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HEADER HYDROLASE 23-JUL-12 4G8D
TITLE CRYSTAL STRUCTURES OF N-ACYL HOMOSERINE LACTONASE AIDH S102G MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FOLD PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: AHL-LACTONASE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OCHROBACTRUM;
SOURCE 3 ORGANISM_TAXID: 680275;
SOURCE 4 STRAIN: T63;
SOURCE 5 GENE: AIDH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA-HYDROLASE FOLD, AHL-LACTONASE, AHL-BINDING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.C.LIANG,X.X.YAN,A.GAO
REVDAT 1 16-JAN-13 4G8D 0
JRNL AUTH A.GAO,G.Y.MEI,S.LIU,P.WANG,Q.TANG,Y.P.LIU,H.WEN,X.M.AN,
JRNL AUTH 2 L.Q.ZHANG,X.X.YAN,D.C.LIANG
JRNL TITL HIGH-RESOLUTION STRUCTURES OF AIDH COMPLEXES PROVIDE
JRNL TITL 2 INSIGHTS INTO A NOVEL CATALYTIC MECHANISM FOR N-ACYL
JRNL TITL 3 HOMOSERINE LACTONASE
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 69 82 2013
JRNL REFN ISSN 0907-4449
JRNL PMID 23275166
JRNL DOI 10.1107/S0907444912042369
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 97703
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.135
REMARK 3 R VALUE (WORKING SET) : 0.133
REMARK 3 FREE R VALUE : 0.168
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 4879
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 19.8272 - 2.9058 0.99 9335 481 0.1276 0.1604
REMARK 3 2 2.9058 - 2.3075 1.00 9353 459 0.1411 0.1834
REMARK 3 3 2.3075 - 2.0161 1.00 9291 452 0.1300 0.1614
REMARK 3 4 2.0161 - 1.8320 1.00 9319 476 0.1305 0.1707
REMARK 3 5 1.8320 - 1.7007 1.00 9246 509 0.1255 0.1589
REMARK 3 6 1.7007 - 1.6005 1.00 9300 518 0.1240 0.1675
REMARK 3 7 1.6005 - 1.5204 1.00 9228 486 0.1263 0.1537
REMARK 3 8 1.5204 - 1.4542 1.00 9259 510 0.1354 0.1575
REMARK 3 9 1.4542 - 1.3982 1.00 9262 474 0.1476 0.1698
REMARK 3 10 1.3982 - 1.3500 0.99 9231 514 0.1747 0.2197
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.39
REMARK 3 B_SOL : 96.00
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.960
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.23
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.33390
REMARK 3 B22 (A**2) : -1.77260
REMARK 3 B33 (A**2) : 0.43860
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.92700
REMARK 3 B23 (A**2) : -0.00000
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 4420
REMARK 3 ANGLE : 1.035 5991
REMARK 3 CHIRALITY : 0.069 626
REMARK 3 PLANARITY : 0.005 812
REMARK 3 DIHEDRAL : 12.296 1633
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (chain A and resid 3:19)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9573 67.5566 22.2895
REMARK 3 T TENSOR
REMARK 3 T11: 0.0730 T22: 0.1230
REMARK 3 T33: 0.1177 T12: 0.0073
REMARK 3 T13: 0.0151 T23: -0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 0.2599 L22: 1.0831
REMARK 3 L33: 1.0443 L12: 0.4444
REMARK 3 L13: -0.1415 L23: -0.4607
REMARK 3 S TENSOR
REMARK 3 S11: -0.0221 S12: -0.0893 S13: 0.1186
REMARK 3 S21: 0.1118 S22: 0.0856 S23: 0.1854
REMARK 3 S31: 0.0203 S32: -0.2822 S33: 0.0045
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (chain A and resid 20:81)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5308 70.3609 18.3609
REMARK 3 T TENSOR
REMARK 3 T11: 0.0531 T22: 0.0564
REMARK 3 T33: 0.0751 T12: 0.0164
REMARK 3 T13: -0.0108 T23: -0.0113
REMARK 3 L TENSOR
REMARK 3 L11: 0.2855 L22: 0.7698
REMARK 3 L33: 0.8197 L12: 0.4562
REMARK 3 L13: 0.1742 L23: 0.1074
REMARK 3 S TENSOR
