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HEADER HYDROLASE 09-JAN-20 6VHD
TITLE FPHF, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
TITLE 2 HYDROLASES F, KT129 BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE FAMILY PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: PUTATIVE ESTERASE,TRIBUTYRIN ESTERASE;
COMPND 5 EC: 3.1.2.12;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 GENE: EP54_00010, EQ90_02595, HMPREF3211_01237, NCTC10654_02801,
SOURCE 5 NCTC10702_04070, RK64_00235;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: M1366
KEYWDS FPHF, FLUOROPHOSPHONATE-BINDING, SERINE HYDROLASES, SODIUM BOUND,
KEYWDS 2 ACYL, KT129, INTERMEDIATE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER,P.D.MACE
REVDAT 1 16-SEP-20 6VHD 0
JRNL AUTH M.FELLNER,C.S.LENTZ,S.A.JAMIESON,J.L.BREWSTER,L.CHEN,
JRNL AUTH 2 M.BOGYO,P.D.MACE
JRNL TITL STRUCTURAL BASIS FOR THE INHIBITOR AND SUBSTRATE SPECIFICITY
JRNL TITL 2 OF THE UNIQUE FPH SERINE HYDROLASES OF STAPHYLOCOCCUS
JRNL TITL 3 AUREUS.
JRNL REF ACS INFECT DIS. 2020
JRNL REFN ESSN 2373-8227
JRNL PMID 32865965
JRNL DOI 10.1021/ACSINFECDIS.0C00503
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV-3699
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.28
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.910
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 72838
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 6711
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.2800 - 6.1500 1.00 4269 226 0.1604 0.1851
REMARK 3 2 6.1500 - 4.8800 1.00 4281 213 0.1531 0.1716
REMARK 3 3 4.8800 - 4.2700 1.00 4272 231 0.1251 0.1712
REMARK 3 4 4.2600 - 3.8800 1.00 4257 241 0.1385 0.1984
REMARK 3 5 3.8800 - 3.6000 1.00 4198 266 0.1444 0.1747
REMARK 3 6 3.6000 - 3.3900 1.00 4279 230 0.1564 0.1677
REMARK 3 7 3.3900 - 3.2200 1.00 4223 250 0.1740 0.2294
REMARK 3 8 3.2200 - 3.0800 1.00 4294 211 0.1904 0.1999
REMARK 3 9 3.0800 - 2.9600 1.00 4310 188 0.1847 0.2300
REMARK 3 10 2.9600 - 2.8600 1.00 4256 227 0.1878 0.1982
REMARK 3 11 2.8600 - 2.7700 1.00 4315 226 0.1812 0.2414
REMARK 3 12 2.7700 - 2.6900 1.00 4276 191 0.1820 0.2341
REMARK 3 13 2.6900 - 2.6200 1.00 4295 196 0.1805 0.1958
REMARK 3 14 2.6200 - 2.5500 1.00 4244 222 0.2007 0.2808
REMARK 3 15 2.5500 - 2.4900 1.00 4267 219 0.1972 0.2841
REMARK 3 16 2.4900 - 2.4400 1.00 4261 245 0.2043 0.2741
REMARK 3 17 2.4400 - 2.3900 1.00 4304 221 0.2066 0.2673
REMARK 3 18 2.3900 - 2.3500 1.00 4218 219 0.2074 0.2366
REMARK 3 19 2.3500 - 2.3100 1.00 4292 215 0.2135 0.2144
REMARK 3 20 2.3100 - 2.2700 1.00 4294 216 0.2158 0.2401
REMARK 3 21 2.2700 - 2.2300 1.00 4237 210 0.2231 0.2965
REMARK 3 22 2.2300 - 2.2000 1.00 4276 237 0.2263 0.2553
REMARK 3 23 2.2000 - 2.1600 1.00 4295 214 0.2354 0.2927
REMARK 3 24 2.1600 - 2.1300 1.00 4238 219 0.2345 0.2807
REMARK 3 25 2.1300 - 2.1000 1.00 4327 236 0.2501 0.2939
REMARK 3 26 2.1000 - 2.0800 1.00 4191 233 0.2610 0.3236
REMARK 3 27 2.0800 - 2.0500 1.00 4322 235 0.2798 0.2855
REMARK 3 28 2.0500 - 2.0300 1.00 4184 216 0.2714 0.3247
REMARK 3 29 2.0300 - 2.0000 1.00 4319 253 0.2820 0.3022
REMARK 3 30 2.0000 - 1.9800 0.97 4055 205 0.3005 0.3331
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.040
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.94
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 : 32
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID -1 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.1209 33.7418 -11.7352
REMARK 3 T TENSOR
REMARK 3 T11: 0.2502 T22: 0.3068
REMARK 3 T33: 0.3056 T12: 0.0897
REMARK 3 T13: 0.0071 T23: 0.0498
REMARK 3 L TENSOR
REMARK 3 L11: 1.1434 L22: 2.5436
REMARK 3 L33: 2.2143 L12: 1.3335
REMARK 3 L13: 1.8276 L23: 1.8851
REMARK 3 S TENSOR
REMARK 3 S11: 0.0337 S12: -0.1363 S13: -0.0084
REMARK 3 S21: -0.1949 S22: 0.1046 S23: -0.3121
REMARK 3 S31: 0.2002 S32: 0.5455 S33: -0.1804
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 25 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): -43.7634 22.4596 -27.3850
REMARK 3 T TENSOR
REMARK 3 T11: 0.5631 T22: 0.3879
REMARK 3 T33: 0.3912 T12: 0.0007
REMARK 3 T13: -0.0755 T23: -0.0590
REMARK 3 L TENSOR
REMARK 3 L11: 8.8748 L22: 2.0957
REMARK 3 L33: 9.8257 L12: -5.7791
REMARK 3 L13: 7.0367 L23: -9.6923
REMARK 3 S TENSOR
REMARK 3 S11: 0.5599 S12: 0.6476 S13: -0.4032
REMARK 3 S21: -0.9154 S22: -0.0432 S23: 0.2906
REMARK 3 S31: 1.0610 S32: -0.0937 S33: -0.4782
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 41 THROUGH 105 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.5255 26.8527 -7.4674
REMARK 3 T TENSOR
REMARK 3 T11: 0.1779 T22: 0.2105
REMARK 3 T33: 0.2565 T12: 0.0374
