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HEADER HYDROLASE 01-JUN-17 5W15
TITLE CRYSTAL STRUCTURE OF AN ALPHA/BETA HYDROLASE FOLD PROTEIN FROM
TITLE 2 BURKHOLDERIA AMBIFARIA.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FOLD PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA AMBIFARIA (STRAIN MC40-6);
SOURCE 3 ORGANISM_TAXID: 398577;
SOURCE 4 STRAIN: MC40-6;
SOURCE 5 GENE: BAMMC406_3075;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: BUAMA.00095.A.B1
KEYWDS SSGCID, BURKHOLDERIA AMBIFARIA, ALPHA/BETA HYDROLASE, FOLD PROTEIN,
KEYWDS 2 STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR
KEYWDS 3 INFECTIOUS DISEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SSGCID,SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE
AUTHOR 2 (SSGCID)
REVDAT 1 14-JUN-17 5W15 0
JRNL AUTH R.M.IRWIN,S.M.MAYCLIN,D.LORIMER,T.E.EDWARDS
JRNL TITL CRYSTAL STRUCTURE OF AN ALPHA/BETA HYDROLASE FOLD PROTEIN
JRNL TITL 2 FROM BURKHOLDERIA AMBIFARIA.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 120149
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.640
REMARK 3 FREE R VALUE TEST SET COUNT : 1970
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 50.0000 - 4.2164 1.00 8546 128 0.1408 0.1508
REMARK 3 2 4.2164 - 3.3471 1.00 8461 153 0.1361 0.1603
REMARK 3 3 3.3471 - 2.9241 1.00 8478 130 0.1531 0.1719
REMARK 3 4 2.9241 - 2.6568 1.00 8456 139 0.1650 0.1989
REMARK 3 5 2.6568 - 2.4664 1.00 8421 130 0.1712 0.1863
REMARK 3 6 2.4664 - 2.3210 1.00 8439 132 0.1744 0.2002
REMARK 3 7 2.3210 - 2.2047 1.00 8449 142 0.1731 0.2019
REMARK 3 8 2.2047 - 2.1088 1.00 8426 126 0.1813 0.2148
REMARK 3 9 2.1088 - 2.0276 1.00 8423 169 0.1883 0.2104
REMARK 3 10 2.0276 - 1.9576 1.00 8419 133 0.1987 0.2073
REMARK 3 11 1.9576 - 1.8964 1.00 8423 132 0.1976 0.2282
REMARK 3 12 1.8964 - 1.8422 1.00 8420 149 0.2037 0.2133
REMARK 3 13 1.8422 - 1.7937 1.00 8404 157 0.2276 0.2543
REMARK 3 14 1.7937 - 1.7500 1.00 8414 150 0.2559 0.2811
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.710
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.13
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 : 0.006 8968
REMARK 3 ANGLE : 0.876 12308
REMARK 3 CHIRALITY : 0.057 1310
REMARK 3 PLANARITY : 0.006 1641
REMARK 3 DIHEDRAL : 14.826 5307
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 22
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID -2 THROUGH 20 )
REMARK 3 ORIGIN FOR THE GROUP (A): 87.7158 -8.3582 -45.3490
REMARK 3 T TENSOR
REMARK 3 T11: 0.1122 T22: 0.1433
REMARK 3 T33: 0.1411 T12: -0.0149
REMARK 3 T13: -0.0092 T23: -0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 4.6522 L22: 4.3840
REMARK 3 L33: 5.4546 L12: 0.1209
REMARK 3 L13: -0.0869 L23: -0.4612
REMARK 3 S TENSOR
REMARK 3 S11: 0.0932 S12: 0.1588 S13: 0.2330
REMARK 3 S21: -0.2541 S22: -0.0249 S23: 0.2409
REMARK 3 S31: -0.1528 S32: -0.2797 S33: -0.1005
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 21 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): 97.6159 -7.0435 -38.3540
REMARK 3 T TENSOR
REMARK 3 T11: 0.1056 T22: 0.1160
REMARK 3 T33: 0.0779 T12: 0.0050
REMARK 3 T13: 0.0224 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 2.0228 L22: 1.7723
REMARK 3 L33: 1.6634 L12: 0.3793
REMARK 3 L13: 0.5857 L23: -0.0277
REMARK 3 S TENSOR
REMARK 3 S11: 0.0039 S12: -0.1400 S13: 0.0633
REMARK 3 S21: 0.0699 S22: -0.0486 S23: 0.0318
REMARK 3 S31: 0.0311 S32: -0.0579 S33: 0.0358
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 131 THROUGH 147 )
REMARK 3 ORIGIN FOR THE GROUP (A): 88.3320 17.8114 -34.8069
REMARK 3 T TENSOR
REMARK 3 T11: 0.4039 T22: 0.3148
REMARK 3 T33: 0.3600 T12: 0.0876
REMARK 3 T13: 0.0112 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 5.2309 L22: 2.2663
REMARK 3 L33: 4.1974 L12: -1.7823
REMARK 3 L13: 3.7088 L23: -1.0898
REMARK 3 S TENSOR
REMARK 3 S11: -0.2995 S12: -0.0502 S13: 0.1299
REMARK 3 S21: 0.5206 S22: 0.0153 S23: 0.4026
REMARK 3 S31: -0.5506 S32: -0.4470 S33: 0.2483
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 148 THROUGH 181 )
