83PW0 EXPRESSION TAG
SEQADV 4ETW HIS C 260 UNP Q83PW0 EXPRESSION TAG
SEQADV 4ETW HIS C 261 UNP Q83PW0 EXPRESSION TAG
SEQADV 4ETW HIS C 262 UNP Q83PW0 EXPRESSION TAG
SEQADV 4ETW HIS C 263 UNP Q83PW0 EXPRESSION TAG
SEQADV 4ETW HIS C 264 UNP Q83PW0 EXPRESSION TAG
SEQRES 1 A 264 MET ASN ASN ILE TRP TRP GLN THR LYS GLY GLN GLY ASN
SEQRES 2 A 264 VAL HIS LEU VAL LEU LEU HIS GLY TRP GLY LEU ASN ALA
SEQRES 3 A 264 GLU VAL TRP ARG CYS ILE ASP GLU GLU LEU SER SER HIS
SEQRES 4 A 264 PHE THR LEU HIS LEU VAL ASP LEU PRO GLY PHE GLY ARG
SEQRES 5 A 264 SER ARG GLY PHE GLY ALA LEU SER LEU ALA ASP MET ALA
SEQRES 6 A 264 GLU ALA VAL LEU GLN GLN ALA PRO ASP LYS ALA ILE TRP
SEQRES 7 A 264 LEU GLY TRP ALA LEU GLY GLY LEU VAL ALA SER GLN ILE
SEQRES 8 A 264 ALA LEU THR HIS PRO GLU ARG VAL GLN ALA LEU VAL THR
SEQRES 9 A 264 VAL ALA SER SER PRO CYS PHE SER ALA ARG ASP GLU TRP
SEQRES 10 A 264 PRO GLY ILE LYS PRO ASP VAL LEU ALA GLY PHE GLN GLN
SEQRES 11 A 264 GLN LEU SER ASP ASP PHE GLN ARG THR VAL GLU ARG PHE
SEQRES 12 A 264 LEU ALA LEU GLN THR MET GLY THR GLU THR ALA ARG GLN
SEQRES 13 A 264 ASP ALA ARG ALA LEU LYS LYS THR VAL LEU ALA LEU PRO
SEQRES 14 A 264 MET PRO GLU VAL ASP VAL LEU ASN GLY GLY LEU GLU ILE
SEQRES 15 A 264 LEU LYS THR VAL ASP LEU ARG GLN PRO LEU GLN ASN VAL
SEQRES 16 A 264 SER MET PRO PHE LEU ARG LEU TYR GLY TYR LEU ASP GLY
SEQRES 17 A 264 LEU VAL PRO ARG LYS VAL VAL PRO MET LEU ASP LYS LEU
SEQRES 18 A 264 TRP PRO HIS SER GLU SER TYR ILE PHE ALA LYS ALA ALA
SEQRES 19 A 264 HIS ALA PRO PHE ILE SER HIS PRO ALA GLU PHE CYS HIS
SEQRES 20 A 264 LEU LEU VAL ALA LEU LYS GLN ARG VAL LEU GLU HIS HIS
SEQRES 21 A 264 HIS HIS HIS HIS
SEQRES 1 C 264 MET ASN ASN ILE TRP TRP GLN THR LYS GLY GLN GLY ASN
SEQRES 2 C 264 VAL HIS LEU VAL LEU LEU HIS GLY TRP GLY LEU ASN ALA
SEQRES 3 C 264 GLU VAL TRP ARG CYS ILE ASP GLU GLU LEU SER SER HIS
SEQRES 4 C 264 PHE THR LEU HIS LEU VAL ASP LEU PRO GLY PHE GLY ARG
SEQRES 5 C 264 SER ARG GLY PHE GLY ALA LEU SER LEU ALA ASP MET ALA
SEQRES 6 C 264 GLU ALA VAL LEU GLN GLN ALA PRO ASP LYS ALA ILE TRP
SEQRES 7 C 264 LEU GLY TRP ALA LEU GLY GLY LEU VAL ALA SER GLN ILE
SEQRES 8 C 264 ALA LEU THR HIS PRO GLU ARG VAL GLN ALA LEU VAL THR
SEQRES 9 C 264 VAL ALA SER SER PRO CYS PHE SER ALA ARG ASP GLU TRP