REMARK 3 T13: -0.0030 T23: 0.0677
REMARK 3 L TENSOR
REMARK 3 L11: 1.6198 L22: 1.3015
REMARK 3 L33: 4.1657 L12: 0.2405
REMARK 3 L13: -0.3185 L23: 0.3374
REMARK 3 S TENSOR
REMARK 3 S11: 0.0933 S12: 0.0118 S13: 0.0864
REMARK 3 S21: 0.0262 S22: -0.1128 S23: -0.1199
REMARK 3 S31: 0.1851 S32: 0.1257 S33: 0.0196
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 106 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.9354 17.4788 -4.0227
REMARK 3 T TENSOR
REMARK 3 T11: 0.2991 T22: 0.2006
REMARK 3 T33: 0.2780 T12: 0.0133
REMARK 3 T13: 0.0369 T23: 0.0236
REMARK 3 L TENSOR
REMARK 3 L11: 4.5313 L22: 4.3701
REMARK 3 L33: 7.5640 L12: 0.3143
REMARK 3 L13: 2.4242 L23: -1.1938
REMARK 3 S TENSOR
REMARK 3 S11: 0.3098 S12: -0.3898 S13: -0.5248
REMARK 3 S21: 0.2785 S22: -0.1206 S23: 0.1083
REMARK 3 S31: 0.6376 S32: -0.2157 S33: -0.2080
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 150 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.9084 28.0317 10.5452
REMARK 3 T TENSOR
REMARK 3 T11: 0.4242 T22: 0.6514
REMARK 3 T33: 0.4425 T12: 0.0337
REMARK 3 T13: -0.0785 T23: 0.0649
REMARK 3 L TENSOR
REMARK 3 L11: 9.1395 L22: 8.8293
REMARK 3 L33: 4.8764 L12: 2.4576
REMARK 3 L13: -1.5328 L23: -3.4235
REMARK 3 S TENSOR
REMARK 3 S11: 0.2368 S12: -0.7237 S13: -0.9189
REMARK 3 S21: 0.4060 S22: -0.5368 S23: -1.0809
REMARK 3 S31: 0.4176 S32: 1.1375 S33: 0.3084
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 168 THROUGH 189 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.5529 16.8737 13.3493
REMARK 3 T TENSOR
REMARK 3 T11: 0.6058 T22: 0.3780
REMARK 3 T33: 0.3862 T12: 0.0051
REMARK 3 T13: 0.0128 T23: 0.1303
REMARK 3 L TENSOR
REMARK 3 L11: 5.8697 L22: 2.2394
REMARK 3 L33: 9.2358 L12: 4.9470
REMARK 3 L13: 3.3772 L23: 8.9389
REMARK 3 S TENSOR
REMARK 3 S11: 0.0415 S12: -0.6712 S13: 0.0007
REMARK 3 S21: 1.3329 S22: -0.1666 S23: 0.5787
REMARK 3 S31: 1.1102 S32: -0.1157 S33: 0.0557
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 190 THROUGH 207 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.2596 10.6727 -0.3425
REMARK 3 T TENSOR
REMARK 3 T11: 0.4506 T22: 0.2208
REMARK 3 T33: 0.3462 T12: 0.0491
REMARK 3 T13: -0.0219 T23: 0.1216
REMARK 3 L TENSOR
REMARK 3 L11: 6.8558 L22: 3.4944
REMARK 3 L33: 5.7484 L12: -0.8901
REMARK 3 L13: 0.7316 L23: 0.2289
REMARK 3 S TENSOR
REMARK 3 S11: -0.1180 S12: -0.3205 S13: -0.4973
REMARK 3 S21: 0.1365 S22: -0.0794 S23: -0.0722
REMARK 3 S31: 0.7713 S32: 0.0961 S33: 0.1811
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 208 THROUGH 235 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.5865 7.1917 1.9390
REMARK 3 T TENSOR
REMARK 3 T11: 0.5039 T22: 0.3067
REMARK 3 T33: 0.4091 T12: 0.1429
REMARK 3 T13: -0.0258 T23: 0.0963
REMARK 3 L TENSOR
REMARK 3 L11: 6.2886 L22: 5.0988
REMARK 3 L33: 4.0572 L12: 2.7558
REMARK 3 L13: 0.0675 L23: -1.2164
REMARK 3 S TENSOR
REMARK 3 S11: 0.1093 S12: -0.2578 S13: -0.5824
REMARK 3 S21: 0.2982 S22: -0.1716 S23: -0.3279
REMARK 3 S31: 0.8604 S32: 0.4279 S33: 0.0908
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 236 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.0060 13.6686 -12.7454
REMARK 3 T TENSOR
REMARK 3 T11: 0.4266 T22: 0.2865
REMARK 3 T33: 0.3515 T12: 0.1546
REMARK 3 T13: 0.0140 T23: 0.0439
REMARK 3 L TENSOR
REMARK 3 L11: 6.7680 L22: 6.6233
REMARK 3 L33: 7.9118 L12: 5.4409
REMARK 3 L13: 3.9304 L23: 3.5422
REMARK 3 S TENSOR
REMARK 3 S11: 0.3963 S12: 0.0608 S13: -0.7155
REMARK 3 S21: 0.3452 S22: -0.1819 S23: -0.3232
REMARK 3 S31: 0.8399 S32: 0.2544 S33: -0.2205
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID -1 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.5705 49.0926 -15.1461
REMARK 3 T TENSOR
REMARK 3 T11: 0.2098 T22: 0.3848
REMARK 3 T33: 0.3488 T12: 0.0223
REMARK 3 T13: 0.0430 T23: 0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 1.5668 L22: 5.6556
REMARK 3 L33: 5.8842 L12: 1.0216
REMARK 3 L13: -0.2891 L23: -2.2255
REMARK 3 S TENSOR
REMARK 3 S11: -0.0524 S12: 0.2807 S13: 0.1232
REMARK 3 S21: -0.4097 S22: 0.0508 S23: -0.3263
REMARK 3 S31: -0.3999 S32: 0.3429 S33: 0.0001
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 41 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.5974 51.9711 -4.2099
REMARK 3 T TENSOR
REMARK 3 T11: 0.1885 T22: 0.2199
REMARK 3 T33: 0.2609 T12: -0.0235
REMARK 3 T13: 0.0168 T23: -0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 1.9948 L22: 1.4892
REMARK 3 L33: 5.9995 L12: -0.3888
REMARK 3 L13: 0.4514 L23: -0.3991
REMARK 3 S TENSOR
REMARK 3 S11: 0.1169 S12: 0.0064 S13: 0.0635
REMARK 3 S21: 0.0228 S22: -0.0619 S23: -0.0222
REMARK 3 S31: -0.4845 S32: 0.1995 S33: -0.0668
