HEADER OXIDOREDUCTASE 24-NOV-16 5U0L
TITLE X-RAY CRYSTAL STRUCTURE OF FATTY ALDEHYDE DEHYDROGENASE ENZYMES FROM
TITLE 2 MARINOBACTER AQUAEOLEI VT8 COMPLEXED WITH A SUBSTRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N-SUCCINYLGLUTAMATE 5-SEMIALDEHYDE DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: SUCCINYLGLUTAMIC SEMIALDEHYDE DEHYDROGENASE,SGSD;
COMPND 5 EC: 1.2.1.71;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MARINOBACTER HYDROCARBONOCLASTICUS (STRAIN ATCC
SOURCE 3 700491 / DSM 11845 / VT8);
SOURCE 4 ORGANISM_TAXID: 351348;
SOURCE 5 STRAIN: ATCC 700491 / DSM 11845 / VT8;
SOURCE 6 GENE: ASTD, MAQU_3316;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DEHYDROGENASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.SHI,K.MULLINER,B.M.BARNEY,H.AIHARA
REVDAT 5 04-OCT-23 5U0L 1 REMARK
REVDAT 4 27-NOV-19 5U0L 1 REMARK
REVDAT 3 13-SEP-17 5U0L 1 REMARK
REVDAT 2 14-JUN-17 5U0L 1 JRNL
REVDAT 1 26-APR-17 5U0L 0
JRNL AUTH J.H.BERTRAM,K.M.MULLINER,K.SHI,M.H.PLUNKETT,P.NIXON,
JRNL AUTH 2 N.A.SERRATORE,C.J.DOUGLAS,H.AIHARA,B.M.BARNEY
JRNL TITL FIVE FATTY ALDEHYDE DEHYDROGENASE ENZYMES FROM MARINOBACTER
JRNL TITL 2 AND ACINETOBACTER SPP. AND STRUCTURAL INSIGHTS INTO THE
JRNL TITL 3 ALDEHYDE BINDING POCKET.
JRNL REF APPL. ENVIRON. MICROBIOL. V. 83 2017
JRNL REFN ESSN 1098-5336
JRNL PMID 28389542
JRNL DOI 10.1128/AEM.00018-17
REMARK 2
REMARK 2 RESOLUTION. 2.29 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_2706
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) : 2.29
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.90
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 56469
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860
REMARK 3 FREE R VALUE TEST SET COUNT : 2742
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 34.9033 - 6.1921 1.00 2999 165 0.1812 0.2295
REMARK 3 2 6.1921 - 4.9192 1.00 2883 123 0.1934 0.2486
REMARK 3 3 4.9192 - 4.2987 0.99 2804 137 0.1585 0.1979
REMARK 3 4 4.2987 - 3.9062 1.00 2794 134 0.1725 0.2372
REMARK 3 5 3.9062 - 3.6265 1.00 2777 144 0.1906 0.2491
REMARK 3 6 3.6265 - 3.4129 1.00 2736 144 0.2075 0.2845
REMARK 3 7 3.4129 - 3.2421 0.99 2703 174 0.2100 0.2818
REMARK 3 8 3.2421 - 3.1011 0.99 2723 124 0.2252 0.2593
REMARK 3 9 3.1011 - 2.9818 0.99 2719 144 0.2407 0.2898
REMARK 3 10 2.9818 - 2.8789 0.99 2743 132 0.2505 0.3044
REMARK 3 11 2.8789 - 2.7889 0.99 2696 134 0.2512 0.3745
REMARK 3 12 2.7889 - 2.7093 0.99 2703 145 0.2590 0.3373
REMARK 3 13 2.7093 - 2.6380 0.99 2680 145 0.2658 0.3003
REMARK 3 14 2.6380 - 2.5736 0.99 2702 118 0.2932 0.3465
REMARK 3 15 2.5736 - 2.5151 0.98 2644 154 0.3134 0.4311
REMARK 3 16 2.5151 - 2.4616 0.95 2542 145 0.3505 0.3703
REMARK 3 17 2.4616 - 2.4124 0.96 2589 136 0.3680 0.4076
REMARK 3 18 2.4124 - 2.3669 0.95 2594 109 0.3965 0.4463
REMARK 3 19 2.3669 - 2.3246 0.92 2494 130 0.4180 0.4388
REMARK 3 20 2.3246 - 2.2852 0.81 2202 105 0.4148 0.4872
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) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.500
