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HEADER HYDROLASE 03-MAY-23 8SPK
TITLE CRYSTAL STRUCTURE OF ANTARCTIC PET-DEGRADING ENZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TRIACYLGLYCEROL LIPASE;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MORAXELLA;
SOURCE 3 ORGANISM_TAXID: 475;
SOURCE 4 GENE: LIP1, L1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A-TEV
KEYWDS PET-DEGRADING ENZYME, ANTARCTIC, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.FURTADO,P.BLAZQUEZ-SANCHEZ,A.GRINEN,J.A.VARGAS,D.A.LEONARDO,
AUTHOR 2 S.A.SCULACCIO,H.M.PEREIRA,B.DIEZ,R.C.GARRATT,C.A.RAMIREZ-SARMIENTO
REVDAT 1 23-AUG-23 8SPK 0
JRNL AUTH P.BLAZQUEZ-SANCHEZ,J.A.VARGAS,A.A.FURTADO,A.GRINEN,
JRNL AUTH 2 D.A.LEONARDO,S.A.SCULACCIO,H.D.PEREIRA,C.SONNENDECKER,
JRNL AUTH 3 W.ZIMMERMANN,B.DIEZ,R.C.GARRATT,C.A.RAMIREZ-SARMIENTO
JRNL TITL ENGINEERING THE CATALYTIC ACTIVITY OF AN ANTARCTIC
JRNL TITL 2 PET-DEGRADING ENZYME BY LOOP EXCHANGE.
JRNL REF PROTEIN SCI. E4757 2023
JRNL REFN ESSN 1469-896X
JRNL PMID 37574805
JRNL DOI 10.1002/PRO.4757
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 92.76
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 99232
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 4908
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 92.7600 - 4.9700 1.00 3315 186 0.1660 0.1735
REMARK 3 2 4.9600 - 3.9400 1.00 3228 149 0.1129 0.1268
REMARK 3 3 3.9400 - 3.4400 1.00 3202 151 0.1223 0.1396
REMARK 3 4 3.4400 - 3.1300 1.00 3188 146 0.1347 0.1912
REMARK 3 5 3.1300 - 2.9000 1.00 3156 168 0.1513 0.1693
REMARK 3 6 2.9000 - 2.7300 1.00 3164 149 0.1530 0.1647
REMARK 3 7 2.7300 - 2.6000 1.00 3174 178 0.1484 0.1548
REMARK 3 8 2.6000 - 2.4800 1.00 3131 179 0.1504 0.1797
REMARK 3 9 2.4800 - 2.3900 1.00 3125 166 0.1419 0.1695
REMARK 3 10 2.3900 - 2.3000 1.00 3157 153 0.1383 0.1631
REMARK 3 11 2.3000 - 2.2300 1.00 3152 152 0.1450 0.1776
REMARK 3 12 2.2300 - 2.1700 1.00 3170 171 0.1567 0.1775
REMARK 3 13 2.1700 - 2.1100 1.00 3102 145 0.1608 0.1809
REMARK 3 14 2.1100 - 2.0600 1.00 3145 163 0.1572 0.1787
REMARK 3 15 2.0600 - 2.0100 1.00 3135 159 0.1546 0.1828
REMARK 3 16 2.0100 - 1.9700 1.00 3107 176 0.1562 0.1856
REMARK 3 17 1.9700 - 1.9300 1.00 3134 136 0.1539 0.1985
REMARK 3 18 1.9300 - 1.8900 1.00 3186 142 0.1592 0.1918
REMARK 3 19 1.8900 - 1.8600 1.00 3103 199 0.1578 0.1897
REMARK 3 20 1.8600 - 1.8300 1.00 3093 173 0.1694 0.2172
REMARK 3 21 1.8300 - 1.8000 1.00 3135 143 0.1825 0.2194
REMARK 3 22 1.8000 - 1.7700 1.00 3126 180 0.2079 0.2126
REMARK 3 23 1.7700 - 1.7500 1.00 3117 151 0.2131 0.3075
REMARK 3 24 1.7500 - 1.7200 1.00 3102 165 0.2268 0.2606
REMARK 3 25 1.7200 - 1.7000 1.00 3118 162 0.2310 0.2878
REMARK 3 26 1.7000 - 1.6800 1.00 3155 167 0.1935 0.2253
REMARK 3 27 1.6800 - 1.6600 1.00 3077 196 0.1957 0.2422