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 134 THROUGH 162 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.0325 53.7538 6.2881
REMARK 3 T TENSOR
REMARK 3 T11: 0.3259 T22: 0.4552
REMARK 3 T33: 0.3278 T12: 0.0070
REMARK 3 T13: -0.0025 T23: -0.0298
REMARK 3 L TENSOR
REMARK 3 L11: 2.8704 L22: 7.1099
REMARK 3 L33: 4.2055 L12: 2.3017
REMARK 3 L13: 0.3136 L23: -0.0746
REMARK 3 S TENSOR
REMARK 3 S11: 0.2703 S12: -0.5315 S13: 0.0921
REMARK 3 S21: 0.3118 S22: -0.2379 S23: 0.5969
REMARK 3 S31: -0.2469 S32: -0.5061 S33: -0.0440
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 163 THROUGH 189 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.3634 53.7205 16.4740
REMARK 3 T TENSOR
REMARK 3 T11: 0.2977 T22: 0.4196
REMARK 3 T33: 0.2942 T12: -0.0190
REMARK 3 T13: 0.0177 T23: -0.0469
REMARK 3 L TENSOR
REMARK 3 L11: 2.4711 L22: 7.8280
REMARK 3 L33: 7.5755 L12: 3.0043
REMARK 3 L13: 0.8532 L23: 2.8551
REMARK 3 S TENSOR
REMARK 3 S11: 0.3668 S12: -0.4076 S13: 0.0611
REMARK 3 S21: 0.6212 S22: -0.3593 S23: 0.1093
REMARK 3 S31: -0.2887 S32: -0.0313 S33: -0.0235
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 190 THROUGH 220 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.1345 66.0101 6.9544
REMARK 3 T TENSOR
REMARK 3 T11: 0.7118 T22: 0.3088
REMARK 3 T33: 0.4209 T12: 0.0389
REMARK 3 T13: 0.0777 T23: -0.0290
REMARK 3 L TENSOR
REMARK 3 L11: 5.7287 L22: 4.7764
REMARK 3 L33: 8.4012 L12: 0.2336
REMARK 3 L13: 2.0777 L23: 1.3139
REMARK 3 S TENSOR
REMARK 3 S11: -0.0015 S12: -0.4704 S13: 0.6886
REMARK 3 S21: 0.3390 S22: -0.0414 S23: 0.0121
REMARK 3 S31: -1.6053 S32: -0.3158 S33: 0.0892
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 221 THROUGH 235 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.8268 67.7760 1.9886
REMARK 3 T TENSOR
REMARK 3 T11: 0.7717 T22: 0.4726
REMARK 3 T33: 0.5407 T12: 0.1157
REMARK 3 T13: 0.1048 T23: -0.1141
REMARK 3 L TENSOR
REMARK 3 L11: 2.2018 L22: 9.6861
REMARK 3 L33: 8.1568 L12: 3.3283
REMARK 3 L13: 5.0989 L23: 2.5477
REMARK 3 S TENSOR
REMARK 3 S11: -0.3107 S12: -0.2502 S13: 0.8804
REMARK 3 S21: -0.3277 S22: -0.1134 S23: 0.4267
REMARK 3 S31: -1.8415 S32: -0.4500 S33: 0.5907
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 236 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.7672 63.6993 -9.0471
REMARK 3 T TENSOR
REMARK 3 T11: 0.5569 T22: 0.3128
REMARK 3 T33: 0.3498 T12: 0.0543
REMARK 3 T13: -0.0268 T23: 0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 6.9666 L22: 8.8973
REMARK 3 L33: 6.0211 L12: 0.4610
REMARK 3 L13: -2.8275 L23: -2.4806
REMARK 3 S TENSOR
REMARK 3 S11: 0.4521 S12: 0.0553 S13: 0.9403
REMARK 3 S21: 0.0558 S22: -0.2888 S23: -0.1024
REMARK 3 S31: -1.2499 S32: -0.0484 S33: -0.2055
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID -1 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.2688 43.4990 -17.2886
REMARK 3 T TENSOR
REMARK 3 T11: 0.2131 T22: 0.4446
REMARK 3 T33: 0.3159 T12: 0.0422
REMARK 3 T13: 0.0051 T23: 0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.6251 L22: 2.4185
REMARK 3 L33: 4.3771 L12: 0.5021
REMARK 3 L13: -1.1678 L23: -0.0194
REMARK 3 S TENSOR
REMARK 3 S11: 0.0602 S12: -0.0726 S13: -0.1237
REMARK 3 S21: 0.2333 S22: 0.0936 S23: -0.1442
REMARK 3 S31: 0.0069 S32: 0.8072 S33: -0.1634
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 41 THROUGH 121 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.2271 37.1757 -27.6587
REMARK 3 T TENSOR
REMARK 3 T11: 0.1911 T22: 0.5625
REMARK 3 T33: 0.3171 T12: 0.0745
REMARK 3 T13: 0.0387 T23: 0.0415
REMARK 3 L TENSOR
REMARK 3 L11: 1.0329 L22: 2.0758
REMARK 3 L33: 1.9014 L12: 0.4219
REMARK 3 L13: -0.4953 L23: 0.3204
REMARK 3 S TENSOR
REMARK 3 S11: -0.0279 S12: 0.2227 S13: 0.0484
REMARK 3 S21: -0.0462 S22: 0.0635 S23: -0.0421
REMARK 3 S31: 0.0034 S32: 0.4757 S33: -0.0444
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 122 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.5707 33.0465 -36.5634
REMARK 3 T TENSOR
REMARK 3 T11: 0.2604 T22: 0.7559
REMARK 3 T33: 0.3305 T12: 0.1545
REMARK 3 T13: 0.0441 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 4.7037 L22: 4.0277
REMARK 3 L33: 2.8749 L12: 1.4794
REMARK 3 L13: 0.4187 L23: -0.2602
REMARK 3 S TENSOR
REMARK 3 S11: 0.0370 S12: 0.5852 S13: -0.0112
REMARK 3 S21: -0.2774 S22: 0.0511 S23: -0.0804
REMARK 3 S31: -0.1166 S32: 0.2952 S33: -0.1125
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 150 THROUGH 189 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.0266 32.8088 -48.1532
REMARK 3 T TENSOR
REMARK 3 T11: 0.4867 T22: 0.8375
REMARK 3 T33: 0.3943 T12: 0.0986
REMARK 3 T13: -0.0011 T23: -0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 9.5618 L22: 1.1833