SEQRES 10 C 264 PRO GLY ILE LYS PRO ASP VAL LEU ALA GLY PHE GLN GLN
SEQRES 11 C 264 GLN LEU SER ASP ASP PHE GLN ARG THR VAL GLU ARG PHE
SEQRES 12 C 264 LEU ALA LEU GLN THR MET GLY THR GLU THR ALA ARG GLN
SEQRES 13 C 264 ASP ALA ARG ALA LEU LYS LYS THR VAL LEU ALA LEU PRO
SEQRES 14 C 264 MET PRO GLU VAL ASP VAL LEU ASN GLY GLY LEU GLU ILE
SEQRES 15 C 264 LEU LYS THR VAL ASP LEU ARG GLN PRO LEU GLN ASN VAL
SEQRES 16 C 264 SER MET PRO PHE LEU ARG LEU TYR GLY TYR LEU ASP GLY
SEQRES 17 C 264 LEU VAL PRO ARG LYS VAL VAL PRO MET LEU ASP LYS LEU
SEQRES 18 C 264 TRP PRO HIS SER GLU SER TYR ILE PHE ALA LYS ALA ALA
SEQRES 19 C 264 HIS ALA PRO PHE ILE SER HIS PRO ALA GLU PHE CYS HIS
SEQRES 20 C 264 LEU LEU VAL ALA LEU LYS GLN ARG VAL LEU GLU HIS HIS
SEQRES 21 C 264 HIS HIS HIS HIS
SEQRES 1 D 77 SER THR ILE GLU GLU ARG VAL LYS LYS ILE ILE GLY GLU
SEQRES 2 D 77 GLN LEU GLY VAL LYS GLN GLU GLU VAL THR ASN ASN ALA
SEQRES 3 D 77 SER PHE VAL GLU ASP LEU GLY ALA ASP SER LEU ASP THR
SEQRES 4 D 77 VAL GLU LEU VAL MET ALA LEU GLU GLU GLU PHE ASP THR
SEQRES 5 D 77 GLU ILE PRO ASP GLU GLU ALA GLU LYS ILE THR THR VAL
SEQRES 6 D 77 GLN ALA ALA ILE ASP TYR ILE ASN GLY HIS GLN ALA
SEQRES 1 B 77 SER THR ILE GLU GLU ARG VAL LYS LYS ILE ILE GLY GLU
SEQRES 2 B 77 GLN LEU GLY VAL LYS GLN GLU GLU VAL THR ASN ASN ALA
SEQRES 3 B 77 SER PHE VAL GLU ASP LEU GLY ALA ASP SER LEU ASP THR
SEQRES 4 B 77 VAL GLU LEU VAL MET ALA LEU GLU GLU GLU PHE ASP THR
SEQRES 5 B 77 GLU ILE PRO ASP GLU GLU ALA GLU LYS ILE THR THR VAL
SEQRES 6 B 77 GLN ALA ALA ILE ASP TYR ILE ASN GLY HIS GLN ALA
HET ZMK D 600 33
HET ZMK B 600 33
HETNAM ZMK METHYL 7-{[2-({N-[(2S)-2-HYDROXY-3,3-DIMETHYL-4-
HETNAM 2 ZMK (PHOSPHONOOXY)BUTANOYL]-BETA-ALANYL}AMINO)
HETNAM 3 ZMK ETHYL]SULFANYL}-7-OXOHEPTANOATE
FORMUL 5 ZMK 2(C19 H35 N2 O10 P S)
FORMUL 7 HOH *223(H2 O)
HELIX 1 1 ASN A 25 CYS A 31 5 7
HELIX 2 2 ILE A 32 SER A 38 1 7
HELIX 3 3 SER A 60 GLN A 70 1 11
HELIX 4 4 ALA A 82 HIS A 95 1 14
HELIX 5 5 LYS A 121 ASP A 134 1 14
HELIX 6 6 ASP A 135 MET A 149 1 15
HELIX 7 7 THR A 153 LEU A 168 1 16
HELIX 8 8 GLU A 172 VAL A 186 1 15
HELIX 9 9 GLN A 190 VAL A 195 5 6
HELIX 10 10 LYS A 213 TRP A 222 1 10
HELIX 11 11 ALA A 236 HIS A 241 1 6
HELIX 12 12 HIS A 241 LEU A 257 1 17
HELIX 13 13 ASN C 25 CYS C 31 5 7
