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HEADER HYDROLASE 07-JAN-19 6NKF
TITLE CRYSTAL STRUCTURE OF THE LIPASE LIP_VUT4 FROM GOAT RUMEN METAGENOME.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIP_VUT4, C3L;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METAGENOME;
SOURCE 3 ORGANISM_TAXID: 256318;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIPASE, GOAT RUMEN METAGENOMICS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KIM,L.WELK,G.MUKENDI,G.NKHI,T.MOTLOI,R.JEDRZEJCZAK,N.FETO,
AUTHOR 2 A.JOACHIMIAK
REVDAT 1 22-JAN-20 6NKF 0
JRNL AUTH Y.KIM,L.WELK,R.JEDRZEJCZAK,A.FETO,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF THE LIPASE LIP_VUT4 FROM GOAT RUMEN
JRNL TITL 2 METAGENOME.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.23 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 119305
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.179
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 5991
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 42.7309 - 6.9248 1.00 4060 246 0.1510 0.1718
REMARK 3 2 6.9248 - 5.5001 1.00 3937 204 0.1487 0.1482
REMARK 3 3 5.5001 - 4.8059 1.00 3866 216 0.1268 0.1388
REMARK 3 4 4.8059 - 4.3670 1.00 3853 197 0.1130 0.1235
REMARK 3 5 4.3670 - 4.0542 1.00 3843 181 0.1216 0.1352
REMARK 3 6 4.0542 - 3.8154 1.00 3823 206 0.1325 0.1768
REMARK 3 7 3.8154 - 3.6244 1.00 3823 208 0.1518 0.1699
REMARK 3 8 3.6244 - 3.4667 1.00 3782 215 0.1657 0.2058
REMARK 3 9 3.4667 - 3.3333 1.00 3811 169 0.1734 0.1960
REMARK 3 10 3.3333 - 3.2183 1.00 3785 196 0.1728 0.1938
REMARK 3 11 3.2183 - 3.1177 1.00 3801 197 0.1732 0.2129
REMARK 3 12 3.1177 - 3.0286 1.00 3751 212 0.1793 0.2087
REMARK 3 13 3.0286 - 2.9489 1.00 3807 179 0.1682 0.2023
REMARK 3 14 2.9489 - 2.8770 1.00 3757 220 0.1671 0.1884
REMARK 3 15 2.8770 - 2.8116 1.00 3770 212 0.1711 0.2257
REMARK 3 16 2.8116 - 2.7518 1.00 3714 224 0.1758 0.2046
REMARK 3 17 2.7518 - 2.6967 1.00 3759 220 0.1711 0.2137
REMARK 3 18 2.6967 - 2.6458 1.00 3733 216 0.1674 0.2014
REMARK 3 19 2.6458 - 2.5986 1.00 3786 174 0.1667 0.2045
REMARK 3 20 2.5986 - 2.5546 1.00 3783 180 0.1668 0.2231
REMARK 3 21 2.5546 - 2.5134 1.00 3748 204 0.1702 0.2128
REMARK 3 22 2.5134 - 2.4747 1.00 3743 188 0.1694 0.2040
REMARK 3 23 2.4747 - 2.4383 1.00 3758 195 0.1725 0.2048
REMARK 3 24 2.4383 - 2.4040 1.00 3795 187 0.1712 0.2148
REMARK 3 25 2.4040 - 2.3715 1.00 3709 193 0.1742 0.2133
REMARK 3 26 2.3715 - 2.3407 1.00 3780 191 0.1751 0.1940
REMARK 3 27 2.3407 - 2.3114 1.00 3756 200 0.1822 0.2231
REMARK 3 28 2.3114 - 2.2836 1.00 3728 188 0.1866 0.2252
REMARK 3 29 2.2836 - 2.2570 1.00 3756 178 0.1965 0.2611
REMARK 3 30 2.2570 - 2.2317 0.89 3297 195 0.2002 0.2360
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.380
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.80
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 : 0.004 9908
REMARK 3 ANGLE : 0.701 13430
REMARK 3 CHIRALITY : 0.048 1423
REMARK 3 PLANARITY : 0.005 1763
REMARK 3 DIHEDRAL : 15.221 5820
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 90 THROUGH 213 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.0832 98.6994 -3.8008
REMARK 3 T TENSOR
REMARK 3 T11: 0.3289 T22: 0.3169
REMARK 3 T33: 0.2585 T12: -0.0675
REMARK 3 T13: 0.0258 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 1.6191 L22: 2.7746
REMARK 3 L33: 1.9531 L12: -1.3169
REMARK 3 L13: 1.0558 L23: -1.0654
REMARK 3 S TENSOR
REMARK 3 S11: -0.0358 S12: 0.1674 S13: 0.1841
REMARK 3 S21: -0.0002 S22: 0.0152 S23: -0.1070
REMARK 3 S31: -0.3017 S32: 0.2007 S33: 0.0203
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 214 THROUGH 278 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.4202 92.7623 -6.4589
REMARK 3 T TENSOR
REMARK 3 T11: 0.3185 T22: 0.2938
REMARK 3 T33: 0.3131 T12: -0.0112
REMARK 3 T13: -0.0356 T23: 0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 1.5392 L22: 2.7472
REMARK 3 L33: 2.8449 L12: 0.1623
REMARK 3 L13: -0.0842 L23: -1.2687
REMARK 3 S TENSOR
REMARK 3 S11: 0.0189 S12: 0.0708 S13: 0.0767
