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HEADER HYDROLASE 07-JAN-19 6NKC
TITLE CRYSTAL STRUCTURE OF THE LIPASE LIP_VUT1 FROM GOAT RUMEN METAGENOME.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE, LIP_VUT1;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 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 6NKC 0
JRNL AUTH Y.KIM,L.WELK,R.JEDRZEJCZAK,A.FETO,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF THE LIPASE LIP_VUT1 FROM GOAT RUMEN
JRNL TITL 2 METAGENOME.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.63 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) : 1.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.26
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 42819
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.710
REMARK 3 FREE R VALUE TEST SET COUNT : 2017
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 35.2716 - 3.9289 1.00 2969 123 0.1402 0.1431
REMARK 3 2 3.9289 - 3.1191 1.00 2892 163 0.1442 0.1716
REMARK 3 3 3.1191 - 2.7250 1.00 2937 138 0.1609 0.1964
REMARK 3 4 2.7250 - 2.4759 1.00 2932 145 0.1574 0.2368
REMARK 3 5 2.4759 - 2.2985 1.00 2949 133 0.1545 0.1847
REMARK 3 6 2.2985 - 2.1630 1.00 2863 156 0.1467 0.1719
REMARK 3 7 2.1630 - 2.0547 1.00 2900 186 0.1536 0.1971
REMARK 3 8 2.0547 - 1.9652 1.00 2925 132 0.1567 0.1832
REMARK 3 9 1.9652 - 1.8896 1.00 2912 130 0.1624 0.2003
REMARK 3 10 1.8896 - 1.8244 1.00 2947 127 0.1759 0.2203
REMARK 3 11 1.8244 - 1.7673 1.00 2880 154 0.1898 0.2238
REMARK 3 12 1.7673 - 1.7168 1.00 2893 136 0.2027 0.2140
REMARK 3 13 1.7168 - 1.6716 1.00 2935 138 0.2165 0.2883
REMARK 3 14 1.6716 - 1.6308 0.98 2868 156 0.2408 0.2443
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.080
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.20
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 : 0.010 2634
REMARK 3 ANGLE : 1.018 3572
REMARK 3 CHIRALITY : 0.069 418
REMARK 3 PLANARITY : 0.006 458
REMARK 3 DIHEDRAL : 13.751 927
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 15 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.5402 10.3005 139.1534
REMARK 3 T TENSOR
REMARK 3 T11: 0.1862 T22: 0.1774
REMARK 3 T33: 0.1762 T12: -0.0164
REMARK 3 T13: -0.0021 T23: 0.0187
REMARK 3 L TENSOR
REMARK 3 L11: 3.9135 L22: 1.6831
REMARK 3 L33: 5.8978 L12: -0.1621
REMARK 3 L13: 1.8910 L23: 0.1133
REMARK 3 S TENSOR
REMARK 3 S11: 0.4300 S12: 0.0169 S13: -0.3273
REMARK 3 S21: 0.1363 S22: -0.1187 S23: -0.2003
REMARK 3 S31: 0.7186 S32: -0.2558 S33: -0.2955
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 16 THROUGH 47 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.3707 7.2126 140.9123
REMARK 3 T TENSOR
REMARK 3 T11: 0.1446 T22: 0.1956
REMARK 3 T33: 0.1693 T12: 0.0243
REMARK 3 T13: 0.0019 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 2.5601 L22: 2.3736
REMARK 3 L33: 2.7180 L12: 0.2893
REMARK 3 L13: -0.0141 L23: -0.7239
REMARK 3 S TENSOR
