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HEADER HYDROLASE 11-OCT-18 6HW1
TITLE ROOM TEMPERATURE STRUCTURE OF LIPASE FROM T. LANUGINOSA AT 2.5 A
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TRIACYLGLYCEROL LIPASE;
COMPND 5 EC: 3.1.1.3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOMYCES LANUGINOSUS;
SOURCE 3 ORGANISM_COMMON: HUMICOLA LANUGINOSA;
SOURCE 4 ORGANISM_TAXID: 5541
KEYWDS LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.GAVIRA,R.FERNADEZ-PENAS,S.MARTINEZ-RODRIGUEZ,C.VERDUGO-ESCAMILLA
REVDAT 1 24-OCT-18 6HW1 0
JRNL AUTH J.A.GAVIRA,R.FERNADEZ-PENAS,S.MARTINEZ-RODRIGUEZ,
JRNL AUTH 2 C.VEDUGO-ESCAMILLA
JRNL TITL ROOM TEMPERATURE STRUCTURE OF LIPASE FROM T. LANUGINOSA AT
JRNL TITL 2 2.5 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 31516
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1573
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 49.0645 - 5.5578 0.95 2776 128 0.1503 0.1414
REMARK 3 2 5.5578 - 4.4123 0.98 2766 134 0.1281 0.1679
REMARK 3 3 4.4123 - 3.8548 0.98 2735 164 0.1359 0.1807
REMARK 3 4 3.8548 - 3.5025 0.98 2791 114 0.1533 0.1694
REMARK 3 5 3.5025 - 3.2515 0.97 2724 139 0.1742 0.2090
REMARK 3 6 3.2515 - 3.0598 0.98 2760 144 0.2068 0.2220
REMARK 3 7 3.0598 - 2.9066 0.98 2713 151 0.2341 0.2625
REMARK 3 8 2.9066 - 2.7801 0.97 2667 171 0.2584 0.3096
REMARK 3 9 2.7801 - 2.6731 0.96 2673 152 0.2832 0.3274
REMARK 3 10 2.6731 - 2.5808 0.96 2676 149 0.3231 0.3713
REMARK 3 11 2.5808 - 2.5001 0.95 2662 127 0.3470 0.3667
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 : 61.63
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.930
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 63.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 83.83
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 : 0.003 4567
REMARK 3 ANGLE : 0.518 6248
REMARK 3 CHIRALITY : 0.040 663
REMARK 3 PLANARITY : 0.003 849
REMARK 3 DIHEDRAL : 12.070 3891
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 22 )
REMARK 3 ORIGIN FOR THE GROUP (A): -36.2907 -50.6231 3.4025
REMARK 3 T TENSOR
REMARK 3 T11: 0.4910 T22: 0.4771
REMARK 3 T33: 0.5221 T12: 0.0922
REMARK 3 T13: 0.0002 T23: -0.0931
REMARK 3 L TENSOR
REMARK 3 L11: 7.0552 L22: 9.3253
REMARK 3 L33: 2.9138 L12: 6.3856
REMARK 3 L13: 4.2815 L23: 2.9154
REMARK 3 S TENSOR
REMARK 3 S11: 0.1059 S12: -0.2813 S13: -0.0878
REMARK 3 S21: 0.2671 S22: -0.4325 S23: 0.6451
REMARK 3 S31: -0.0177 S32: 0.1106 S33: 0.3862
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 23 THROUGH 41 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.5234 -47.5199 2.0224
REMARK 3 T TENSOR
