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HEADER TRANSFERASE 18-JUL-19 6PUX
TITLE HOMOSERINE TRANSACETYLASE META FROM MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOMOSERINE O-ACETYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HAT,HOMOSERINE TRANSACETYLASE,HTA;
COMPND 5 EC: 2.3.1.31;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN ATCC 25618 /
SOURCE 3 H37RV);
SOURCE 4 ORGANISM_TAXID: 83332;
SOURCE 5 STRAIN: ATCC 25618 / H37RV;
SOURCE 6 ATCC: 25618;
SOURCE 7 GENE: METXA, META, RV3341, MTV016.41;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_VARIANT: ROSETTA2
KEYWDS METHIONINE BIOSYNTHESIS, HOMOSERINE O-ACETYLTRANSFERASE, HOMOSERINE
KEYWDS 2 O-TRANSACETYLASE, HTA, METX, RV3341, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.T.CHATON,K.V.KOROTKOV
REVDAT 1 31-JUL-19 6PUX 0
JRNL AUTH C.T.CHATON,K.V.KOROTKOV
JRNL TITL HOMOSERINE TRANSACETYLASE META FROM MYCOBACTERIUM
JRNL TITL 2 TUBERCULOSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.16_3549
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.100
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 68843
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 6562
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 44.7130 - 5.8993 1.00 4085 259 0.1980 0.1968
REMARK 3 2 5.8993 - 4.6841 0.99 4150 200 0.1468 0.1767
REMARK 3 3 4.6841 - 4.0924 1.00 4140 234 0.1193 0.1532
REMARK 3 4 4.0924 - 3.7185 1.00 4106 241 0.1180 0.1479
REMARK 3 5 3.7185 - 3.4521 1.00 4152 222 0.1256 0.1574
REMARK 3 6 3.4521 - 3.2486 1.00 4161 207 0.1362 0.1896
REMARK 3 7 3.2486 - 3.0859 1.00 4140 214 0.1467 0.1625
REMARK 3 8 3.0859 - 2.9516 1.00 4121 220 0.1511 0.1970
REMARK 3 9 2.9516 - 2.8380 0.99 4142 218 0.1552 0.2141
REMARK 3 10 2.8380 - 2.7401 0.99 4114 207 0.1565 0.1882
REMARK 3 11 2.7401 - 2.6544 0.99 4145 195 0.1622 0.2433
REMARK 3 12 2.6544 - 2.5786 0.99 4120 220 0.1733 0.2046
REMARK 3 13 2.5786 - 2.5107 1.00 4113 236 0.1736 0.2531
REMARK 3 14 2.5107 - 2.4494 1.00 4139 247 0.1749 0.2077
REMARK 3 15 2.4494 - 2.3938 1.00 4088 256 0.1732 0.2122
REMARK 3 16 2.3938 - 2.3428 1.00 4103 202 0.1777 0.1878
REMARK 3 17 2.3428 - 2.2960 1.00 4181 197 0.1842 0.2245
REMARK 3 18 2.2960 - 2.2526 1.00 4096 255 0.1853 0.2396
REMARK 3 19 2.2526 - 2.2124 1.00 4201 213 0.1919 0.1913
REMARK 3 20 2.2124 - 2.1749 1.00 4111 223 0.1986 0.2174
REMARK 3 21 2.1749 - 2.1398 1.00 4113 243 0.2053 0.2347
REMARK 3 22 2.1398 - 2.1069 1.00 4220 174 0.2132 0.2709
REMARK 3 23 2.1069 - 2.0759 1.00 4153 183 0.2405 0.2703
REMARK 3 24 2.0759 - 2.0467 1.00 4150 213 0.2435 0.2912
REMARK 3 25 2.0467 - 2.0190 1.00 4110 260 0.2560 0.3013
REMARK 3 26 2.0190 - 1.9928 0.99 4120 217 0.2743 0.3357
REMARK 3 27 1.9928 - 1.9679 1.00 4110 204 0.2751 0.2936
REMARK 3 28 1.9679 - 1.9442 0.99 4171 192 0.2917 0.3210
REMARK 3 29 1.9442 - 1.9216 1.00 4182 194 0.2997 0.3289
REMARK 3 30 1.9216 - 1.9000 0.99 4061 216 0.3149 0.3147
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.020
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.31
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.18
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 7 THROUGH 219 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.0342 8.3938 51.2787
REMARK 3 T TENSOR
REMARK 3 T11: 0.2271 T22: 0.1786
REMARK 3 T33: 0.2181 T12: 0.0163
REMARK 3 T13: 0.0079 T23: -0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 0.3078 L22: 0.7422
REMARK 3 L33: 1.3107 L12: 0.1154
REMARK 3 L13: 0.3142 L23: 0.3293