REMARK 3 S11: 0.0499 S12: 0.0879 S13: -0.0370
REMARK 3 S21: -0.1028 S22: -0.0876 S23: -0.2453
REMARK 3 S31: 0.0265 S32: 0.2423 S33: 0.0309
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 48 THROUGH 79 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9996 16.8001 134.4855
REMARK 3 T TENSOR
REMARK 3 T11: 0.1625 T22: 0.1801
REMARK 3 T33: 0.1941 T12: 0.0050
REMARK 3 T13: 0.0024 T23: 0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 1.7886 L22: 1.4902
REMARK 3 L33: 2.8642 L12: -0.1606
REMARK 3 L13: -1.1870 L23: -0.7678
REMARK 3 S TENSOR
REMARK 3 S11: 0.1127 S12: 0.1199 S13: 0.1831
REMARK 3 S21: -0.0125 S22: -0.0804 S23: -0.0901
REMARK 3 S31: -0.2102 S32: 0.0345 S33: -0.0275
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 80 THROUGH 102 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6895 19.8299 136.1891
REMARK 3 T TENSOR
REMARK 3 T11: 0.1942 T22: 0.1872
REMARK 3 T33: 0.2155 T12: 0.0286
REMARK 3 T13: 0.0165 T23: 0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 1.4405 L22: 2.4806
REMARK 3 L33: 2.8777 L12: 0.5386
REMARK 3 L13: -0.5364 L23: -0.7160
REMARK 3 S TENSOR
REMARK 3 S11: 0.1141 S12: 0.2045 S13: 0.2402
REMARK 3 S21: -0.0303 S22: -0.0025 S23: 0.0558
REMARK 3 S31: -0.2928 S32: -0.1428 S33: -0.1044
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 119 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.6933 21.7141 140.1986
REMARK 3 T TENSOR
REMARK 3 T11: 0.2123 T22: 0.2294
REMARK 3 T33: 0.2352 T12: 0.0714
REMARK 3 T13: 0.0072 T23: 0.0218
REMARK 3 L TENSOR
REMARK 3 L11: 2.4400 L22: 5.0229
REMARK 3 L33: 2.9792 L12: -0.2578
REMARK 3 L13: -0.7157 L23: 1.0053
REMARK 3 S TENSOR
REMARK 3 S11: -0.0426 S12: 0.1391 S13: 0.1711
REMARK 3 S21: -0.2467 S22: -0.0683 S23: 0.4589
REMARK 3 S31: -0.7756 S32: -0.7155 S33: 0.1422
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 120 THROUGH 158 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6507 12.9186 151.0706
REMARK 3 T TENSOR
REMARK 3 T11: 0.1360 T22: 0.1694
REMARK 3 T33: 0.1678 T12: -0.0020
REMARK 3 T13: 0.0094 T23: -0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 1.6284 L22: 0.9853
REMARK 3 L33: 2.4859 L12: 0.0616
REMARK 3 L13: -0.1200 L23: 0.2495
REMARK 3 S TENSOR
REMARK 3 S11: 0.0621 S12: -0.1162 S13: 0.0738
REMARK 3 S21: 0.0208 S22: -0.0459 S23: 0.0998
REMARK 3 S31: -0.0436 S32: -0.2597 S33: -0.0089
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 159 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.0330 3.3940 142.2082
REMARK 3 T TENSOR
REMARK 3 T11: 0.1619 T22: 0.1810
REMARK 3 T33: 0.2217 T12: -0.0627
REMARK 3 T13: -0.0001 T23: -0.0256
REMARK 3 L TENSOR
REMARK 3 L11: 4.0816 L22: 5.8534
REMARK 3 L33: 7.9320 L12: -0.1674
REMARK 3 L13: 0.6676 L23: -1.2567
REMARK 3 S TENSOR
REMARK 3 S11: 0.2078 S12: -0.1602 S13: -0.1577
REMARK 3 S21: -0.1926 S22: 0.0053 S23: 0.5469
REMARK 3 S31: 0.5059 S32: -0.8439 S33: -0.2179