REMARK 3 S11: -0.0579 S12: -0.0507 S13: 0.0725
REMARK 3 S21: 0.0721 S22: -0.0172 S23: 0.1400
REMARK 3 S31: -0.0796 S32: -0.0680 S33: 0.0739
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain A and resid 82:89)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.1775 61.9442 12.7656
REMARK 3 T TENSOR
REMARK 3 T11: 0.0571 T22: 0.0891
REMARK 3 T33: 0.0937 T12: 0.0001
REMARK 3 T13: -0.0125 T23: -0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 0.6950 L22: 1.6363
REMARK 3 L33: 1.4767 L12: 0.9907
REMARK 3 L13: -0.2333 L23: 0.0803
REMARK 3 S TENSOR
REMARK 3 S11: -0.0634 S12: 0.0445 S13: 0.1091
REMARK 3 S21: 0.0011 S22: -0.0334 S23: 0.2114
REMARK 3 S31: 0.1154 S32: -0.2076 S33: 0.0983
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain A and resid 90:142)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.2859 67.7031 9.0476
REMARK 3 T TENSOR
REMARK 3 T11: 0.0475 T22: 0.0205
REMARK 3 T33: 0.0410 T12: -0.0051
REMARK 3 T13: -0.0151 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.3299 L22: 0.9751
REMARK 3 L33: 0.5506 L12: 0.2499
REMARK 3 L13: -0.1090 L23: 0.2415
REMARK 3 S TENSOR
REMARK 3 S11: -0.0701 S12: 0.0037 S13: -0.0361
REMARK 3 S21: -0.0973 S22: 0.0368 S23: -0.0161
REMARK 3 S31: -0.0316 S32: 0.0321 S33: 0.0288
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (chain A and resid 143:158)
REMARK 3 ORIGIN FOR THE GROUP (A): 41.7999 66.7378 30.4037
REMARK 3 T TENSOR
REMARK 3 T11: 0.1409 T22: 0.0984
REMARK 3 T33: 0.0962 T12: -0.0106
REMARK 3 T13: -0.0515 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 1.4116 L22: 1.1790
REMARK 3 L33: 0.7975 L12: 0.2040
REMARK 3 L13: 0.9606 L23: -0.0197
REMARK 3 S TENSOR
REMARK 3 S11: -0.0501 S12: -0.0668 S13: 0.0983
REMARK 3 S21: 0.2691 S22: 0.0312 S23: -0.1325
REMARK 3 S31: -0.1308 S32: 0.1507 S33: 0.0767
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (chain A and resid 159:185)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.2837 72.2544 28.6513
REMARK 3 T TENSOR
REMARK 3 T11: 0.1248 T22: 0.0841
REMARK 3 T33: 0.0796 T12: -0.0073
REMARK 3 T13: -0.0240 T23: -0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.2507 L22: 0.9318
REMARK 3 L33: 0.1390 L12: 0.1078
REMARK 3 L13: 0.0359 L23: 0.2217
REMARK 3 S TENSOR
REMARK 3 S11: 0.0228 S12: -0.0570 S13: 0.0444
REMARK 3 S21: 0.2266 S22: -0.0622 S23: -0.0327
REMARK 3 S31: 0.0007 S32: -0.0049 S33: 0.0319
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (chain A and resid 186:198)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.8468 56.5153 16.5440
REMARK 3 T TENSOR
REMARK 3 T11: 0.0669 T22: 0.1331
REMARK 3 T33: 0.1019 T12: 0.0091
REMARK 3 T13: -0.0176 T23: -0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 1.6010 L22: 1.2060
REMARK 3 L33: 5.1036 L12: 0.6132
REMARK 3 L13: 2.8523 L23: 1.1622
REMARK 3 S TENSOR
REMARK 3 S11: 0.0065 S12: 0.2707 S13: 0.0116
REMARK 3 S21: 0.1099 S22: 0.1988 S23: -0.3123
REMARK 3 S31: -0.0275 S32: 0.7519 S33: -0.1585
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (chain A and resid 199:218)
REMARK 3 ORIGIN FOR THE GROUP (A): 37.0604 70.4127 3.3441
REMARK 3 T TENSOR
REMARK 3 T11: 0.1152 T22: 0.0648
REMARK 3 T33: 0.0659 T12: -0.0256
REMARK 3 T13: 0.0027 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.4321 L22: 0.7991
REMARK 3 L33: 0.3691 L12: 0.1385
REMARK 3 L13: 0.0937 L23: 0.4555
REMARK 3 S TENSOR
REMARK 3 S11: -0.0524 S12: 0.0744 S13: -0.0051
REMARK 3 S21: -0.2417 S22: -0.0102 S23: -0.0500