REMARK 3 S TENSOR
REMARK 3 S11: 0.0338 S12: 0.0462 S13: -0.0825
REMARK 3 S21: -0.0547 S22: 0.0117 S23: -0.0319
REMARK 3 S31: 0.1987 S32: 0.0748 S33: -0.0480
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 220 THROUGH 260 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9430 18.1016 76.9973
REMARK 3 T TENSOR
REMARK 3 T11: 0.1986 T22: 0.2533
REMARK 3 T33: 0.2401 T12: -0.0323
REMARK 3 T13: 0.0056 T23: 0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 1.8686 L22: 1.9198
REMARK 3 L33: 0.7767 L12: -1.5046
REMARK 3 L13: -0.0950 L23: 0.7418
REMARK 3 S TENSOR
REMARK 3 S11: -0.0890 S12: -0.1372 S13: -0.1854
REMARK 3 S21: 0.0832 S22: 0.0544 S23: 0.3095
REMARK 3 S31: 0.1480 S32: -0.1675 S33: 0.0589
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 261 THROUGH 334 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6566 20.8120 58.7256
REMARK 3 T TENSOR
REMARK 3 T11: 0.1781 T22: 0.1870
REMARK 3 T33: 0.2087 T12: -0.0163
REMARK 3 T13: 0.0091 T23: -0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 0.4284 L22: 0.6220
REMARK 3 L33: 1.0494 L12: -0.2697
REMARK 3 L13: 0.1419 L23: 0.5068
REMARK 3 S TENSOR
REMARK 3 S11: -0.0015 S12: 0.0413 S13: -0.0241
REMARK 3 S21: -0.0070 S22: -0.0007 S23: -0.0545
REMARK 3 S31: -0.0122 S32: 0.0012 S33: 0.0042
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 335 THROUGH 372 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.6599 26.1108 50.0695
REMARK 3 T TENSOR
REMARK 3 T11: 0.2782 T22: 0.2386
REMARK 3 T33: 0.2616 T12: 0.0229
REMARK 3 T13: -0.0193 T23: 0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 1.2480 L22: 1.2642
REMARK 3 L33: 2.1760 L12: 0.1957
REMARK 3 L13: -0.2345 L23: 0.0391
REMARK 3 S TENSOR
REMARK 3 S11: 0.0723 S12: 0.0577 S13: 0.0480
REMARK 3 S21: -0.2708 S22: -0.0489 S23: 0.1634
REMARK 3 S31: -0.1319 S32: -0.2246 S33: -0.0280
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 8 THROUGH 35 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6247 29.4904 107.3580
REMARK 3 T TENSOR
REMARK 3 T11: 0.3083 T22: 0.2896
REMARK 3 T33: 0.2695 T12: 0.0118
REMARK 3 T13: -0.0369 T23: 0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 2.7933 L22: 2.0252
REMARK 3 L33: 1.1202 L12: 1.3263
REMARK 3 L13: 0.5620 L23: 0.1837
REMARK 3 S TENSOR
REMARK 3 S11: -0.0485 S12: -0.2116 S13: 0.0163
REMARK 3 S21: 0.2710 S22: -0.0198 S23: -0.1970
REMARK 3 S31: -0.1428 S32: 0.1051 S33: 0.0815
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 36 THROUGH 92 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7892 39.9126 97.7447
REMARK 3 T TENSOR
REMARK 3 T11: 0.2476 T22: 0.2555
REMARK 3 T33: 0.2686 T12: -0.0286
REMARK 3 T13: -0.0505 T23: 0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 1.0327 L22: 1.0565
REMARK 3 L33: 0.7720 L12: -0.0253
REMARK 3 L13: 0.2136 L23: -0.4970
REMARK 3 S TENSOR
REMARK 3 S11: -0.0357 S12: -0.0968 S13: 0.0996
REMARK 3 S21: 0.2303 S22: -0.0452 S23: -0.2665
REMARK 3 S31: -0.1399 S32: 0.1476 S33: 0.0474
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 93 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.1475 25.4674 101.3309
REMARK 3 T TENSOR
REMARK 3 T11: 0.1979 T22: 0.2562
REMARK 3 T33: 0.1980 T12: 0.0077
REMARK 3 T13: -0.0170 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.7849 L22: 1.4939
REMARK 3 L33: 0.9350 L12: 0.1669
REMARK 3 L13: 0.0116 L23: -0.5906
REMARK 3 S TENSOR
REMARK 3 S11: -0.0355 S12: -0.1484 S13: -0.0378
REMARK 3 S21: 0.0840 S22: 0.0831 S23: -0.0326
REMARK 3 S31: 0.0195 S32: 0.0237 S33: -0.0524