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 15 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.2028 -15.2265 134.5851
REMARK 3 T TENSOR
REMARK 3 T11: 0.1947 T22: 0.1746
REMARK 3 T33: 0.1755 T12: 0.0204
REMARK 3 T13: -0.0064 T23: -0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 4.2357 L22: 1.7971
REMARK 3 L33: 5.1693 L12: 0.2718
REMARK 3 L13: 0.9754 L23: 0.1774
REMARK 3 S TENSOR
REMARK 3 S11: 0.3925 S12: 0.0367 S13: -0.4710
REMARK 3 S21: -0.0933 S22: -0.0618 S23: 0.1833
REMARK 3 S31: 0.7001 S32: 0.4238 S33: -0.2990
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 16 THROUGH 47 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4382 -17.7217 132.3161
REMARK 3 T TENSOR
REMARK 3 T11: 0.1549 T22: 0.1958
REMARK 3 T33: 0.1840 T12: -0.0340
REMARK 3 T13: -0.0044 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 2.5164 L22: 2.1708
REMARK 3 L33: 2.5370 L12: -0.4641
REMARK 3 L13: -0.0698 L23: 0.5806
REMARK 3 S TENSOR
REMARK 3 S11: 0.0357 S12: -0.0824 S13: -0.0698
REMARK 3 S21: 0.0711 S22: -0.0703 S23: 0.2394
REMARK 3 S31: 0.0170 S32: -0.2244 S33: 0.0341
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 48 THROUGH 79 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.0637 -8.1400 138.7422
REMARK 3 T TENSOR
REMARK 3 T11: 0.1536 T22: 0.1696
REMARK 3 T33: 0.1913 T12: -0.0011
REMARK 3 T13: 0.0078 T23: -0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 1.6761 L22: 1.3126
REMARK 3 L33: 2.6679 L12: 0.2443
REMARK 3 L13: -1.2454 L23: 0.5923
REMARK 3 S TENSOR
REMARK 3 S11: 0.1502 S12: -0.1139 S13: 0.1502
REMARK 3 S21: -0.0214 S22: -0.1036 S23: 0.1048
REMARK 3 S31: -0.1830 S32: -0.0072 S33: -0.0396
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 80 THROUGH 102 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.2489 -5.1001 137.0487
REMARK 3 T TENSOR
REMARK 3 T11: 0.1795 T22: 0.1809
REMARK 3 T33: 0.2125 T12: -0.0381
REMARK 3 T13: 0.0131 T23: -0.0272
REMARK 3 L TENSOR
REMARK 3 L11: 1.3990 L22: 2.2026
REMARK 3 L33: 2.8798 L12: -0.5187
REMARK 3 L13: -0.4973 L23: 0.7688
REMARK 3 S TENSOR
REMARK 3 S11: 0.0955 S12: -0.2288 S13: 0.2598
REMARK 3 S21: 0.1031 S22: 0.0083 S23: -0.0805
REMARK 3 S31: -0.3028 S32: 0.1284 S33: -0.0981
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 103 THROUGH 119 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6885 -3.4504 133.5483
REMARK 3 T TENSOR
REMARK 3 T11: 0.2418 T22: 0.2451
REMARK 3 T33: 0.2485 T12: -0.0714
REMARK 3 T13: 0.0125 T23: -0.0285
REMARK 3 L TENSOR
REMARK 3 L11: 2.0262 L22: 4.7301
REMARK 3 L33: 4.1544 L12: 0.5400
REMARK 3 L13: -0.8526 L23: -1.1399
REMARK 3 S TENSOR
REMARK 3 S11: -0.0279 S12: -0.1601 S13: 0.2508
REMARK 3 S21: 0.3515 S22: -0.1027 S23: -0.3668
REMARK 3 S31: -0.7663 S32: 0.8070 S33: 0.1633
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 120 THROUGH 158 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.2747 -12.0201 122.1405
REMARK 3 T TENSOR
REMARK 3 T11: 0.1453 T22: 0.1701