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 : 0.009 7563
REMARK 3 ANGLE : 1.045 10257
REMARK 3 CHIRALITY : 0.057 1135
REMARK 3 PLANARITY : 0.007 1352
REMARK 3 DIHEDRAL : 9.214 4478
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 3 THROUGH 62 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.1290 10.4617 57.2727
REMARK 3 T TENSOR
REMARK 3 T11: 0.7598 T22: 0.5103
REMARK 3 T33: 0.5180 T12: 0.0299
REMARK 3 T13: 0.0039 T23: -0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 0.5965 L22: 0.3860
REMARK 3 L33: 1.0194 L12: 0.4653
REMARK 3 L13: 0.4956 L23: 0.1574
REMARK 3 S TENSOR
REMARK 3 S11: -0.1608 S12: -0.4554 S13: 0.1237
REMARK 3 S21: 0.4203 S22: 0.1928 S23: -0.0804
REMARK 3 S31: -0.1730 S32: 0.0326 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 63 THROUGH 279 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.6509 1.9589 43.5632
REMARK 3 T TENSOR
REMARK 3 T11: 0.5870 T22: 0.4022
REMARK 3 T33: 0.5396 T12: -0.0368
REMARK 3 T13: -0.0249 T23: 0.0461
REMARK 3 L TENSOR
REMARK 3 L11: 0.7387 L22: 0.4997
REMARK 3 L33: 1.4155 L12: -0.1650
REMARK 3 L13: 0.0802 L23: 0.1257
REMARK 3 S TENSOR
REMARK 3 S11: -0.0027 S12: -0.1631 S13: -0.0611
REMARK 3 S21: 0.0610 S22: 0.0527 S23: 0.1023
REMARK 3 S31: -0.0240 S32: -0.0192 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 280 THROUGH 400 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.0896 17.8809 25.6188
REMARK 3 T TENSOR
REMARK 3 T11: 0.6830 T22: 0.5719
REMARK 3 T33: 0.6673 T12: 0.1592
REMARK 3 T13: -0.0875 T23: 0.0735
REMARK 3 L TENSOR
REMARK 3 L11: 1.2838 L22: 1.9253
REMARK 3 L33: 0.6486 L12: 0.1276
REMARK 3 L13: 0.1935 L23: 0.1070
REMARK 3 S TENSOR
REMARK 3 S11: 0.0409 S12: 0.0840 S13: 0.1839
REMARK 3 S21: -0.1652 S22: 0.1089 S23: 0.0612
REMARK 3 S31: -0.1218 S32: 0.0489 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 401 THROUGH 490 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.2157 -7.0781 28.5871
REMARK 3 T TENSOR
REMARK 3 T11: 0.7114 T22: 0.5271
REMARK 3 T33: 0.5559 T12: 0.0232
REMARK 3 T13: -0.1140 T23: 0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 0.4844 L22: 0.2456
REMARK 3 L33: 0.2962 L12: -0.8300
REMARK 3 L13: -0.4547 L23: -0.3157
REMARK 3 S TENSOR
REMARK 3 S11: 0.1724 S12: 0.1816 S13: -0.1552
REMARK 3 S21: -0.0831 S22: -0.0793 S23: 0.1184
REMARK 3 S31: 0.1276 S32: 0.1407 S33: 0.0148
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 120 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.7411 -11.7949 13.6759
REMARK 3 T TENSOR
REMARK 3 T11: 0.6438 T22: 0.6612
REMARK 3 T33: 0.5213 T12: 0.1048
REMARK 3 T13: -0.0425 T23: 0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.7604 L22: 0.3484
REMARK 3 L33: 1.1591 L12: -0.3098
REMARK 3 L13: -0.5262 L23: -0.0992
REMARK 3 S TENSOR
REMARK 3 S11: 0.0599 S12: 0.1691 S13: -0.0249
REMARK 3 S21: -0.1324 S22: -0.0760 S23: 0.0575
REMARK 3 S31: 0.3544 S32: 0.4472 S33: -0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 121 THROUGH 153 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.0110 -8.7807 24.0162
REMARK 3 T TENSOR
REMARK 3 T11: 0.6270 T22: 0.5595