REMARK 3 L33: 2.9988 L12: -0.0869
REMARK 3 L13: -2.0925 L23: -0.1257
REMARK 3 S TENSOR
REMARK 3 S11: -0.1368 S12: 1.3994 S13: 0.0891
REMARK 3 S21: -0.3776 S22: 0.1267 S23: 0.1983
REMARK 3 S31: 0.2320 S32: 0.1665 S33: 0.0474
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 190 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.6329 23.0059 -34.1972
REMARK 3 T TENSOR
REMARK 3 T11: 0.3122 T22: 0.6499
REMARK 3 T33: 0.3761 T12: 0.2103
REMARK 3 T13: 0.0269 T23: -0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 4.6169 L22: 1.8150
REMARK 3 L33: 4.0054 L12: 0.5680
REMARK 3 L13: -2.2030 L23: 0.4197
REMARK 3 S TENSOR
REMARK 3 S11: -0.0766 S12: 0.2269 S13: -0.1657
REMARK 3 S21: -0.1055 S22: 0.0784 S23: -0.2467
REMARK 3 S31: 0.3425 S32: 0.5915 S33: 0.0316
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND (RESID -1 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.2249 36.2987 -24.7770
REMARK 3 T TENSOR
REMARK 3 T11: 0.2643 T22: 0.3375
REMARK 3 T33: 0.3180 T12: 0.1077
REMARK 3 T13: 0.0107 T23: 0.0871
REMARK 3 L TENSOR
REMARK 3 L11: 2.2059 L22: 1.2685
REMARK 3 L33: 2.1643 L12: 1.4891
REMARK 3 L13: 0.7776 L23: -0.3974
REMARK 3 S TENSOR
REMARK 3 S11: 0.1952 S12: -0.0076 S13: 0.0157
REMARK 3 S21: -0.1224 S22: -0.0134 S23: -0.2720
REMARK 3 S31: -0.2226 S32: 0.3118 S33: -0.1550
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 25 THROUGH 53 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.1211 39.2871 -19.2195
REMARK 3 T TENSOR
REMARK 3 T11: 0.2120 T22: 0.3835
REMARK 3 T33: 0.2713 T12: 0.0847
REMARK 3 T13: -0.0283 T23: -0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.1389 L22: 5.6519
REMARK 3 L33: 6.3186 L12: 0.9832
REMARK 3 L13: -1.0825 L23: -5.0712
REMARK 3 S TENSOR
REMARK 3 S11: -0.0037 S12: -0.0296 S13: 0.0492
REMARK 3 S21: 0.1010 S22: 0.1204 S23: 0.2297
REMARK 3 S31: -0.0260 S32: -0.3241 S33: -0.1287
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 54 THROUGH 74 )
REMARK 3 ORIGIN FOR THE GROUP (A): -40.7015 48.9016 -19.1304
REMARK 3 T TENSOR
REMARK 3 T11: 0.3280 T22: 0.4504
REMARK 3 T33: 0.3478 T12: 0.1391
REMARK 3 T13: -0.0450 T23: 0.0710
REMARK 3 L TENSOR
REMARK 3 L11: 2.1252 L22: 3.6049
REMARK 3 L33: 2.3644 L12: 1.6661
REMARK 3 L13: 0.9734 L23: 0.9750
REMARK 3 S TENSOR
REMARK 3 S11: -0.0477 S12: 0.0568 S13: 0.2094
REMARK 3 S21: 0.0897 S22: -0.1080 S23: 0.1375
REMARK 3 S31: -0.3907 S32: -0.3812 S33: 0.1394
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 75 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.0235 40.7335 -34.3833
REMARK 3 T TENSOR
REMARK 3 T11: 0.1998 T22: 0.4374
REMARK 3 T33: 0.3235 T12: 0.1004
REMARK 3 T13: -0.0329 T23: 0.0464
REMARK 3 L TENSOR
REMARK 3 L11: 0.5132 L22: 2.6989
REMARK 3 L33: 3.2607 L12: -0.4288
REMARK 3 L13: 0.8345 L23: -0.8897
REMARK 3 S TENSOR
REMARK 3 S11: 0.0211 S12: 0.2926 S13: 0.0144
REMARK 3 S21: -0.1639 S22: -0.0427 S23: 0.0048
REMARK 3 S31: -0.1398 S32: -0.2307 S33: 0.0206
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 134 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): -47.8294 49.1397 -36.2281
REMARK 3 T TENSOR
REMARK 3 T11: 0.2931 T22: 0.3718
REMARK 3 T33: 0.3358 T12: 0.1716
REMARK 3 T13: -0.0723 T23: 0.1042
REMARK 3 L TENSOR
REMARK 3 L11: 8.3621 L22: 5.4178
REMARK 3 L33: 2.5150 L12: 2.5177
REMARK 3 L13: -1.5453 L23: 2.8357
REMARK 3 S TENSOR
REMARK 3 S11: 0.0382 S12: 0.0385 S13: 0.0693
REMARK 3 S21: -0.4204 S22: -0.0854 S23: -0.0589
REMARK 3 S31: -0.2123 S32: -0.3141 S33: 0.0420
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 150 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.5209 52.3641 -44.9948
REMARK 3 T TENSOR
REMARK 3 T11: 0.5462 T22: 0.7332
REMARK 3 T33: 0.4874 T12: 0.0182
REMARK 3 T13: 0.0206 T23: 0.1228
REMARK 3 L TENSOR
REMARK 3 L11: 7.1830 L22: 7.3548
REMARK 3 L33: 6.2572 L12: 1.6674
REMARK 3 L13: 6.1867 L23: 2.6335
REMARK 3 S TENSOR
REMARK 3 S11: -0.5574 S12: 0.8652 S13: 0.7109
REMARK 3 S21: -0.6102 S22: 0.4691 S23: 0.1834
REMARK 3 S31: -1.0406 S32: 0.5605 S33: 0.0613
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 168 THROUGH 189 )
REMARK 3 ORIGIN FOR THE GROUP (A): -44.3427 48.8958 -50.6608
REMARK 3 T TENSOR
REMARK 3 T11: 0.5125 T22: 0.6875
REMARK 3 T33: 0.3835 T12: 0.2004
REMARK 3 T13: -0.0784 T23: 0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 2.1294 L22: 6.5107
REMARK 3 L33: 7.0743 L12: 2.0504
REMARK 3 L13: -2.5244 L23: -1.3789
REMARK 3 S TENSOR
REMARK 3 S11: -0.0385 S12: 1.1630 S13: -0.0921
REMARK 3 S21: -0.5404 S22: -0.2093 S23: -0.4082
REMARK 3 S31: -0.0229 S32: 0.5846 S33: 0.2982
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 190 THROUGH 207 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.2262 55.2674 -36.9205