REMARK 3 T11: 0.6409 T22: 1.1729
REMARK 3 T33: 0.9134 T12: -0.0271
REMARK 3 T13: 0.0809 T23: -0.0228
REMARK 3 L TENSOR
REMARK 3 L11: 4.7872 L22: 4.8253
REMARK 3 L33: 6.0193 L12: -4.6779
REMARK 3 L13: -5.1748 L23: 5.1156
REMARK 3 S TENSOR
REMARK 3 S11: 0.5903 S12: 0.1942 S13: 0.9131
REMARK 3 S21: -0.3893 S22: 0.5102 S23: -1.6515
REMARK 3 S31: -1.4885 S32: 2.0427 S33: -0.9447
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 42 THROUGH 70 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.7566 -44.4516 -3.2985
REMARK 3 T TENSOR
REMARK 3 T11: 0.5822 T22: 0.7628
REMARK 3 T33: 0.4363 T12: -0.0129
REMARK 3 T13: 0.0075 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 7.7685 L22: 7.8963
REMARK 3 L33: 8.6693 L12: -1.8828
REMARK 3 L13: -0.8975 L23: -2.0093
REMARK 3 S TENSOR
REMARK 3 S11: -0.0062 S12: 0.3688 S13: 0.1885
REMARK 3 S21: -0.4516 S22: -0.1179 S23: -1.2365
REMARK 3 S31: -0.7324 S32: 0.8695 S33: 0.0232
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 71 THROUGH 91 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.7813 -38.7874 2.4042
REMARK 3 T TENSOR
REMARK 3 T11: 0.7603 T22: 0.5110
REMARK 3 T33: 0.5223 T12: -0.0093
REMARK 3 T13: -0.1145 T23: 0.0406
REMARK 3 L TENSOR
REMARK 3 L11: 5.3348 L22: 2.1498
REMARK 3 L33: 6.4125 L12: -2.3277
REMARK 3 L13: -2.8496 L23: 3.4613
REMARK 3 S TENSOR
REMARK 3 S11: 0.3611 S12: -0.0506 S13: 0.4807
REMARK 3 S21: -0.1268 S22: -0.1700 S23: -0.6705
REMARK 3 S31: -0.9474 S32: 0.5035 S33: -0.3219
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 92 THROUGH 107 )
REMARK 3 ORIGIN FOR THE GROUP (A): -40.1999 -23.4427 -5.2030
REMARK 3 T TENSOR
REMARK 3 T11: 1.4717 T22: 0.9925
REMARK 3 T33: 0.8359 T12: 0.2932
REMARK 3 T13: 0.1167 T23: 0.2392
REMARK 3 L TENSOR
REMARK 3 L11: 5.2794 L22: 7.5568
REMARK 3 L33: 2.5631 L12: -0.1130
REMARK 3 L13: 0.1423 L23: 1.6361
REMARK 3 S TENSOR
REMARK 3 S11: 0.4427 S12: 1.5559 S13: 1.1385
REMARK 3 S21: -1.1501 S22: -0.5296 S23: -0.0330
REMARK 3 S31: -2.1926 S32: 0.1900 S33: 0.1844
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 108 THROUGH 134 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.1520 -34.5299 -12.2677
REMARK 3 T TENSOR
REMARK 3 T11: 1.0776 T22: 1.0933
REMARK 3 T33: 0.6400 T12: 0.1902
REMARK 3 T13: -0.0522 T23: 0.2157
REMARK 3 L TENSOR
REMARK 3 L11: 4.0993 L22: 7.0048
REMARK 3 L33: 5.8354 L12: -3.5211
REMARK 3 L13: -4.1995 L23: 5.2936
REMARK 3 S TENSOR
REMARK 3 S11: 0.8788 S12: 1.2732 S13: 0.3720
REMARK 3 S21: -1.8361 S22: -0.9247 S23: 0.0490
REMARK 3 S31: -1.6883 S32: 0.1023 S33: -0.1694