REMARK 3 S31: -0.1526 S32: 0.0623 S33: 0.0493
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (chain A and resid 219:256)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.9859 78.4197 8.7829
REMARK 3 T TENSOR
REMARK 3 T11: 0.1317 T22: 0.0536
REMARK 3 T33: 0.0802 T12: -0.0420
REMARK 3 T13: -0.0061 T23: 0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 0.3796 L22: 0.5835
REMARK 3 L33: 0.8951 L12: 0.1600
REMARK 3 L13: 0.0966 L23: 0.4680
REMARK 3 S TENSOR
REMARK 3 S11: -0.0885 S12: 0.0139 S13: 0.0607
REMARK 3 S21: -0.1828 S22: 0.1001 S23: -0.1161
REMARK 3 S31: -0.2913 S32: 0.1223 S33: 0.0005
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (chain A and resid 257:271)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.9631 83.2748 4.5084
REMARK 3 T TENSOR
REMARK 3 T11: 0.2404 T22: 0.0500
REMARK 3 T33: 0.1375 T12: -0.0051
REMARK 3 T13: -0.1285 T23: 0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 0.5838 L22: 0.9070
REMARK 3 L33: 0.8574 L12: 0.6207
REMARK 3 L13: 0.5747 L23: 0.3422
REMARK 3 S TENSOR
REMARK 3 S11: -0.2750 S12: -0.0312 S13: 0.2612
REMARK 3 S21: -0.5172 S22: 0.0407 S23: 0.3953
REMARK 3 S31: -0.3343 S32: -0.1045 S33: 0.2405
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (chain B and resid 3:15)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4251 43.7322 13.5814
REMARK 3 T TENSOR
REMARK 3 T11: 0.0912 T22: 0.1073
REMARK 3 T33: 0.0969 T12: 0.0314
REMARK 3 T13: -0.0017 T23: -0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 2.1900 L22: 4.6685
REMARK 3 L33: 1.0044 L12: -3.0713
REMARK 3 L13: 1.0341 L23: -1.1982
REMARK 3 S TENSOR
REMARK 3 S11: -0.1716 S12: -0.3051 S13: -0.1404
REMARK 3 S21: 0.3163 S22: 0.2434 S23: 0.5105
REMARK 3 S31: -0.1348 S32: -0.2364 S33: -0.0486
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (chain B and resid 16:26)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2018 32.0147 17.5798
REMARK 3 T TENSOR
REMARK 3 T11: 0.0783 T22: 0.0923
REMARK 3 T33: 0.1133 T12: 0.0160
REMARK 3 T13: 0.0154 T23: 0.0249
REMARK 3 L TENSOR
REMARK 3 L11: 1.0469 L22: 3.4944
REMARK 3 L33: 2.7299 L12: -1.8781
REMARK 3 L13: 1.6905 L23: -3.0326
REMARK 3 S TENSOR
REMARK 3 S11: -0.0649 S12: -0.2702 S13: -0.2270
REMARK 3 S21: 0.1980 S22: 0.2793 S23: 0.3174
REMARK 3 S31: -0.0821 S32: -0.3506 S33: -0.2075
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (chain B and resid 27:64)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.5580 33.3263 9.2127
REMARK 3 T TENSOR
REMARK 3 T11: 0.0469 T22: 0.0538
REMARK 3 T33: 0.0844 T12: 0.0013
REMARK 3 T13: -0.0081 T23: 0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 0.3257 L22: 0.5619
REMARK 3 L33: 0.5046 L12: -0.2941
REMARK 3 L13: 0.2904 L23: -0.2191
REMARK 3 S TENSOR
REMARK 3 S11: 0.0110 S12: 0.0063 S13: -0.0417
REMARK 3 S21: -0.0184 S22: 0.0361 S23: 0.1257
REMARK 3 S31: 0.0453 S32: -0.0290 S33: -0.0498
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (chain B and resid 65:108)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.8721 45.9470 9.8461
REMARK 3 T TENSOR
REMARK 3 T11: 0.0444 T22: 0.0499
REMARK 3 T33: 0.0696 T12: 0.0018
REMARK 3 T13: -0.0052 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.4997 L22: 0.4856
REMARK 3 L33: 0.4806 L12: 0.0383
REMARK 3 L13: 0.1814 L23: 0.1487
REMARK 3 S TENSOR
REMARK 3 S11: -0.0278 S12: -0.0071 S13: 0.0764
REMARK 3 S21: 0.0106 S22: 0.0086 S23: 0.0415
REMARK 3 S31: -0.0400 S32: -0.0182 S33: 0.0205