REMARK 3 S21: -0.1907 S22: 0.0872 S23: 0.2090
REMARK 3 S31: -0.0011 S32: -0.0698 S33: -0.1099
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 279 THROUGH 303 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.6242 76.8896 3.4371
REMARK 3 T TENSOR
REMARK 3 T11: 0.4115 T22: 0.3225
REMARK 3 T33: 0.3641 T12: 0.0189
REMARK 3 T13: -0.0263 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 4.6474 L22: 2.8746
REMARK 3 L33: 5.2127 L12: 1.3581
REMARK 3 L13: -0.9535 L23: 0.9512
REMARK 3 S TENSOR
REMARK 3 S11: -0.0401 S12: -0.0518 S13: -0.3163
REMARK 3 S21: -0.0288 S22: 0.2157 S23: -0.1724
REMARK 3 S31: 0.4701 S32: 0.3923 S33: -0.0971
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 2 THROUGH 23 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8181 68.6152 -3.0555
REMARK 3 T TENSOR
REMARK 3 T11: 0.3305 T22: 0.3081
REMARK 3 T33: 0.3450 T12: -0.0494
REMARK 3 T13: -0.0059 T23: 0.0726
REMARK 3 L TENSOR
REMARK 3 L11: 4.2906 L22: 5.9349
REMARK 3 L33: 2.2752 L12: -4.2185
REMARK 3 L13: -1.9416 L23: 3.0515
REMARK 3 S TENSOR
REMARK 3 S11: -0.0222 S12: 0.1204 S13: -0.1780
REMARK 3 S21: 0.1304 S22: -0.2245 S23: 0.5700
REMARK 3 S31: 0.0594 S32: -0.2643 S33: 0.1906
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 24 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4694 53.5090 -16.0982
REMARK 3 T TENSOR
REMARK 3 T11: 0.3610 T22: 0.3322
REMARK 3 T33: 0.3125 T12: -0.0306
REMARK 3 T13: -0.0872 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 3.8361 L22: 1.8489
REMARK 3 L33: 1.8960 L12: -0.2106
REMARK 3 L13: -1.5357 L23: 0.1733
REMARK 3 S TENSOR
REMARK 3 S11: 0.1102 S12: 0.2256 S13: -0.1666
REMARK 3 S21: -0.2536 S22: -0.0970 S23: 0.2564
REMARK 3 S31: 0.0942 S32: -0.3053 S33: 0.0631
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 90 THROUGH 188 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.4351 50.5220 -27.7369
REMARK 3 T TENSOR
REMARK 3 T11: 0.4198 T22: 0.3914
REMARK 3 T33: 0.3444 T12: 0.0120
REMARK 3 T13: -0.0567 T23: -0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 2.6007 L22: 0.9685
REMARK 3 L33: 1.6580 L12: -0.8988
REMARK 3 L13: -1.2179 L23: 0.3576
REMARK 3 S TENSOR
REMARK 3 S11: 0.0152 S12: 0.4673 S13: -0.2104
REMARK 3 S21: -0.3150 S22: -0.0982 S23: 0.1939
REMARK 3 S31: 0.0310 S32: -0.3964 S33: -0.0011
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 189 THROUGH 258 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.2365 50.7794 -28.1266
REMARK 3 T TENSOR
REMARK 3 T11: 0.3970 T22: 0.3333
REMARK 3 T33: 0.3423 T12: 0.0031
REMARK 3 T13: 0.0320 T23: 0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 1.8634 L22: 2.3605
REMARK 3 L33: 1.5851 L12: -0.7209
REMARK 3 L13: -0.6495 L23: 0.5108
REMARK 3 S TENSOR
REMARK 3 S11: 0.1243 S12: 0.1472 S13: 0.1384
REMARK 3 S21: -0.2484 S22: -0.1034 S23: -0.1944
REMARK 3 S31: -0.1747 S32: 0.0714 S33: 0.0903
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 259 THROUGH 278 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.9847 63.6430 -22.3872
REMARK 3 T TENSOR
REMARK 3 T11: 0.4511 T22: 0.3287
REMARK 3 T33: 0.4570 T12: -0.0213
REMARK 3 T13: 0.0485 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 1.8157 L22: 3.0565
REMARK 3 L33: 6.3363 L12: -0.7284
REMARK 3 L13: -1.2069 L23: 0.1855
REMARK 3 S TENSOR
REMARK 3 S11: 0.2104 S12: 0.0994 S13: 0.3857
REMARK 3 S21: -0.4973 S22: -0.0011 S23: -0.1080
REMARK 3 S31: -0.6766 S32: 0.0917 S33: -0.0042
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 279 THROUGH 296 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.5160 68.9289 -22.3082
REMARK 3 T TENSOR
REMARK 3 T11: 0.5144 T22: 0.3206
REMARK 3 T33: 0.4680 T12: 0.1046
REMARK 3 T13: 0.0360 T23: 0.0303
REMARK 3 L TENSOR
REMARK 3 L11: 3.7386 L22: 2.6138
REMARK 3 L33: 3.5745 L12: 1.7491
REMARK 3 L13: 1.5538 L23: -0.5168
REMARK 3 S TENSOR
REMARK 3 S11: 0.1301 S12: 0.1959 S13: 0.4725
REMARK 3 S21: -0.2877 S22: -0.1172 S23: 0.1434
REMARK 3 S31: -0.7640 S32: -0.2826 S33: -0.0502