REMARK 3 T TENSOR
REMARK 3 T11: 0.3871 T22: 0.4454
REMARK 3 T33: 0.3513 T12: 0.1804
REMARK 3 T13: -0.0845 T23: 0.1129
REMARK 3 L TENSOR
REMARK 3 L11: 2.2889 L22: 4.8327
REMARK 3 L33: 3.4988 L12: 1.2132
REMARK 3 L13: 0.1706 L23: 0.2156
REMARK 3 S TENSOR
REMARK 3 S11: 0.0180 S12: 0.0698 S13: 0.0113
REMARK 3 S21: -0.2588 S22: -0.0694 S23: 0.1614
REMARK 3 S31: -0.4186 S32: -0.3241 S33: 0.0712
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 208 THROUGH 221 )
REMARK 3 ORIGIN FOR THE GROUP (A): -50.1630 61.3427 -43.2590
REMARK 3 T TENSOR
REMARK 3 T11: 0.6390 T22: 0.6063
REMARK 3 T33: 0.4727 T12: 0.3033
REMARK 3 T13: 0.0002 T23: 0.1180
REMARK 3 L TENSOR
REMARK 3 L11: 2.0661 L22: 8.9437
REMARK 3 L33: 6.5311 L12: 9.4348
REMARK 3 L13: 5.7206 L23: 6.0243
REMARK 3 S TENSOR
REMARK 3 S11: -0.2565 S12: 0.4904 S13: 0.3248
REMARK 3 S21: -0.3901 S22: 0.1585 S23: 0.2259
REMARK 3 S31: -0.8490 S32: -0.3312 S33: 0.1744
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 222 THROUGH 235 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.6042 61.2940 -33.3747
REMARK 3 T TENSOR
REMARK 3 T11: 0.5622 T22: 0.5956
REMARK 3 T33: 0.4489 T12: 0.2947
REMARK 3 T13: -0.0438 T23: 0.0492
REMARK 3 L TENSOR
REMARK 3 L11: 6.3126 L22: 0.2422
REMARK 3 L33: 5.5325 L12: -0.5783
REMARK 3 L13: 5.6423 L23: -0.5470
REMARK 3 S TENSOR
REMARK 3 S11: -0.3160 S12: -0.0624 S13: 0.4134
REMARK 3 S21: -0.0105 S22: 0.0312 S23: 0.2607
REMARK 3 S31: -1.4171 S32: -0.5050 S33: 0.4189
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 236 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): -47.0321 55.3539 -23.9113
REMARK 3 T TENSOR
REMARK 3 T11: 0.4120 T22: 0.4528
REMARK 3 T33: 0.3504 T12: 0.2185
REMARK 3 T13: -0.0524 T23: 0.0703
REMARK 3 L TENSOR
REMARK 3 L11: 6.0048 L22: 5.9004
REMARK 3 L33: 4.9061 L12: 1.1070
REMARK 3 L13: -0.6554 L23: -0.4526
REMARK 3 S TENSOR
REMARK 3 S11: -0.0978 S12: 0.3588 S13: 0.6638
REMARK 3 S21: 0.1418 S22: 0.2598 S23: 0.7757
REMARK 3 S31: -0.7407 S32: -0.9426 S33: -0.1845
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID -1 THROUGH 55 OR
REMARK 3 RESID 57 THROUGH 253 OR RESID 301))
REMARK 3 SELECTION : (CHAIN B AND (RESID -1 THROUGH 55 OR
REMARK 3 RESID 57 THROUGH 253 OR RESID 301))
REMARK 3 ATOM PAIRS NUMBER : 4885
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID -1 THROUGH 55 OR
REMARK 3 RESID 57 THROUGH 253 OR RESID 301))
REMARK 3 SELECTION : (CHAIN C AND (RESID -1 THROUGH 55 OR
REMARK 3 RESID 57 THROUGH 253 OR RESID 301))
REMARK 3 ATOM PAIRS NUMBER : 4885
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID -1 THROUGH 55 OR
REMARK 3 RESID 57 THROUGH 253 OR RESID 301))
REMARK 3 SELECTION : (CHAIN D AND (RESID -1 THROUGH 55 OR
REMARK 3 RESID 57 THROUGH 253 OR RESID 301))
REMARK 3 ATOM PAIRS NUMBER : 4885
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6VHD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JAN-20.
REMARK 100 THE DEPOSITION ID IS D_1000246407.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JUL-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.954
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73040
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 49.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 27.10
REMARK 200 R MERGE (I) : 0.15100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 24.90
REMARK 200 R MERGE FOR SHELL (I) : 2.67600
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 2.8.3
REMARK 200 STARTING MODEL: 6VH9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 UL ~7.5 MG/ML FPHF+KT129 (0.12MM
REMARK 280 KT129, 12% DMSO, 18 MM HEPES PH 7.5, 8 MM NACL) WERE MIXED WITH
REMARK 280 0.2 UL OF RESERVOIR SOLUTION. SITTING DROP RESERVOIR CONTAINED
REMARK 280 50 UL OF 0.2 M SODIUM CITRATE, 0.1 M BIS-TRIS PROPANE PH 6.5, 20%
REMARK 280 W/V PEG 3350. CRYSTALS WERE SOAKED FOR ~20 SECONDS IN 75%
REMARK 280 RESERVOIR SOLUTION AND 25% GLYCEROL PRIOR TO FREEZING IN LIQUID
REMARK 280 NITROGEN, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 151.73233
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 303.46467
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 227.59850
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 379.33083
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 75.86617
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 151.73233
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 303.46467
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 379.33083
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 227.59850
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 75.86617