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 135 THROUGH 269 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.9440 -39.3594 2.9923
REMARK 3 T TENSOR
REMARK 3 T11: 0.5774 T22: 0.5495
REMARK 3 T33: 0.4756 T12: 0.1908
REMARK 3 T13: -0.1098 T23: -0.0579
REMARK 3 L TENSOR
REMARK 3 L11: 3.4868 L22: 3.1778
REMARK 3 L33: 3.0396 L12: -0.7096
REMARK 3 L13: -0.0802 L23: 0.1629
REMARK 3 S TENSOR
REMARK 3 S11: 0.0505 S12: 0.5772 S13: -0.0019
REMARK 3 S21: -0.3592 S22: -0.3028 S23: 0.5050
REMARK 3 S31: -0.7233 S32: -0.5597 S33: 0.2221
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 22 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.8235 -53.6181 32.8207
REMARK 3 T TENSOR
REMARK 3 T11: 0.4746 T22: 0.7454
REMARK 3 T33: 0.6351 T12: 0.2253
REMARK 3 T13: 0.0626 T23: 0.1642
REMARK 3 L TENSOR
REMARK 3 L11: 7.4635 L22: 4.4389
REMARK 3 L33: 4.9508 L12: 4.6698
REMARK 3 L13: -0.9480 L23: -3.3076
REMARK 3 S TENSOR
REMARK 3 S11: -0.3643 S12: -0.2696 S13: -0.7765
REMARK 3 S21: 0.5113 S22: 0.3330 S23: 0.0624
REMARK 3 S31: -0.6722 S32: -0.7491 S33: -0.1275
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 23 THROUGH 36 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.8807 -34.3897 36.1547
REMARK 3 T TENSOR
REMARK 3 T11: 1.7735 T22: 1.1930
REMARK 3 T33: 0.9461 T12: 0.5092
REMARK 3 T13: 0.1657 T23: -0.0793
REMARK 3 L TENSOR
REMARK 3 L11: 6.9339 L22: 3.8639
REMARK 3 L33: 4.3104 L12: -5.0948
REMARK 3 L13: -4.1125 L23: 3.4995
REMARK 3 S TENSOR
REMARK 3 S11: -0.3415 S12: -1.4532 S13: 1.4926
REMARK 3 S21: 0.7678 S22: 1.0187 S23: -0.8682
REMARK 3 S31: -3.3858 S32: -0.1525 S33: -0.5408
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 37 THROUGH 70 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.1882 -39.2538 36.6942
REMARK 3 T TENSOR
REMARK 3 T11: 1.0941 T22: 0.8236
REMARK 3 T33: 0.5195 T12: 0.3470
REMARK 3 T13: -0.0486 T23: 0.0281
REMARK 3 L TENSOR
REMARK 3 L11: 6.6752 L22: 4.1320
REMARK 3 L33: 7.4773 L12: -0.8593
REMARK 3 L13: 2.1507 L23: 0.4269
REMARK 3 S TENSOR
REMARK 3 S11: -0.9196 S12: -1.0809 S13: 0.6224
REMARK 3 S21: 0.4795 S22: 0.3176 S23: 0.2273
REMARK 3 S31: -1.8648 S32: -0.7981 S33: 0.5071
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 71 THROUGH 107 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.0847 -45.2292 36.5024
REMARK 3 T TENSOR
REMARK 3 T11: 0.8369 T22: 0.9419
REMARK 3 T33: 0.5904 T12: -0.0410
REMARK 3 T13: -0.1461 T23: 0.0523
REMARK 3 L TENSOR
REMARK 3 L11: 2.1878 L22: 3.8883
REMARK 3 L33: 6.1823 L12: -2.1950
REMARK 3 L13: -0.0658 L23: -1.1098
REMARK 3 S TENSOR
REMARK 3 S11: -0.5057 S12: -0.4412 S13: 0.4074
REMARK 3 S21: 0.5944 S22: 0.1835 S23: -0.6308