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 23 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.4716 63.5518 -12.7953
REMARK 3 T TENSOR
REMARK 3 T11: 0.3923 T22: 0.2943
REMARK 3 T33: 0.4638 T12: 0.0295
REMARK 3 T13: 0.0487 T23: -0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 7.8571 L22: 5.6702
REMARK 3 L33: 7.2705 L12: 4.8446
REMARK 3 L13: -5.1079 L23: -3.3321
REMARK 3 S TENSOR
REMARK 3 S11: 0.3219 S12: -0.6000 S13: 0.5167
REMARK 3 S21: -0.2055 S22: -0.3534 S23: -0.2811
REMARK 3 S31: -0.4822 S32: 0.6903 S33: -0.0114
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 24 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.1470 52.7014 0.1689
REMARK 3 T TENSOR
REMARK 3 T11: 0.3299 T22: 0.2900
REMARK 3 T33: 0.2762 T12: -0.0313
REMARK 3 T13: -0.0423 T23: 0.0311
REMARK 3 L TENSOR
REMARK 3 L11: 3.4608 L22: 1.8608
REMARK 3 L33: 1.5817 L12: -0.7843
REMARK 3 L13: -0.9759 L23: 0.5020
REMARK 3 S TENSOR
REMARK 3 S11: 0.0154 S12: 0.0061 S13: -0.0855
REMARK 3 S21: 0.0250 S22: -0.0054 S23: 0.1420
REMARK 3 S31: 0.0858 S32: -0.0667 S33: -0.0180
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 90 THROUGH 213 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2026 52.2318 10.9922
REMARK 3 T TENSOR
REMARK 3 T11: 0.2888 T22: 0.3112
REMARK 3 T33: 0.3777 T12: -0.0347
REMARK 3 T13: 0.0291 T23: 0.0571
REMARK 3 L TENSOR
REMARK 3 L11: 2.9020 L22: 2.1040
REMARK 3 L33: 1.5302 L12: -0.4289
REMARK 3 L13: -0.3814 L23: -0.2349
REMARK 3 S TENSOR
REMARK 3 S11: -0.0943 S12: -0.1296 S13: -0.3797
REMARK 3 S21: 0.1328 S22: 0.1192 S23: 0.4702
REMARK 3 S31: 0.2510 S32: -0.2043 S33: -0.0075
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 214 THROUGH 302 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9332 65.7660 11.7339
REMARK 3 T TENSOR
REMARK 3 T11: 0.2543 T22: 0.2612
REMARK 3 T33: 0.3235 T12: -0.0062
REMARK 3 T13: 0.0206 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 2.0211 L22: 2.6195
REMARK 3 L33: 2.3283 L12: -0.1073
REMARK 3 L13: -0.0000 L23: -0.7523
REMARK 3 S TENSOR
REMARK 3 S11: -0.0496 S12: -0.1299 S13: -0.0591
REMARK 3 S21: 0.2332 S22: 0.0922 S23: 0.2234
REMARK 3 S31: -0.0866 S32: -0.1356 S33: -0.1192
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 23 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.2751 87.8153 9.2571
REMARK 3 T TENSOR
REMARK 3 T11: 0.3622 T22: 0.3768
REMARK 3 T33: 0.3895 T12: 0.0682
REMARK 3 T13: 0.0483 T23: 0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 5.7903 L22: 3.1110
REMARK 3 L33: 5.7659 L12: 3.6452
REMARK 3 L13: 4.1475 L23: 2.5255
REMARK 3 S TENSOR
REMARK 3 S11: 0.0900 S12: -0.3969 S13: 0.0556
REMARK 3 S21: 0.1290 S22: -0.1027 S23: 0.2084
REMARK 3 S31: -0.1002 S32: -0.5230 S33: 0.0362
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 24 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.6555 94.2927 24.7382
REMARK 3 T TENSOR
REMARK 3 T11: 0.4307 T22: 0.3606
REMARK 3 T33: 0.2670 T12: -0.0203
REMARK 3 T13: 0.0169 T23: -0.0719
REMARK 3 L TENSOR
REMARK 3 L11: 4.3999 L22: 1.8936
REMARK 3 L33: 2.4276 L12: -0.5698
REMARK 3 L13: 1.8440 L23: -0.7476
REMARK 3 S TENSOR
REMARK 3 S11: -0.0476 S12: -0.2301 S13: 0.3828
REMARK 3 S21: 0.2570 S22: 0.0800 S23: 0.0119
REMARK 3 S31: -0.2758 S32: -0.0293 S33: -0.0401
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 90 THROUGH 213 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.9886 91.6698 37.7438
REMARK 3 T TENSOR
REMARK 3 T11: 0.6069 T22: 0.5279
REMARK 3 T33: 0.3524 T12: -0.0308
REMARK 3 T13: -0.0242 T23: -0.1152
REMARK 3 L TENSOR
REMARK 3 L11: 3.8923 L22: 1.0014
REMARK 3 L33: 2.1250 L12: -0.0491
REMARK 3 L13: 2.0127 L23: -0.2930
REMARK 3 S TENSOR
REMARK 3 S11: -0.0526 S12: -0.3461 S13: 0.1819
REMARK 3 S21: 0.3599 S22: 0.0627 S23: -0.1289
REMARK 3 S31: -0.3257 S32: -0.0582 S33: -0.0074
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 214 THROUGH 238 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.2491 84.1206 45.0928
REMARK 3 T TENSOR
REMARK 3 T11: 0.5897 T22: 0.5369
REMARK 3 T33: 0.3324 T12: -0.0241