REMARK 3 T33: 0.6093 T12: 0.0472
REMARK 3 T13: -0.0690 T23: 0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 0.0329 L22: 0.1511
REMARK 3 L33: 0.6221 L12: 0.0510
REMARK 3 L13: -0.1488 L23: -0.2364
REMARK 3 S TENSOR
REMARK 3 S11: 0.2197 S12: -0.1834 S13: -0.1383
REMARK 3 S21: -0.0173 S22: -0.0491 S23: 0.0212
REMARK 3 S31: 0.1250 S32: 0.0866 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 154 THROUGH 248 )
REMARK 3 ORIGIN FOR THE GROUP (A): 59.4441 -3.3227 19.2098
REMARK 3 T TENSOR
REMARK 3 T11: 0.5360 T22: 0.6066
REMARK 3 T33: 0.4914 T12: 0.0790
REMARK 3 T13: -0.0469 T23: 0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 0.3993 L22: 0.2864
REMARK 3 L33: 0.8977 L12: 0.2871
REMARK 3 L13: -0.2481 L23: -0.4743
REMARK 3 S TENSOR
REMARK 3 S11: -0.0123 S12: 0.0162 S13: -0.0471
REMARK 3 S21: 0.0064 S22: -0.1131 S23: 0.0876
REMARK 3 S31: 0.1377 S32: 0.5380 S33: 0.0002
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 249 THROUGH 278 )
REMARK 3 ORIGIN FOR THE GROUP (A): 71.3657 -22.0962 42.7466
REMARK 3 T TENSOR
REMARK 3 T11: 0.8180 T22: 1.1608
REMARK 3 T33: 0.6893 T12: 0.3028
REMARK 3 T13: -0.0759 T23: 0.1075
REMARK 3 L TENSOR
REMARK 3 L11: 0.3798 L22: 0.0827
REMARK 3 L33: 0.2068 L12: 0.1323
REMARK 3 L13: -0.0662 L23: 0.1448
REMARK 3 S TENSOR
REMARK 3 S11: -0.1223 S12: -0.4105 S13: -0.0618
REMARK 3 S21: 0.4166 S22: 0.1027 S23: 0.0099
REMARK 3 S31: -0.1086 S32: 0.4376 S33: 0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 279 THROUGH 309 )
REMARK 3 ORIGIN FOR THE GROUP (A): 76.8514 -21.2071 45.7217
REMARK 3 T TENSOR
REMARK 3 T11: 0.8927 T22: 1.1521
REMARK 3 T33: 0.7251 T12: 0.2018
REMARK 3 T13: -0.2152 T23: 0.1269
REMARK 3 L TENSOR
REMARK 3 L11: 0.0630 L22: 0.1076
REMARK 3 L33: 0.0159 L12: -0.1961
REMARK 3 L13: 0.0901 L23: -0.0888
REMARK 3 S TENSOR
REMARK 3 S11: 0.1226 S12: 0.0469 S13: -0.1390
REMARK 3 S21: 0.3199 S22: -0.0989 S23: -0.1256
REMARK 3 S31: -0.1428 S32: 0.4487 S33: 0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 310 THROUGH 345 )
REMARK 3 ORIGIN FOR THE GROUP (A): 83.1150 -14.1377 31.0473
REMARK 3 T TENSOR
REMARK 3 T11: 0.6549 T22: 1.4244
REMARK 3 T33: 0.9000 T12: 0.2125
REMARK 3 T13: -0.0139 T23: 0.0801
REMARK 3 L TENSOR
REMARK 3 L11: 0.2010 L22: 0.1216
REMARK 3 L33: 0.0613 L12: 0.1622
REMARK 3 L13: -0.1357 L23: -0.0785
REMARK 3 S TENSOR
REMARK 3 S11: 0.2590 S12: 0.2262 S13: 0.0088
REMARK 3 S21: 0.1423 S22: -0.3347 S23: -0.7985
REMARK 3 S31: 0.4636 S32: 1.0790 S33: 0.0002
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 346 THROUGH 400 )
REMARK 3 ORIGIN FOR THE GROUP (A): 79.0268 -12.1576 43.9254
REMARK 3 T TENSOR
REMARK 3 T11: 0.8153 T22: 1.3815
REMARK 3 T33: 0.7699 T12: 0.2589
REMARK 3 T13: -0.1989 T23: 0.1122
REMARK 3 L TENSOR
REMARK 3 L11: 0.2349 L22: 1.0885
REMARK 3 L33: 0.1041 L12: 0.0994
REMARK 3 L13: -0.1083 L23: 0.3391
REMARK 3 S TENSOR
REMARK 3 S11: 0.2901 S12: -0.2804 S13: -0.1067
REMARK 3 S21: 0.2366 S22: -0.1232 S23: -0.0693
REMARK 3 S31: -0.0815 S32: 0.6815 S33: 0.0059