REMARK 3 S31: -1.1693 S32: 0.8391 S33: 0.3460
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 108 THROUGH 159 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.5221 -45.0693 45.3868
REMARK 3 T TENSOR
REMARK 3 T11: 1.0371 T22: 1.0728
REMARK 3 T33: 0.5171 T12: 0.2520
REMARK 3 T13: -0.1537 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 3.9601 L22: 4.2662
REMARK 3 L33: 5.8088 L12: -0.3965
REMARK 3 L13: -1.6082 L23: -0.5452
REMARK 3 S TENSOR
REMARK 3 S11: -0.6481 S12: -1.6790 S13: 0.3508
REMARK 3 S21: 1.4012 S22: 0.3503 S23: -0.3048
REMARK 3 S31: -1.4483 S32: 0.0907 S33: 0.1668
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 160 THROUGH 178 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.8055 -52.7932 41.4927
REMARK 3 T TENSOR
REMARK 3 T11: 0.6476 T22: 0.8516
REMARK 3 T33: 0.5093 T12: 0.1527
REMARK 3 T13: -0.0038 T23: 0.2282
REMARK 3 L TENSOR
REMARK 3 L11: 3.9598 L22: 3.0282
REMARK 3 L33: 1.5754 L12: 0.4131
REMARK 3 L13: -0.2460 L23: -1.2128
REMARK 3 S TENSOR
REMARK 3 S11: -0.1175 S12: -0.9999 S13: -0.4625
REMARK 3 S21: 0.9223 S22: 0.1274 S23: -0.0363
REMARK 3 S31: -0.2645 S32: 0.2251 S33: -0.0154
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 179 THROUGH 211 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.9887 -56.7789 33.9915
REMARK 3 T TENSOR
REMARK 3 T11: 0.3945 T22: 0.8807
REMARK 3 T33: 0.6111 T12: 0.1579
REMARK 3 T13: 0.0138 T23: 0.2384
REMARK 3 L TENSOR
REMARK 3 L11: 4.4245 L22: 2.4161
REMARK 3 L33: 0.7732 L12: 0.1052
REMARK 3 L13: 1.1597 L23: 0.3211
REMARK 3 S TENSOR
REMARK 3 S11: -0.3687 S12: -0.5118 S13: -0.5591
REMARK 3 S21: 0.4088 S22: -0.0534 S23: -0.3099
REMARK 3 S31: 0.0616 S32: 0.9308 S33: 0.3413
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 212 THROUGH 269 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.8549 -57.7183 25.2987
REMARK 3 T TENSOR
REMARK 3 T11: 0.3571 T22: 0.5602
REMARK 3 T33: 0.4797 T12: 0.1102
REMARK 3 T13: 0.0615 T23: 0.0781
REMARK 3 L TENSOR
REMARK 3 L11: 6.4678 L22: 3.8101
REMARK 3 L33: 5.4076 L12: -1.0131
REMARK 3 L13: 2.2419 L23: -1.0786
REMARK 3 S TENSOR
REMARK 3 S11: 0.0882 S12: -0.0159 S13: -0.8428
REMARK 3 S21: -0.1257 S22: -0.1143 S23: -0.1978
REMARK 3 S31: 0.4270 S32: 0.6268 S33: 0.0515
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 6HW1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1200012391.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAR-17
REMARK 200 TEMPERATURE (KELVIN) : 295
REMARK 200 PH : 4.0-7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID30B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31982