REMARK 3 ORIGIN FOR THE GROUP (A): 92.7990 11.5657 -48.7372
REMARK 3 T TENSOR
REMARK 3 T11: 0.2411 T22: 0.1652
REMARK 3 T33: 0.2231 T12: 0.0315
REMARK 3 T13: -0.0508 T23: 0.0313
REMARK 3 L TENSOR
REMARK 3 L11: 2.3445 L22: 2.0273
REMARK 3 L33: 1.2624 L12: -0.4826
REMARK 3 L13: 0.6113 L23: -0.3594
REMARK 3 S TENSOR
REMARK 3 S11: -0.0225 S12: 0.3907 S13: 0.2902
REMARK 3 S21: -0.2843 S22: -0.0371 S23: 0.2354
REMARK 3 S31: -0.1579 S32: -0.0748 S33: 0.0797
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 182 THROUGH 237 )
REMARK 3 ORIGIN FOR THE GROUP (A): 102.3137 3.2843 -31.8967
REMARK 3 T TENSOR
REMARK 3 T11: 0.1853 T22: 0.1687
REMARK 3 T33: 0.1274 T12: -0.0007
REMARK 3 T13: -0.0039 T23: -0.0389
REMARK 3 L TENSOR
REMARK 3 L11: 2.1886 L22: 1.5778
REMARK 3 L33: 1.0321 L12: -0.4457
REMARK 3 L13: 0.5159 L23: -0.0865
REMARK 3 S TENSOR
REMARK 3 S11: -0.0234 S12: -0.2614 S13: 0.1389
REMARK 3 S21: 0.2074 S22: -0.0473 S23: 0.0851
REMARK 3 S31: -0.1274 S32: -0.0519 S33: 0.0444
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 238 THROUGH 267 )
REMARK 3 ORIGIN FOR THE GROUP (A): 111.3368 -0.1270 -44.2373
REMARK 3 T TENSOR
REMARK 3 T11: 0.0816 T22: 0.1515
REMARK 3 T33: 0.1049 T12: -0.0207
REMARK 3 T13: 0.0337 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 3.7769 L22: 2.7937
REMARK 3 L33: 6.9643 L12: 0.6169
REMARK 3 L13: 2.3154 L23: -0.1677
REMARK 3 S TENSOR
REMARK 3 S11: -0.0140 S12: 0.0118 S13: 0.0478
REMARK 3 S21: 0.0190 S22: -0.0395 S23: -0.2167
REMARK 3 S31: -0.0590 S32: 0.3848 S33: 0.0220
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID -2 THROUGH 20 )
REMARK 3 ORIGIN FOR THE GROUP (A): 113.3038 -21.8344 -19.7688
REMARK 3 T TENSOR
REMARK 3 T11: 0.1563 T22: 0.1394
REMARK 3 T33: 0.1247 T12: 0.0051
REMARK 3 T13: -0.0325 T23: 0.0280
REMARK 3 L TENSOR
REMARK 3 L11: 4.7501 L22: 3.3392
REMARK 3 L33: 3.4615 L12: -0.5128
REMARK 3 L13: 0.3077 L23: 0.9391
REMARK 3 S TENSOR
REMARK 3 S11: -0.0269 S12: -0.0496 S13: 0.0179
REMARK 3 S21: 0.0004 S22: 0.1003 S23: 0.2538
REMARK 3 S31: 0.2269 S32: -0.2730 S33: -0.0035
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 21 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): 124.6700 -23.5545 -16.8619
REMARK 3 T TENSOR
REMARK 3 T11: 0.1320 T22: 0.1081
REMARK 3 T33: 0.1015 T12: -0.0124
REMARK 3 T13: -0.0025 T23: 0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 2.3990 L22: 1.6554
REMARK 3 L33: 1.8806 L12: 0.0484
REMARK 3 L13: 0.5678 L23: -0.1895
REMARK 3 S TENSOR
REMARK 3 S11: -0.0983 S12: 0.0654 S13: 0.1260
REMARK 3 S21: -0.0623 S22: 0.0425 S23: -0.0890
REMARK 3 S31: -0.0824 S32: 0.0407 S33: 0.0497
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 131 THROUGH 162 )
REMARK 3 ORIGIN FOR THE GROUP (A): 120.3400 -45.5424 -27.8657
REMARK 3 T TENSOR
REMARK 3 T11: 0.2752 T22: 0.2054
REMARK 3 T33: 0.2205 T12: -0.0754
REMARK 3 T13: 0.0340 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 2.2805 L22: 3.2885
REMARK 3 L33: 2.5361 L12: 0.5947
REMARK 3 L13: 1.2494 L23: 1.7834
REMARK 3 S TENSOR
REMARK 3 S11: -0.2687 S12: 0.3898 S13: 0.0034
REMARK 3 S21: -0.4074 S22: 0.2191 S23: -0.3857
REMARK 3 S31: -0.2031 S32: 0.2768 S33: 0.0616
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 163 THROUGH 219 )
REMARK 3 ORIGIN FOR THE GROUP (A): 126.1756 -33.4246 -20.1347
REMARK 3 T TENSOR
REMARK 3 T11: 0.1524 T22: 0.0870
REMARK 3 T33: 0.1343 T12: 0.0298
REMARK 3 T13: 0.0294 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 2.4707 L22: 1.6334
REMARK 3 L33: 2.4853 L12: 1.0067
REMARK 3 L13: 1.2401 L23: 0.6155
REMARK 3 S TENSOR
REMARK 3 S11: -0.1415 S12: 0.1498 S13: 0.0602
REMARK 3 S21: -0.2255 S22: 0.0781 S23: -0.0741
REMARK 3 S31: 0.0677 S32: 0.1256 S33: 0.0703
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 220 THROUGH 267 )
REMARK 3 ORIGIN FOR THE GROUP (A): 132.6929 -34.9143 -7.6334
REMARK 3 T TENSOR
REMARK 3 T11: 0.1404 T22: 0.1517
REMARK 3 T33: 0.1627 T12: 0.0342
REMARK 3 T13: -0.0267 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 5.5351 L22: 2.5158