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 401 THROUGH 443 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.4852 -17.9708 46.0991
REMARK 3 T TENSOR
REMARK 3 T11: 0.8976 T22: 0.7554
REMARK 3 T33: 0.6367 T12: 0.2219
REMARK 3 T13: -0.0986 T23: 0.0956
REMARK 3 L TENSOR
REMARK 3 L11: 0.4543 L22: 0.2414
REMARK 3 L33: 0.2302 L12: 0.1887
REMARK 3 L13: 0.1795 L23: -0.1331
REMARK 3 S TENSOR
REMARK 3 S11: 0.1031 S12: -0.1564 S13: -0.2551
REMARK 3 S21: -0.0000 S22: -0.3037 S23: 0.4621
REMARK 3 S31: 0.0713 S32: 0.1578 S33: -0.0001
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 444 THROUGH 490 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.5201 -4.4320 29.7670
REMARK 3 T TENSOR
REMARK 3 T11: 0.5745 T22: 0.3930
REMARK 3 T33: 0.5007 T12: -0.0243
REMARK 3 T13: -0.0329 T23: 0.0333
REMARK 3 L TENSOR
REMARK 3 L11: 0.3358 L22: 0.2415
REMARK 3 L33: 0.5951 L12: -0.8237
REMARK 3 L13: 0.0625 L23: -0.0717
REMARK 3 S TENSOR
REMARK 3 S11: 0.2921 S12: -0.3240 S13: -0.1073
REMARK 3 S21: 0.0061 S22: -0.1367 S23: 0.0324
REMARK 3 S31: 0.1331 S32: -0.0248 S33: 0.0000
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 5U0L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1000224474.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57651
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.285
REMARK 200 RESOLUTION RANGE LOW (A) : 92.041
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 14.60
REMARK 200 R MERGE (I) : 0.17100
REMARK 200 R SYM (I) : 0.17100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : 14.10
REMARK 200 R MERGE FOR SHELL (I) : 5.19000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: PHASER
REMARK 200 STARTING MODEL: 3JU8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50%MPD, PH 7, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 127.36250
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 49.35500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 49.35500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 63.68125
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 49.35500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 49.35500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 191.04375
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 49.35500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.35500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 63.68125
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 49.35500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.35500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 191.04375
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 127.36250
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: 10140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 MET A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 ALA A 2
REMARK 465 ASP A 491
REMARK 465 MET B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 HIS B 1
REMARK 465 ALA B 2
REMARK 465 ASN B 3
REMARK 465 ASP B 491
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 OE2 GLU B 98 OG SER B 277 2.03