REMARK 3 T33: 0.1804 T12: 0.0008
REMARK 3 T13: 0.0116 T23: 0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 1.8751 L22: 1.0642
REMARK 3 L33: 2.5188 L12: 0.0491
REMARK 3 L13: -0.0549 L23: -0.2949
REMARK 3 S TENSOR
REMARK 3 S11: 0.0586 S12: 0.1663 S13: 0.0841
REMARK 3 S21: -0.0256 S22: -0.0199 S23: -0.1247
REMARK 3 S31: -0.0932 S32: 0.2509 S33: -0.0311
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 159 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8836 -21.5316 131.0051
REMARK 3 T TENSOR
REMARK 3 T11: 0.1748 T22: 0.1994
REMARK 3 T33: 0.2105 T12: 0.0446
REMARK 3 T13: -0.0124 T23: 0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 4.5938 L22: 6.5506
REMARK 3 L33: 1.9487 L12: 0.4618
REMARK 3 L13: 1.2673 L23: 1.9637
REMARK 3 S TENSOR
REMARK 3 S11: 0.3342 S12: 0.0691 S13: -0.3448
REMARK 3 S21: 0.1459 S22: 0.0811 S23: -0.5290
REMARK 3 S31: 0.4526 S32: 0.7498 S33: -0.4271
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 6NKC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1000238889.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-DEC-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : 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 : 42897
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.630
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 : 6.500
REMARK 200 R MERGE (I) : 0.17200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.81900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.670
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: HKL-3000, MOLREP
REMARK 200 STARTING MODEL: 1T2N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 % TRYPTONE, 0.05 M HEPES SODIUM PH
REMARK 280 7.0, 12% W/V POLYETHYLENE GLYCOL 3,350, 0.001 M SODIUM AZIDE,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
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,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 70.81250
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 106.21875
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 35.40625
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: MONOMERIC
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 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 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 0
REMARK 465 ALA A 1
REMARK 465 GLY A 173
REMARK 465 LYS A 174
REMARK 465 HIS A 175
REMARK 465 HIS A 176
REMARK 465 HIS A 177
REMARK 465 HIS A 178
REMARK 465 HIS A 179
REMARK 465 HIS A 180
REMARK 465 MSE B 0
REMARK 465 GLY B 173
REMARK 465 LYS B 174
REMARK 465 HIS B 175
REMARK 465 HIS B 176
REMARK 465 HIS B 177
REMARK 465 HIS B 178
REMARK 465 HIS B 179
REMARK 465 HIS B 180
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 77 -132.23 61.93
REMARK 500 LEU A 90 -140.75 -107.79
REMARK 500 PHE A 157 43.49 -140.75
REMARK 500 SER B 77 -133.02 61.28
REMARK 500 LEU B 90 -140.17 -105.68