REMARK 3 T13: -0.0641 T23: -0.0364
REMARK 3 L TENSOR
REMARK 3 L11: 4.1821 L22: 3.3268
REMARK 3 L33: 4.1321 L12: 2.0881
REMARK 3 L13: 3.4014 L23: 2.3900
REMARK 3 S TENSOR
REMARK 3 S11: -0.0265 S12: -0.5580 S13: 0.2081
REMARK 3 S21: 0.1233 S22: -0.0299 S23: 0.0205
REMARK 3 S31: -0.1639 S32: -0.3686 S33: 0.0638
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 239 THROUGH 278 )
REMARK 3 ORIGIN FOR THE GROUP (A): 49.1377 74.3906 36.8986
REMARK 3 T TENSOR
REMARK 3 T11: 0.5328 T22: 0.4687
REMARK 3 T33: 0.3725 T12: -0.0201
REMARK 3 T13: -0.1371 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 3.5703 L22: 3.8591
REMARK 3 L33: 5.8684 L12: 0.9306
REMARK 3 L13: -0.6814 L23: 0.7057
REMARK 3 S TENSOR
REMARK 3 S11: 0.0896 S12: -0.3418 S13: -0.2830
REMARK 3 S21: 0.5533 S22: 0.0100 S23: -0.2124
REMARK 3 S31: 0.4054 S32: 0.0634 S33: -0.1102
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 279 THROUGH 296 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.1284 76.7277 31.2965
REMARK 3 T TENSOR
REMARK 3 T11: 0.4691 T22: 0.5629
REMARK 3 T33: 0.4117 T12: -0.1170
REMARK 3 T13: -0.0432 T23: 0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 3.5103 L22: 7.1893
REMARK 3 L33: 7.5597 L12: -4.0383
REMARK 3 L13: -4.9209 L23: 4.3442
REMARK 3 S TENSOR
REMARK 3 S11: 0.0612 S12: 0.1111 S13: -0.4999
REMARK 3 S21: 0.1451 S22: -0.0681 S23: 0.4369
REMARK 3 S31: 0.0552 S32: -0.4252 S33: -0.0262
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 2 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.9518 86.9347 13.0329
REMARK 3 T TENSOR
REMARK 3 T11: 0.3435 T22: 0.3816
REMARK 3 T33: 0.3319 T12: -0.0585
REMARK 3 T13: 0.0029 T23: -0.0433
REMARK 3 L TENSOR
REMARK 3 L11: 1.6088 L22: 2.1408
REMARK 3 L33: 3.2339 L12: -0.8523
REMARK 3 L13: 1.2933 L23: -1.2092
REMARK 3 S TENSOR
REMARK 3 S11: 0.0569 S12: 0.0998 S13: 0.0690
REMARK 3 S21: 0.1444 S22: -0.0521 S23: -0.1697
REMARK 3 S31: 0.0198 S32: 0.2611 S33: 0.0163
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 6NKF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1000238900.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-OCT-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 119411
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.230
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.900
REMARK 200 R MERGE (I) : 0.14500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.10
REMARK 200 R MERGE FOR SHELL (I) : 0.99000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000, MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM THIOCYANATE PH 6.9, 20 %
REMARK 280 (W/V) PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 97.74600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 78.92800
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 78.92800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 146.61900
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 78.92800
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 78.92800
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 48.87300
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 78.92800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 78.92800
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 146.61900
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 78.92800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 78.92800
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 48.87300
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 97.74600
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: 8310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 MSE A 1
REMARK 465 HIS A 303
REMARK 465 HIS A 304
REMARK 465 MSE B 1
REMARK 465 LYS B 297
REMARK 465 ALA B 298
REMARK 465 HIS B 299
REMARK 465 HIS B 300
REMARK 465 HIS B 301
REMARK 465 HIS B 302
REMARK 465 HIS B 303
REMARK 465 HIS B 304
REMARK 465 MSE C 1
REMARK 465 ALA C 298
REMARK 465 HIS C 304
REMARK 465 MSE D 1
REMARK 465 LYS D 297
REMARK 465 ALA D 298
REMARK 465 HIS D 299
REMARK 465 HIS D 300
REMARK 465 HIS D 301