REMARK 3 28 1.6500 - 1.6400 1.00 3134 166 0.1921 0.2019
REMARK 3 29 1.6300 - 1.6200 1.00 3079 174 0.2015 0.2292
REMARK 3 30 1.6200 - 1.6000 1.00 3114 163 0.2037 0.2366
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.080
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 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 : 0.017 4216
REMARK 3 ANGLE : 1.501 5724
REMARK 3 CHIRALITY : 0.104 614
REMARK 3 PLANARITY : 0.015 747
REMARK 3 DIHEDRAL : 12.079 1552
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 55:71 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.901 -21.914 5.548
REMARK 3 T TENSOR
REMARK 3 T11: 0.3174 T22: 0.2154
REMARK 3 T33: 0.1680 T12: 0.0377
REMARK 3 T13: 0.0495 T23: -0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 0.7207 L22: 5.9475
REMARK 3 L33: 0.5824 L12: 0.7417
REMARK 3 L13: -0.2808 L23: 0.6641
REMARK 3 S TENSOR
REMARK 3 S11: -0.2508 S12: -0.0095 S13: -0.3795
REMARK 3 S21: 0.0953 S22: 0.0119 S23: -0.1584
REMARK 3 S31: 0.7746 S32: 0.0702 S33: -0.1044
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 72:97 )
REMARK 3 ORIGIN FOR THE GROUP (A): 52.159 -23.012 -11.796
REMARK 3 T TENSOR
REMARK 3 T11: 0.1914 T22: 0.2160
REMARK 3 T33: 0.1384 T12: 0.0183
REMARK 3 T13: -0.0091 T23: -0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 1.1412 L22: 0.5489
REMARK 3 L33: 4.2982 L12: -0.4609
REMARK 3 L13: -1.4324 L23: 1.2232
REMARK 3 S TENSOR
REMARK 3 S11: -0.0131 S12: -0.3665 S13: 0.1380
REMARK 3 S21: 0.0761 S22: 0.1458 S23: -0.0949
REMARK 3 S31: -0.2576 S32: 0.5641 S33: -0.3514
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 98:225 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.555 -24.660 -16.335
REMARK 3 T TENSOR
REMARK 3 T11: 0.1257 T22: 0.0837
REMARK 3 T33: 0.0772 T12: 0.0060
REMARK 3 T13: 0.0104 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 1.2972 L22: 0.8765
REMARK 3 L33: 1.4608 L12: -0.1904
REMARK 3 L13: -0.5135 L23: 0.1967
REMARK 3 S TENSOR
REMARK 3 S11: -0.0690 S12: -0.0871 S13: -0.0520
REMARK 3 S21: 0.0972 S22: 0.0318 S23: 0.0079
REMARK 3 S31: 0.1236 S32: 0.0641 S33: 0.0286
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN A AND RESID 226:259 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.443 -12.477 -18.657
REMARK 3 T TENSOR
REMARK 3 T11: 0.1070 T22: 0.0985
REMARK 3 T33: 0.0909 T12: 0.0217
REMARK 3 T13: 0.0044 T23: -0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 2.0328 L22: 2.7932
REMARK 3 L33: 3.3629 L12: 0.8828
REMARK 3 L13: -0.7727 L23: -0.4953
REMARK 3 S TENSOR
REMARK 3 S11: -0.0105 S12: 0.0496 S13: 0.0766
REMARK 3 S21: -0.0633 S22: -0.0016 S23: 0.0238
REMARK 3 S31: -0.1327 S32: -0.2064 S33: -0.0163
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN A AND RESID 260:319 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.846 -13.500 -6.606