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 49.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.90000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 4GWL
REMARK 200
REMARK 200 REMARK: BI-PYRAMIDAL HEXAGON
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 300 MM NA/K PHOSPHATE, 50 MM NAAC PH
REMARK 280 4.5, PH 7.5, COUNTER-DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 26.90700
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 53.81400
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.36050
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 67.26750
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 13.45350
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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 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 ND2 ASN B 33 C2 NAG B 301 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 146 -126.10 62.99
REMARK 500 ASN A 162 33.34 -91.99
REMARK 500 THR A 199 -122.00 33.86
REMARK 500 ASN A 200 44.09 -102.06
REMARK 500 PHE A 262 -9.68 65.84
REMARK 500 ASP B 27 52.28 -113.28
REMARK 500 LYS B 74 64.89 65.96
REMARK 500 ILE B 100 64.99 -113.43
REMARK 500 ILE B 100 64.99 -116.48
REMARK 500 SER B 146 -123.44 64.00
REMARK 500 THR B 199 -117.10 31.69
REMARK 500 PRO B 250 30.28 -85.91
REMARK 500 PHE B 262 -0.77 65.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 419 O
REMARK 620 2 HOH B 409 O 111.0
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 301 bound
REMARK 800 to ASN A 33
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 301 bound
REMARK 800 to ASN B 33
DBREF 6HW1 A 1 269 UNP O59952 LIP_THELA 23 291
DBREF 6HW1 B 1 269 UNP O59952 LIP_THELA 23 291
SEQRES 1 A 269 GLU VAL SER GLN ASP LEU PHE ASN GLN PHE ASN LEU PHE
SEQRES 2 A 269 ALA GLN TYR SER ALA ALA ALA TYR CYS GLY LYS ASN ASN
SEQRES 3 A 269 ASP ALA PRO ALA GLY THR ASN ILE THR CYS THR GLY ASN
SEQRES 4 A 269 ALA CYS PRO GLU VAL GLU LYS ALA ASP ALA THR PHE LEU
SEQRES 5 A 269 TYR SER PHE GLU ASP SER GLY VAL GLY ASP VAL THR GLY
SEQRES 6 A 269 PHE LEU ALA LEU ASP ASN THR ASN LYS LEU ILE VAL LEU
SEQRES 7 A 269 SER PHE ARG GLY SER ARG SER ILE GLU ASN TRP ILE GLY
SEQRES 8 A 269 ASN LEU ASN PHE ASP LEU LYS GLU ILE ASN ASP ILE CYS
SEQRES 9 A 269 SER GLY CYS ARG GLY HIS ASP GLY PHE THR SER SER TRP
SEQRES 10 A 269 ARG SER VAL ALA ASP THR LEU ARG GLN LYS VAL GLU ASP
SEQRES 11 A 269 ALA VAL ARG GLU HIS PRO ASP TYR ARG VAL VAL PHE THR
SEQRES 12 A 269 GLY HIS SER LEU GLY GLY ALA LEU ALA THR VAL ALA GLY
SEQRES 13 A 269 ALA ASP LEU ARG GLY ASN GLY TYR ASP ILE ASP VAL PHE
SEQRES 14 A 269 SER TYR GLY ALA PRO ARG VAL GLY ASN ARG ALA PHE ALA