REMARK 465 HIS D 302
REMARK 465 HIS D 303
REMARK 465 HIS D 304
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 30 -127.33 57.35
REMARK 500 CYS A 67 17.06 -166.56
REMARK 500 SER A 140 -122.86 53.60
REMARK 500 PHE A 178 50.33 36.41
REMARK 500 GLU B 30 -118.99 52.16
REMARK 500 CYS B 67 18.21 -168.13
REMARK 500 SER B 140 -125.18 56.71
REMARK 500 PHE B 178 52.88 32.77
REMARK 500 GLU C 30 -117.71 64.35
REMARK 500 CYS C 67 19.14 -163.18
REMARK 500 SER C 140 -126.65 54.40
REMARK 500 PHE C 178 53.48 37.01
REMARK 500 GLU D 30 -117.20 38.15
REMARK 500 CYS D 67 17.06 -165.90
REMARK 500 SER D 140 -115.47 41.25
REMARK 500 PHE D 178 53.17 36.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SBT A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 406
DBREF 6NKF A 1 304 PDB 6NKF 6NKF 1 304
DBREF 6NKF B 1 304 PDB 6NKF 6NKF 1 304
DBREF 6NKF C 1 304 PDB 6NKF 6NKF 1 304
DBREF 6NKF D 1 304 PDB 6NKF 6NKF 1 304
SEQRES 1 A 304 MSE THR ASN HIS ILE LYS GLU ILE ASN TRP GLU GLN ASN
SEQRES 2 A 304 THR ASN SER TYR ILE GLN LEU ILE PRO ASN ILE GLU TYR
SEQRES 3 A 304 THR LYS VAL GLU ASP THR SER LEU THR LEU HIS LEU LEU
SEQRES 4 A 304 VAL TYR ARG ASN PRO MSE ASP ALA LEU PHE ASN ARG LYS
SEQRES 5 A 304 GLY ASN GLN GLU THR TYR PRO LEU ILE ILE TYR LEU GLN
SEQRES 6 A 304 GLY CYS GLY TRP GLY TRP THR LYS GLN ASP THR SER ALA
SEQRES 7 A 304 PHE ILE PRO GLN LEU VAL PRO PHE VAL GLU GLN GLY TYR
SEQRES 8 A 304 VAL VAL ALA SER VAL GLN TYR ARG GLY SER GLY GLU ALA
SEQRES 9 A 304 VAL PHE PRO ALA GLN LEU HIS ASP VAL LYS THR ALA VAL
SEQRES 10 A 304 ARG PHE LEU LYS ALA ASN ALA ALA ARG TYR ASN ILE ASP
SEQRES 11 A 304 PRO ASP ARG VAL GLY VAL TRP GLY ASP SER SER GLY GLY
SEQRES 12 A 304 HIS LEU ALA LEU LEU LEU GLY LEU THR GLU GLY ILE GLU
SEQRES 13 A 304 GLU PHE GLU GLY PRO ASP GLU TYR ARG HIS VAL SER SER
SEQRES 14 A 304 LYS VAL ASP ALA VAL ALA ASP TRP PHE GLY PRO VAL ASP
SEQRES 15 A 304 LEU LEU SER MSE SER LYS TYR PRO SER ILE PHE ASP HIS
SEQRES 16 A 304 ASP SER PRO ASN SER PRO GLU SER LYS LEU ILE GLY GLY
SEQRES 17 A 304 ALA VAL GLN GLU ASN ARG VAL GLN ALA LYS GLN ALA SER
SEQRES 18 A 304 PRO ILE SER TYR VAL HIS ARG GLU ALA PRO PRO ILE LEU
SEQRES 19 A 304 ILE MSE HIS GLY ASP GLN ASP ASP VAL VAL PRO TYR GLN
SEQRES 20 A 304 GLN SER VAL GLN LEU PHE GLU ALA LEU ILE LYS GLU GLY
SEQRES 21 A 304 HIS ASP ALA LEU MSE TYR LYS ILE ASN GLY ALA GLY HIS
SEQRES 22 A 304 ASN GLY PHE THR GLN ALA HIS THR LEU ASP ILE VAL LYS
SEQRES 23 A 304 SER PHE PHE ARG LYS HIS LEU LYS PRO GLY LYS ALA HIS
SEQRES 24 A 304 HIS HIS HIS HIS HIS
SEQRES 1 B 304 MSE THR ASN HIS ILE LYS GLU ILE ASN TRP GLU GLN ASN
SEQRES 2 B 304 THR ASN SER TYR ILE GLN LEU ILE PRO ASN ILE GLU TYR
SEQRES 3 B 304 THR LYS VAL GLU ASP THR SER LEU THR LEU HIS LEU LEU
SEQRES 4 B 304 VAL TYR ARG ASN PRO MSE ASP ALA LEU PHE ASN ARG LYS
SEQRES 5 B 304 GLY ASN GLN GLU THR TYR PRO LEU ILE ILE TYR LEU GLN
SEQRES 6 B 304 GLY CYS GLY TRP GLY TRP THR LYS GLN ASP THR SER ALA
SEQRES 7 B 304 PHE ILE PRO GLN LEU VAL PRO PHE VAL GLU GLN GLY TYR
SEQRES 8 B 304 VAL VAL ALA SER VAL GLN TYR ARG GLY SER GLY GLU ALA
SEQRES 9 B 304 VAL PHE PRO ALA GLN LEU HIS ASP VAL LYS THR ALA VAL
SEQRES 10 B 304 ARG PHE LEU LYS ALA ASN ALA ALA ARG TYR ASN ILE ASP
SEQRES 11 B 304 PRO ASP ARG VAL GLY VAL TRP GLY ASP SER SER GLY GLY
SEQRES 12 B 304 HIS LEU ALA LEU LEU LEU GLY LEU THR GLU GLY ILE GLU
SEQRES 13 B 304 GLU PHE GLU GLY PRO ASP GLU TYR ARG HIS VAL SER SER
SEQRES 14 B 304 LYS VAL ASP ALA VAL ALA ASP TRP PHE GLY PRO VAL ASP
SEQRES 15 B 304 LEU LEU SER MSE SER LYS TYR PRO SER ILE PHE ASP HIS
SEQRES 16 B 304 ASP SER PRO ASN SER PRO GLU SER LYS LEU ILE GLY GLY
SEQRES 17 B 304 ALA VAL GLN GLU ASN ARG VAL GLN ALA LYS GLN ALA SER
SEQRES 18 B 304 PRO ILE SER TYR VAL HIS ARG GLU ALA PRO PRO ILE LEU
SEQRES 19 B 304 ILE MSE HIS GLY ASP GLN ASP ASP VAL VAL PRO TYR GLN
SEQRES 20 B 304 GLN SER VAL GLN LEU PHE GLU ALA LEU ILE LYS GLU GLY
SEQRES 21 B 304 HIS ASP ALA LEU MSE TYR LYS ILE ASN GLY ALA GLY HIS
SEQRES 22 B 304 ASN GLY PHE THR GLN ALA HIS THR LEU ASP ILE VAL LYS