REMARK 3 T TENSOR
REMARK 3 T11: 0.1483 T22: 0.1250
REMARK 3 T33: 0.1058 T12: 0.0040
REMARK 3 T13: 0.0032 T23: -0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 0.6043 L22: 1.4379
REMARK 3 L33: 2.2949 L12: -0.1066
REMARK 3 L13: -0.5273 L23: -0.5934
REMARK 3 S TENSOR
REMARK 3 S11: -0.0220 S12: -0.0598 S13: 0.0271
REMARK 3 S21: 0.0841 S22: 0.0245 S23: 0.0309
REMARK 3 S31: -0.0573 S32: 0.0269 S33: 0.0008
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN B AND RESID 56:71 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.929 24.198 -44.238
REMARK 3 T TENSOR
REMARK 3 T11: 0.3351 T22: 0.1395
REMARK 3 T33: 0.2613 T12: 0.0048
REMARK 3 T13: 0.0035 T23: 0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 1.2875 L22: 0.4815
REMARK 3 L33: 4.7021 L12: -0.3249
REMARK 3 L13: -0.4949 L23: 1.4263
REMARK 3 S TENSOR
REMARK 3 S11: -0.3658 S12: 0.1534 S13: 0.3891
REMARK 3 S21: -0.4490 S22: -0.0534 S23: -0.2422
REMARK 3 S31: -0.3037 S32: -0.4367 S33: -0.0006
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ( CHAIN B AND RESID 72:97 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.497 5.898 -45.024
REMARK 3 T TENSOR
REMARK 3 T11: 0.1380 T22: 0.1397
REMARK 3 T33: 0.0989 T12: 0.0189
REMARK 3 T13: 0.0006 T23: -0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 1.4570 L22: 4.8352
REMARK 3 L33: 0.4874 L12: 0.5803
REMARK 3 L13: 0.3295 L23: 1.0787
REMARK 3 S TENSOR
REMARK 3 S11: -0.0132 S12: -0.1047 S13: 0.1798
REMARK 3 S21: 0.1933 S22: -0.0643 S23: 0.4437
REMARK 3 S31: -0.0874 S32: -0.1092 S33: 0.1848
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ( CHAIN B AND RESID 98:169 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.177 2.754 -44.312
REMARK 3 T TENSOR
REMARK 3 T11: 0.0673 T22: 0.0829
REMARK 3 T33: 0.0512 T12: -0.0009
REMARK 3 T13: -0.0034 T23: -0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 1.1176 L22: 1.9082
REMARK 3 L33: 1.1133 L12: -0.1757
REMARK 3 L13: 0.0124 L23: 0.2960
REMARK 3 S TENSOR
REMARK 3 S11: 0.0074 S12: -0.0280 S13: 0.0629
REMARK 3 S21: 0.0101 S22: -0.0136 S23: 0.0483
REMARK 3 S31: -0.1289 S32: -0.0702 S33: -0.0116
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: ( CHAIN B AND RESID 170:182 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.583 8.481 -57.246
REMARK 3 T TENSOR
REMARK 3 T11: 0.1649 T22: 0.1322
REMARK 3 T33: 0.0536 T12: 0.0186
REMARK 3 T13: -0.0015 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 3.1725 L22: 7.3355
REMARK 3 L33: 5.4069 L12: 1.0832
REMARK 3 L13: 1.8624 L23: 0.0096
REMARK 3 S TENSOR
REMARK 3 S11: 0.1219 S12: 0.2042 S13: 0.2764
REMARK 3 S21: -0.0626 S22: -0.1415 S23: 0.2653
REMARK 3 S31: -0.1867 S32: -0.2207 S33: 0.0636
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: ( CHAIN B AND RESID 183:225 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.231 -0.788 -43.224
