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HEADER HYDROLASE 23-JUL-12 4G9G
TITLE CRYSTAL STRUCTURES OF N-ACYL HOMOSERINE LACTONASE AIDH E219G 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 4G9G 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) : 19.87
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 95339
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.143
REMARK 3 R VALUE (WORKING SET) : 0.141
REMARK 3 FREE R VALUE : 0.177
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4770
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 19.8714 - 2.9058 0.95 8954 481 0.1371 0.1733
REMARK 3 2 2.9058 - 2.3075 0.99 9254 496 0.1444 0.1834
REMARK 3 3 2.3075 - 2.0161 0.99 9193 492 0.1388 0.1758
REMARK 3 4 2.0161 - 1.8320 0.98 9197 471 0.1385 0.1737
REMARK 3 5 1.8320 - 1.7007 0.98 9087 505 0.1374 0.1734
REMARK 3 6 1.7007 - 1.6005 0.97 9059 478 0.1309 0.1676
REMARK 3 7 1.6005 - 1.5204 0.97 9011 508 0.1351 0.1688
REMARK 3 8 1.5204 - 1.4542 0.96 8975 440 0.1404 0.1784
REMARK 3 9 1.4542 - 1.3982 0.95 8924 457 0.1612 0.1960
REMARK 3 10 1.3982 - 1.3500 0.95 8915 442 0.1888 0.2246
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.49
REMARK 3 K_SOL : 0.41
REMARK 3 B_SOL : 111.48
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.040
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.81
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.88250
REMARK 3 B22 (A**2) : -3.87980
REMARK 3 B33 (A**2) : 1.99730
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.88610
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 4471
REMARK 3 ANGLE : 1.046 6073
REMARK 3 CHIRALITY : 0.070 637
REMARK 3 PLANARITY : 0.005 829
REMARK 3 DIHEDRAL : 12.097 1658
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 2:19)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7019 2.5793 19.0919
REMARK 3 T TENSOR
REMARK 3 T11: 0.1575 T22: 0.0966
REMARK 3 T33: 0.1202 T12: -0.0145
REMARK 3 T13: 0.0543 T23: -0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 0.2163 L22: 1.2757
REMARK 3 L33: 1.0957 L12: -0.1235
REMARK 3 L13: -0.3165 L23: 0.4254
REMARK 3 S TENSOR
REMARK 3 S11: 0.0150 S12: -0.0477 S13: 0.0323
REMARK 3 S21: -0.2554 S22: 0.0337 S23: -0.2655
REMARK 3 S31: -0.0025 S32: 0.1759 S33: -0.0560
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (chain A and resid 20:86)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.3724 4.7290 23.7116
REMARK 3 T TENSOR
REMARK 3 T11: 0.0536 T22: 0.0421
REMARK 3 T33: 0.0340 T12: -0.0151
REMARK 3 T13: 0.0073 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.0912 L22: 1.4976
REMARK 3 L33: 0.6577 L12: -0.2987
REMARK 3 L13: 0.0516 L23: 0.2021
REMARK 3 S TENSOR
REMARK 3 S11: -0.0414 S12: 0.0239 S13: 0.0083
REMARK 3 S21: -0.2392 S22: 0.0543 S23: -0.1217
REMARK 3 S31: -0.0444 S32: 0.0405 S33: -0.0137
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain A and resid 87:142)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4230 2.4136 32.0609
REMARK 3 T TENSOR
REMARK 3 T11: 0.0596 T22: 0.0646
REMARK 3 T33: 0.0662 T12: 0.0013
REMARK 3 T13: -0.0089 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.2199 L22: 1.5030