REMARK 3 L33: 2.1684 L12: 1.5743
REMARK 3 L13: -0.9656 L23: -0.5990
REMARK 3 S TENSOR
REMARK 3 S11: -0.0564 S12: -0.0233 S13: -0.3771
REMARK 3 S21: 0.0311 S22: 0.0311 S23: -0.4213
REMARK 3 S31: 0.2024 S32: 0.1641 S33: 0.0188
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID -2 THROUGH 20 )
REMARK 3 ORIGIN FOR THE GROUP (A): 101.5790 6.0482 8.5410
REMARK 3 T TENSOR
REMARK 3 T11: 0.1245 T22: 0.1823
REMARK 3 T33: 0.2749 T12: -0.0268
REMARK 3 T13: 0.0051 T23: 0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 2.7688 L22: 3.7082
REMARK 3 L33: 7.4268 L12: 1.0201
REMARK 3 L13: -1.7507 L23: -0.2032
REMARK 3 S TENSOR
REMARK 3 S11: 0.2066 S12: 0.0652 S13: 0.5411
REMARK 3 S21: 0.2380 S22: -0.1127 S23: -0.2424
REMARK 3 S31: -0.4413 S32: -0.0114 S33: -0.0788
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 21 THROUGH 108 )
REMARK 3 ORIGIN FOR THE GROUP (A): 97.7707 -2.9139 5.5112
REMARK 3 T TENSOR
REMARK 3 T11: 0.0650 T22: 0.1512
REMARK 3 T33: 0.1293 T12: 0.0020
REMARK 3 T13: 0.0115 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 1.5056 L22: 2.4141
REMARK 3 L33: 1.2444 L12: -0.2576
REMARK 3 L13: -0.0691 L23: 0.0863
REMARK 3 S TENSOR
REMARK 3 S11: 0.0277 S12: 0.0928 S13: 0.0528
REMARK 3 S21: -0.0205 S22: -0.0089 S23: -0.1897
REMARK 3 S31: -0.0112 S32: 0.1228 S33: -0.0035
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 109 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): 92.1153 -11.2584 -0.3997
REMARK 3 T TENSOR
REMARK 3 T11: 0.1243 T22: 0.1654
REMARK 3 T33: 0.1322 T12: 0.0274
REMARK 3 T13: 0.0158 T23: -0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 2.4662 L22: 3.2867
REMARK 3 L33: 1.7699 L12: -0.4127
REMARK 3 L13: -0.3960 L23: 0.1850
REMARK 3 S TENSOR
REMARK 3 S11: 0.1555 S12: 0.3768 S13: -0.0635
REMARK 3 S21: -0.2780 S22: -0.1002 S23: 0.0958
REMARK 3 S31: 0.0512 S32: 0.0287 S33: 0.0207
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 131 THROUGH 147 )
REMARK 3 ORIGIN FOR THE GROUP (A): 86.4067 11.0169 -14.8541
REMARK 3 T TENSOR
REMARK 3 T11: 0.4427 T22: 0.3195
REMARK 3 T33: 0.3688 T12: 0.1476
REMARK 3 T13: 0.0180 T23: 0.0369
REMARK 3 L TENSOR
REMARK 3 L11: 2.4163 L22: 2.8214
REMARK 3 L33: 2.4768 L12: -1.6825
REMARK 3 L13: 0.3031 L23: -0.0644
REMARK 3 S TENSOR
REMARK 3 S11: 0.5831 S12: 0.5776 S13: -0.3478
REMARK 3 S21: -0.9703 S22: -0.5384 S23: -0.1581
REMARK 3 S31: 0.1286 S32: 0.2282 S33: 0.0969
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 148 THROUGH 206 )
REMARK 3 ORIGIN FOR THE GROUP (A): 88.0782 6.7605 -4.4856
REMARK 3 T TENSOR
REMARK 3 T11: 0.1252 T22: 0.1876
REMARK 3 T33: 0.1389 T12: 0.0246
REMARK 3 T13: 0.0145 T23: 0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 1.1174 L22: 3.6488
REMARK 3 L33: 0.7145 L12: -0.4128
REMARK 3 L13: 0.1805 L23: -0.4191
REMARK 3 S TENSOR
REMARK 3 S11: 0.0889 S12: 0.2183 S13: 0.1140
REMARK 3 S21: -0.1839 S22: -0.0720 S23: -0.0434
REMARK 3 S31: -0.1099 S32: -0.0238 S33: -0.0041
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 207 THROUGH 237 )
REMARK 3 ORIGIN FOR THE GROUP (A): 83.3070 -13.2140 -0.3346
REMARK 3 T TENSOR
REMARK 3 T11: 0.1653 T22: 0.1815
REMARK 3 T33: 0.1541 T12: 0.0053
REMARK 3 T13: -0.0297 T23: -0.0273
REMARK 3 L TENSOR
REMARK 3 L11: 1.6419 L22: 3.7427
REMARK 3 L33: 0.9897 L12: -0.3983
REMARK 3 L13: -0.0815 L23: -0.1127
REMARK 3 S TENSOR
REMARK 3 S11: 0.0810 S12: 0.0940 S13: -0.2098
REMARK 3 S21: -0.2760 S22: 0.0262 S23: 0.2750
REMARK 3 S31: -0.0211 S32: -0.0552 S33: -0.0743
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 238 THROUGH 267 )
REMARK 3 ORIGIN FOR THE GROUP (A): 81.9977 -8.2827 9.5661
REMARK 3 T TENSOR
REMARK 3 T11: 0.0674 T22: 0.1359
REMARK 3 T33: 0.1068 T12: -0.0004
REMARK 3 T13: 0.0198 T23: 0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 1.7104 L22: 4.6703
REMARK 3 L33: 4.0588 L12: 1.1889
REMARK 3 L13: -0.5936 L23: 3.1954
REMARK 3 S TENSOR
REMARK 3 S11: 0.0392 S12: -0.0360 S13: -0.0199
REMARK 3 S21: 0.2133 S22: 0.0203 S23: 0.0451
REMARK 3 S31: 0.1475 S32: 0.0690 S33: -0.0778