REMARK 500 O GLY A 279 NH2 ARG A 286 2.11
REMARK 500 OE2 GLU B 314 NZ LYS B 357 2.14
REMARK 500 NH2 ARG A 60 OE1 GLU B 425 2.15
REMARK 500 NZ LYS A 477 OG SER B 261 2.19
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 LEU A 165 CA - CB - CG ANGL. DEV. = 13.9 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 THR A 121 45.40 -141.00
REMARK 500 GLN A 240 63.27 -118.82
REMARK 500 ASN A 259 64.20 76.20
REMARK 500 ASP A 359 60.07 -109.83
REMARK 500 LYS A 391 -83.79 -108.87
REMARK 500 THR A 403 146.21 -174.32
REMARK 500 LEU A 407 -73.05 -90.21
REMARK 500 VAL A 449 -166.89 -109.89
REMARK 500 SER A 458 -147.78 -101.29
REMARK 500 ALA A 459 -126.98 47.93
REMARK 500 GLU B 176 -7.70 -59.56
REMARK 500 ASN B 259 64.97 72.42
REMARK 500 ASP B 359 65.55 -116.73
REMARK 500 LYS B 391 -78.61 -107.06
REMARK 500 THR B 403 148.59 -173.84
REMARK 500 LEU B 407 -75.30 -91.53
REMARK 500 VAL B 449 -166.97 -107.89
REMARK 500 SER B 458 -148.83 -102.63
REMARK 500 ALA B 459 -123.31 43.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 8YP A 507
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8YP A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5U0M RELATED DB: PDB
DBREF 5U0L A 2 491 UNP A1U5W8 ASTD_MARHV 2 491
DBREF 5U0L B 2 491 UNP A1U5W8 ASTD_MARHV 2 491
SEQADV 5U0L MET A -5 UNP A1U5W8 INITIATING METHIONINE
SEQADV 5U0L HIS A -4 UNP A1U5W8 EXPRESSION TAG
SEQADV 5U0L HIS A -3 UNP A1U5W8 EXPRESSION TAG
SEQADV 5U0L HIS A -2 UNP A1U5W8 EXPRESSION TAG
SEQADV 5U0L HIS A -1 UNP A1U5W8 EXPRESSION TAG
SEQADV 5U0L HIS A 0 UNP A1U5W8 EXPRESSION TAG
SEQADV 5U0L HIS A 1 UNP A1U5W8 EXPRESSION TAG
SEQADV 5U0L MET B -5 UNP A1U5W8 INITIATING METHIONINE
SEQADV 5U0L HIS B -4 UNP A1U5W8 EXPRESSION TAG
SEQADV 5U0L HIS B -3 UNP A1U5W8 EXPRESSION TAG
SEQADV 5U0L HIS B -2 UNP A1U5W8 EXPRESSION TAG
SEQADV 5U0L HIS B -1 UNP A1U5W8 EXPRESSION TAG
SEQADV 5U0L HIS B 0 UNP A1U5W8 EXPRESSION TAG
SEQADV 5U0L HIS B 1 UNP A1U5W8 EXPRESSION TAG
SEQRES 1 A 497 MET HIS HIS HIS HIS HIS HIS ALA ASN LEU THR GLY ASN
SEQRES 2 A 497 VAL TYR ILE ASP GLY LEU TRP LEU PRO GLY HIS GLY ALA
SEQRES 3 A 497 PRO PHE GLU SER VAL GLN PRO VAL THR GLY GLU THR VAL
SEQRES 4 A 497 TRP ASP GLY ASN ALA ALA SER LEU GLU ASP VAL ASP ALA
SEQRES 5 A 497 ALA VAL ARG GLU ALA ARG LYS ALA PHE LEU ALA TRP ARG
SEQRES 6 A 497 ARG LYS SER LEU ALA GLU ARG GLN ALA VAL ILE GLU ALA
SEQRES 7 A 497 PHE GLY GLU LEU LEU GLU ALA ASN LYS GLU GLU LEU ALA
SEQRES 8 A 497 HIS GLN ILE GLY LEU GLU THR GLY LYS PRO LEU TRP GLU
SEQRES 9 A 497 SER ARG THR GLU VAL ALA ALA MET MET GLY LYS ILE PRO
SEQRES 10 A 497 ILE SER VAL LYS ALA TYR ASN GLU ARG THR GLY HIS THR
SEQRES 11 A 497 GLU SER ASP VAL ALA GLY GLY HIS ALA VAL LEU ARG HIS
SEQRES 12 A 497 ARG PRO HIS GLY VAL VAL ALA VAL PHE GLY PRO TYR ASN
SEQRES 13 A 497 PHE PRO GLY HIS LEU PRO ASN GLY HIS ILE VAL PRO ALA
SEQRES 14 A 497 LEU LEU ALA GLY ASN THR VAL VAL PHE LYS PRO SER GLU
SEQRES 15 A 497 LEU THR PRO GLY VAL ALA GLU LEU THR VAL ARG LEU TRP
SEQRES 16 A 497 GLU LYS ALA GLY LEU PRO ASP GLY VAL ILE ASN LEU VAL