SEQRES 23 B 304 SER PHE PHE ARG LYS HIS LEU LYS PRO GLY LYS ALA HIS
SEQRES 24 B 304 HIS HIS HIS HIS HIS
SEQRES 1 C 304 MSE THR ASN HIS ILE LYS GLU ILE ASN TRP GLU GLN ASN
SEQRES 2 C 304 THR ASN SER TYR ILE GLN LEU ILE PRO ASN ILE GLU TYR
SEQRES 3 C 304 THR LYS VAL GLU ASP THR SER LEU THR LEU HIS LEU LEU
SEQRES 4 C 304 VAL TYR ARG ASN PRO MSE ASP ALA LEU PHE ASN ARG LYS
SEQRES 5 C 304 GLY ASN GLN GLU THR TYR PRO LEU ILE ILE TYR LEU GLN
SEQRES 6 C 304 GLY CYS GLY TRP GLY TRP THR LYS GLN ASP THR SER ALA
SEQRES 7 C 304 PHE ILE PRO GLN LEU VAL PRO PHE VAL GLU GLN GLY TYR
SEQRES 8 C 304 VAL VAL ALA SER VAL GLN TYR ARG GLY SER GLY GLU ALA
SEQRES 9 C 304 VAL PHE PRO ALA GLN LEU HIS ASP VAL LYS THR ALA VAL
SEQRES 10 C 304 ARG PHE LEU LYS ALA ASN ALA ALA ARG TYR ASN ILE ASP
SEQRES 11 C 304 PRO ASP ARG VAL GLY VAL TRP GLY ASP SER SER GLY GLY
SEQRES 12 C 304 HIS LEU ALA LEU LEU LEU GLY LEU THR GLU GLY ILE GLU
SEQRES 13 C 304 GLU PHE GLU GLY PRO ASP GLU TYR ARG HIS VAL SER SER
SEQRES 14 C 304 LYS VAL ASP ALA VAL ALA ASP TRP PHE GLY PRO VAL ASP
SEQRES 15 C 304 LEU LEU SER MSE SER LYS TYR PRO SER ILE PHE ASP HIS
SEQRES 16 C 304 ASP SER PRO ASN SER PRO GLU SER LYS LEU ILE GLY GLY
SEQRES 17 C 304 ALA VAL GLN GLU ASN ARG VAL GLN ALA LYS GLN ALA SER
SEQRES 18 C 304 PRO ILE SER TYR VAL HIS ARG GLU ALA PRO PRO ILE LEU
SEQRES 19 C 304 ILE MSE HIS GLY ASP GLN ASP ASP VAL VAL PRO TYR GLN
SEQRES 20 C 304 GLN SER VAL GLN LEU PHE GLU ALA LEU ILE LYS GLU GLY
SEQRES 21 C 304 HIS ASP ALA LEU MSE TYR LYS ILE ASN GLY ALA GLY HIS
SEQRES 22 C 304 ASN GLY PHE THR GLN ALA HIS THR LEU ASP ILE VAL LYS
SEQRES 23 C 304 SER PHE PHE ARG LYS HIS LEU LYS PRO GLY LYS ALA HIS
SEQRES 24 C 304 HIS HIS HIS HIS HIS
SEQRES 1 D 304 MSE THR ASN HIS ILE LYS GLU ILE ASN TRP GLU GLN ASN
SEQRES 2 D 304 THR ASN SER TYR ILE GLN LEU ILE PRO ASN ILE GLU TYR
SEQRES 3 D 304 THR LYS VAL GLU ASP THR SER LEU THR LEU HIS LEU LEU
SEQRES 4 D 304 VAL TYR ARG ASN PRO MSE ASP ALA LEU PHE ASN ARG LYS
SEQRES 5 D 304 GLY ASN GLN GLU THR TYR PRO LEU ILE ILE TYR LEU GLN
SEQRES 6 D 304 GLY CYS GLY TRP GLY TRP THR LYS GLN ASP THR SER ALA
SEQRES 7 D 304 PHE ILE PRO GLN LEU VAL PRO PHE VAL GLU GLN GLY TYR
SEQRES 8 D 304 VAL VAL ALA SER VAL GLN TYR ARG GLY SER GLY GLU ALA
SEQRES 9 D 304 VAL PHE PRO ALA GLN LEU HIS ASP VAL LYS THR ALA VAL
SEQRES 10 D 304 ARG PHE LEU LYS ALA ASN ALA ALA ARG TYR ASN ILE ASP
SEQRES 11 D 304 PRO ASP ARG VAL GLY VAL TRP GLY ASP SER SER GLY GLY
SEQRES 12 D 304 HIS LEU ALA LEU LEU LEU GLY LEU THR GLU GLY ILE GLU
SEQRES 13 D 304 GLU PHE GLU GLY PRO ASP GLU TYR ARG HIS VAL SER SER
SEQRES 14 D 304 LYS VAL ASP ALA VAL ALA ASP TRP PHE GLY PRO VAL ASP
SEQRES 15 D 304 LEU LEU SER MSE SER LYS TYR PRO SER ILE PHE ASP HIS
SEQRES 16 D 304 ASP SER PRO ASN SER PRO GLU SER LYS LEU ILE GLY GLY
SEQRES 17 D 304 ALA VAL GLN GLU ASN ARG VAL GLN ALA LYS GLN ALA SER
SEQRES 18 D 304 PRO ILE SER TYR VAL HIS ARG GLU ALA PRO PRO ILE LEU
SEQRES 19 D 304 ILE MSE HIS GLY ASP GLN ASP ASP VAL VAL PRO TYR GLN
SEQRES 20 D 304 GLN SER VAL GLN LEU PHE GLU ALA LEU ILE LYS GLU GLY
SEQRES 21 D 304 HIS ASP ALA LEU MSE TYR LYS ILE ASN GLY ALA GLY HIS
SEQRES 22 D 304 ASN GLY PHE THR GLN ALA HIS THR LEU ASP ILE VAL LYS
SEQRES 23 D 304 SER PHE PHE ARG LYS HIS LEU LYS PRO GLY LYS ALA HIS
SEQRES 24 D 304 HIS HIS HIS HIS HIS
HET MSE A 45 8
HET MSE A 186 8
HET MSE A 236 8
HET MSE A 265 8
HET MSE B 45 8
HET MSE B 186 8
HET MSE B 236 8
HET MSE B 265 8
HET MSE C 45 8
HET MSE C 186 8
HET MSE C 236 8
HET MSE C 265 8
HET MSE D 45 8
HET MSE D 186 8
HET MSE D 236 8
HET MSE D 265 8
HET EDO A 401 4
HET PEG A 402 7
HET EDO A 403 4
HET EDO A 404 4
HET EDO A 405 4
HET EDO A 406 4
HET EDO A 407 4
HET SBT A 408 5
HET PEG B 401 7
HET EDO B 402 4
HET EDO B 403 4
HET EDO B 404 4
HET EDO B 405 4
HET EDO B 406 4
HET PEG C 401 7
HET EDO C 402 4
HET EDO C 403 4
HET EDO C 404 4
HET EDO C 405 4
HET EDO C 406 4
HET EDO D 401 4
HET EDO D 402 4
HET EDO D 403 4
HET EDO D 404 4
HET EDO D 405 4