REMARK 3 L33: 0.1386 L12: -0.0442
REMARK 3 L13: -0.2117 L23: -0.1278
REMARK 3 S TENSOR
REMARK 3 S11: -0.0409 S12: -0.0009 S13: -0.0121
REMARK 3 S21: 0.0115 S22: 0.0297 S23: 0.0561
REMARK 3 S31: 0.0157 S32: 0.0121 S33: -0.0215
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain A and resid 143:156)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.7305 0.8310 11.0468
REMARK 3 T TENSOR
REMARK 3 T11: 0.4088 T22: 0.0992
REMARK 3 T33: 0.2407 T12: 0.0081
REMARK 3 T13: -0.2478 T23: -0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 0.2457 L22: 3.1672
REMARK 3 L33: 0.0681 L12: 0.1883
REMARK 3 L13: 0.1016 L23: 0.1557
REMARK 3 S TENSOR
REMARK 3 S11: -0.0147 S12: 0.0445 S13: -0.0166
REMARK 3 S21: -1.0989 S22: 0.0637 S23: 0.6374
REMARK 3 S31: 0.0167 S32: -0.1373 S33: -0.0374
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (chain A and resid 157:170)
REMARK 3 ORIGIN FOR THE GROUP (A): -12.6082 12.3556 13.5838
REMARK 3 T TENSOR
REMARK 3 T11: 0.2472 T22: 0.0992
REMARK 3 T33: 0.1496 T12: -0.0012
REMARK 3 T13: -0.1026 T23: 0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 0.5992 L22: 2.0087
REMARK 3 L33: 1.8857 L12: 0.4668
REMARK 3 L13: 0.6564 L23: -0.5236
REMARK 3 S TENSOR
REMARK 3 S11: 0.1339 S12: 0.0964 S13: 0.0644
REMARK 3 S21: -0.6836 S22: -0.0052 S23: 0.3898
REMARK 3 S31: 0.2886 S32: 0.1803 S33: -0.1220
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (chain A and resid 171:185)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.0382 2.2143 11.6409
REMARK 3 T TENSOR
REMARK 3 T11: 0.2899 T22: 0.0941
REMARK 3 T33: 0.0701 T12: -0.0057
REMARK 3 T13: -0.0339 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.2205 L22: 2.2992
REMARK 3 L33: 0.0179 L12: -0.2468
REMARK 3 L13: -0.0445 L23: 0.2742
REMARK 3 S TENSOR
REMARK 3 S11: 0.0318 S12: 0.0750 S13: -0.0044
REMARK 3 S21: -0.7668 S22: 0.0250 S23: 0.0681
REMARK 3 S31: 0.0621 S32: -0.0069 S33: -0.0535
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (chain A and resid 186:195)
REMARK 3 ORIGIN FOR THE GROUP (A): -12.8188 -8.4474 22.9031
REMARK 3 T TENSOR
REMARK 3 T11: 0.1177 T22: 0.1291
REMARK 3 T33: 0.1214 T12: -0.0248
REMARK 3 T13: -0.0540 T23: 0.0193
REMARK 3 L TENSOR
REMARK 3 L11: 6.3389 L22: 1.4537
REMARK 3 L33: 3.8756 L12: -0.3994
REMARK 3 L13: 4.8318 L23: 0.1316
REMARK 3 S TENSOR
REMARK 3 S11: -0.0191 S12: -0.5302 S13: -0.0717
REMARK 3 S21: -0.2883 S22: 0.0539 S23: 0.4340
REMARK 3 S31: -0.0115 S32: -0.5946 S33: -0.0623
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (chain A and resid 196:207)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4476 -2.9717 39.4967
REMARK 3 T TENSOR
REMARK 3 T11: 0.0797 T22: 0.0519
REMARK 3 T33: 0.0732 T12: 0.0078
REMARK 3 T13: 0.0273 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 0.4578 L22: 0.9433
REMARK 3 L33: 0.5097 L12: -0.4720
REMARK 3 L13: -0.2704 L23: -0.1216
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: -0.0168 S13: -0.0642
REMARK 3 S21: 0.1037 S22: -0.0103 S23: 0.2277
REMARK 3 S31: 0.0043 S32: -0.0498 S33: -0.0047
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (chain A and resid 208:256)