SEQRES 17 A 497 GLN GLY GLY SER ASP THR GLY LYS CYS LEU ALA ARG HIS
SEQRES 18 A 497 SER LEU ILE ASP GLY LEU PHE PHE THR GLY SER SER THR
SEQRES 19 A 497 VAL GLY HIS LEU LEU HIS GLU GLN PHE GLY GLY GLN PRO
SEQRES 20 A 497 GLU LYS ILE LEU ALA LEU GLU MET GLY GLY ASN ASN PRO
SEQRES 21 A 497 LEU ILE VAL GLN ASN VAL SER ASP LEU ASP GLY ALA VAL
SEQRES 22 A 497 HIS HIS ALA LEU GLN SER ALA PHE LEU SER ALA GLY GLN
SEQRES 23 A 497 ARG CYS THR CYS ALA ARG ARG LEU LEU VAL PRO LYS GLY
SEQRES 24 A 497 LYS LYS GLY ASP GLU PHE LEU ALA ARG LEU VAL GLU VAL
SEQRES 25 A 497 ALA ALA ARG ILE THR VAL ALA GLU PHE ASP ALA ASP PRO
SEQRES 26 A 497 GLN PRO PHE MET GLY SER VAL ILE SER ALA GLU ALA ALA
SEQRES 27 A 497 ASN GLN LEU LEU LYS ALA GLN ALA ALA MET LEU GLU LYS
SEQRES 28 A 497 GLY ALA THR SER LEU LEU GLU MET LYS GLN LEU LYS PRO
SEQRES 29 A 497 ASP THR GLY LEU LEU SER PRO GLY ILE VAL ASP ALA THR
SEQRES 30 A 497 GLY ILE GLU LEU GLU ASP GLN GLU PHE PHE GLY PRO LEU
SEQRES 31 A 497 LEU THR VAL TYR ARG TYR LYS GLY PHE ASP GLU ALA LEU
SEQRES 32 A 497 GLU LEU ALA ASN ASN THR ARG TYR GLY LEU SER ALA GLY
SEQRES 33 A 497 ILE LEU SER ASP ASP ARG LYS LEU TYR ASN ARG LEU VAL
SEQRES 34 A 497 GLU GLU VAL ARG ALA GLY ILE VAL ASN TRP ASN ARG PRO
SEQRES 35 A 497 LEU THR GLY ALA SER SER ALA ALA PRO PHE GLY GLY VAL
SEQRES 36 A 497 GLY ALA SER GLY ASN HIS ARG PRO SER ALA TYR TYR ALA
SEQRES 37 A 497 ALA ASP TYR CYS ALA TRP PRO MET ALA SER LEU GLU ALA
SEQRES 38 A 497 GLY LYS SER GLU LEU PRO ASP SER LEU ALA PRO GLY LEU
SEQRES 39 A 497 ASN PHE ASP
SEQRES 1 B 497 MET HIS HIS HIS HIS HIS HIS ALA ASN LEU THR GLY ASN
SEQRES 2 B 497 VAL TYR ILE ASP GLY LEU TRP LEU PRO GLY HIS GLY ALA
SEQRES 3 B 497 PRO PHE GLU SER VAL GLN PRO VAL THR GLY GLU THR VAL
SEQRES 4 B 497 TRP ASP GLY ASN ALA ALA SER LEU GLU ASP VAL ASP ALA
SEQRES 5 B 497 ALA VAL ARG GLU ALA ARG LYS ALA PHE LEU ALA TRP ARG
SEQRES 6 B 497 ARG LYS SER LEU ALA GLU ARG GLN ALA VAL ILE GLU ALA
SEQRES 7 B 497 PHE GLY GLU LEU LEU GLU ALA ASN LYS GLU GLU LEU ALA
SEQRES 8 B 497 HIS GLN ILE GLY LEU GLU THR GLY LYS PRO LEU TRP GLU
SEQRES 9 B 497 SER ARG THR GLU VAL ALA ALA MET MET GLY LYS ILE PRO
SEQRES 10 B 497 ILE SER VAL LYS ALA TYR ASN GLU ARG THR GLY HIS THR
SEQRES 11 B 497 GLU SER ASP VAL ALA GLY GLY HIS ALA VAL LEU ARG HIS
SEQRES 12 B 497 ARG PRO HIS GLY VAL VAL ALA VAL PHE GLY PRO TYR ASN
SEQRES 13 B 497 PHE PRO GLY HIS LEU PRO ASN GLY HIS ILE VAL PRO ALA
SEQRES 14 B 497 LEU LEU ALA GLY ASN THR VAL VAL PHE LYS PRO SER GLU
SEQRES 15 B 497 LEU THR PRO GLY VAL ALA GLU LEU THR VAL ARG LEU TRP
SEQRES 16 B 497 GLU LYS ALA GLY LEU PRO ASP GLY VAL ILE ASN LEU VAL
SEQRES 17 B 497 GLN GLY GLY SER ASP THR GLY LYS CYS LEU ALA ARG HIS
SEQRES 18 B 497 SER LEU ILE ASP GLY LEU PHE PHE THR GLY SER SER THR
SEQRES 19 B 497 VAL GLY HIS LEU LEU HIS GLU GLN PHE GLY GLY GLN PRO
SEQRES 20 B 497 GLU LYS ILE LEU ALA LEU GLU MET GLY GLY ASN ASN PRO
SEQRES 21 B 497 LEU ILE VAL GLN ASN VAL SER ASP LEU ASP GLY ALA VAL
SEQRES 22 B 497 HIS HIS ALA LEU GLN SER ALA PHE LEU SER ALA GLY GLN
SEQRES 23 B 497 ARG CYS THR CYS ALA ARG ARG LEU LEU VAL PRO LYS GLY