HET EDO D 406 4
HETNAM MSE SELENOMETHIONINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM SBT 2-BUTANOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 16(C5 H11 N O2 SE)
FORMUL 5 EDO 22(C2 H6 O2)
FORMUL 6 PEG 3(C4 H10 O3)
FORMUL 12 SBT C4 H10 O
FORMUL 31 HOH *674(H2 O)
HELIX 1 AA1 ASN A 43 PHE A 49 1 7
HELIX 2 AA2 PHE A 79 GLN A 89 1 11
HELIX 3 AA3 PRO A 107 ASN A 123 1 17
HELIX 4 AA4 ALA A 124 TYR A 127 5 4
HELIX 5 AA5 SER A 140 THR A 152 1 13
HELIX 6 AA6 ILE A 155 GLU A 159 5 5
HELIX 7 AA7 SER A 185 TYR A 189 5 5
HELIX 8 AA8 SER A 200 GLY A 207 1 8
HELIX 9 AA9 ALA A 209 GLU A 212 5 4
HELIX 10 AB1 ASN A 213 ALA A 220 1 8
HELIX 11 AB2 SER A 221 VAL A 226 5 6
HELIX 12 AB3 PRO A 245 GLU A 259 1 15
HELIX 13 AB4 GLN A 278 LYS A 294 1 17
HELIX 14 AB5 ASN B 43 PHE B 49 1 7
HELIX 15 AB6 PHE B 79 GLN B 89 1 11
HELIX 16 AB7 PRO B 107 ASN B 123 1 17
HELIX 17 AB8 ALA B 124 TYR B 127 5 4
HELIX 18 AB9 SER B 140 THR B 152 1 13
HELIX 19 AC1 ILE B 155 GLU B 159 5 5
HELIX 20 AC2 ASP B 182 TYR B 189 5 8
HELIX 21 AC3 SER B 200 GLY B 207 1 8
HELIX 22 AC4 ALA B 209 GLU B 212 5 4
HELIX 23 AC5 ASN B 213 ALA B 220 1 8
HELIX 24 AC6 SER B 221 VAL B 226 5 6
HELIX 25 AC7 PRO B 245 GLU B 259 1 15
HELIX 26 AC8 GLN B 278 LYS B 294 1 17
HELIX 27 AC9 ASN C 43 PHE C 49 1 7
HELIX 28 AD1 PHE C 79 GLN C 89 1 11
HELIX 29 AD2 PRO C 107 ASN C 123 1 17
HELIX 30 AD3 ALA C 124 TYR C 127 5 4
HELIX 31 AD4 SER C 140 THR C 152 1 13
HELIX 32 AD5 ILE C 155 GLU C 159 5 5
HELIX 33 AD6 ASP C 182 TYR C 189 5 8
HELIX 34 AD7 SER C 200 GLY C 207 1 8
HELIX 35 AD8 ALA C 209 GLU C 212 5 4
HELIX 36 AD9 ASN C 213 ALA C 220 1 8
HELIX 37 AE1 SER C 221 VAL C 226 5 6
HELIX 38 AE2 PRO C 245 GLU C 259 1 15
HELIX 39 AE3 GLN C 278 LYS C 294 1 17
HELIX 40 AE4 ASN D 43 PHE D 49 1 7
HELIX 41 AE5 PHE D 79 GLN D 89 1 11
HELIX 42 AE6 PRO D 107 ASN D 123 1 17
HELIX 43 AE7 ALA D 124 TYR D 127 5 4
HELIX 44 AE8 SER D 140 THR D 152 1 13
HELIX 45 AE9 ILE D 155 GLU D 159 5 5
HELIX 46 AF1 SER D 185 TYR D 189 5 5
HELIX 47 AF2 SER D 200 GLY D 207 1 8
HELIX 48 AF3 ALA D 209 GLU D 212 5 4
HELIX 49 AF4 ASN D 213 ALA D 220 1 8
HELIX 50 AF5 SER D 221 VAL D 226 5 6
HELIX 51 AF6 PRO D 245 GLU D 259 1 15
HELIX 52 AF7 GLN D 278 LYS D 294 1 17
SHEET 1 AA1 9 LYS A 6 ASN A 9 0
SHEET 2 AA1 9 ALA D 263 ASN D 269 1 O LYS D 267 N LYS A 6
SHEET 3 AA1 9 ILE D 233 GLY D 238 1 N ILE D 235 O LEU D 264
SHEET 4 AA1 9 ALA D 173 TRP D 177 1 N ASP D 176 O LEU D 234
SHEET 5 AA1 9 ILE D 129 ASP D 139 1 N GLY D 138 O TRP D 177
SHEET 6 AA1 9 TYR D 58 LEU D 64 1 N LEU D 60 O GLY D 135
SHEET 7 AA1 9 VAL D 92 VAL D 96 1 O ALA D 94 N TYR D 63
SHEET 8 AA1 9 THR D 32 TYR D 41 -1 N LEU D 39 O VAL D 93
SHEET 9 AA1 9 ILE D 18 VAL D 29 -1 N ILE D 21 O LEU D 38
SHEET 1 AA2 9 ILE A 18 VAL A 29 0
SHEET 2 AA2 9 THR A 32 TYR A 41 -1 O LEU A 38 N ILE A 21
SHEET 3 AA2 9 VAL A 92 VAL A 96 -1 O VAL A 93 N LEU A 39
SHEET 4 AA2 9 TYR A 58 LEU A 64 1 N TYR A 63 O ALA A 94
SHEET 5 AA2 9 ILE A 129 ASP A 139 1 O GLY A 135 N LEU A 60
SHEET 6 AA2 9 ALA A 173 TRP A 177 1 O ALA A 175 N VAL A 136
SHEET 7 AA2 9 ILE A 233 GLY A 238 1 O LEU A 234 N VAL A 174
SHEET 8 AA2 9 ALA A 263 ILE A 268 1 O TYR A 266 N ILE A 235
SHEET 9 AA2 9 LYS D 6 ILE D 8 1 O LYS D 6 N LYS A 267
SHEET 1 AA3 9 LYS B 6 ILE B 8 0
SHEET 2 AA3 9 ALA C 263 ILE C 268 1 O LYS C 267 N LYS B 6
SHEET 3 AA3 9 ILE C 233 GLY C 238 1 N ILE C 235 O LEU C 264
SHEET 4 AA3 9 ALA C 173 TRP C 177 1 N ASP C 176 O LEU C 234
SHEET 5 AA3 9 ILE C 129 ASP C 139 1 N GLY C 138 O TRP C 177
SHEET 6 AA3 9 TYR C 58 LEU C 64 1 N LEU C 60 O GLY C 135
SHEET 7 AA3 9 VAL C 92 VAL C 96 1 O ALA C 94 N TYR C 63
SHEET 8 AA3 9 THR C 32 TYR C 41 -1 N LEU C 39 O VAL C 93
SHEET 9 AA3 9 ILE C 18 VAL C 29 -1 N ILE C 21 O LEU C 38
SHEET 1 AA4 9 ILE B 18 VAL B 29 0
SHEET 2 AA4 9 THR B 32 TYR B 41 -1 O LEU B 38 N ILE B 21
SHEET 3 AA4 9 VAL B 92 VAL B 96 -1 O VAL B 93 N LEU B 39
SHEET 4 AA4 9 TYR B 58 LEU B 64 1 N TYR B 63 O ALA B 94
SHEET 5 AA4 9 ILE B 129 ASP B 139 1 O GLY B 135 N LEU B 60