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 131 THROUGH 151 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5827 36.1251 103.5106
REMARK 3 T TENSOR
REMARK 3 T11: 0.2890 T22: 0.2601
REMARK 3 T33: 0.2265 T12: 0.0206
REMARK 3 T13: 0.0346 T23: -0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 1.5216 L22: 1.4137
REMARK 3 L33: 2.3229 L12: 1.0995
REMARK 3 L13: 1.1067 L23: -0.0663
REMARK 3 S TENSOR
REMARK 3 S11: 0.0275 S12: -0.1677 S13: 0.0372
REMARK 3 S21: 0.3220 S22: 0.0691 S23: 0.0442
REMARK 3 S31: -0.1732 S32: -0.0285 S33: -0.0601
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 152 THROUGH 187 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.9933 38.9249 92.6163
REMARK 3 T TENSOR
REMARK 3 T11: 0.2161 T22: 0.2397
REMARK 3 T33: 0.2132 T12: 0.0377
REMARK 3 T13: 0.0206 T23: 0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 1.6492 L22: 1.7374
REMARK 3 L33: 0.6772 L12: 0.4515
REMARK 3 L13: 0.2757 L23: 0.0567
REMARK 3 S TENSOR
REMARK 3 S11: -0.0347 S12: -0.0454 S13: 0.0814
REMARK 3 S21: 0.2053 S22: 0.0559 S23: 0.1036
REMARK 3 S31: -0.1510 S32: -0.1222 S33: -0.0147
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 188 THROUGH 260 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8752 19.2418 77.8845
REMARK 3 T TENSOR
REMARK 3 T11: 0.1919 T22: 0.2278
REMARK 3 T33: 0.2349 T12: 0.0119
REMARK 3 T13: -0.0188 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.6535 L22: 1.2039
REMARK 3 L33: 1.0807 L12: 0.1053
REMARK 3 L13: -0.4727 L23: -0.0993
REMARK 3 S TENSOR
REMARK 3 S11: -0.0654 S12: -0.0422 S13: -0.0770
REMARK 3 S21: 0.0665 S22: 0.0194 S23: -0.2165
REMARK 3 S31: 0.0707 S32: 0.1992 S33: 0.0379
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 261 THROUGH 290 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9497 22.1174 84.0994
REMARK 3 T TENSOR
REMARK 3 T11: 0.1767 T22: 0.2907
REMARK 3 T33: 0.2489 T12: 0.0109
REMARK 3 T13: -0.0136 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 0.0817 L22: 0.2814
REMARK 3 L33: 1.4824 L12: -0.0868
REMARK 3 L13: -0.3185 L23: 0.1209
REMARK 3 S TENSOR
REMARK 3 S11: -0.0498 S12: -0.0740 S13: -0.0893
REMARK 3 S21: 0.0645 S22: 0.0361 S23: -0.1400
REMARK 3 S31: 0.0985 S32: 0.3323 S33: 0.0128
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 291 THROUGH 334 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.5040 38.4158 84.0497
REMARK 3 T TENSOR
REMARK 3 T11: 0.1830 T22: 0.2486
REMARK 3 T33: 0.2329 T12: 0.0208
REMARK 3 T13: 0.0153 T23: 0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 0.4216 L22: 0.6016
REMARK 3 L33: 0.7559 L12: 0.1251
REMARK 3 L13: -0.0523 L23: -0.2302
REMARK 3 S TENSOR
REMARK 3 S11: -0.0572 S12: -0.0561 S13: 0.0484
REMARK 3 S21: -0.0341 S22: 0.1056 S23: 0.1425
REMARK 3 S31: -0.0577 S32: -0.0991 S33: -0.0529
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 335 THROUGH 372 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8807 46.0921 83.3061
REMARK 3 T TENSOR
REMARK 3 T11: 0.2525 T22: 0.2336
REMARK 3 T33: 0.2618 T12: -0.0039
REMARK 3 T13: 0.0031 T23: 0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 1.8950 L22: 1.4954
REMARK 3 L33: 2.0689 L12: -0.1350
REMARK 3 L13: -0.3848 L23: 0.5065
REMARK 3 S TENSOR
REMARK 3 S11: -0.0103 S12: 0.0186 S13: 0.2140
REMARK 3 S21: -0.0221 S22: 0.0655 S23: -0.1139
REMARK 3 S31: -0.3646 S32: 0.1522 S33: -0.0725
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 6PUX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-19.