REMARK 3 T TENSOR
REMARK 3 T11: 0.0960 T22: 0.0814
REMARK 3 T33: 0.0910 T12: -0.0129
REMARK 3 T13: 0.0018 T23: -0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 1.3567 L22: 2.5571
REMARK 3 L33: 2.9255 L12: -0.5141
REMARK 3 L13: 0.3097 L23: -1.2014
REMARK 3 S TENSOR
REMARK 3 S11: -0.0082 S12: 0.0596 S13: -0.0288
REMARK 3 S21: -0.1170 S22: -0.0118 S23: -0.1438
REMARK 3 S31: 0.1150 S32: 0.0799 S33: 0.0236
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: ( CHAIN B AND RESID 226:272 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.779 2.098 -30.530
REMARK 3 T TENSOR
REMARK 3 T11: 0.1045 T22: 0.0819
REMARK 3 T33: 0.0735 T12: -0.0132
REMARK 3 T13: -0.0185 T23: -0.0187
REMARK 3 L TENSOR
REMARK 3 L11: 2.0551 L22: 1.8476
REMARK 3 L33: 2.4260 L12: 0.6775
REMARK 3 L13: -1.2118 L23: -0.2965
REMARK 3 S TENSOR
REMARK 3 S11: 0.0376 S12: -0.0699 S13: 0.0054
REMARK 3 S21: 0.2118 S22: -0.0004 S23: -0.0394
REMARK 3 S31: 0.0642 S32: -0.0823 S33: -0.0181
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: ( CHAIN B AND RESID 273:319 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.619 15.992 -36.539
REMARK 3 T TENSOR
REMARK 3 T11: 0.1324 T22: 0.0947
REMARK 3 T33: 0.1474 T12: 0.0007
REMARK 3 T13: 0.0042 T23: -0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 1.1790 L22: 1.0445
REMARK 3 L33: 1.9161 L12: 0.2759
REMARK 3 L13: 0.3154 L23: -0.1836
REMARK 3 S TENSOR
REMARK 3 S11: 0.0021 S12: -0.0243 S13: 0.1755
REMARK 3 S21: -0.0118 S22: -0.0335 S23: 0.0153
REMARK 3 S31: -0.1576 S32: -0.0075 S33: 0.0395
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 8SPK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-23.
REMARK 100 THE DEPOSITION ID IS D_1000274230.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-22
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 : LNLS SIRIUS
REMARK 200 BEAMLINE : MANACA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9772
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 99279
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 92.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 38.40
REMARK 200 R MERGE (I) : 0.27200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 39.30
REMARK 200 R MERGE FOR SHELL (I) : 2.19500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M SODIUM MALONATE DIBASIC
REMARK 280 MONOHYDRATE AT PH 7.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+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 65.59000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.59000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.59000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.59000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 65.59000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.59000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 