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESID -2 THROUGH 20 )
REMARK 3 ORIGIN FOR THE GROUP (A): 126.2422 -45.4192 19.3148
REMARK 3 T TENSOR
REMARK 3 T11: 0.2101 T22: 0.1610
REMARK 3 T33: 0.2386 T12: 0.0224
REMARK 3 T13: -0.0739 T23: 0.0422
REMARK 3 L TENSOR
REMARK 3 L11: 4.3458 L22: 4.5098
REMARK 3 L33: 7.3763 L12: 0.1141
REMARK 3 L13: -3.7535 L23: -2.0081
REMARK 3 S TENSOR
REMARK 3 S11: 0.0381 S12: -0.0349 S13: -0.4745
REMARK 3 S21: -0.0951 S22: -0.0558 S23: -0.1527
REMARK 3 S31: 0.5858 S32: 0.0305 S33: 0.0217
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 21 THROUGH 147 )
REMARK 3 ORIGIN FOR THE GROUP (A): 116.6137 -38.0723 19.4307
REMARK 3 T TENSOR
REMARK 3 T11: 0.1446 T22: 0.1196
REMARK 3 T33: 0.1097 T12: -0.0183
REMARK 3 T13: -0.0033 T23: 0.0325
REMARK 3 L TENSOR
REMARK 3 L11: 1.3651 L22: 1.8050
REMARK 3 L33: 1.3447 L12: -0.0182
REMARK 3 L13: 0.1659 L23: 0.3062
REMARK 3 S TENSOR
REMARK 3 S11: 0.0691 S12: -0.1009 S13: -0.1768
REMARK 3 S21: 0.2031 S22: -0.0626 S23: 0.0794
REMARK 3 S31: 0.1443 S32: -0.0041 S33: -0.0122
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 148 THROUGH 237 )
REMARK 3 ORIGIN FOR THE GROUP (A): 107.7043 -40.1248 14.7276
REMARK 3 T TENSOR
REMARK 3 T11: 0.1339 T22: 0.1497
REMARK 3 T33: 0.1771 T12: -0.0205
REMARK 3 T13: 0.0136 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 1.2944 L22: 2.1590
REMARK 3 L33: 0.7939 L12: -0.0135
REMARK 3 L13: 0.2843 L23: 0.1863
REMARK 3 S TENSOR
REMARK 3 S11: 0.0736 S12: -0.0221 S13: -0.2380
REMARK 3 S21: 0.0698 S22: -0.0664 S23: 0.2366
REMARK 3 S31: 0.1506 S32: -0.0794 S33: 0.0117
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 238 THROUGH 267 )
REMARK 3 ORIGIN FOR THE GROUP (A): 113.6588 -28.4881 6.0346
REMARK 3 T TENSOR
REMARK 3 T11: 0.1095 T22: 0.1425
REMARK 3 T33: 0.0829 T12: 0.0007
REMARK 3 T13: -0.0088 T23: 0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 3.1504 L22: 3.4915
REMARK 3 L33: 2.5653 L12: -3.1854
REMARK 3 L13: -1.5985 L23: 0.9429
REMARK 3 S TENSOR
REMARK 3 S11: 0.1085 S12: 0.0834 S13: 0.1160
REMARK 3 S21: -0.2830 S22: -0.1113 S23: -0.0891
REMARK 3 S31: -0.0676 S32: 0.0707 S33: 0.0333
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 5W15 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1000228260.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : DIAMOND [111]
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 120204
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.082
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.9200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.93
REMARK 200 R MERGE FOR SHELL (I) : 0.56500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.730
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 4K2A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: JCGS+ B8 (283558B8): 100 MM TRIS-HCL
REMARK 280 PH 7.0, 200 MM MGCL2, 10% PEG 8000, PROTEIN CONC. 19. 9MG/ML,
REMARK 280 CRYO 20% ETHYLENE GLYCOL: PUCK ID VKW3-6, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 71.79500
REMARK 290 SMTRY3 2 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -123.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 27.60194
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -70.64953
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 207.81194
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 71.79500
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 -70.64953
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 -7
REMARK 465 ALA A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 MET B -7
REMARK 465 ALA B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 MET C -7
REMARK 465 ALA C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 MET D -7
REMARK 465 ALA D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 228 CG CD OE1 OE2
REMARK 470 LYS A 241 CG CD CE NZ
REMARK 470 ARG A 247 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 267 CG CD NE CZ NH1 NH2