HELIX 14 14 ILE C 32 SER C 38 1 7
HELIX 15 15 SER C 60 GLN C 70 1 11
HELIX 16 16 ALA C 82 HIS C 95 1 14
HELIX 17 17 LYS C 121 ASP C 134 1 14
HELIX 18 18 ASP C 135 MET C 149 1 15
HELIX 19 19 THR C 153 LEU C 168 1 16
HELIX 20 20 GLU C 172 VAL C 186 1 15
HELIX 21 21 GLN C 190 VAL C 195 5 6
HELIX 22 22 LYS C 213 TRP C 222 1 10
HELIX 23 23 ALA C 236 HIS C 241 1 6
HELIX 24 24 HIS C 241 LEU C 257 1 17
HELIX 25 25 THR D 501 GLY D 515 1 15
HELIX 26 26 ASP D 534 ASP D 550 1 17
HELIX 27 27 PRO D 554 GLU D 559 1 6
HELIX 28 28 THR D 563 GLY D 573 1 11
HELIX 29 29 THR B 501 GLY B 515 1 15
HELIX 30 30 ASP B 534 ASP B 550 1 17
HELIX 31 31 PRO B 554 GLU B 559 1 6
HELIX 32 32 THR B 563 GLY B 573 1 11
SHEET 1 A 7 TRP A 6 LYS A 9 0
SHEET 2 A 7 PHE A 40 VAL A 45 -1 O LEU A 42 N LYS A 9
SHEET 3 A 7 VAL A 14 LEU A 19 1 N LEU A 16 O HIS A 43
SHEET 4 A 7 ALA A 76 TRP A 81 1 O TRP A 81 N LEU A 19
SHEET 5 A 7 VAL A 99 VAL A 105 1 O VAL A 103 N TRP A 78
SHEET 6 A 7 PHE A 199 GLY A 204 1 O LEU A 202 N THR A 104
SHEET 7 A 7 GLU A 226 PHE A 230 1 O PHE A 230 N TYR A 203
SHEET 1 B 7 TRP C 6 LYS C 9 0
SHEET 2 B 7 PHE C 40 VAL C 45 -1 O LEU C 42 N LYS C 9
SHEET 3 B 7 VAL C 14 LEU C 19 1 N LEU C 16 O HIS C 43
SHEET 4 B 7 ALA C 76 TRP C 81 1 O TRP C 81 N LEU C 19
SHEET 5 B 7 VAL C 99 VAL C 105 1 O VAL C 103 N TRP C 78
SHEET 6 B 7 PHE C 199 GLY C 204 1 O LEU C 202 N THR C 104
SHEET 7 B 7 GLU C 226 PHE C 230 1 O PHE C 230 N TYR C 203
LINK CB SER B 535 OAK ZMK B 600 1555 1555 1.33
LINK CB SER D 535 OAJ ZMK D 600 1555 1555 1.33
SITE 1 AC1 13 GLY C 21 TRP C 22 ALA C 82 LEU C 83
SITE 2 AC1 13 VAL C 124 PHE C 128 PHE C 143 LEU C 146
SITE 3 AC1 13 GLN C 147 LEU C 183 HIS C 235 SER D 535
SITE 4 AC1 13 LEU D 536
SITE 1 AC2 13 GLY A 21 TRP A 22 ALA A 82 LEU A 83
SITE 2 AC2 13 VAL A 124 LEU A 125 PHE A 128 PHE A 143
SITE 3 AC2 13 GLN A 147 LEU A 183 HIS A 235 SER B 535
SITE 4 AC2 13 LEU B 536
CRYST1 57.080 57.210 60.950 101.99 90.10 112.74 P 1 2
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017519 0.007343 0.001735 0.00000
SCALE2 0.000000 0.018953 0.004397 0.00000
SCALE3 0.000000 0.000000 0.016843 0.00000
TER 2003 LEU A 257
TER 4006 LEU C 257
TER 4580 HIS D 574
TER 5154 HIS B 574
MASTER 820 0 2 32 14 0 8 6 5439 4 68 54
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