65.59000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 65.59000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 65.59000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 65.59000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 65.59000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 65.59000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 65.59000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 65.59000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 65.59000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 65.59000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 65.59000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 65.59000
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 MET A 38
REMARK 465 GLY A 39
REMARK 465 SER A 40
REMARK 465 SER A 41
REMARK 465 HIS A 42
REMARK 465 HIS A 43
REMARK 465 HIS A 44
REMARK 465 HIS A 45
REMARK 465 HIS A 46
REMARK 465 HIS A 47
REMARK 465 SER A 48
REMARK 465 SER A 49
REMARK 465 GLY A 50
REMARK 465 LEU A 51
REMARK 465 VAL A 52
REMARK 465 PRO A 53
REMARK 465 ARG A 54
REMARK 465 MET B 38
REMARK 465 GLY B 39
REMARK 465 SER B 40
REMARK 465 SER B 41
REMARK 465 HIS B 42
REMARK 465 HIS B 43
REMARK 465 HIS B 44
REMARK 465 HIS B 45
REMARK 465 HIS B 46
REMARK 465 HIS B 47
REMARK 465 SER B 48
REMARK 465 SER B 49
REMARK 465 GLY B 50
REMARK 465 LEU B 51
REMARK 465 VAL B 52
REMARK 465 PRO B 53
REMARK 465 ARG B 54
REMARK 465 GLY B 55
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 56 OG
REMARK 470 SER B 56 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 424 O HOH B 691 1.95
REMARK 500 O HOH B 525 O HOH B 665 1.99
REMARK 500 ND2 ASN B 249 O HOH B 401 2.01
REMARK 500 O HOH B 525 O HOH B 563 2.02
REMARK 500 OE1 GLN B 90 O HOH B 402 2.02
REMARK 500 O HOH A 611 O HOH A 750 2.03
REMARK 500 OD1 ASP A 63 O HOH A 501 2.04
REMARK 500 O HOH B 698 O HOH B 701 2.09
REMARK 500 O HOH A 602 O HOH A 740 2.09
REMARK 500 O HOH A 664 O HOH A 695 2.10
REMARK 500 O HOH A 635 O HOH A 768 2.11
REMARK 500 O HOH A 556 O HOH A 763 2.12
REMARK 500 OE1 GLU B 221 O HOH B 403 2.14
REMARK 500 O HOH B 503 O HOH B 604 2.15
REMARK 500 OG SER B 218 O HOH B 404 2.16
REMARK 500 OD2 ASP A 233 O HOH A 502 2.17
REMARK 500 O HOH A 550 O HOH A 658 2.17
REMARK 500 O HOH A 700 O HOH A 746 2.17
REMARK 500 O HOH B 609 O HOH B 629 2.18
REMARK 500 OD2 ASP A 233 O HOH A 503 2.18
REMARK 500 N ASN B 272 O HOH B 405 2.18
REMARK 500 O HOH A 565 O HOH A 705 2.18
REMARK 500 O HOH A 505 O HOH A 673 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 676 O HOH A 726 8544 1.88
REMARK 500 O HOH A 635 O HOH A 646 11545 2.01
REMARK 500 O HOH A 711 O HOH B 478 2555 2.09
REMARK 500 O HOH A 646 O HOH A 768 8544 2.14
REMARK 500 O HOH A 522 O HOH B 584 2555 2.14