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (chain B and resid 109:143)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.9060 42.3229 2.8722
REMARK 3 T TENSOR
REMARK 3 T11: 0.0483 T22: 0.0556
REMARK 3 T33: 0.0833 T12: 0.0053
REMARK 3 T13: -0.0024 T23: 0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 0.5391 L22: 0.5674
REMARK 3 L33: 0.6534 L12: 0.0762
REMARK 3 L13: -0.4682 L23: 0.0815
REMARK 3 S TENSOR
REMARK 3 S11: 0.0297 S12: 0.0504 S13: 0.0538
REMARK 3 S21: -0.0176 S22: 0.0021 S23: -0.0391
REMARK 3 S31: -0.0592 S32: -0.0220 S33: -0.0329
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (chain B and resid 144:170)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5160 37.5976 -9.9321
REMARK 3 T TENSOR
REMARK 3 T11: 0.1417 T22: 0.0808
REMARK 3 T33: 0.1051 T12: -0.0171
REMARK 3 T13: -0.0464 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.5732 L22: 0.3227
REMARK 3 L33: 0.8252 L12: -0.4133
REMARK 3 L13: 0.3753 L23: -0.3906
REMARK 3 S TENSOR
REMARK 3 S11: 0.0343 S12: 0.0424 S13: -0.0808
REMARK 3 S21: -0.1909 S22: 0.0370 S23: 0.1869
REMARK 3 S31: 0.1040 S32: -0.0350 S33: -0.1193
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (chain B and resid 171:193)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3255 46.1803 -3.7694
REMARK 3 T TENSOR
REMARK 3 T11: 0.0719 T22: 0.0799
REMARK 3 T33: 0.1022 T12: -0.0092
REMARK 3 T13: -0.0312 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 1.8356 L22: 1.3685
REMARK 3 L33: 1.2451 L12: 1.4294
REMARK 3 L13: 0.9182 L23: 0.7903
REMARK 3 S TENSOR
REMARK 3 S11: -0.0349 S12: 0.2161 S13: -0.0648
REMARK 3 S21: -0.1197 S22: 0.0922 S23: 0.0156
REMARK 3 S31: -0.0271 S32: 0.1072 S33: -0.0517
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (chain B and resid 194:209)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.4014 47.5742 6.7290
REMARK 3 T TENSOR
REMARK 3 T11: 0.0427 T22: 0.0754
REMARK 3 T33: 0.0994 T12: -0.0018
REMARK 3 T13: 0.0008 T23: -0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.1390 L22: 0.7993
REMARK 3 L33: 0.1660 L12: 0.2280
REMARK 3 L13: -0.1258 L23: -0.2399
REMARK 3 S TENSOR
REMARK 3 S11: -0.0162 S12: 0.0312 S13: 0.0207
REMARK 3 S21: -0.0184 S22: -0.0549 S23: -0.1828
REMARK 3 S31: -0.0102 S32: 0.0369 S33: 0.0684
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (chain B and resid 210:267)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.0152 29.5909 2.4330
REMARK 3 T TENSOR
REMARK 3 T11: 0.0521 T22: 0.0545
REMARK 3 T33: 0.0848 T12: 0.0133
REMARK 3 T13: -0.0034 T23: -0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 0.6563 L22: 0.5166
REMARK 3 L33: 0.3716 L12: -0.0205
REMARK 3 L13: 0.3385 L23: -0.1000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0580 S12: 0.0705 S13: -0.1310
REMARK 3 S21: -0.0423 S22: 0.0027 S23: -0.1103
REMARK 3 S31: 0.0760 S32: 0.0522 S33: -0.0609
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (chain B and resid 268:273)
REMARK 3 ORIGIN FOR THE GROUP (A): 37.2533 28.0863 21.2793
REMARK 3 T TENSOR
REMARK 3 T11: 0.2042 T22: 0.0881
REMARK 3 T33: 0.1348 T12: 0.0193
REMARK 3 T13: -0.0644 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.6981 L22: 0.1390
REMARK 3 L33: 1.3300 L12: 0.2647
REMARK 3 L13: 0.9443 L23: 0.4030
REMARK 3 S TENSOR
REMARK 3 S11: 0.0341 S12: -0.1327 S13: -0.1128
REMARK 3 S21: 0.4993 S22: 0.0746 S23: -0.4209
REMARK 3 S31: 0.4053 S32: 0.2962 S33: -0.1388
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 4G8D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-AUG-12.