REMARK 100 THE DEPOSITION ID IS D_1000243102.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : ROSENBAUM-ROCK DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR: LIQUID NITROGEN
REMARK 200 COOLED; SAGITALLY FOCUSING 2ND
REMARK 200 CRYSTAL, ROSENBAUM-ROCK VERTICAL
REMARK 200 FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300-HS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS VERSION MAR 15, 2019
REMARK 200 DATA SCALING SOFTWARE : XSCALE VERSION MAR 15, 2019
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68862
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 44.713
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.373
REMARK 200 R MERGE (I) : 0.14300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.2100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 7.35
REMARK 200 R MERGE FOR SHELL (I) : 1.36100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.290
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.3
REMARK 200 STARTING MODEL: 5W8P
REMARK 200
REMARK 200 REMARK: BROKEN PRIZM
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL, PH 8.5, 1.8 M
REMARK 280 MAGNESIUM SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
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
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 23.73000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 104.38500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.34000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 104.38500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.73000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.34000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 6380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -197.0 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 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 GLY B 7
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 ALA A 8 24.73 -141.23
REMARK 500 SER A 157 -131.52 65.16
REMARK 500 ALA A 245 -143.43 49.47
REMARK 500 ASP A 293 96.22 -170.47
REMARK 500 TYR A 323 76.82 -118.37
REMARK 500 SER B 157 -131.73 58.78
REMARK 500 ALA B 245 -138.71 46.34
REMARK 500 ALA B 256 41.40 -143.26
REMARK 500 ASP B 293 94.47 -172.32
REMARK 500 TYR B 323 76.76 -117.72
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 A 406 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 131 N
REMARK 620 2 ALA A 288 O 99.3
REMARK 620 3 SER A 291 OG 130.8 83.8
REMARK 620 4 HOH A 662 O 73.1 144.8 127.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 404 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 293 OD2
REMARK 620 2 HOH A 575 O 77.9
REMARK 620 3 HOH A 705 O 83.8 160.6
REMARK 620 4 HOH A 708 O 97.8 96.7 92.2