SEQRES 15 A 269 GLU PHE LEU THR VAL GLN THR GLY GLY THR LEU TYR ARG
SEQRES 16 A 269 ILE THR HIS THR ASN ASP ILE VAL PRO ARG LEU PRO PRO
SEQRES 17 A 269 ARG GLU PHE GLY TYR SER HIS SER SER PRO GLU TYR TRP
SEQRES 18 A 269 ILE LYS SER GLY THR LEU VAL PRO VAL THR ARG ASN ASP
SEQRES 19 A 269 ILE VAL LYS ILE GLU GLY ILE ASP ALA THR GLY GLY ASN
SEQRES 20 A 269 ASN GLN PRO ASN ILE PRO ASP ILE PRO ALA HIS LEU TRP
SEQRES 21 A 269 TYR PHE GLY LEU ILE GLY THR CYS LEU
SEQRES 1 B 269 GLU VAL SER GLN ASP LEU PHE ASN GLN PHE ASN LEU PHE
SEQRES 2 B 269 ALA GLN TYR SER ALA ALA ALA TYR CYS GLY LYS ASN ASN
SEQRES 3 B 269 ASP ALA PRO ALA GLY THR ASN ILE THR CYS THR GLY ASN
SEQRES 4 B 269 ALA CYS PRO GLU VAL GLU LYS ALA ASP ALA THR PHE LEU
SEQRES 5 B 269 TYR SER PHE GLU ASP SER GLY VAL GLY ASP VAL THR GLY
SEQRES 6 B 269 PHE LEU ALA LEU ASP ASN THR ASN LYS LEU ILE VAL LEU
SEQRES 7 B 269 SER PHE ARG GLY SER ARG SER ILE GLU ASN TRP ILE GLY
SEQRES 8 B 269 ASN LEU ASN PHE ASP LEU LYS GLU ILE ASN ASP ILE CYS
SEQRES 9 B 269 SER GLY CYS ARG GLY HIS ASP GLY PHE THR SER SER TRP
SEQRES 10 B 269 ARG SER VAL ALA ASP THR LEU ARG GLN LYS VAL GLU ASP
SEQRES 11 B 269 ALA VAL ARG GLU HIS PRO ASP TYR ARG VAL VAL PHE THR
SEQRES 12 B 269 GLY HIS SER LEU GLY GLY ALA LEU ALA THR VAL ALA GLY
SEQRES 13 B 269 ALA ASP LEU ARG GLY ASN GLY TYR ASP ILE ASP VAL PHE
SEQRES 14 B 269 SER TYR GLY ALA PRO ARG VAL GLY ASN ARG ALA PHE ALA
SEQRES 15 B 269 GLU PHE LEU THR VAL GLN THR GLY GLY THR LEU TYR ARG
SEQRES 16 B 269 ILE THR HIS THR ASN ASP ILE VAL PRO ARG LEU PRO PRO
SEQRES 17 B 269 ARG GLU PHE GLY TYR SER HIS SER SER PRO GLU TYR TRP
SEQRES 18 B 269 ILE LYS SER GLY THR LEU VAL PRO VAL THR ARG ASN ASP
SEQRES 19 B 269 ILE VAL LYS ILE GLU GLY ILE ASP ALA THR GLY GLY ASN
SEQRES 20 B 269 ASN GLN PRO ASN ILE PRO ASP ILE PRO ALA HIS LEU TRP
SEQRES 21 B 269 TYR PHE GLY LEU ILE GLY THR CYS LEU
HET NAG A 301 14
HET PO4 A 302 5
HET MG A 303 1
HET NAG B 301 14
HET MG B 302 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM PO4 PHOSPHATE ION
HETNAM MG MAGNESIUM ION
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 4 PO4 O4 P 3-
FORMUL 5 MG 2(MG 2+)
FORMUL 8 HOH *47(H2 O)
HELIX 1 AA1 SER A 3 GLY A 23 1 21
HELIX 2 AA2 CYS A 41 ALA A 47 1 7
HELIX 3 AA3 SER A 85 ASN A 92 1 8
HELIX 4 AA4 ASP A 111 HIS A 135 1 25
HELIX 5 AA5 SER A 146 ARG A 160 1 15
HELIX 6 AA6 ASN A 178 GLN A 188 1 11
HELIX 7 AA7 ILE A 202 LEU A 206 5 5
HELIX 8 AA8 PRO A 208 GLY A 212 5 5
HELIX 9 AA9 THR A 231 ASN A 233 5 3
HELIX 10 AB1 ILE A 255 TRP A 260 5 6
HELIX 11 AB2 SER B 3 GLY B 23 1 21
HELIX 12 AB3 CYS B 36 ALA B 40 5 5
HELIX 13 AB4 CYS B 41 ALA B 47 1 7