REMARK 470 HIS B 0 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 49 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 87 CG CD CE NZ
REMARK 470 ARG B 134 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 138 CG CD OE1 NE2
REMARK 470 ARG B 267 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 49 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 87 CG CD CE NZ
REMARK 470 GLN C 128 CG CD OE1 NE2
REMARK 470 ARG C 134 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 138 CG CD OE1 NE2
REMARK 470 LYS C 241 CG CD CE NZ
REMARK 470 ARG C 247 CG CD NE CZ NH1 NH2
REMARK 470 HIS D 0 CG ND1 CD2 CE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH C 410 O HOH C 540 2.08
REMARK 500 NH1 ARG A 244 O HOH A 401 2.12
REMARK 500 O HOH C 562 O HOH C 653 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 4 78.48 -110.15
REMARK 500 PRO A 33 55.74 -97.62
REMARK 500 PHE A 34 -144.31 -114.25
REMARK 500 ASP A 97 -121.80 56.51
REMARK 500 ASN A 121 59.40 31.49
REMARK 500 ALA A 124 -20.94 -146.07
REMARK 500 HIS A 139 46.67 -144.91
REMARK 500 ALA A 256 59.03 -158.06
REMARK 500 PRO B 33 57.42 -96.63
REMARK 500 PHE B 34 -148.64 -113.30
REMARK 500 ASP B 97 -123.37 56.95
REMARK 500 ASP B 116 140.97 -176.07
REMARK 500 ASN B 121 59.11 30.59
REMARK 500 ALA B 124 -22.31 -149.57
REMARK 500 ALA B 256 59.22 -160.68
REMARK 500 PHE C 34 -147.71 -116.77
REMARK 500 ILE C 42 -53.91 -121.42
REMARK 500 ASP C 97 -120.34 59.34
REMARK 500 ASN C 121 61.86 27.98
REMARK 500 ALA C 256 60.63 -158.23
REMARK 500 ASP C 266 33.38 -96.98
REMARK 500 LEU D 4 79.77 -104.64
REMARK 500 PRO D 33 54.71 -99.01
REMARK 500 PHE D 34 -147.32 -111.73
REMARK 500 ASP D 97 -122.70 57.38
REMARK 500 ASN D 121 61.78 28.20
REMARK 500 ALA D 124 -19.34 -140.73
REMARK 500 HIS D 139 44.29 -145.11
REMARK 500 ASP D 211 36.39 -77.90
REMARK 500 ASP D 211 49.93 -89.51
REMARK 500 ALA D 256 59.06 -160.95
REMARK 500 ASP D 266 68.06 -100.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 758 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH A 759 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A 760 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH A 761 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH A 762 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH B 721 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH C 712 DISTANCE = 6.85 ANGSTROMS
REMARK 525 HOH D 766 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH D 767 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH D 768 DISTANCE = 6.02 ANGSTROMS
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 302
DBREF 5W15 A 1 267 UNP B1YPY7 B1YPY7_BURA4 1 267
DBREF 5W15 B 1 267 UNP B1YPY7 B1YPY7_BURA4 1 267
DBREF 5W15 C 1 267 UNP B1YPY7 B1YPY7_BURA4 1 267
DBREF 5W15 D 1 267 UNP B1YPY7 B1YPY7_BURA4 1 267
SEQADV 5W15 MET A -7 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 ALA A -6 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS A -5 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS A -4 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS A -3 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS A -2 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS A -1 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS A 0 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 MET B -7 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 ALA B -6 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS B -5 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS B -4 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS B -3 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS B -2 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS B -1 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS B 0 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 MET C -7 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 ALA C -6 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS C -5 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS C -4 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS C -3 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS C -2 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS C -1 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS C 0 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 MET D -7 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 ALA D -6 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS D -5 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS D -4 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS D -3 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS D -2 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS D -1 UNP B1YPY7 EXPRESSION TAG