REMARK 500 O HOH A 548 O HOH B 625 6555 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 134 CG - CD - NE ANGL. DEV. = -18.3 DEGREES
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 56 -113.21 47.41
REMARK 500 ARG A 75 -133.02 57.68
REMARK 500 SER A 189 -124.44 64.29
REMARK 500 ALA A 237 68.45 -112.56
REMARK 500 TYR A 242 -91.38 -113.72
REMARK 500 CYS A 299 -131.84 57.19
REMARK 500 ARG B 75 -130.41 53.31
REMARK 500 SER B 189 -124.69 63.04
REMARK 500 ALA B 237 71.23 -111.15
REMARK 500 TYR B 242 -90.08 -112.56
REMARK 500 CYS B 299 -134.40 55.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 157 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8SPK A 59 319 UNP P19833 LIP1_MORS1 59 319
DBREF 8SPK B 59 319 UNP P19833 LIP1_MORS1 59 319
SEQADV 8SPK MET A 38 UNP P19833 EXPRESSION TAG
SEQADV 8SPK GLY A 39 UNP P19833 EXPRESSION TAG
SEQADV 8SPK SER A 40 UNP P19833 EXPRESSION TAG
SEQADV 8SPK SER A 41 UNP P19833 EXPRESSION TAG
SEQADV 8SPK HIS A 42 UNP P19833 EXPRESSION TAG
SEQADV 8SPK HIS A 43 UNP P19833 EXPRESSION TAG
SEQADV 8SPK HIS A 44 UNP P19833 EXPRESSION TAG
SEQADV 8SPK HIS A 45 UNP P19833 EXPRESSION TAG
SEQADV 8SPK HIS A 46 UNP P19833 EXPRESSION TAG
SEQADV 8SPK HIS A 47 UNP P19833 EXPRESSION TAG
SEQADV 8SPK SER A 48 UNP P19833 EXPRESSION TAG
SEQADV 8SPK SER A 49 UNP P19833 EXPRESSION TAG
SEQADV 8SPK GLY A 50 UNP P19833 EXPRESSION TAG
SEQADV 8SPK LEU A 51 UNP P19833 EXPRESSION TAG
SEQADV 8SPK VAL A 52 UNP P19833 EXPRESSION TAG
SEQADV 8SPK PRO A 53 UNP P19833 EXPRESSION TAG
SEQADV 8SPK ARG A 54 UNP P19833 EXPRESSION TAG
SEQADV 8SPK GLY A 55 UNP P19833 EXPRESSION TAG
SEQADV 8SPK SER A 56 UNP P19833 EXPRESSION TAG
SEQADV 8SPK HIS A 57 UNP P19833 EXPRESSION TAG
SEQADV 8SPK MET A 58 UNP P19833 EXPRESSION TAG
SEQADV 8SPK MET B 38 UNP P19833 EXPRESSION TAG
SEQADV 8SPK GLY B 39 UNP P19833 EXPRESSION TAG
SEQADV 8SPK SER B 40 UNP P19833 EXPRESSION TAG
SEQADV 8SPK SER B 41 UNP P19833 EXPRESSION TAG
SEQADV 8SPK HIS B 42 UNP P19833 EXPRESSION TAG
SEQADV 8SPK HIS B 43 UNP P19833 EXPRESSION TAG
SEQADV 8SPK HIS B 44 UNP P19833 EXPRESSION TAG
SEQADV 8SPK HIS B 45 UNP P19833 EXPRESSION TAG
SEQADV 8SPK HIS B 46 UNP P19833 EXPRESSION TAG
SEQADV 8SPK HIS B 47 UNP P19833 EXPRESSION TAG
SEQADV 8SPK SER B 48 UNP P19833 EXPRESSION TAG
SEQADV 8SPK SER B 49 UNP P19833 EXPRESSION TAG
SEQADV 8SPK GLY B 50 UNP P19833 EXPRESSION TAG
SEQADV 8SPK LEU B 51 UNP P19833 EXPRESSION TAG
SEQADV 8SPK VAL B 52 UNP P19833 EXPRESSION TAG
SEQADV 8SPK PRO B 53 UNP P19833 EXPRESSION TAG
SEQADV 8SPK ARG B 54 UNP P19833 EXPRESSION TAG
SEQADV 8SPK GLY B 55 UNP P19833 EXPRESSION TAG
SEQADV 8SPK SER B 56 UNP P19833 EXPRESSION TAG
SEQADV 8SPK HIS B 57 UNP P19833 EXPRESSION TAG
SEQADV 8SPK MET B 58 UNP P19833 EXPRESSION TAG
SEQRES 1 A 282 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 282 LEU VAL PRO ARG GLY SER HIS MET ASP CYS ILE ALA ASP