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER C 121 O1 6WG C 301 1.83
REMARK 500 OG SER B 121 O1 6WG B 301 1.99
REMARK 500 OG SER D 121 O1 6WG D 301 2.03
REMARK 500 OG SER A 121 O1 6WG A 301 2.05
REMARK 500 O HOH D 445 O HOH D 457 2.09
REMARK 500 O HOH A 412 O HOH A 472 2.15
REMARK 500 O THR A 59 O HOH A 401 2.18
REMARK 500 O MET A 56 O HOH A 401 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP B 179 C PRO B 180 N 0.156
REMARK 500 LYS C 111 CE LYS C 111 NZ 0.159
REMARK 500 ILE D 194 C PRO D 195 N 0.154
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 LYS A 37 CD - CE - NZ ANGL. DEV. = 13.9 DEGREES
REMARK 500 PRO B 180 C - N - CA ANGL. DEV. = 10.3 DEGREES
REMARK 500 LYS B 196 CB - CG - CD ANGL. DEV. = 16.6 DEGREES
REMARK 500 LYS C 69 CD - CE - NZ ANGL. DEV. = -16.3 DEGREES
REMARK 500 LYS C 174 CG - CD - CE ANGL. DEV. = -24.4 DEGREES
REMARK 500 LYS C 174 CD - CE - NZ ANGL. DEV. = 30.6 DEGREES
REMARK 500 GLU D 67 CA - CB - CG ANGL. DEV. = 19.0 DEGREES
REMARK 500 GLU D 67 OE1 - CD - OE2 ANGL. DEV. = -11.4 DEGREES
REMARK 500 GLU D 67 CG - CD - OE1 ANGL. DEV. = 16.2 DEGREES
REMARK 500 LYS D 111 CB - CG - CD ANGL. DEV. = 21.9 DEGREES
REMARK 500 LYS D 111 CD - CE - NZ ANGL. DEV. = 35.2 DEGREES
REMARK 500 PRO D 195 C - N - CA ANGL. DEV. = 11.0 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 49 -9.36 82.02
REMARK 500 ASP A 78 -135.89 65.23
REMARK 500 SER A 121 -117.57 57.01
REMARK 500 GLU A 157 34.93 -98.18
REMARK 500 ASP A 229 -157.11 -120.31
REMARK 500 ASP A 233 -167.94 -117.11
REMARK 500 SER B 49 -10.78 83.11
REMARK 500 ASP B 78 -135.45 65.03
REMARK 500 SER B 121 -117.46 55.51
REMARK 500 GLU B 157 77.09 -100.99
REMARK 500 ASP B 229 -155.84 -120.98
REMARK 500 ASP B 233 -167.82 -118.23
REMARK 500 SER C 49 -10.20 83.07
REMARK 500 ASP C 78 -134.55 65.39
REMARK 500 SER C 121 -116.88 56.27
REMARK 500 GLU C 157 72.36 -105.49
REMARK 500 ASP C 229 -154.50 -119.56
REMARK 500 ASP C 233 -164.34 -118.86
REMARK 500 SER D 49 -11.36 83.58
REMARK 500 ASP D 78 -136.41 64.93
REMARK 500 SER D 121 -116.59 55.38
REMARK 500 GLU D 157 73.64 -102.73
REMARK 500 ASP D 229 -157.45 -121.02
REMARK 500 ASP D 233 -163.86 -117.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLN C 241 -10.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6WG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 6WG B 301 and SER B
REMARK 800 121
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 6WG C 301 and SER C
REMARK 800 121
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 6WG D 301 and SER D
REMARK 800 121
DBREF1 6VHD A 2 253 UNP A0A0D6GS23_STAAU
DBREF2 6VHD A A0A0D6GS23 2 253
DBREF1 6VHD B 2 253 UNP A0A0D6GS23_STAAU
DBREF2 6VHD B A0A0D6GS23 2 253
DBREF1 6VHD C 2 253 UNP A0A0D6GS23_STAAU
DBREF2 6VHD C A0A0D6GS23 2 253
DBREF1 6VHD D 2 253 UNP A0A0D6GS23_STAAU
DBREF2 6VHD D A0A0D6GS23 2 253
SEQADV 6VHD GLY A -1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHD PRO A 0 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHD GLY A 1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHD GLY B -1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHD PRO B 0 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHD GLY B 1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHD GLY C -1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHD PRO C 0 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHD GLY C 1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHD GLY D -1 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHD PRO D 0 UNP A0A0D6GS2 EXPRESSION TAG
SEQADV 6VHD GLY D 1 UNP A0A0D6GS2 EXPRESSION TAG
SEQRES 1 A 255 GLY PRO GLY ALA TYR ILE SER LEU ASN TYR HIS SER PRO
SEQRES 2 A 255 THR ILE GLY MET HIS GLN ASN LEU THR VAL ILE LEU PRO
SEQRES 3 A 255 GLU ASP GLN SER PHE PHE ASN SER ASP THR THR VAL LYS
SEQRES 4 A 255 PRO LEU LYS THR LEU MET LEU LEU HIS GLY LEU SER SER
SEQRES 5 A 255 ASP GLU THR THR TYR MET ARG TYR THR SER ILE GLU ARG
SEQRES 6 A 255 TYR ALA ASN GLU HIS LYS LEU ALA VAL ILE MET PRO ASN
SEQRES 7 A 255 VAL ASP HIS SER ALA TYR ALA ASN MET ALA TYR GLY HIS
SEQRES 8 A 255 SER TYR TYR ASP TYR ILE LEU GLU VAL TYR ASP TYR VAL
SEQRES 9 A 255 HIS GLN ILE PHE PRO LEU SER LYS LYS ARG ASP ASP ASN
SEQRES 10 A 255 PHE ILE ALA GLY HIS SER MET GLY GLY TYR GLY THR ILE
SEQRES 11 A 255 LYS PHE ALA LEU THR GLN GLY ASP LYS PHE ALA LYS ALA
SEQRES 12 A 255 VAL PRO LEU SER ALA VAL PHE GLU ALA GLN ASN LEU MET
SEQRES 13 A 255 ASP LEU GLU TRP ASN ASP PHE SER LYS GLU ALA ILE ILE
SEQRES 14 A 255 GLY ASN LEU SER SER VAL LYS GLY THR GLU HIS ASP PRO
SEQRES 15 A 255 TYR TYR LEU LEU ASP LYS ALA VAL ALA GLU ASP LYS GLN
SEQRES 16 A 255 ILE PRO LYS LEU LEU ILE MET CYS GLY LYS GLN ASP PHE