SHEET 6 AA4 9 ALA B 173 TRP B 177 1 O TRP B 177 N GLY B 138
SHEET 7 AA4 9 ILE B 233 GLY B 238 1 O LEU B 234 N ASP B 176
SHEET 8 AA4 9 ALA B 263 ASN B 269 1 O LEU B 264 N ILE B 235
SHEET 9 AA4 9 LYS C 6 ASN C 9 1 O LYS C 6 N LYS B 267
LINK C PRO A 44 N MSE A 45 1555 1555 1.33
LINK C MSE A 45 N ASP A 46 1555 1555 1.34
LINK C SER A 185 N MSE A 186 1555 1555 1.34
LINK C MSE A 186 N SER A 187 1555 1555 1.33
LINK C ILE A 235 N MSE A 236 1555 1555 1.33
LINK C MSE A 236 N HIS A 237 1555 1555 1.33
LINK C LEU A 264 N MSE A 265 1555 1555 1.33
LINK C MSE A 265 N TYR A 266 1555 1555 1.33
LINK C PRO B 44 N MSE B 45 1555 1555 1.33
LINK C MSE B 45 N ASP B 46 1555 1555 1.34
LINK C SER B 185 N MSE B 186 1555 1555 1.33
LINK C MSE B 186 N SER B 187 1555 1555 1.33
LINK C ILE B 235 N MSE B 236 1555 1555 1.33
LINK C MSE B 236 N HIS B 237 1555 1555 1.33
LINK C LEU B 264 N MSE B 265 1555 1555 1.33
LINK C MSE B 265 N TYR B 266 1555 1555 1.33
LINK C PRO C 44 N MSE C 45 1555 1555 1.33
LINK C MSE C 45 N ASP C 46 1555 1555 1.34
LINK C SER C 185 N MSE C 186 1555 1555 1.33
LINK C MSE C 186 N SER C 187 1555 1555 1.33
LINK C ILE C 235 N MSE C 236 1555 1555 1.33
LINK C MSE C 236 N HIS C 237 1555 1555 1.33
LINK C LEU C 264 N MSE C 265 1555 1555 1.33
LINK C MSE C 265 N TYR C 266 1555 1555 1.33
LINK C PRO D 44 N MSE D 45 1555 1555 1.33
LINK C MSE D 45 N ASP D 46 1555 1555 1.34
LINK C SER D 185 N MSE D 186 1555 1555 1.33
LINK C MSE D 186 N SER D 187 1555 1555 1.33
LINK C ILE D 235 N MSE D 236 1555 1555 1.33
LINK C MSE D 236 N HIS D 237 1555 1555 1.33
LINK C LEU D 264 N MSE D 265 1555 1555 1.33
LINK C MSE D 265 N TYR D 266 1555 1555 1.33
CISPEP 1 PHE A 106 PRO A 107 0 8.57
CISPEP 2 PHE B 106 PRO B 107 0 7.66
CISPEP 3 PHE C 106 PRO C 107 0 9.50
CISPEP 4 PHE D 106 PRO D 107 0 9.01
SITE 1 AC1 5 ARG A 51 LYS A 52 GLN A 55 EDO A 406
SITE 2 AC1 5 HOH A 564
SITE 1 AC2 1 EDO A 403
SITE 1 AC3 5 PHE A 193 ASP A 194 ASN A 199 SER A 200
SITE 2 AC3 5 PEG A 402
SITE 1 AC4 8 GLY A 68 TRP A 69 SER A 140 PRO A 180
SITE 2 AC4 8 PRO A 201 GLU A 202 EDO A 405 HOH A 504
SITE 1 AC5 7 GLY A 66 CYS A 67 SER A 140 HIS A 273
SITE 2 AC5 7 EDO A 404 HOH A 504 HOH A 514
SITE 1 AC6 6 ARG A 51 GLN A 55 EDO A 401 ILE D 192
SITE 2 AC6 6 ASP D 242 VAL D 243
SITE 1 AC7 2 GLU A 25 PHE A 119
SITE 1 AC8 8 PRO A 22 HIS A 37 SER A 77 HOH A 501
SITE 2 AC8 8 PRO D 22 HIS D 37 SER D 77 ILE D 80
SITE 1 AC9 1 PHE B 193
SITE 1 AD1 7 TRP B 69 SER B 140 SER B 141 PRO B 180
SITE 2 AD1 7 PRO B 201 GLU B 202 EDO B 403
SITE 1 AD2 7 GLY B 66 CYS B 67 SER B 140 HIS B 273
SITE 2 AD2 7 EDO B 402 HOH B 506 HOH B 513
SITE 1 AD3 8 ASN A 269 GLU B 7 ILE B 8 ASN B 9
SITE 2 AD3 8 ASN C 269 GLU D 7 ILE D 8 ASN D 9
SITE 1 AD4 5 PRO B 22 HIS B 37 SER B 77 ILE B 80
SITE 2 AD4 5 SER C 77
SITE 1 AD5 4 TRP B 10 ASN B 43 HOH B 543 HOH B 563
SITE 1 AD6 2 PHE B 49 EDO C 402
SITE 1 AD7 5 PHE C 193 ASP C 194 ASN C 199 SER C 200
SITE 2 AD7 5 PEG C 401
SITE 1 AD8 4 GLN C 55 ALA C 125 ASN C 128 HOH C 582
SITE 1 AD9 7 GLY C 68 TRP C 69 SER C 140 SER C 141
SITE 2 AD9 7 HIS C 195 GLU C 202 EDO C 405
SITE 1 AE1 6 GLY C 66 CYS C 67 ASP C 139 SER C 140
SITE 2 AE1 6 HIS C 273 EDO C 404
SITE 1 AE2 3 HIS C 227 GLU C 259 HOH C 648
SITE 1 AE3 5 PRO D 180 HIS D 195 PRO D 201 GLU D 202
SITE 2 AE3 5 HOH D 546
SITE 1 AE4 3 GLN D 55 ALA D 125 HOH D 617
SITE 1 AE5 7 GLY D 66 CYS D 67 GLY D 68 SER D 140
SITE 2 AE5 7 HIS D 273 HOH D 524 HOH D 546
SITE 1 AE6 7 PRO A 131 HOH A 506 PHE D 193 ASP D 194
SITE 2 AE6 7 SER D 197 SER D 200 EDO D 405
SITE 1 AE7 7 LYS A 121 HOH A 620 TRP D 71 ASN D 199
SITE 2 AE7 7 LYS D 204 EDO D 404 HOH D 571
SITE 1 AE8 4 ARG A 126 HOH A 590 TRP D 71 THR D 72
CRYST1 157.856 157.856 195.492 90.00 90.00 90.00 P 43 21 2 32
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006335 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006335 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005115 0.00000
TER 2426 HIS A 302
TER 4764 GLY B 296
TER 7196 HIS C 303
TER 9554 GLY D 296
MASTER 718 0 42 52 36 0 43 610249 4 274 96
END |