REMARK 100 THE RCSB ID CODE IS RCSB073866.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 180
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 99376
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 50.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHENIX
REMARK 200 STARTING MODEL: 4G5X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG8000, 0.2M LIAC, 0.1M NAAC, PH
REMARK 280 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 64.97050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 HIS A 279
REMARK 465 MET B 1
REMARK 465 HIS B 275
REMARK 465 HIS B 276
REMARK 465 HIS B 277
REMARK 465 HIS B 278
REMARK 465 HIS B 279
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 267 N CA C O CB CG CD
REMARK 480 ARG A 267 NE CZ NH1 NH2
REMARK 480 LEU A 272 C
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 35 -156.30 -107.22
REMARK 500 ASP A 218 35.26 -99.97
REMARK 500 SER B 35 -155.91 -106.25
REMARK 500 ASN B 234 76.57 -155.77
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 598 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH A 599 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH A 796 DISTANCE = 8.07 ANGSTROMS
REMARK 525 HOH B 703 DISTANCE = 5.41 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4G5X RELATED DB: PDB
REMARK 900 RELATED ID: 4G8B RELATED DB: PDB
REMARK 900 RELATED ID: 4G8C RELATED DB: PDB
REMARK 900 RELATED ID: 4G9E RELATED DB: PDB
REMARK 900 RELATED ID: 4G9G RELATED DB: PDB
DBREF 4G8D A 1 271 UNP D2J2T6 D2J2T6_9RHIZ 1 271
DBREF 4G8D B 1 271 UNP D2J2T6 D2J2T6_9RHIZ 1 271
SEQADV 4G8D GLY A 102 UNP D2J2T6 SER 102 ENGINEERED MUTATION
SEQADV 4G8D LEU A 272 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G8D GLU A 273 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G8D HIS A 274 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G8D HIS A 275 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G8D HIS A 276 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G8D HIS A 277 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G8D HIS A 278 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G8D HIS A 279 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G8D GLY B 102 UNP D2J2T6 SER 102 ENGINEERED MUTATION
SEQADV 4G8D LEU B 272 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G8D GLU B 273 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G8D HIS B 274 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G8D HIS B 275 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G8D HIS B 276 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G8D HIS B 277 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G8D HIS B 278 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G8D HIS B 279 UNP D2J2T6 EXPRESSION TAG