SEQRES 17 A 255 LEU TYR GLN ASP ASN LEU ASP PHE ILE ASP TYR LEU SER
SEQRES 18 A 255 ARG ILE ASN VAL PRO TYR GLN PHE GLU ASP GLY PRO GLY
SEQRES 19 A 255 ASP HIS ASP TYR ALA TYR TRP ASP GLN ALA ILE LYS ARG
SEQRES 20 A 255 ALA ILE THR TRP MET VAL ASN ASP
SEQRES 1 B 255 GLY PRO GLY ALA TYR ILE SER LEU ASN TYR HIS SER PRO
SEQRES 2 B 255 THR ILE GLY MET HIS GLN ASN LEU THR VAL ILE LEU PRO
SEQRES 3 B 255 GLU ASP GLN SER PHE PHE ASN SER ASP THR THR VAL LYS
SEQRES 4 B 255 PRO LEU LYS THR LEU MET LEU LEU HIS GLY LEU SER SER
SEQRES 5 B 255 ASP GLU THR THR TYR MET ARG TYR THR SER ILE GLU ARG
SEQRES 6 B 255 TYR ALA ASN GLU HIS LYS LEU ALA VAL ILE MET PRO ASN
SEQRES 7 B 255 VAL ASP HIS SER ALA TYR ALA ASN MET ALA TYR GLY HIS
SEQRES 8 B 255 SER TYR TYR ASP TYR ILE LEU GLU VAL TYR ASP TYR VAL
SEQRES 9 B 255 HIS GLN ILE PHE PRO LEU SER LYS LYS ARG ASP ASP ASN
SEQRES 10 B 255 PHE ILE ALA GLY HIS SER MET GLY GLY TYR GLY THR ILE
SEQRES 11 B 255 LYS PHE ALA LEU THR GLN GLY ASP LYS PHE ALA LYS ALA
SEQRES 12 B 255 VAL PRO LEU SER ALA VAL PHE GLU ALA GLN ASN LEU MET
SEQRES 13 B 255 ASP LEU GLU TRP ASN ASP PHE SER LYS GLU ALA ILE ILE
SEQRES 14 B 255 GLY ASN LEU SER SER VAL LYS GLY THR GLU HIS ASP PRO
SEQRES 15 B 255 TYR TYR LEU LEU ASP LYS ALA VAL ALA GLU ASP LYS GLN
SEQRES 16 B 255 ILE PRO LYS LEU LEU ILE MET CYS GLY LYS GLN ASP PHE
SEQRES 17 B 255 LEU TYR GLN ASP ASN LEU ASP PHE ILE ASP TYR LEU SER
SEQRES 18 B 255 ARG ILE ASN VAL PRO TYR GLN PHE GLU ASP GLY PRO GLY
SEQRES 19 B 255 ASP HIS ASP TYR ALA TYR TRP ASP GLN ALA ILE LYS ARG
SEQRES 20 B 255 ALA ILE THR TRP MET VAL ASN ASP
SEQRES 1 C 255 GLY PRO GLY ALA TYR ILE SER LEU ASN TYR HIS SER PRO
SEQRES 2 C 255 THR ILE GLY MET HIS GLN ASN LEU THR VAL ILE LEU PRO
SEQRES 3 C 255 GLU ASP GLN SER PHE PHE ASN SER ASP THR THR VAL LYS
SEQRES 4 C 255 PRO LEU LYS THR LEU MET LEU LEU HIS GLY LEU SER SER
SEQRES 5 C 255 ASP GLU THR THR TYR MET ARG TYR THR SER ILE GLU ARG
SEQRES 6 C 255 TYR ALA ASN GLU HIS LYS LEU ALA VAL ILE MET PRO ASN
SEQRES 7 C 255 VAL ASP HIS SER ALA TYR ALA ASN MET ALA TYR GLY HIS
SEQRES 8 C 255 SER TYR TYR ASP TYR ILE LEU GLU VAL TYR ASP TYR VAL
SEQRES 9 C 255 HIS GLN ILE PHE PRO LEU SER LYS LYS ARG ASP ASP ASN
SEQRES 10 C 255 PHE ILE ALA GLY HIS SER MET GLY GLY TYR GLY THR ILE
SEQRES 11 C 255 LYS PHE ALA LEU THR GLN GLY ASP LYS PHE ALA LYS ALA
SEQRES 12 C 255 VAL PRO LEU SER ALA VAL PHE GLU ALA GLN ASN LEU MET
SEQRES 13 C 255 ASP LEU GLU TRP ASN ASP PHE SER LYS GLU ALA ILE ILE
SEQRES 14 C 255 GLY ASN LEU SER SER VAL LYS GLY THR GLU HIS ASP PRO
SEQRES 15 C 255 TYR TYR LEU LEU ASP LYS ALA VAL ALA GLU ASP LYS GLN
SEQRES 16 C 255 ILE PRO LYS LEU LEU ILE MET CYS GLY LYS GLN ASP PHE
SEQRES 17 C 255 LEU TYR GLN ASP ASN LEU ASP PHE ILE ASP TYR LEU SER
SEQRES 18 C 255 ARG ILE ASN VAL PRO TYR GLN PHE GLU ASP GLY PRO GLY
SEQRES 19 C 255 ASP HIS ASP TYR ALA TYR TRP ASP GLN ALA ILE LYS ARG
SEQRES 20 C 255 ALA ILE THR TRP MET VAL ASN ASP
SEQRES 1 D 255 GLY PRO GLY ALA TYR ILE SER LEU ASN TYR HIS SER PRO
SEQRES 2 D 255 THR ILE GLY MET HIS GLN ASN LEU THR VAL ILE LEU PRO
SEQRES 3 D 255 GLU ASP GLN SER PHE PHE ASN SER ASP THR THR VAL LYS
SEQRES 4 D 255 PRO LEU LYS THR LEU MET LEU LEU HIS GLY LEU SER SER
SEQRES 5 D 255 ASP GLU THR THR TYR MET ARG TYR THR SER ILE GLU ARG
SEQRES 6 D 255 TYR ALA ASN GLU HIS LYS LEU ALA VAL ILE MET PRO ASN
SEQRES 7 D 255 VAL ASP HIS SER ALA TYR ALA ASN MET ALA TYR GLY HIS
SEQRES 8 D 255 SER TYR TYR ASP TYR ILE LEU GLU VAL TYR ASP TYR VAL
SEQRES 9 D 255 HIS GLN ILE PHE PRO LEU SER LYS LYS ARG ASP ASP ASN
SEQRES 10 D 255 PHE ILE ALA GLY HIS SER MET GLY GLY TYR GLY THR ILE
SEQRES 11 D 255 LYS PHE ALA LEU THR GLN GLY ASP LYS PHE ALA LYS ALA
SEQRES 12 D 255 VAL PRO LEU SER ALA VAL PHE GLU ALA GLN ASN LEU MET
SEQRES 13 D 255 ASP LEU GLU TRP ASN ASP PHE SER LYS GLU ALA ILE ILE
SEQRES 14 D 255 GLY ASN LEU SER SER VAL LYS GLY THR GLU HIS ASP PRO
SEQRES 15 D 255 TYR TYR LEU LEU ASP LYS ALA VAL ALA GLU ASP LYS GLN
SEQRES 16 D 255 ILE PRO LYS LEU LEU ILE MET CYS GLY LYS GLN ASP PHE
SEQRES 17 D 255 LEU TYR GLN ASP ASN LEU ASP PHE ILE ASP TYR LEU SER
SEQRES 18 D 255 ARG ILE ASN VAL PRO TYR GLN PHE GLU ASP GLY PRO GLY
SEQRES 19 D 255 ASP HIS ASP TYR ALA TYR TRP ASP GLN ALA ILE LYS ARG
SEQRES 20 D 255 ALA ILE THR TRP MET VAL ASN ASP
HET 6WG A 301 14
HET 6WG B 301 14
HET 6WG C 301 14
HET 6WG D 301 14
HETNAM 6WG (2~{R})-2-PHENYLPIPERIDINE-1-CARBALDEHYDE
FORMUL 5 6WG 4(C12 H15 N O)
FORMUL 9 HOH *258(H2 O)
HELIX 1 AA1 ASP A 26 ASN A 31 5 6
HELIX 2 AA2 THR A 53 THR A 59 1 7
HELIX 3 AA3 SER A 60 HIS A 68 1 9
HELIX 4 AA4 SER A 90 PHE A 106 1 17
HELIX 5 AA5 LYS A 111 ASP A 113 5 3