REMARK 620 5 HOH A 742 O 171.5 94.1 103.8 85.9
REMARK 620 6 HOH B 658 O 83.5 82.7 88.8 178.3 92.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 405 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 332 O
REMARK 620 2 LEU A 335 O 86.5
REMARK 620 3 HOH A 723 O 157.8 101.2
REMARK 620 4 HOH A 725 O 126.0 132.7 62.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 408 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE B 131 N
REMARK 620 2 ALA B 288 O 99.3
REMARK 620 3 SER B 291 OG 132.4 86.3
REMARK 620 4 HOH B 690 O 70.0 141.6 128.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 410 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 293 OD2
REMARK 620 2 HOH A 560 O 99.3
REMARK 620 3 HOH B 746 O 161.4 99.3
REMARK 620 4 HOH B 565 O 84.0 95.9 94.2
REMARK 620 5 HOH B 540 O 86.9 171.1 74.7 91.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 409 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU B 335 O
REMARK 620 2 HOH B 734 O 156.4
REMARK 620 3 HOH B 714 O 108.0 64.5
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 411
DBREF 6PUX A 10 372 UNP P9WJY9 METXA_MYCTU 10 372
DBREF 6PUX B 10 372 UNP P9WJY9 METXA_MYCTU 10 372
SEQADV 6PUX GLY A 7 UNP P9WJY9 EXPRESSION TAG
SEQADV 6PUX ALA A 8 UNP P9WJY9 EXPRESSION TAG
SEQADV 6PUX MET A 9 UNP P9WJY9 EXPRESSION TAG
SEQADV 6PUX GLY B 7 UNP P9WJY9 EXPRESSION TAG
SEQADV 6PUX ALA B 8 UNP P9WJY9 EXPRESSION TAG
SEQADV 6PUX MET B 9 UNP P9WJY9 EXPRESSION TAG
SEQRES 1 A 366 GLY ALA MET THR LEU PRO ALA GLU GLY GLU ILE GLY LEU
SEQRES 2 A 366 ILE ASP VAL GLY SER LEU GLN LEU GLU SER GLY ALA VAL
SEQRES 3 A 366 ILE ASP ASP VAL CYS ILE ALA VAL GLN ARG TRP GLY LYS
SEQRES 4 A 366 LEU SER PRO ALA ARG ASP ASN VAL VAL VAL VAL LEU HIS
SEQRES 5 A 366 ALA LEU THR GLY ASP SER HIS ILE THR GLY PRO ALA GLY
SEQRES 6 A 366 PRO GLY HIS PRO THR PRO GLY TRP TRP ASP GLY VAL ALA
SEQRES 7 A 366 GLY PRO GLY ALA PRO ILE ASP THR THR ARG TRP CYS ALA
SEQRES 8 A 366 VAL ALA THR ASN VAL LEU GLY GLY CYS ARG GLY SER THR
SEQRES 9 A 366 GLY PRO SER SER LEU ALA ARG ASP GLY LYS PRO TRP GLY
SEQRES 10 A 366 SER ARG PHE PRO LEU ILE SER ILE ARG ASP GLN VAL GLN
SEQRES 11 A 366 ALA ASP VAL ALA ALA LEU ALA ALA LEU GLY ILE THR GLU
SEQRES 12 A 366 VAL ALA ALA VAL VAL GLY GLY SER MET GLY GLY ALA ARG
SEQRES 13 A 366 ALA LEU GLU TRP VAL VAL GLY TYR PRO ASP ARG VAL ARG
SEQRES 14 A 366 ALA GLY LEU LEU LEU ALA VAL GLY ALA ARG ALA THR ALA
SEQRES 15 A 366 ASP GLN ILE GLY THR GLN THR THR GLN ILE ALA ALA ILE
SEQRES 16 A 366 LYS ALA ASP PRO ASP TRP GLN SER GLY ASP TYR HIS GLU
SEQRES 17 A 366 THR GLY ARG ALA PRO ASP ALA GLY LEU ARG LEU ALA ARG
SEQRES 18 A 366 ARG PHE ALA HIS LEU THR TYR ARG GLY GLU ILE GLU LEU