SEQRES 1 A 279 MET THR ILE ASN TYR HIS GLU LEU GLU THR SER HIS GLY
SEQRES 2 A 279 ARG ILE ALA VAL ARG GLU SER GLU GLY GLU GLY ALA PRO
SEQRES 3 A 279 LEU LEU MET ILE HIS GLY ASN SER SER SER GLY ALA ILE
SEQRES 4 A 279 PHE ALA PRO GLN LEU GLU GLY GLU ILE GLY LYS LYS TRP
SEQRES 5 A 279 ARG VAL ILE ALA PRO ASP LEU PRO GLY HIS GLY LYS SER
SEQRES 6 A 279 THR ASP ALA ILE ASP PRO ASP ARG SER TYR SER MET GLU
SEQRES 7 A 279 GLY TYR ALA ASP ALA MET THR GLU VAL MET GLN GLN LEU
SEQRES 8 A 279 GLY ILE ALA ASP ALA VAL VAL PHE GLY TRP GLY LEU GLY
SEQRES 9 A 279 GLY HIS ILE GLY ILE GLU MET ILE ALA ARG TYR PRO GLU
SEQRES 10 A 279 MET ARG GLY LEU MET ILE THR GLY THR PRO PRO VAL ALA
SEQRES 11 A 279 ARG GLU GLU VAL GLY GLN GLY PHE LYS SER GLY PRO ASP
SEQRES 12 A 279 MET ALA LEU ALA GLY GLN GLU ILE PHE SER GLU ARG ASP
SEQRES 13 A 279 VAL GLU SER TYR ALA ARG SER THR CYS GLY GLU PRO PHE
SEQRES 14 A 279 GLU ALA SER LEU LEU ASP ILE VAL ALA ARG THR ASP GLY
SEQRES 15 A 279 ARG ALA ARG ARG ILE MET PHE GLU LYS PHE GLY SER GLY
SEQRES 16 A 279 THR GLY GLY ASN GLN ARG ASP ILE VAL ALA GLU ALA GLN
SEQRES 17 A 279 LEU PRO ILE ALA VAL VAL ASN GLY ARG ASP GLU PRO PHE
SEQRES 18 A 279 VAL GLU LEU ASP PHE VAL SER LYS VAL LYS PHE GLY ASN
SEQRES 19 A 279 LEU TRP GLU GLY LYS THR HIS VAL ILE ASP ASN ALA GLY
SEQRES 20 A 279 HIS ALA PRO PHE ARG GLU ALA PRO ALA GLU PHE ASP ALA
SEQRES 21 A 279 TYR LEU ALA ARG PHE ILE ARG ASP CYS THR GLN LEU GLU
SEQRES 22 A 279 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 279 MET THR ILE ASN TYR HIS GLU LEU GLU THR SER HIS GLY
SEQRES 2 B 279 ARG ILE ALA VAL ARG GLU SER GLU GLY GLU GLY ALA PRO
SEQRES 3 B 279 LEU LEU MET ILE HIS GLY ASN SER SER SER GLY ALA ILE
SEQRES 4 B 279 PHE ALA PRO GLN LEU GLU GLY GLU ILE GLY LYS LYS TRP
SEQRES 5 B 279 ARG VAL ILE ALA PRO ASP LEU PRO GLY HIS GLY LYS SER
SEQRES 6 B 279 THR ASP ALA ILE ASP PRO ASP ARG SER TYR SER MET GLU
SEQRES 7 B 279 GLY TYR ALA ASP ALA MET THR GLU VAL MET GLN GLN LEU
SEQRES 8 B 279 GLY ILE ALA ASP ALA VAL VAL PHE GLY TRP GLY LEU GLY
SEQRES 9 B 279 GLY HIS ILE GLY ILE GLU MET ILE ALA ARG TYR PRO GLU
SEQRES 10 B 279 MET ARG GLY LEU MET ILE THR GLY THR PRO PRO VAL ALA
SEQRES 11 B 279 ARG GLU GLU VAL GLY GLN GLY PHE LYS SER GLY PRO ASP
SEQRES 12 B 279 MET ALA LEU ALA GLY GLN GLU ILE PHE SER GLU ARG ASP
SEQRES 13 B 279 VAL GLU SER TYR ALA ARG SER THR CYS GLY GLU PRO PHE
SEQRES 14 B 279 GLU ALA SER LEU LEU ASP ILE VAL ALA ARG THR ASP GLY
SEQRES 15 B 279 ARG ALA ARG ARG ILE MET PHE GLU LYS PHE GLY SER GLY
SEQRES 16 B 279 THR GLY GLY ASN GLN ARG ASP ILE VAL ALA GLU ALA GLN
SEQRES 17 B 279 LEU PRO ILE ALA VAL VAL ASN GLY ARG ASP GLU PRO PHE
SEQRES 18 B 279 VAL GLU LEU ASP PHE VAL SER LYS VAL LYS PHE GLY ASN