HELIX 6 AA6 SER A 121 GLN A 134 1 14
HELIX 7 AA7 GLU A 149 LEU A 156 1 8
HELIX 8 AA8 SER A 162 GLY A 168 1 7
HELIX 9 AA9 ASP A 179 GLU A 190 1 12
HELIX 10 AB1 LEU A 207 ILE A 221 1 15
HELIX 11 AB2 ASP A 235 ASN A 252 1 18
HELIX 12 AB3 ASP B 26 ASN B 31 5 6
HELIX 13 AB4 THR B 53 THR B 59 1 7
HELIX 14 AB5 SER B 60 HIS B 68 1 9
HELIX 15 AB6 SER B 90 PHE B 106 1 17
HELIX 16 AB7 LYS B 111 ASP B 113 5 3
HELIX 17 AB8 SER B 121 GLN B 134 1 14
HELIX 18 AB9 GLU B 149 ASP B 155 1 7
HELIX 19 AC1 SER B 162 GLY B 168 1 7
HELIX 20 AC2 ASP B 179 GLU B 190 1 12
HELIX 21 AC3 LEU B 207 ILE B 221 1 15
HELIX 22 AC4 ASP B 235 ASN B 252 1 18
HELIX 23 AC5 ASP C 26 ASN C 31 5 6
HELIX 24 AC6 THR C 53 THR C 59 1 7
HELIX 25 AC7 SER C 60 HIS C 68 1 9
HELIX 26 AC8 SER C 90 PHE C 106 1 17
HELIX 27 AC9 LYS C 111 ASP C 113 5 3
HELIX 28 AD1 SER C 121 GLN C 134 1 14
HELIX 29 AD2 GLU C 149 ASP C 155 1 7
HELIX 30 AD3 SER C 162 GLY C 168 1 7
HELIX 31 AD4 ASP C 179 GLU C 190 1 12
HELIX 32 AD5 LEU C 207 ILE C 221 1 15
HELIX 33 AD6 ASP C 235 ASN C 252 1 18
HELIX 34 AD7 ASP D 26 ASN D 31 5 6
HELIX 35 AD8 THR D 53 THR D 59 1 7
HELIX 36 AD9 SER D 60 HIS D 68 1 9
HELIX 37 AE1 SER D 90 PHE D 106 1 17
HELIX 38 AE2 LYS D 111 ASP D 113 5 3
HELIX 39 AE3 SER D 121 GLN D 134 1 14
HELIX 40 AE4 GLY D 135 PHE D 138 5 4
HELIX 41 AE5 GLU D 149 ASP D 155 1 7
HELIX 42 AE6 SER D 162 GLY D 168 1 7
HELIX 43 AE7 ASP D 179 GLU D 190 1 12
HELIX 44 AE8 LEU D 207 ILE D 221 1 15
HELIX 45 AE9 ASP D 235 ASN D 252 1 18
SHEET 1 AA116 GLN A 226 GLU A 228 0
SHEET 2 AA116 LYS A 196 MET A 200 1 N ILE A 199 O GLN A 226
SHEET 3 AA116 LYS A 140 LEU A 144 1 N ALA A 141 O LYS A 196
SHEET 4 AA116 ASN A 115 HIS A 120 1 N GLY A 119 O LEU A 144
SHEET 5 AA116 LYS A 40 LEU A 45 1 N MET A 43 O PHE A 116
SHEET 6 AA116 LEU A 70 MET A 74 1 O ILE A 73 N LEU A 44
SHEET 7 AA116 MET A 15 PRO A 24 -1 N THR A 20 O MET A 74
SHEET 8 AA116 GLY A 1 SER A 10 -1 N LEU A 6 O LEU A 19
SHEET 9 AA116 GLY D 1 SER D 10 -1 O ASN D 7 N TYR A 3
SHEET 10 AA116 MET D 15 PRO D 24 -1 O LEU D 19 N LEU D 6
SHEET 11 AA116 LEU D 70 MET D 74 -1 O MET D 74 N THR D 20
SHEET 12 AA116 LYS D 40 LEU D 45 1 N LEU D 42 O ILE D 73
SHEET 13 AA116 ASN D 115 HIS D 120 1 O ALA D 118 N LEU D 45
SHEET 14 AA116 LYS D 140 LEU D 144 1 O LEU D 144 N GLY D 119
SHEET 15 AA116 LYS D 196 MET D 200 1 O LYS D 196 N ALA D 141
SHEET 16 AA116 GLN D 226 GLU D 228 1 O GLN D 226 N ILE D 199
SHEET 1 AA216 GLN B 226 GLU B 228 0
SHEET 2 AA216 LYS B 196 MET B 200 1 N ILE B 199 O GLN B 226
SHEET 3 AA216 LYS B 140 LEU B 144 1 N ALA B 141 O LYS B 196
SHEET 4 AA216 ASN B 115 HIS B 120 1 N GLY B 119 O LEU B 144
SHEET 5 AA216 LYS B 40 LEU B 45 1 N LEU B 45 O ALA B 118
SHEET 6 AA216 LEU B 70 MET B 74 1 O ILE B 73 N LEU B 42
SHEET 7 AA216 MET B 15 PRO B 24 -1 N THR B 20 O MET B 74
SHEET 8 AA216 GLY B 1 SER B 10 -1 N ALA B 2 O LEU B 23
SHEET 9 AA216 ALA C 2 SER C 10 -1 O SER C 5 N SER B 5
SHEET 10 AA216 MET C 15 LEU C 23 -1 O LEU C 19 N LEU C 6
SHEET 11 AA216 ALA C 71 MET C 74 -1 O MET C 74 N THR C 20
SHEET 12 AA216 THR C 41 LEU C 45 1 N LEU C 44 O ILE C 73
SHEET 13 AA216 ASN C 115 HIS C 120 1 O PHE C 116 N MET C 43
SHEET 14 AA216 LYS C 140 LEU C 144 1 O LEU C 144 N GLY C 119
SHEET 15 AA216 LYS C 196 MET C 200 1 O LYS C 196 N ALA C 141
SHEET 16 AA216 GLN C 226 GLU C 228 1 O GLN C 226 N ILE C 199
LINK OG SER A 121 C12 6WG A 301 1555 1555 1.38
LINK OG SER B 121 C12 6WG B 301 1555 1555 1.38
LINK OG SER C 121 C12 6WG C 301 1555 1555 1.38
LINK OG SER D 121 C12 6WG D 301 1555 1555 1.38
SITE 1 AC1 11 LEU A 48 SER A 121 MET A 122 VAL A 147
SITE 2 AC1 11 ASN A 152 LEU A 153 LEU A 156 TRP A 158
SITE 3 AC1 11 PHE A 206 LEU A 207 HIS A 234
SITE 1 AC2 16 LEU B 48 HIS B 120 MET B 122 GLY B 123
SITE 2 AC2 16 GLY B 124 TYR B 125 LEU B 144 SER B 145
SITE 3 AC2 16 VAL B 147 ASN B 152 LEU B 153 TRP B 158
SITE 4 AC2 16 PHE B 206 LEU B 207 HIS B 234 HOH B 446
SITE 1 AC3 14 LEU C 48 HIS C 120 MET C 122 GLY C 123
SITE 2 AC3 14 GLY C 124 TYR C 125 LEU C 144 SER C 145
SITE 3 AC3 14 VAL C 147 ASN C 152 LEU C 153 PHE C 206
SITE 4 AC3 14 HIS C 234 HOH C 447
SITE 1 AC4 15 LEU D 48 HIS D 120 MET D 122 GLY D 123
SITE 2 AC4 15 GLY D 124 TYR D 125 LEU D 144 SER D 145
SITE 3 AC4 15 VAL D 147 ASN D 152 LEU D 153 LEU D 156
SITE 4 AC4 15 TRP D 158 PHE D 206 HIS D 234
CRYST1 87.202 87.202 455.197 90.00 90.00 120.00 P 61 2 2 48
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 0.011468 0.006621 0.000000 0.00000
SCALE2 0.000000 0.013242 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002197 0.00000
TER 2068 ASP A 253
TER 4136 ASP B 253
TER 6204 ASP C 253
TER 8272 ASP D 253
MASTER 903 0 4 45 32 0 15 6 8550 4 60 80
END |