SEQRES 19 A 366 ASP THR ARG PHE ALA ASN HIS ASN GLN GLY ASN GLU ASP
SEQRES 20 A 366 PRO THR ALA GLY GLY ARG TYR ALA VAL GLN SER TYR LEU
SEQRES 21 A 366 GLU HIS GLN GLY ASP LYS LEU LEU SER ARG PHE ASP ALA
SEQRES 22 A 366 GLY SER TYR VAL ILE LEU THR GLU ALA LEU ASN SER HIS
SEQRES 23 A 366 ASP VAL GLY ARG GLY ARG GLY GLY VAL SER ALA ALA LEU
SEQRES 24 A 366 ARG ALA CYS PRO VAL PRO VAL VAL VAL GLY GLY ILE THR
SEQRES 25 A 366 SER ASP ARG LEU TYR PRO LEU ARG LEU GLN GLN GLU LEU
SEQRES 26 A 366 ALA ASP LEU LEU PRO GLY CYS ALA GLY LEU ARG VAL VAL
SEQRES 27 A 366 GLU SER VAL TYR GLY HIS ASP GLY PHE LEU VAL GLU THR
SEQRES 28 A 366 GLU ALA VAL GLY GLU LEU ILE ARG GLN THR LEU GLY LEU
SEQRES 29 A 366 ALA ASP
SEQRES 1 B 366 GLY ALA MET THR LEU PRO ALA GLU GLY GLU ILE GLY LEU
SEQRES 2 B 366 ILE ASP VAL GLY SER LEU GLN LEU GLU SER GLY ALA VAL
SEQRES 3 B 366 ILE ASP ASP VAL CYS ILE ALA VAL GLN ARG TRP GLY LYS
SEQRES 4 B 366 LEU SER PRO ALA ARG ASP ASN VAL VAL VAL VAL LEU HIS
SEQRES 5 B 366 ALA LEU THR GLY ASP SER HIS ILE THR GLY PRO ALA GLY
SEQRES 6 B 366 PRO GLY HIS PRO THR PRO GLY TRP TRP ASP GLY VAL ALA
SEQRES 7 B 366 GLY PRO GLY ALA PRO ILE ASP THR THR ARG TRP CYS ALA
SEQRES 8 B 366 VAL ALA THR ASN VAL LEU GLY GLY CYS ARG GLY SER THR
SEQRES 9 B 366 GLY PRO SER SER LEU ALA ARG ASP GLY LYS PRO TRP GLY
SEQRES 10 B 366 SER ARG PHE PRO LEU ILE SER ILE ARG ASP GLN VAL GLN
SEQRES 11 B 366 ALA ASP VAL ALA ALA LEU ALA ALA LEU GLY ILE THR GLU
SEQRES 12 B 366 VAL ALA ALA VAL VAL GLY GLY SER MET GLY GLY ALA ARG
SEQRES 13 B 366 ALA LEU GLU TRP VAL VAL GLY TYR PRO ASP ARG VAL ARG
SEQRES 14 B 366 ALA GLY LEU LEU LEU ALA VAL GLY ALA ARG ALA THR ALA
SEQRES 15 B 366 ASP GLN ILE GLY THR GLN THR THR GLN ILE ALA ALA ILE
SEQRES 16 B 366 LYS ALA ASP PRO ASP TRP GLN SER GLY ASP TYR HIS GLU
SEQRES 17 B 366 THR GLY ARG ALA PRO ASP ALA GLY LEU ARG LEU ALA ARG
SEQRES 18 B 366 ARG PHE ALA HIS LEU THR TYR ARG GLY GLU ILE GLU LEU
SEQRES 19 B 366 ASP THR ARG PHE ALA ASN HIS ASN GLN GLY ASN GLU ASP
SEQRES 20 B 366 PRO THR ALA GLY GLY ARG TYR ALA VAL GLN SER TYR LEU
SEQRES 21 B 366 GLU HIS GLN GLY ASP LYS LEU LEU SER ARG PHE ASP ALA
SEQRES 22 B 366 GLY SER TYR VAL ILE LEU THR GLU ALA LEU ASN SER HIS
SEQRES 23 B 366 ASP VAL GLY ARG GLY ARG GLY GLY VAL SER ALA ALA LEU
SEQRES 24 B 366 ARG ALA CYS PRO VAL PRO VAL VAL VAL GLY GLY ILE THR
SEQRES 25 B 366 SER ASP ARG LEU TYR PRO LEU ARG LEU GLN GLN GLU LEU
SEQRES 26 B 366 ALA ASP LEU LEU PRO GLY CYS ALA GLY LEU ARG VAL VAL
SEQRES 27 B 366 GLU SER VAL TYR GLY HIS ASP GLY PHE LEU VAL GLU THR
SEQRES 28 B 366 GLU ALA VAL GLY GLU LEU ILE ARG GLN THR LEU GLY LEU
SEQRES 29 B 366 ALA ASP
HET SO4 A 401 5
HET SO4 A 402 5
HET SO4 A 403 5
HET MG A 404 1