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 CL A 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AZI A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 201
DBREF1 6NKC A 1 174 UNP A0A1D8GR37_BACLI
DBREF2 6NKC A A0A1D8GR37 31 204
DBREF1 6NKC B 1 174 UNP A0A1D8GR37_BACLI
DBREF2 6NKC B A0A1D8GR37 31 204
SEQADV 6NKC MSE A 0 UNP A0A1D8GR3 INITIATING METHIONINE
SEQADV 6NKC HIS A 175 UNP A0A1D8GR3 EXPRESSION TAG
SEQADV 6NKC HIS A 176 UNP A0A1D8GR3 EXPRESSION TAG
SEQADV 6NKC HIS A 177 UNP A0A1D8GR3 EXPRESSION TAG
SEQADV 6NKC HIS A 178 UNP A0A1D8GR3 EXPRESSION TAG
SEQADV 6NKC HIS A 179 UNP A0A1D8GR3 EXPRESSION TAG
SEQADV 6NKC HIS A 180 UNP A0A1D8GR3 EXPRESSION TAG
SEQADV 6NKC MSE B 0 UNP A0A1D8GR3 INITIATING METHIONINE
SEQADV 6NKC HIS B 175 UNP A0A1D8GR3 EXPRESSION TAG
SEQADV 6NKC HIS B 176 UNP A0A1D8GR3 EXPRESSION TAG
SEQADV 6NKC HIS B 177 UNP A0A1D8GR3 EXPRESSION TAG
SEQADV 6NKC HIS B 178 UNP A0A1D8GR3 EXPRESSION TAG
SEQADV 6NKC HIS B 179 UNP A0A1D8GR3 EXPRESSION TAG
SEQADV 6NKC HIS B 180 UNP A0A1D8GR3 EXPRESSION TAG
SEQRES 1 A 181 MSE ALA SER HIS ASN PRO VAL VAL MSE VAL HIS GLY ILE
SEQRES 2 A 181 GLY GLY ALA ASP TYR ASN PHE ILE GLY ILE LYS SER TYR
SEQRES 3 A 181 LEU GLN SER GLN GLY TRP THR SER SER GLU LEU TYR ALA
SEQRES 4 A 181 ILE ASN PHE ILE ASP LYS THR GLY ASN ASN ILE ASN ASN
SEQRES 5 A 181 ALA PRO ARG LEU SER GLU TYR ILE LYS ARG VAL LEU ASN
SEQRES 6 A 181 GLN THR GLY ALA SER LYS VAL ASP ILE VAL ALA HIS SER
SEQRES 7 A 181 MSE GLY GLY ALA ASN THR LEU TYR TYR ILE LYS ASN LEU
SEQRES 8 A 181 ASP GLY ALA ASP LYS VAL GLY HIS VAL VAL THR LEU GLY
SEQRES 9 A 181 GLY ALA ASN ARG LEU VAL THR ASN THR ALA PRO GLN ASN
SEQRES 10 A 181 ASP LYS ILE SER TYR THR SER ILE TYR SER THR SER ASP
SEQRES 11 A 181 TYR ILE VAL LEU ASN SER LEU SER LYS LEU ASP GLY ALA
SEQRES 12 A 181 ASN ASN VAL GLN ILE SER GLY VAL SER HIS VAL GLY LEU
SEQRES 13 A 181 LEU PHE SER SER LYS VAL ASN ALA LEU ILE LYS ASP GLY
SEQRES 14 A 181 LEU THR ALA SER GLY LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 181 MSE ALA SER HIS ASN PRO VAL VAL MSE VAL HIS GLY ILE
SEQRES 2 B 181 GLY GLY ALA ASP TYR ASN PHE ILE GLY ILE LYS SER TYR
SEQRES 3 B 181 LEU GLN SER GLN GLY TRP THR SER SER GLU LEU TYR ALA
SEQRES 4 B 181 ILE ASN PHE ILE ASP LYS THR GLY ASN ASN ILE ASN ASN
SEQRES 5 B 181 ALA PRO ARG LEU SER GLU TYR ILE LYS ARG VAL LEU ASN
SEQRES 6 B 181 GLN THR GLY ALA SER LYS VAL ASP ILE VAL ALA HIS SER
SEQRES 7 B 181 MSE GLY GLY ALA ASN THR LEU TYR TYR ILE LYS ASN LEU
SEQRES 8 B 181 ASP GLY ALA ASP LYS VAL GLY HIS VAL VAL THR LEU GLY
SEQRES 9 B 181 GLY ALA ASN ARG LEU VAL THR ASN THR ALA PRO GLN ASN
SEQRES 10 B 181 ASP LYS ILE SER TYR THR SER ILE TYR SER THR SER ASP
SEQRES 11 B 181 TYR ILE VAL LEU ASN SER LEU SER LYS LEU ASP GLY ALA
SEQRES 12 B 181 ASN ASN VAL GLN ILE SER GLY VAL SER HIS VAL GLY LEU
SEQRES 13 B 181 LEU PHE SER SER LYS VAL ASN ALA LEU ILE LYS ASP GLY
SEQRES 14 B 181 LEU THR ALA SER GLY LYS HIS HIS HIS HIS HIS HIS