SEQRES 3 A 282 SER LYS ILE THR ALA VAL ALA LEU SER ASP THR ARG ASP
SEQRES 4 A 282 ASN GLY PRO PHE SER ILE ARG THR LYS ARG ILE SER ARG
SEQRES 5 A 282 GLN SER ALA LYS GLY PHE GLY GLY GLY THR ILE HIS TYR
SEQRES 6 A 282 PRO THR ASN ALA SER GLY CYS GLY LEU LEU GLY ALA ILE
SEQRES 7 A 282 ALA VAL VAL PRO GLY TYR VAL SER TYR GLU ASN SER ILE
SEQRES 8 A 282 LYS TRP TRP GLY PRO ARG LEU ALA SER TRP GLY PHE VAL
SEQRES 9 A 282 VAL ILE THR ILE ASN THR ASN SER ILE TYR ASP ASP PRO
SEQRES 10 A 282 ASP SER ARG ALA ALA GLN LEU ASN ALA ALA LEU ASP ASN
SEQRES 11 A 282 MET ILE ALA ASP ASP THR VAL GLY SER MET ILE ASP PRO
SEQRES 12 A 282 LYS ARG LEU GLY ALA ILE GLY TRP SER MET GLY GLY GLY
SEQRES 13 A 282 GLY ALA LEU LYS LEU ALA THR GLU ARG SER THR VAL ARG
SEQRES 14 A 282 ALA ILE MET PRO LEU ALA PRO TYR HIS ASP LYS SER TYR
SEQRES 15 A 282 GLY GLU VAL LYS THR PRO THR LEU VAL ILE ALA CYS GLU
SEQRES 16 A 282 ASP ASP ARG ILE ALA GLU THR LYS LYS TYR ALA ASN ALA
SEQRES 17 A 282 PHE TYR LYS ASN ALA ILE GLY PRO LYS MET LYS VAL GLU
SEQRES 18 A 282 VAL ASN ASN GLY SER HIS PHE CYS PRO SER TYR ARG PHE
SEQRES 19 A 282 ASN GLU ILE LEU LEU SER LYS PRO GLY ILE ALA TRP MET
SEQRES 20 A 282 GLN ARG TYR ILE ASN ASN ASP THR ARG PHE ASP LYS PHE
SEQRES 21 A 282 LEU CYS ALA ASN GLU ASN TYR SER LYS SER PRO ARG ILE
SEQRES 22 A 282 SER ALA TYR ASP TYR LYS ASP CYS PRO
SEQRES 1 B 282 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 282 LEU VAL PRO ARG GLY SER HIS MET ASP CYS ILE ALA ASP
SEQRES 3 B 282 SER LYS ILE THR ALA VAL ALA LEU SER ASP THR ARG ASP
SEQRES 4 B 282 ASN GLY PRO PHE SER ILE ARG THR LYS ARG ILE SER ARG
SEQRES 5 B 282 GLN SER ALA LYS GLY PHE GLY GLY GLY THR ILE HIS TYR
SEQRES 6 B 282 PRO THR ASN ALA SER GLY CYS GLY LEU LEU GLY ALA ILE
SEQRES 7 B 282 ALA VAL VAL PRO GLY TYR VAL SER TYR GLU ASN SER ILE
SEQRES 8 B 282 LYS TRP TRP GLY PRO ARG LEU ALA SER TRP GLY PHE VAL
SEQRES 9 B 282 VAL ILE THR ILE ASN THR ASN SER ILE TYR ASP ASP PRO
SEQRES 10 B 282 ASP SER ARG ALA ALA GLN LEU ASN ALA ALA LEU ASP ASN
SEQRES 11 B 282 MET ILE ALA ASP ASP THR VAL GLY SER MET ILE ASP PRO
SEQRES 12 B 282 LYS ARG LEU GLY ALA ILE GLY TRP SER MET GLY GLY GLY
SEQRES 13 B 282 GLY ALA LEU LYS LEU ALA THR GLU ARG SER THR VAL ARG
SEQRES 14 B 282 ALA ILE MET PRO LEU ALA PRO TYR HIS ASP LYS SER TYR
SEQRES 15 B 282 GLY GLU VAL LYS THR PRO THR LEU VAL ILE ALA CYS GLU
SEQRES 16 B 282 ASP ASP ARG ILE ALA GLU THR LYS LYS TYR ALA ASN ALA
SEQRES 17 B 282 PHE TYR LYS ASN ALA ILE GLY PRO LYS MET LYS VAL GLU
SEQRES 18 B 282 VAL ASN ASN GLY SER HIS PHE CYS PRO SER TYR ARG PHE
SEQRES 19 B 282 ASN GLU ILE LEU LEU SER LYS PRO GLY ILE ALA TRP MET
SEQRES 20 B 282 GLN ARG TYR ILE ASN ASN ASP THR ARG PHE ASP LYS PHE
SEQRES 21 B 282 LEU CYS ALA ASN GLU ASN TYR SER LYS SER PRO ARG ILE