SEQADV 5W15 HIS D 0 UNP B1YPY7 EXPRESSION TAG
SEQRES 1 A 275 MET ALA HIS HIS HIS HIS HIS HIS MET LEU ASP LEU ALA
SEQRES 2 A 275 ASN ARG PHE ASN PHE GLU GLY HIS ARG ILE ALA TRP GLY
SEQRES 3 A 275 THR LEU GLY GLU GLY PRO PRO LEU VAL LEU VAL HIS GLY
SEQRES 4 A 275 THR PRO PHE SER SER GLN VAL TRP ARG ARG ILE ALA PRO
SEQRES 5 A 275 TRP LEU ALA ARG ARG HIS ARG VAL PHE PHE TYR ASP LEU
SEQRES 6 A 275 LEU GLY TYR GLY GLN SER ASP MET PRO ASP ALA ASP VAL
SEQRES 7 A 275 SER LEU GLY ARG GLN ASN VAL LEU PHE GLY ALA LEU LEU
SEQRES 8 A 275 ASP GLU TRP LYS ILE SER ARG PRO ARG VAL LEU ALA HIS
SEQRES 9 A 275 ASP TYR GLY GLY ALA THR VAL LEU ARG ALA HIS PHE LEU
SEQRES 10 A 275 ASP GLY ILE ALA TYR SER ASP LEU THR LEU VAL ASN PRO
SEQRES 11 A 275 VAL ALA ILE ALA PRO GLN GLY SER PRO PHE VAL ARG HIS
SEQRES 12 A 275 VAL ALA GLN HIS GLU ALA ALA PHE THR GLY LEU PRO ALA
SEQRES 13 A 275 TYR ALA HIS HIS ALA LEU VAL SER ALA TYR ILE GLY GLN
SEQRES 14 A 275 ALA VAL ALA GLN PRO LEU SER ASP ASP VAL LEU SER ILE
SEQRES 15 A 275 TYR ARG ALA PRO TRP LEU THR PRO ALA GLY GLN ALA ALA
SEQRES 16 A 275 PHE TYR ARG GLN ILE ALA GLN MET ARG GLN ARG TYR ILE
SEQRES 17 A 275 GLU ASP ALA GLU ALA ARG TYR ALA PRO PRO ASP PHE PRO
SEQRES 18 A 275 VAL ARG ILE VAL TRP GLY GLU ASP ASP ARG TRP ILE PRO
SEQRES 19 A 275 LEU GLU GLN GLY GLN ALA LEU ALA ASP ARG ILE ALA ASN
SEQRES 20 A 275 GLY LYS LEU ILE ARG VAL PRO ARG ALA GLY HIS LEU VAL
SEQRES 21 A 275 GLN GLU ASP ALA PRO GLU ALA ILE VAL ALA ALA VAL LEU
SEQRES 22 A 275 ASP ARG
SEQRES 1 B 275 MET ALA HIS HIS HIS HIS HIS HIS MET LEU ASP LEU ALA
SEQRES 2 B 275 ASN ARG PHE ASN PHE GLU GLY HIS ARG ILE ALA TRP GLY
SEQRES 3 B 275 THR LEU GLY GLU GLY PRO PRO LEU VAL LEU VAL HIS GLY
SEQRES 4 B 275 THR PRO PHE SER SER GLN VAL TRP ARG ARG ILE ALA PRO
SEQRES 5 B 275 TRP LEU ALA ARG ARG HIS ARG VAL PHE PHE TYR ASP LEU
SEQRES 6 B 275 LEU GLY TYR GLY GLN SER ASP MET PRO ASP ALA ASP VAL
SEQRES 7 B 275 SER LEU GLY ARG GLN ASN VAL LEU PHE GLY ALA LEU LEU
SEQRES 8 B 275 ASP GLU TRP LYS ILE SER ARG PRO ARG VAL LEU ALA HIS
SEQRES 9 B 275 ASP TYR GLY GLY ALA THR VAL LEU ARG ALA HIS PHE LEU
SEQRES 10 B 275 ASP GLY ILE ALA TYR SER ASP LEU THR LEU VAL ASN PRO
SEQRES 11 B 275 VAL ALA ILE ALA PRO GLN GLY SER PRO PHE VAL ARG HIS
SEQRES 12 B 275 VAL ALA GLN HIS GLU ALA ALA PHE THR GLY LEU PRO ALA
SEQRES 13 B 275 TYR ALA HIS HIS ALA LEU VAL SER ALA TYR ILE GLY GLN
SEQRES 14 B 275 ALA VAL ALA GLN PRO LEU SER ASP ASP VAL LEU SER ILE
SEQRES 15 B 275 TYR ARG ALA PRO TRP LEU THR PRO ALA GLY GLN ALA ALA
SEQRES 16 B 275 PHE TYR ARG GLN ILE ALA GLN MET ARG GLN ARG TYR ILE
SEQRES 17 B 275 GLU ASP ALA GLU ALA ARG TYR ALA PRO PRO ASP PHE PRO
SEQRES 18 B 275 VAL ARG ILE VAL TRP GLY GLU ASP ASP ARG TRP ILE PRO
SEQRES 19 B 275 LEU GLU GLN GLY GLN ALA LEU ALA ASP ARG ILE ALA ASN
SEQRES 20 B 275 GLY LYS LEU ILE ARG VAL PRO ARG ALA GLY HIS LEU VAL
SEQRES 21 B 275 GLN GLU ASP ALA PRO GLU ALA ILE VAL ALA ALA VAL LEU
SEQRES 22 B 275 ASP ARG
SEQRES 1 C 275 MET ALA HIS HIS HIS HIS HIS HIS MET LEU ASP LEU ALA
SEQRES 2 C 275 ASN ARG PHE ASN PHE GLU GLY HIS ARG ILE ALA TRP GLY
SEQRES 3 C 275 THR LEU GLY GLU GLY PRO PRO LEU VAL LEU VAL HIS GLY
SEQRES 4 C 275 THR PRO PHE SER SER GLN VAL TRP ARG ARG ILE ALA PRO
SEQRES 5 C 275 TRP LEU ALA ARG ARG HIS ARG VAL PHE PHE TYR ASP LEU
SEQRES 6 C 275 LEU GLY TYR GLY GLN SER ASP MET PRO ASP ALA ASP VAL
SEQRES 7 C 275 SER LEU GLY ARG GLN ASN VAL LEU PHE GLY ALA LEU LEU