SEQRES 24 B 497 LYS LYS GLY ASP GLU PHE LEU ALA ARG LEU VAL GLU VAL
SEQRES 25 B 497 ALA ALA ARG ILE THR VAL ALA GLU PHE ASP ALA ASP PRO
SEQRES 26 B 497 GLN PRO PHE MET GLY SER VAL ILE SER ALA GLU ALA ALA
SEQRES 27 B 497 ASN GLN LEU LEU LYS ALA GLN ALA ALA MET LEU GLU LYS
SEQRES 28 B 497 GLY ALA THR SER LEU LEU GLU MET LYS GLN LEU LYS PRO
SEQRES 29 B 497 ASP THR GLY LEU LEU SER PRO GLY ILE VAL ASP ALA THR
SEQRES 30 B 497 GLY ILE GLU LEU GLU ASP GLN GLU PHE PHE GLY PRO LEU
SEQRES 31 B 497 LEU THR VAL TYR ARG TYR LYS GLY PHE ASP GLU ALA LEU
SEQRES 32 B 497 GLU LEU ALA ASN ASN THR ARG TYR GLY LEU SER ALA GLY
SEQRES 33 B 497 ILE LEU SER ASP ASP ARG LYS LEU TYR ASN ARG LEU VAL
SEQRES 34 B 497 GLU GLU VAL ARG ALA GLY ILE VAL ASN TRP ASN ARG PRO
SEQRES 35 B 497 LEU THR GLY ALA SER SER ALA ALA PRO PHE GLY GLY VAL
SEQRES 36 B 497 GLY ALA SER GLY ASN HIS ARG PRO SER ALA TYR TYR ALA
SEQRES 37 B 497 ALA ASP TYR CYS ALA TRP PRO MET ALA SER LEU GLU ALA
SEQRES 38 B 497 GLY LYS SER GLU LEU PRO ASP SER LEU ALA PRO GLY LEU
SEQRES 39 B 497 ASN PHE ASP
HET EDO A 501 10
HET EDO A 502 10
HET EDO A 503 10
HET EDO A 504 10
HET EDO A 505 10
HET EDO A 506 10
HET 8YP A 507 25
HET EDO A 508 10
HET EDO A 509 10
HET MPD B 501 8
HET MPD B 502 8
HET CL B 503 1
HET PO4 B 504 5
HETNAM EDO 1,2-ETHANEDIOL
HETNAM 8YP DECANAL
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM CL CHLORIDE ION
HETNAM PO4 PHOSPHATE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 8(C2 H6 O2)
FORMUL 9 8YP C10 H20 O
FORMUL 12 MPD 2(C6 H14 O2)
FORMUL 14 CL CL 1-
FORMUL 15 PO4 O4 P 3-
FORMUL 16 HOH *60(H2 O)
HELIX 1 AA1 SER A 40 ARG A 59 1 20
HELIX 2 AA2 SER A 62 ASN A 80 1 19
HELIX 3 AA3 ASN A 80 GLY A 93 1 14
HELIX 4 AA4 PRO A 95 THR A 121 1 27
HELIX 5 AA5 GLY A 153 ALA A 166 1 14
HELIX 6 AA6 THR A 178 ALA A 192 1 15
HELIX 7 AA7 GLY A 205 ARG A 214 1 10
HELIX 8 AA8 SER A 226 PHE A 237 1 12
HELIX 9 AA9 ASP A 262 LEU A 276 1 15
HELIX 10 AB1 SER A 277 GLN A 280 5 4
HELIX 11 AB2 GLY A 293 ALA A 308 1 16
HELIX 12 AB3 SER A 328 LYS A 345 1 18
HELIX 13 AB4 GLY A 392 ASN A 401 1 10
HELIX 14 AB5 ASP A 415 VAL A 426 1 12
HELIX 15 AB6 VAL A 449 GLY A 453 5 5
HELIX 16 AB7 TYR A 461 CYS A 466 1 6
HELIX 17 AB8 SER B 40 ARG B 59 1 20
HELIX 18 AB9 SER B 62 ASN B 80 1 19
HELIX 19 AC1 ASN B 80 GLY B 93 1 14
HELIX 20 AC2 PRO B 95 THR B 121 1 27
HELIX 21 AC3 GLY B 153 ALA B 166 1 14
HELIX 22 AC4 THR B 178 ALA B 192 1 15
HELIX 23 AC5 GLY B 205 ARG B 214 1 10
HELIX 24 AC6 SER B 226 PHE B 237 1 12
HELIX 25 AC7 ASP B 262 LEU B 276 1 15
HELIX 26 AC8 SER B 277 GLY B 279 5 3
HELIX 27 AC9 GLY B 293 ALA B 308 1 16
HELIX 28 AD1 SER B 328 LYS B 345 1 18
HELIX 29 AD2 GLY B 392 ASN B 401 1 10
HELIX 30 AD3 ASP B 415 VAL B 426 1 12
HELIX 31 AD4 VAL B 449 GLY B 453 5 5
HELIX 32 AD5 TYR B 461 CYS B 466 1 6
SHEET 1 AA1 2 VAL A 8 ILE A 10 0
SHEET 2 AA1 2 LEU A 13 LEU A 15 -1 O LEU A 13 N ILE A 10
SHEET 1 AA2 2 PRO A 21 VAL A 25 0
SHEET 2 AA2 2 THR A 32 ASN A 37 -1 O VAL A 33 N SER A 24
SHEET 1 AA3 3 THR A 124 VAL A 128 0