SEQRES 19 B 279 LEU TRP GLU GLY LYS THR HIS VAL ILE ASP ASN ALA GLY
SEQRES 20 B 279 HIS ALA PRO PHE ARG GLU ALA PRO ALA GLU PHE ASP ALA
SEQRES 21 B 279 TYR LEU ALA ARG PHE ILE ARG ASP CYS THR GLN LEU GLU
SEQRES 22 B 279 HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *1138(H2 O)
HELIX 1 1 SER A 36 ILE A 39 5 4
HELIX 2 2 PHE A 40 GLY A 46 1 7
HELIX 3 3 GLY A 46 LYS A 51 1 6
HELIX 4 4 ASP A 70 TYR A 75 1 6
HELIX 5 5 SER A 76 LEU A 91 1 16
HELIX 6 6 GLY A 102 TYR A 115 1 14
HELIX 7 7 ALA A 130 GLU A 132 5 3
HELIX 8 8 GLU A 133 PHE A 138 1 6
HELIX 9 9 GLY A 141 ALA A 147 1 7
HELIX 10 10 SER A 153 GLY A 166 1 14
HELIX 11 11 ALA A 171 THR A 180 1 10
HELIX 12 12 ASP A 181 GLY A 195 1 15
HELIX 13 13 ASN A 199 ALA A 207 1 9
HELIX 14 14 GLU A 223 SER A 228 1 6
HELIX 15 15 LEU A 235 LYS A 239 5 5
HELIX 16 16 ALA A 249 ALA A 254 1 6
HELIX 17 17 ALA A 254 LEU A 272 1 19
HELIX 18 18 SER B 36 ILE B 39 5 4
HELIX 19 19 PHE B 40 GLY B 46 1 7
HELIX 20 20 GLY B 46 LYS B 51 1 6
HELIX 21 21 ASP B 70 TYR B 75 1 6
HELIX 22 22 SER B 76 GLY B 92 1 17
HELIX 23 23 GLY B 102 TYR B 115 1 14
HELIX 24 24 ALA B 130 GLU B 132 5 3
HELIX 25 25 GLU B 133 PHE B 138 1 6
HELIX 26 26 GLY B 141 ALA B 147 1 7
HELIX 27 27 SER B 153 GLY B 166 1 14
HELIX 28 28 GLU B 170 THR B 180 1 11
HELIX 29 29 ASP B 181 SER B 194 1 14
HELIX 30 30 ASN B 199 ALA B 207 1 9
HELIX 31 31 GLU B 223 SER B 228 1 6
HELIX 32 32 LEU B 235 LYS B 239 5 5
HELIX 33 33 ALA B 249 ALA B 254 1 6
HELIX 34 34 ALA B 254 GLN B 271 1 18
SHEET 1 A 8 ASN A 4 THR A 10 0
SHEET 2 A 8 GLY A 13 GLU A 19 -1 O VAL A 17 N HIS A 6
SHEET 3 A 8 TRP A 52 PRO A 57 -1 O ALA A 56 N ARG A 18
SHEET 4 A 8 GLY A 24 ILE A 30 1 N LEU A 27 O ILE A 55
SHEET 5 A 8 VAL A 97 TRP A 101 1 O PHE A 99 N LEU A 28
SHEET 6 A 8 GLY A 120 THR A 124 1 O MET A 122 N VAL A 98
SHEET 7 A 8 ILE A 211 GLY A 216 1 O ALA A 212 N ILE A 123
SHEET 8 A 8 HIS A 241 ILE A 243 1 O HIS A 241 N VAL A 213
SHEET 1 B 8 ASN B 4 THR B 10 0
SHEET 2 B 8 GLY B 13 GLU B 19 -1 O VAL B 17 N HIS B 6
SHEET 3 B 8 TRP B 52 PRO B 57 -1 O ALA B 56 N ARG B 18
SHEET 4 B 8 GLY B 24 ILE B 30 1 N LEU B 27 O ILE B 55
SHEET 5 B 8 VAL B 97 TRP B 101 1 O PHE B 99 N LEU B 28
SHEET 6 B 8 GLY B 120 THR B 124 1 O MET B 122 N VAL B 98
SHEET 7 B 8 ILE B 211 GLY B 216 1 O ALA B 212 N ILE B 123
SHEET 8 B 8 HIS B 241 ILE B 243 1 O ILE B 243 N ASN B 215
CISPEP 1 GLU A 167 PRO A 168 0 4.73
CISPEP 2 GLU B 167 PRO B 168 0 1.74
CRYST1 42.426 129.941 44.387 90.00 110.84 90.00 P 1 21 1 4
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 0.023570 0.000000 0.008972 0.00000
SCALE2 0.000000 0.007696 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024106 0.00000
TER 2201 HIS A 278
TER 4363 HIS B 274
MASTER 569 0 0 34 16 0 0 6 5364 2 0 44
END |