REMARK 3 ORIGIN FOR THE GROUP (A): -13.0344 13.4308 33.3316
REMARK 3 T TENSOR
REMARK 3 T11: 0.0712 T22: 0.0632
REMARK 3 T33: 0.0952 T12: 0.0138
REMARK 3 T13: 0.0028 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 0.1262 L22: 1.1990
REMARK 3 L33: 0.8635 L12: 0.2260
REMARK 3 L13: -0.1319 L23: -0.1611
REMARK 3 S TENSOR
REMARK 3 S11: -0.0125 S12: 0.0181 S13: 0.0375
REMARK 3 S21: 0.0588 S22: 0.0498 S23: 0.2231
REMARK 3 S31: -0.1295 S32: -0.0310 S33: -0.0290
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (chain A and resid 257:273)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3742 18.5925 36.7922
REMARK 3 T TENSOR
REMARK 3 T11: 0.1073 T22: 0.0723
REMARK 3 T33: 0.0927 T12: -0.0026
REMARK 3 T13: -0.0290 T23: -0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.4319 L22: 1.2887
REMARK 3 L33: 0.5010 L12: 0.2971
REMARK 3 L13: 0.3859 L23: 0.3177
REMARK 3 S TENSOR
REMARK 3 S11: -0.0814 S12: -0.0074 S13: 0.0744
REMARK 3 S21: 0.1385 S22: -0.0017 S23: -0.0880
REMARK 3 S31: -0.1185 S32: 0.0056 S33: 0.0893
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (chain B and resid 3:17)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3391 -22.0237 28.0448
REMARK 3 T TENSOR
REMARK 3 T11: 0.0960 T22: 0.1267
REMARK 3 T33: 0.1112 T12: -0.0492
REMARK 3 T13: 0.0006 T23: -0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 3.2122 L22: 3.2879
REMARK 3 L33: 1.1117 L12: 3.1789
REMARK 3 L13: 1.2568 L23: 1.1797
REMARK 3 S TENSOR
REMARK 3 S11: -0.2163 S12: 0.3988 S13: -0.2503
REMARK 3 S21: -0.3658 S22: 0.2225 S23: -0.4291
REMARK 3 S31: -0.2061 S32: 0.2837 S33: -0.0298
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (chain B and resid 18:51)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.4183 -33.7383 30.9745
REMARK 3 T TENSOR
REMARK 3 T11: 0.0426 T22: 0.0614
REMARK 3 T33: 0.0988 T12: 0.0018
REMARK 3 T13: -0.0037 T23: -0.0238
REMARK 3 L TENSOR
REMARK 3 L11: 0.7078 L22: 0.3649
REMARK 3 L33: 0.3943 L12: 0.3413
REMARK 3 L13: 0.1311 L23: 0.2370
REMARK 3 S TENSOR
REMARK 3 S11: -0.0455 S12: 0.0075 S13: -0.1493
REMARK 3 S21: 0.0090 S22: 0.0588 S23: -0.1206
REMARK 3 S31: 0.0194 S32: 0.0454 S33: -0.0216
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (chain B and resid 52:73)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.5032 -20.6121 33.3821
REMARK 3 T TENSOR
REMARK 3 T11: 0.0643 T22: 0.0679
REMARK 3 T33: 0.1241 T12: -0.0086
REMARK 3 T13: -0.0265 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 1.0556 L22: 1.7166
REMARK 3 L33: 2.1750 L12: 1.0164
REMARK 3 L13: 0.9790 L23: 1.8650
REMARK 3 S TENSOR
REMARK 3 S11: -0.1602 S12: 0.0381 S13: 0.1899
REMARK 3 S21: -0.2562 S22: -0.0032 S23: 0.1075
REMARK 3 S31: -0.2707 S32: 0.0501 S33: 0.1626
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (chain B and resid 74:131)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.8246 -21.5544 31.4890
REMARK 3 T TENSOR
REMARK 3 T11: 0.0563 T22: 0.0652
REMARK 3 T33: 0.0738 T12: 0.0038
REMARK 3 T13: -0.0116 T23: -0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 0.2305 L22: 0.6703
REMARK 3 L33: 0.1124 L12: 0.3267
REMARK 3 L13: -0.1286 L23: 0.0273
REMARK 3 S TENSOR