HET MG A 405 1
HET MG A 406 1
HET CL A 407 1
HET CL A 408 1
HET GOL B 401 14
HET SO4 B 402 5
HET SO4 B 403 5
HET SO4 B 404 5
HET SO4 B 405 5
HET SO4 B 406 5
HET SO4 B 407 5
HET MG B 408 1
HET MG B 409 1
HET MG B 410 1
HET CL B 411 1
HETNAM SO4 SULFATE ION
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 SO4 9(O4 S 2-)
FORMUL 6 MG 6(MG 2+)
FORMUL 9 CL 3(CL 1-)
FORMUL 11 GOL C3 H8 O3
FORMUL 22 HOH *514(H2 O)
HELIX 1 AA1 TRP A 122 PHE A 126 5 5
HELIX 2 AA2 SER A 130 LEU A 145 1 16
HELIX 3 AA3 SER A 157 TYR A 170 1 14
HELIX 4 AA4 THR A 187 ASP A 204 1 18
HELIX 5 AA5 TRP A 207 ASP A 211 5 5
HELIX 6 AA6 PRO A 219 ARG A 235 1 17
HELIX 7 AA7 GLY A 236 PHE A 244 1 9
HELIX 8 AA8 ASP A 253 GLY A 257 5 5
HELIX 9 AA9 TYR A 260 SER A 275 1 16
HELIX 10 AB1 ASP A 278 SER A 291 1 14
HELIX 11 AB2 GLY A 300 ALA A 307 1 8
HELIX 12 AB3 PRO A 324 LEU A 335 1 12
HELIX 13 AB4 TYR A 348 HIS A 350 5 3
HELIX 14 AB5 ASP A 351 GLU A 356 1 6
HELIX 15 AB6 GLU A 356 ASP A 372 1 17
HELIX 16 AB7 TRP B 122 PHE B 126 5 5
HELIX 17 AB8 SER B 130 LEU B 145 1 16
HELIX 18 AB9 SER B 157 TYR B 170 1 14
HELIX 19 AC1 THR B 187 ASP B 204 1 18
HELIX 20 AC2 TRP B 207 ASP B 211 5 5
HELIX 21 AC3 PRO B 219 TYR B 234 1 16
HELIX 22 AC4 GLY B 236 ALA B 245 1 10
HELIX 23 AC5 ASP B 253 GLY B 257 5 5
HELIX 24 AC6 TYR B 260 SER B 275 1 16
HELIX 25 AC7 ASP B 278 SER B 291 1 14
HELIX 26 AC8 GLY B 300 ALA B 307 1 8
HELIX 27 AC9 PRO B 324 LEU B 335 1 12
HELIX 28 AD1 TYR B 348 HIS B 350 5 3
HELIX 29 AD2 ASP B 351 GLU B 356 1 6
HELIX 30 AD3 GLU B 356 ASP B 372 1 17
SHEET 1 AA1 8 GLY A 18 GLN A 26 0
SHEET 2 AA1 8 VAL A 32 TRP A 43 -1 O VAL A 40 N GLY A 18
SHEET 3 AA1 8 CYS A 96 THR A 100 -1 O ALA A 97 N TRP A 43
SHEET 4 AA1 8 VAL A 53 LEU A 57 1 N VAL A 56 O VAL A 98
SHEET 5 AA1 8 VAL A 150 GLY A 156 1 O ALA A 152 N VAL A 55
SHEET 6 AA1 8 VAL A 174 LEU A 180 1 O LEU A 178 N VAL A 153
SHEET 7 AA1 8 VAL A 312 ILE A 317 1 O VAL A 313 N LEU A 179
SHEET 8 AA1 8 ARG A 342 VAL A 344 1 O VAL A 344 N GLY A 316
SHEET 1 AA2 2 ALA A 84 GLY A 85 0
SHEET 2 AA2 2 ILE A 90 ASP A 91 1 O ILE A 90 N GLY A 85
SHEET 1 AA3 8 GLY B 18 GLN B 26 0
SHEET 2 AA3 8 VAL B 32 TRP B 43 -1 O VAL B 40 N GLY B 18
SHEET 3 AA3 8 CYS B 96 THR B 100 -1 O ALA B 99 N GLN B 41
SHEET 4 AA3 8 VAL B 53 LEU B 57 1 N VAL B 56 O VAL B 98
SHEET 5 AA3 8 VAL B 150 GLY B 156 1 O ALA B 152 N VAL B 55
SHEET 6 AA3 8 VAL B 174 LEU B 180 1 O LEU B 178 N VAL B 153
SHEET 7 AA3 8 VAL B 312 ILE B 317 1 O VAL B 313 N LEU B 179
SHEET 8 AA3 8 CYS B 338 VAL B 344 1 O VAL B 344 N GLY B 316
SHEET 1 AA4 2 ALA B 84 GLY B 85 0
SHEET 2 AA4 2 ILE B 90 ASP B 91 1 O ILE B 90 N GLY B 85
LINK N ILE A 131 MG MG A 406 1555 1555 2.94
LINK O ALA A 288 MG MG A 406 1555 1555 2.64