HELIX 14 AB5 SER B 85 ASN B 92 1 8
HELIX 15 AB6 ASP B 111 HIS B 135 1 25
HELIX 16 AB7 SER B 146 ARG B 160 1 15
HELIX 17 AB8 ASN B 178 GLN B 188 1 11
HELIX 18 AB9 ILE B 202 LEU B 206 5 5
HELIX 19 AC1 PRO B 208 GLY B 212 5 5
HELIX 20 AC2 THR B 231 ASN B 233 5 3
HELIX 21 AC3 ILE B 255 TRP B 260 5 6
SHEET 1 AA1 8 ALA A 49 SER A 58 0
SHEET 2 AA1 8 VAL A 63 ASP A 70 -1 O LEU A 67 N TYR A 53
SHEET 3 AA1 8 LEU A 75 PHE A 80 -1 O VAL A 77 N ALA A 68
SHEET 4 AA1 8 ARG A 139 HIS A 145 1 O ARG A 139 N ILE A 76
SHEET 5 AA1 8 ILE A 166 TYR A 171 1 O ASP A 167 N PHE A 142
SHEET 6 AA1 8 LEU A 193 HIS A 198 1 O TYR A 194 N VAL A 168
SHEET 7 AA1 8 GLU A 219 ILE A 222 1 O ILE A 222 N THR A 197
SHEET 8 AA1 8 ILE A 235 ILE A 238 -1 O VAL A 236 N TRP A 221
SHEET 1 AA2 2 LEU A 97 GLU A 99 0
SHEET 2 AA2 2 ARG A 108 HIS A 110 -1 O GLY A 109 N LYS A 98
SHEET 1 AA3 8 ALA B 49 SER B 58 0
SHEET 2 AA3 8 VAL B 63 ASP B 70 -1 O LEU B 67 N LEU B 52
SHEET 3 AA3 8 LEU B 75 PHE B 80 -1 O VAL B 77 N ALA B 68
SHEET 4 AA3 8 ARG B 139 HIS B 145 1 O THR B 143 N LEU B 78
SHEET 5 AA3 8 ILE B 166 TYR B 171 1 O ASP B 167 N PHE B 142
SHEET 6 AA3 8 LEU B 193 HIS B 198 1 O TYR B 194 N VAL B 168
SHEET 7 AA3 8 GLU B 219 ILE B 222 1 O TYR B 220 N ARG B 195
SHEET 8 AA3 8 ILE B 235 ILE B 238 -1 O ILE B 238 N GLU B 219
SHEET 1 AA4 2 LEU B 97 GLU B 99 0
SHEET 2 AA4 2 ARG B 108 HIS B 110 -1 O GLY B 109 N LYS B 98
SSBOND 1 CYS A 22 CYS A 268 1555 1555 2.03
SSBOND 2 CYS A 36 CYS A 41 1555 1555 2.03
SSBOND 3 CYS A 104 CYS A 107 1555 1555 2.03
SSBOND 4 CYS B 22 CYS B 268 1555 1555 2.03
SSBOND 5 CYS B 36 CYS B 41 1555 1555 2.03
SSBOND 6 CYS B 104 CYS B 107 1555 1555 2.03
LINK ND2 ASN A 33 C1 NAG A 301 1555 1555 1.44
LINK ND2 ASN B 33 C1 NAG B 301 1555 1555 1.39
LINK MG MG B 302 O HOH B 419 1555 1555 2.44
LINK MG MG B 302 O HOH B 409 1555 1555 2.15
CISPEP 1 LEU A 206 PRO A 207 0 -10.12
CISPEP 2 SER A 217 PRO A 218 0 0.62
CISPEP 3 LEU B 206 PRO B 207 0 -10.19
CISPEP 4 SER B 217 PRO B 218 0 0.82
SITE 1 AC1 6 ARG A 209 GLU A 210 HOH A 402 PRO B 208
SITE 2 AC1 6 ARG B 209 GLU B 210
SITE 1 AC2 2 HIS A 215 SER A 216
SITE 1 AC3 5 ARG B 195 HIS B 215 SER B 216 HOH B 409
SITE 2 AC3 5 HOH B 419
SITE 1 AC4 2 ASN A 33 ASP A 48
SITE 1 AC5 1 ASN B 33
CRYST1 142.652 142.652 80.721 90.00 90.00 120.00 P 61 12
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 0.007010 0.004047 0.000000 0.00000
SCALE2 0.000000 0.008095 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012388 0.00000
TER 2189 LEU A 269
TER 4406 LEU B 269
MASTER 509 0 5 21 20 0 7 6 4224 2 50 42
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