SHEET 2 AA3 3 GLY A 131 PRO A 139 -1 O ALA A 133 N SER A 126
SHEET 3 AA3 3 ALA A 467 GLU A 474 -1 O GLU A 474 N HIS A 132
SHEET 1 AA4 5 ILE A 199 LEU A 201 0
SHEET 2 AA4 5 THR A 169 LYS A 173 1 N PHE A 172 O ASN A 200
SHEET 3 AA4 5 VAL A 142 PHE A 146 1 N VAL A 145 O LYS A 173
SHEET 4 AA4 5 GLY A 220 THR A 224 1 O PHE A 222 N ALA A 144
SHEET 5 AA4 5 ILE A 244 GLU A 248 1 O ALA A 246 N PHE A 223
SHEET 1 AA5 7 THR A 348 LEU A 351 0
SHEET 2 AA5 7 GLY A 366 ASP A 369 -1 O ASP A 369 N THR A 348
SHEET 3 AA5 7 LEU A 384 TYR A 390 1 O VAL A 387 N VAL A 368
SHEET 4 AA5 7 ALA A 285 PRO A 291 1 N LEU A 288 O THR A 386
SHEET 5 AA5 7 ASN A 253 VAL A 257 1 N LEU A 255 O LEU A 289
SHEET 6 AA5 7 SER A 408 LEU A 412 1 O LEU A 412 N ILE A 256
SHEET 7 AA5 7 ILE A 430 TRP A 433 1 O ASN A 432 N ILE A 411
SHEET 1 AA6 2 PRO A 445 PHE A 446 0
SHEET 2 AA6 2 SER A 458 ALA A 459 -1 O SER A 458 N PHE A 446
SHEET 1 AA7 2 VAL B 8 ILE B 10 0
SHEET 2 AA7 2 LEU B 13 LEU B 15 -1 O LEU B 15 N VAL B 8
SHEET 1 AA8 2 PRO B 21 VAL B 25 0
SHEET 2 AA8 2 THR B 32 ASN B 37 -1 O VAL B 33 N SER B 24
SHEET 1 AA9 3 THR B 124 VAL B 128 0
SHEET 2 AA9 3 GLY B 131 PRO B 139 -1 O ALA B 133 N SER B 126
SHEET 3 AA9 3 ALA B 467 GLU B 474 -1 O GLU B 474 N HIS B 132
SHEET 1 AB1 5 ILE B 199 LEU B 201 0
SHEET 2 AB1 5 THR B 169 LYS B 173 1 N PHE B 172 O ASN B 200
SHEET 3 AB1 5 VAL B 142 PHE B 146 1 N VAL B 145 O LYS B 173
SHEET 4 AB1 5 GLY B 220 THR B 224 1 O PHE B 222 N ALA B 144
SHEET 5 AB1 5 ILE B 244 GLU B 248 1 O ALA B 246 N PHE B 223
SHEET 1 AB2 7 THR B 348 LEU B 351 0
SHEET 2 AB2 7 GLY B 366 ASP B 369 -1 O ASP B 369 N THR B 348
SHEET 3 AB2 7 LEU B 384 TYR B 390 1 O LEU B 385 N GLY B 366
SHEET 4 AB2 7 ALA B 285 PRO B 291 1 N LEU B 288 O THR B 386
SHEET 5 AB2 7 ASN B 253 VAL B 257 1 N LEU B 255 O LEU B 289
SHEET 6 AB2 7 SER B 408 LEU B 412 1 O GLY B 410 N ILE B 256
SHEET 7 AB2 7 ILE B 430 TRP B 433 1 O ASN B 432 N ILE B 411
SHEET 1 AB3 2 PRO B 445 PHE B 446 0
SHEET 2 AB3 2 SER B 458 ALA B 459 -1 O SER B 458 N PHE B 446
SITE 1 AC1 3 PHE A 393 ASP A 394 ARG A 421
SITE 1 AC2 7 GLY A 147 LYS A 173 PRO A 174 SER A 175
SITE 2 AC2 7 GLU A 176 EDO A 508 HOH A 622
SITE 1 AC3 4 SER A 441 SER A 442 HOH A 608 VAL B 128
SITE 1 AC4 3 HIS A 123 ARG A 136 ARG A 138
SITE 1 AC5 5 ASN A 252 ARG A 287 GLU A 376 TYR A 388
SITE 2 AC5 5 ASN A 402
SITE 1 AC6 5 PRO A 457 TYR A 461 ASP A 464 ASP B 464
SITE 2 AC6 5 PRO B 469
SITE 1 AC7 8 LYS A 109 HIS A 154 LEU A 155 GLY A 158
SITE 2 AC7 8 HIS A 159 THR A 224 SER A 458 ALA A 459
SITE 1 AC8 2 SER A 206 EDO A 502
SITE 1 AC9 3 CYS A 282 THR A 283 THR A 438
SITE 1 AD1 3 GLN B 258 PHE B 393 ARG B 421
SITE 1 AD2 5 HIS A 234 ASN A 454 ARG A 456 LEU B 245
SITE 2 AD2 5 ARG B 456
SITE 1 AD3 1 ARG B 138
SITE 1 AD4 4 ASP A 359 ARG A 416 GLU B 125 GLU B 474
CRYST1 98.710 98.710 254.725 90.00 90.00 90.00 P 41 21 2 16
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 0.010131 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010131 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003926 0.00000
(ATOM LINES ARE NOT SHOWN.)
END