SEQRES 8 C 275 ASP GLU TRP LYS ILE SER ARG PRO ARG VAL LEU ALA HIS
SEQRES 9 C 275 ASP TYR GLY GLY ALA THR VAL LEU ARG ALA HIS PHE LEU
SEQRES 10 C 275 ASP GLY ILE ALA TYR SER ASP LEU THR LEU VAL ASN PRO
SEQRES 11 C 275 VAL ALA ILE ALA PRO GLN GLY SER PRO PHE VAL ARG HIS
SEQRES 12 C 275 VAL ALA GLN HIS GLU ALA ALA PHE THR GLY LEU PRO ALA
SEQRES 13 C 275 TYR ALA HIS HIS ALA LEU VAL SER ALA TYR ILE GLY GLN
SEQRES 14 C 275 ALA VAL ALA GLN PRO LEU SER ASP ASP VAL LEU SER ILE
SEQRES 15 C 275 TYR ARG ALA PRO TRP LEU THR PRO ALA GLY GLN ALA ALA
SEQRES 16 C 275 PHE TYR ARG GLN ILE ALA GLN MET ARG GLN ARG TYR ILE
SEQRES 17 C 275 GLU ASP ALA GLU ALA ARG TYR ALA PRO PRO ASP PHE PRO
SEQRES 18 C 275 VAL ARG ILE VAL TRP GLY GLU ASP ASP ARG TRP ILE PRO
SEQRES 19 C 275 LEU GLU GLN GLY GLN ALA LEU ALA ASP ARG ILE ALA ASN
SEQRES 20 C 275 GLY LYS LEU ILE ARG VAL PRO ARG ALA GLY HIS LEU VAL
SEQRES 21 C 275 GLN GLU ASP ALA PRO GLU ALA ILE VAL ALA ALA VAL LEU
SEQRES 22 C 275 ASP ARG
SEQRES 1 D 275 MET ALA HIS HIS HIS HIS HIS HIS MET LEU ASP LEU ALA
SEQRES 2 D 275 ASN ARG PHE ASN PHE GLU GLY HIS ARG ILE ALA TRP GLY
SEQRES 3 D 275 THR LEU GLY GLU GLY PRO PRO LEU VAL LEU VAL HIS GLY
SEQRES 4 D 275 THR PRO PHE SER SER GLN VAL TRP ARG ARG ILE ALA PRO
SEQRES 5 D 275 TRP LEU ALA ARG ARG HIS ARG VAL PHE PHE TYR ASP LEU
SEQRES 6 D 275 LEU GLY TYR GLY GLN SER ASP MET PRO ASP ALA ASP VAL
SEQRES 7 D 275 SER LEU GLY ARG GLN ASN VAL LEU PHE GLY ALA LEU LEU
SEQRES 8 D 275 ASP GLU TRP LYS ILE SER ARG PRO ARG VAL LEU ALA HIS
SEQRES 9 D 275 ASP TYR GLY GLY ALA THR VAL LEU ARG ALA HIS PHE LEU
SEQRES 10 D 275 ASP GLY ILE ALA TYR SER ASP LEU THR LEU VAL ASN PRO
SEQRES 11 D 275 VAL ALA ILE ALA PRO GLN GLY SER PRO PHE VAL ARG HIS
SEQRES 12 D 275 VAL ALA GLN HIS GLU ALA ALA PHE THR GLY LEU PRO ALA
SEQRES 13 D 275 TYR ALA HIS HIS ALA LEU VAL SER ALA TYR ILE GLY GLN
SEQRES 14 D 275 ALA VAL ALA GLN PRO LEU SER ASP ASP VAL LEU SER ILE
SEQRES 15 D 275 TYR ARG ALA PRO TRP LEU THR PRO ALA GLY GLN ALA ALA
SEQRES 16 D 275 PHE TYR ARG GLN ILE ALA GLN MET ARG GLN ARG TYR ILE
SEQRES 17 D 275 GLU ASP ALA GLU ALA ARG TYR ALA PRO PRO ASP PHE PRO
SEQRES 18 D 275 VAL ARG ILE VAL TRP GLY GLU ASP ASP ARG TRP ILE PRO
SEQRES 19 D 275 LEU GLU GLN GLY GLN ALA LEU ALA ASP ARG ILE ALA ASN
SEQRES 20 D 275 GLY LYS LEU ILE ARG VAL PRO ARG ALA GLY HIS LEU VAL
SEQRES 21 D 275 GLN GLU ASP ALA PRO GLU ALA ILE VAL ALA ALA VAL LEU
SEQRES 22 D 275 ASP ARG
HET EDO A 301 4
HET EDO A 302 4
HET CL A 303 1
HET CL A 304 1
HET CL A 305 1
HET CL B 301 1
HET CL B 302 1
HET MG C 301 1
HET CL C 302 1
HET CL C 303 1
HET MG D 301 1
HET CL D 302 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 EDO 2(C2 H6 O2)
FORMUL 7 CL 8(CL 1-)
FORMUL 12 MG 2(MG 2+)
FORMUL 17 HOH *1363(H2 O)
HELIX 1 AA1 SER A 35 ARG A 40 5 6
HELIX 2 AA2 ILE A 42 ALA A 47 1 6
HELIX 3 AA3 SER A 71 LYS A 87 1 17
HELIX 4 AA4 ASP A 97 LEU A 109 1 13
HELIX 5 AA5 SER A 130 ALA A 137 1 8
HELIX 6 AA6 HIS A 139 GLY A 145 1 7
HELIX 7 AA7 PRO A 147 GLN A 161 1 15
HELIX 8 AA8 SER A 168 ALA A 177 1 10
HELIX 9 AA9 PRO A 178 LEU A 180 5 3
HELIX 10 AB1 THR A 181 GLN A 194 1 14
HELIX 11 AB2 GLN A 197 ALA A 205 1 9
HELIX 12 AB3 PRO A 226 ALA A 238 1 13
HELIX 13 AB4 LEU A 251 ALA A 256 1 6
HELIX 14 AB5 ALA A 256 ASP A 266 1 11
HELIX 15 AB6 SER B 35 ARG B 40 5 6
HELIX 16 AB7 ILE B 42 ALA B 47 1 6
HELIX 17 AB8 SER B 71 TRP B 86 1 16
HELIX 18 AB9 ASP B 97 LEU B 109 1 13
HELIX 19 AC1 SER B 130 ALA B 137 1 8
HELIX 20 AC2 HIS B 139 GLY B 145 1 7
HELIX 21 AC3 PRO B 147 GLN B 161 1 15
HELIX 22 AC4 SER B 168 ALA B 177 1 10
HELIX 23 AC5 PRO B 178 LEU B 180 5 3
HELIX 24 AC6 THR B 181 GLN B 194 1 14
HELIX 25 AC7 GLN B 197 ALA B 205 1 9
HELIX 26 AC8 PRO B 226 ALA B 238 1 13
HELIX 27 AC9 LEU B 251 ALA B 256 1 6
HELIX 28 AD1 ALA B 256 ASP B 266 1 11
HELIX 29 AD2 SER C 35 ARG C 40 5 6
HELIX 30 AD3 ILE C 42 ALA C 47 1 6
HELIX 31 AD4 SER C 71 TRP C 86 1 16
HELIX 32 AD5 ASP C 97 LEU C 109 1 13
HELIX 33 AD6 SER C 130 ALA C 137 1 8
HELIX 34 AD7 HIS C 139 GLY C 145 1 7