MODRES 6NKC MSE A 8 MET MODIFIED RESIDUE
MODRES 6NKC MSE A 78 MET MODIFIED RESIDUE
MODRES 6NKC MSE B 8 MET MODIFIED RESIDUE
MODRES 6NKC MSE B 78 MET MODIFIED RESIDUE
HET MSE A 8 8
HET MSE A 78 8
HET MSE B 8 8
HET MSE B 78 8
HET CL A 200 1
HET EDO A 201 4
HET AZI A 202 3
HET CL B 200 1
HET EDO B 201 4
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM AZI AZIDE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 3 CL 2(CL 1-)
FORMUL 4 EDO 2(C2 H6 O2)
FORMUL 5 AZI N3 1-
FORMUL 8 HOH *386(H2 O)
HELIX 1 AA1 ALA A 15 ASN A 18 5 4
HELIX 2 AA2 PHE A 19 GLN A 29 1 11
HELIX 3 AA3 THR A 32 SER A 34 5 3
HELIX 4 AA4 ASN A 47 GLY A 67 1 21
HELIX 5 AA5 MSE A 78 LEU A 90 1 13
HELIX 6 AA6 ASP A 91 ASP A 94 5 4
HELIX 7 AA7 ALA A 105 VAL A 109 5 5
HELIX 8 AA8 LEU A 133 LYS A 138 1 6
HELIX 9 AA9 HIS A 152 PHE A 157 5 6
HELIX 10 AB1 SER A 158 THR A 170 1 13
HELIX 11 AB2 ALA B 15 ASN B 18 5 4
HELIX 12 AB3 PHE B 19 GLN B 29 1 11
HELIX 13 AB4 THR B 32 SER B 34 5 3
HELIX 14 AB5 ASN B 47 GLY B 67 1 21
HELIX 15 AB6 MSE B 78 LEU B 90 1 13
HELIX 16 AB7 ASP B 91 ASP B 94 5 4
HELIX 17 AB8 ALA B 105 VAL B 109 5 5
HELIX 18 AB9 LEU B 133 LYS B 138 1 6
HELIX 19 AC1 HIS B 152 PHE B 157 5 6
HELIX 20 AC2 SER B 158 THR B 170 1 13
SHEET 1 AA1 6 LEU A 36 ALA A 38 0
SHEET 2 AA1 6 VAL A 6 VAL A 9 1 N VAL A 6 O TYR A 37
SHEET 3 AA1 6 VAL A 71 HIS A 76 1 O ASP A 72 N VAL A 7
SHEET 4 AA1 6 VAL A 96 LEU A 102 1 O GLY A 97 N VAL A 71
SHEET 5 AA1 6 SER A 120 SER A 126 1 O ILE A 124 N THR A 101
SHEET 6 AA1 6 ASN A 143 ILE A 147 1 O VAL A 145 N SER A 123
SHEET 1 AA2 6 LEU B 36 ALA B 38 0
SHEET 2 AA2 6 VAL B 6 VAL B 9 1 N VAL B 6 O TYR B 37
SHEET 3 AA2 6 VAL B 71 HIS B 76 1 O ASP B 72 N VAL B 7
SHEET 4 AA2 6 VAL B 96 LEU B 102 1 O GLY B 97 N VAL B 71
SHEET 5 AA2 6 SER B 120 SER B 126 1 O SER B 120 N VAL B 99
SHEET 6 AA2 6 ASN B 143 ILE B 147 1 O VAL B 145 N SER B 123
LINK C VAL A 7 N MSE A 8 1555 1555 1.33
LINK C MSE A 8 N VAL A 9 1555 1555 1.33
LINK C SER A 77 N MSE A 78 1555 1555 1.33
LINK C MSE A 78 N GLY A 79 1555 1555 1.34
LINK C VAL B 7 N MSE B 8 1555 1555 1.33
LINK C MSE B 8 N VAL B 9 1555 1555 1.33
LINK C SER B 77 N MSE B 78 1555 1555 1.33
LINK C MSE B 78 N GLY B 79 1555 1555 1.35
SITE 1 AC1 3 TYR A 130 HIS A 152 ILE B 20
SITE 1 AC2 5 ARG A 61 VAL A 62 GLN A 65 HOH A 304
SITE 2 AC2 5 HOH A 317
SITE 1 AC3 5 SER A 159 HOH A 330 HOH A 375 SER B 159
SITE 2 AC3 5 HOH B 402
SITE 1 AC4 3 ILE A 20 TYR B 130 HIS B 152
SITE 1 AC5 7 TYR B 58 ARG B 61 VAL B 62 GLN B 65
SITE 2 AC5 7 HOH B 308 HOH B 323 HOH B 430
CRYST1 49.870 49.870 141.625 90.00 90.00 90.00 P 43 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.020052 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020052 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007061 0.00000
TER 1286 SER A 172
TER 2585 SER B 172
MASTER 487 0 9 20 12 0 8 6 2974 2 51 28
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