LINK OG SER A 291 MG MG A 406 1555 1555 1.80
LINK OD2 ASP A 293 MG MG A 404 1555 1555 2.51
LINK O ALA A 332 MG MG A 405 1555 1555 2.88
LINK O LEU A 335 MG MG A 405 1555 1555 2.84
LINK N ILE B 131 MG MG B 408 1555 1555 2.93
LINK O ALA B 288 MG MG B 408 1555 1555 2.60
LINK OG SER B 291 MG MG B 408 1555 1555 2.14
LINK OD2 ASP B 293 MG MG B 410 1555 1555 2.27
LINK O LEU B 335 MG MG B 409 1555 1555 2.79
LINK MG MG A 404 O HOH A 575 1555 1555 2.65
LINK MG MG A 404 O HOH A 705 1555 1555 2.57
LINK MG MG A 404 O HOH A 708 1555 1555 2.16
LINK MG MG A 404 O HOH A 742 1555 1555 2.27
LINK MG MG A 404 O HOH B 658 1555 1555 2.34
LINK MG MG A 405 O HOH A 723 1555 1555 2.69
LINK MG MG A 405 O HOH A 725 1555 1555 2.28
LINK MG MG A 406 O HOH A 662 1555 1555 2.36
LINK MG MG B 408 O HOH B 690 1555 1555 2.60
LINK MG MG B 409 O HOH B 734 1555 1555 2.70
LINK MG MG B 409 O HOH B 714 1555 1555 2.65
LINK MG MG B 410 O HOH A 560 1555 1555 2.22
LINK MG MG B 410 O HOH B 746 1555 1555 2.14
LINK MG MG B 410 O HOH B 565 1555 1555 2.36
LINK MG MG B 410 O HOH B 540 1555 4456 2.39
SITE 1 AC1 5 GLY A 297 ARG A 298 GLY A 299 GLY A 300
SITE 2 AC1 5 HOH A 502
SITE 1 AC2 4 ARG A 227 GLN A 269 LYS A 272 ARG A 276
SITE 1 AC3 3 LYS A 202 TRP A 207 HOH A 591
SITE 1 AC4 7 ASP A 293 HOH A 502 HOH A 575 HOH A 705
SITE 2 AC4 7 HOH A 708 HOH A 742 HOH B 658
SITE 1 AC5 6 ALA A 332 ASP A 333 LEU A 335 CYS A 338
SITE 2 AC5 6 HOH A 723 HOH A 725
SITE 1 AC6 6 SER A 130 ILE A 131 ALA A 288 SER A 291
SITE 2 AC6 6 HIS A 292 HOH A 662
SITE 1 AC7 3 VAL A 301 SER A 302 HOH A 609
SITE 1 AC8 1 THR A 61
SITE 1 AC9 5 ASP A 241 ARG B 185 ARG B 326 LEU B 327
SITE 2 AC9 5 GLU B 330
SITE 1 AD1 8 ARG A 50 GLN B 329 GLY B 340 LEU B 341
SITE 2 AD1 8 HOH B 514 HOH B 517 HOH B 627 HOH B 636
SITE 1 AD2 6 ARG B 117 GLY B 297 HOH B 518 HOH B 537
SITE 2 AD2 6 HOH B 540 HOH B 649
SITE 1 AD3 6 HOH A 560 ARG B 185 GLY B 300 VAL B 301
SITE 2 AD3 6 HOH B 513 HOH B 565
SITE 1 AD4 2 LYS B 202 TRP B 207
SITE 1 AD5 4 ARG B 227 LYS B 272 ARG B 276 HOH B 644
SITE 1 AD6 4 ARG B 42 LYS B 45 LEU B 46 HOH B 532
SITE 1 AD7 6 SER B 130 ILE B 131 ALA B 288 SER B 291
SITE 2 AD7 6 HIS B 292 HOH B 690
SITE 1 AD8 6 ALA B 332 ASP B 333 LEU B 335 CYS B 338
SITE 2 AD8 6 HOH B 714 HOH B 734
SITE 1 AD9 5 HOH A 560 ASP B 293 HOH B 540 HOH B 565
SITE 2 AD9 5 HOH B 746
SITE 1 AE1 2 ALA B 31 VAL B 32
CRYST1 47.460 86.680 208.770 90.00 90.00 90.00 P 21 21 21 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 0.021070 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011537 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004790 0.00000
TER 5345 ASP A 372
TER 10695 ASP B 372
MASTER 593 0 19 30 20 0 30 6 5958 2 91 58
END |