SEQRES 22 B 282 SER ALA TYR ASP TYR LYS ASP CYS PRO
HET MLI A 401 7
HET MLI A 402 7
HETNAM MLI MALONATE ION
FORMUL 3 MLI 2(C3 H2 O4 2-)
FORMUL 5 HOH *672(H2 O)
HELIX 1 AA1 ALA A 62 ILE A 66 5 5
HELIX 2 AA2 THR A 67 SER A 72 1 6
HELIX 3 AA3 ALA A 106 GLY A 110 5 5
HELIX 4 AA4 TYR A 124 LYS A 129 5 6
HELIX 5 AA5 TRP A 130 SER A 137 1 8
HELIX 6 AA6 ASP A 153 ASP A 171 1 19
HELIX 7 AA7 VAL A 174 SER A 176 5 3
HELIX 8 AA8 SER A 189 ARG A 202 1 14
HELIX 9 AA9 TYR A 242 ALA A 250 1 9
HELIX 10 AB1 ASN A 272 ASN A 290 1 19
HELIX 11 AB2 ASP A 291 GLU A 302 5 12
HELIX 12 AB3 ASN A 303 SER A 307 5 5
HELIX 13 AB4 ALA B 62 ILE B 66 5 5
HELIX 14 AB5 THR B 67 SER B 72 1 6
HELIX 15 AB6 ALA B 106 GLY B 110 5 5
HELIX 16 AB7 TYR B 124 LYS B 129 5 6
HELIX 17 AB8 TRP B 130 SER B 137 1 8
HELIX 18 AB9 ASP B 153 ASP B 171 1 19
HELIX 19 AC1 VAL B 174 SER B 176 5 3
HELIX 20 AC2 SER B 189 ARG B 202 1 14
HELIX 21 AC3 TYR B 242 ALA B 250 1 9
HELIX 22 AC4 ASN B 272 ASN B 289 1 18
HELIX 23 AC5 ASP B 291 GLU B 302 5 12
HELIX 24 AC6 ASN B 303 SER B 307 5 5
SHEET 1 AA1 6 ILE A 82 ILE A 87 0
SHEET 2 AA1 6 GLY A 98 PRO A 103 -1 O GLY A 98 N ILE A 87
SHEET 3 AA1 6 VAL A 141 ILE A 145 -1 O VAL A 142 N HIS A 101
SHEET 4 AA1 6 LEU A 112 VAL A 118 1 N ILE A 115 O VAL A 141
SHEET 5 AA1 6 ILE A 178 TRP A 188 1 O ASP A 179 N LEU A 112
SHEET 6 AA1 6 VAL A 205 LEU A 211 1 O LEU A 211 N GLY A 187
SHEET 1 AA2 3 THR A 226 CYS A 231 0
SHEET 2 AA2 3 LYS A 254 VAL A 259 1 O VAL A 259 N ALA A 230
SHEET 3 AA2 3 ILE A 310 LYS A 316 -1 O ASP A 314 N LYS A 256
SHEET 1 AA3 6 ILE B 82 ILE B 87 0
SHEET 2 AA3 6 GLY B 98 PRO B 103 -1 O ILE B 100 N LYS B 85
SHEET 3 AA3 6 VAL B 141 ILE B 145 -1 O VAL B 142 N HIS B 101
SHEET 4 AA3 6 LEU B 112 VAL B 118 1 N VAL B 117 O ILE B 143
SHEET 5 AA3 6 ILE B 178 TRP B 188 1 O ASP B 179 N LEU B 112
SHEET 6 AA3 6 VAL B 205 LEU B 211 1 O LEU B 211 N GLY B 187
SHEET 1 AA4 3 THR B 226 CYS B 231 0
SHEET 2 AA4 3 LYS B 254 VAL B 259 1 O MET B 255 N VAL B 228
SHEET 3 AA4 3 ILE B 310 LYS B 316 -1 O ASP B 314 N LYS B 256
SSBOND 1 CYS A 60 CYS A 109 1555 1555 2.02
SSBOND 2 CYS A 231 CYS A 266 1555 1555 2.07
SSBOND 3 CYS A 299 CYS A 318 1555 1555 2.12
SSBOND 4 CYS B 60 CYS B 109 1555 1555 2.01
SSBOND 5 CYS B 231 CYS B 266 1555 1555 2.09
SSBOND 6 CYS B 299 CYS B 318 1555 1555 2.07
CISPEP 1 CYS A 318 PRO A 319 0 -6.08
CISPEP 2 PRO B 119 GLY B 120 0 -4.81
CISPEP 3 CYS B 318 PRO B 319 0 -6.75
CRYST1 131.180 131.180 131.180 90.00 90.00 90.00 P 21 3 24
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 0.007623 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007623 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007623 0.00000
TER 2044 PRO A 319
TER 4099 PRO B 319
MASTER 605 0 2 24 18 0 0 6 4756 2 26 44
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