HELIX 35 AD8 PRO C 147 GLN C 161 1 15
HELIX 36 AD9 SER C 168 ALA C 177 1 10
HELIX 37 AE1 PRO C 178 LEU C 180 5 3
HELIX 38 AE2 THR C 181 GLN C 194 1 14
HELIX 39 AE3 GLN C 197 ALA C 205 1 9
HELIX 40 AE4 PRO C 226 ALA C 238 1 13
HELIX 41 AE5 LEU C 251 ALA C 256 1 6
HELIX 42 AE6 ALA C 256 ASP C 266 1 11
HELIX 43 AE7 SER D 35 ARG D 40 5 6
HELIX 44 AE8 ILE D 42 ALA D 47 1 6
HELIX 45 AE9 SER D 71 TRP D 86 1 16
HELIX 46 AF1 ASP D 97 LEU D 109 1 13
HELIX 47 AF2 SER D 130 ALA D 137 1 8
HELIX 48 AF3 HIS D 139 GLY D 145 1 7
HELIX 49 AF4 PRO D 147 GLN D 161 1 15
HELIX 50 AF5 SER D 168 ALA D 177 1 10
HELIX 51 AF6 PRO D 178 LEU D 180 5 3
HELIX 52 AF7 THR D 181 GLN D 194 1 14
HELIX 53 AF8 GLN D 197 ALA D 205 1 9
HELIX 54 AF9 PRO D 226 ALA D 238 1 13
HELIX 55 AG1 LEU D 251 ALA D 256 1 6
HELIX 56 AG2 ALA D 256 ASP D 266 1 11
SHEET 1 AA1 8 ASN A 6 PHE A 10 0
SHEET 2 AA1 8 HIS A 13 LEU A 20 -1 O HIS A 13 N PHE A 10
SHEET 3 AA1 8 ARG A 51 TYR A 55 -1 O VAL A 52 N LEU A 20
SHEET 4 AA1 8 PRO A 25 VAL A 29 1 N LEU A 28 O PHE A 53
SHEET 5 AA1 8 ARG A 92 HIS A 96 1 O ARG A 92 N VAL A 27
SHEET 6 AA1 8 ASP A 116 VAL A 120 1 O THR A 118 N VAL A 93
SHEET 7 AA1 8 VAL A 214 GLY A 219 1 O VAL A 217 N LEU A 119
SHEET 8 AA1 8 ILE A 243 VAL A 245 1 O ILE A 243 N ILE A 216
SHEET 1 AA2 8 ASN B 6 PHE B 10 0
SHEET 2 AA2 8 HIS B 13 LEU B 20 -1 O HIS B 13 N PHE B 10
SHEET 3 AA2 8 ARG B 51 TYR B 55 -1 O VAL B 52 N LEU B 20
SHEET 4 AA2 8 PRO B 25 VAL B 29 1 N LEU B 26 O PHE B 53
SHEET 5 AA2 8 ARG B 92 HIS B 96 1 O LEU B 94 N VAL B 27
SHEET 6 AA2 8 ASP B 116 VAL B 120 1 O THR B 118 N VAL B 93
SHEET 7 AA2 8 VAL B 214 GLY B 219 1 O VAL B 217 N LEU B 119
SHEET 8 AA2 8 ILE B 243 VAL B 245 1 O ILE B 243 N ILE B 216
SHEET 1 AA3 8 ASN C 6 PHE C 10 0
SHEET 2 AA3 8 HIS C 13 LEU C 20 -1 O HIS C 13 N PHE C 10
SHEET 3 AA3 8 ARG C 51 TYR C 55 -1 O VAL C 52 N LEU C 20
SHEET 4 AA3 8 PRO C 25 VAL C 29 1 N LEU C 28 O PHE C 53
SHEET 5 AA3 8 ARG C 92 HIS C 96 1 O ARG C 92 N VAL C 27
SHEET 6 AA3 8 ASP C 116 VAL C 120 1 O THR C 118 N VAL C 93
SHEET 7 AA3 8 VAL C 214 GLY C 219 1 O VAL C 217 N LEU C 119
SHEET 8 AA3 8 ILE C 243 VAL C 245 1 O ILE C 243 N ILE C 216
SHEET 1 AA4 8 ASN D 6 PHE D 10 0
SHEET 2 AA4 8 HIS D 13 LEU D 20 -1 O HIS D 13 N PHE D 10
SHEET 3 AA4 8 ARG D 51 TYR D 55 -1 O VAL D 52 N LEU D 20
SHEET 4 AA4 8 PRO D 25 VAL D 29 1 N LEU D 28 O PHE D 53
SHEET 5 AA4 8 ARG D 92 HIS D 96 1 O LEU D 94 N VAL D 27
SHEET 6 AA4 8 ASP D 116 VAL D 120 1 O THR D 118 N VAL D 93
SHEET 7 AA4 8 VAL D 214 GLY D 219 1 O VAL D 217 N LEU D 119
SHEET 8 AA4 8 ILE D 243 VAL D 245 1 O ILE D 243 N ILE D 216
LINK OH TYR C 149 MG MG C 301 1555 1555 2.89
CISPEP 1 THR A 32 PRO A 33 0 -2.74
CISPEP 2 ALA A 126 PRO A 127 0 -3.34
CISPEP 3 THR B 32 PRO B 33 0 -3.28
CISPEP 4 ALA B 126 PRO B 127 0 -3.19
CISPEP 5 THR C 32 PRO C 33 0 -1.02
CISPEP 6 ALA C 126 PRO C 127 0 -0.13
CISPEP 7 THR D 32 PRO D 33 0 -2.30
CISPEP 8 ALA D 126 PRO D 127 0 -1.89
SITE 1 AC1 7 ALA A 5 ASN A 6 ARG A 7 HOH A 502
SITE 2 AC1 7 PRO D 209 PRO D 210 ASP D 211
SITE 1 AC2 5 PRO A 213 VAL A 214 HOH A 460 HOH A 478
SITE 2 AC2 5 HOH A 510
SITE 1 AC3 5 HIS A -2 HIS A -1 ARG A 40 HOH A 407
SITE 2 AC3 5 HOH A 694
SITE 1 AC4 2 ARG A 196 GLN A 197
SITE 1 AC5 4 ASN A 9 PHE A 10 GLU A 11 HOH A 738
SITE 1 AC6 3 ARG B 196 GLN B 197 HOH B 626
SITE 1 AC7 4 SER B 173 ARG B 176 LEU B 180 HOH B 700
SITE 1 AC8 1 TYR C 149
SITE 1 AC9 3 ARG C 196 GLN C 197 HOH C 623
SITE 1 AD1 5 ASN C 9 PHE C 10 GLU C 11 HOH C 684
SITE 2 AD1 5 HOH C 694
SITE 1 AD2 5 ARG C 90 HOH C 563 GLN D 231 ARG D 244
SITE 2 AD2 5 HOH D 675
SITE 1 AD3 2 ARG D 196 GLN D 197
CRYST1 60.070 143.590 75.850 90.00 111.34 90.00 P 1 21 1 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 0.016647 0.000000 0.006504 0.00000
SCALE2 0.000000 0.006964 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014154 0.00000
TER 2164 ARG A 267
TER 4339 ARG B 267
TER 6502 ARG C 267
TER 8671 ARG D 267
MASTER 720 0 12 56 32 0 17 6 9850 4 10 88
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