REMARK 3 S11: -0.0194 S12: 0.0046 S13: 0.0310
REMARK 3 S21: -0.0271 S22: 0.0178 S23: 0.0269
REMARK 3 S31: -0.0263 S32: -0.0001 S33: 0.0014
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (chain B and resid 132:143)
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3770 -22.4748 51.7044
REMARK 3 T TENSOR
REMARK 3 T11: 0.1382 T22: 0.1802
REMARK 3 T33: 0.1038 T12: 0.0295
REMARK 3 T13: 0.0035 T23: -0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 2.1186 L22: 1.5211
REMARK 3 L33: 0.2835 L12: -1.0669
REMARK 3 L13: -0.5546 L23: -0.0347
REMARK 3 S TENSOR
REMARK 3 S11: -0.1598 S12: -0.3686 S13: 0.0573
REMARK 3 S21: 0.3497 S22: 0.1541 S23: -0.0364
REMARK 3 S31: -0.1397 S32: 0.1995 S33: -0.0212
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (chain B and resid 144:162)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.4687 -22.9110 53.5885
REMARK 3 T TENSOR
REMARK 3 T11: 0.1593 T22: 0.1137
REMARK 3 T33: 0.1133 T12: 0.0150
REMARK 3 T13: -0.0385 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 0.7925 L22: 0.1083
REMARK 3 L33: 0.3287 L12: 0.0506
REMARK 3 L13: 0.3148 L23: -0.0650
REMARK 3 S TENSOR
REMARK 3 S11: 0.0224 S12: -0.1154 S13: -0.0409
REMARK 3 S21: 0.0741 S22: -0.0650 S23: 0.0373
REMARK 3 S31: 0.0627 S32: -0.0388 S33: 0.0061
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (chain B and resid 163:169)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.7549 -34.4340 48.8939
REMARK 3 T TENSOR
REMARK 3 T11: 0.1103 T22: 0.0742
REMARK 3 T33: 0.0983 T12: 0.0353
REMARK 3 T13: -0.0435 T23: -0.0290
REMARK 3 L TENSOR
REMARK 3 L11: 1.3482 L22: 0.6891
REMARK 3 L33: 1.6137 L12: -0.9552
REMARK 3 L13: 1.0287 L23: -0.6718
REMARK 3 S TENSOR
REMARK 3 S11: -0.0208 S12: -0.1723 S13: 0.0781
REMARK 3 S21: 0.3122 S22: 0.1428 S23: -0.4185
REMARK 3 S31: 0.3058 S32: 0.1452 S33: -0.1199
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (chain B and resid 170:189)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4984 -21.3156 45.8761
REMARK 3 T TENSOR
REMARK 3 T11: 0.0902 T22: 0.0924
REMARK 3 T33: 0.1156 T12: 0.0238
REMARK 3 T13: -0.0372 T23: -0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 0.8133 L22: 0.2336
REMARK 3 L33: 0.4840 L12: -0.1805
REMARK 3 L13: 0.4790 L23: -0.1688
REMARK 3 S TENSOR
REMARK 3 S11: -0.0174 S12: -0.0568 S13: -0.0256
REMARK 3 S21: 0.0723 S22: 0.0456 S23: -0.0926
REMARK 3 S31: -0.0012 S32: 0.0164 S33: -0.0269
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (chain B and resid 190:197)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8314 -10.1698 43.1819
REMARK 3 T TENSOR
REMARK 3 T11: 0.1261 T22: 0.1890
REMARK 3 T33: 0.0920 T12: 0.0372
REMARK 3 T13: 0.0143 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 4.7212 L22: 2.2515
REMARK 3 L33: 3.5297 L12: -1.4847
REMARK 3 L13: 4.0597 L23: -1.5586
REMARK 3 S TENSOR
REMARK 3 S11: -0.3662 S12: -0.6966 S13: 0.1475
REMARK 3 S21: 0.4215 S22: 0.2066 S23: 0.0278
REMARK 3 S31: -0.3025 S32: -0.7836 S33: 0.1096
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (chain B and resid 198:273)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.5498 -32.6568 37.2360
REMARK 3 T TENSOR
REMARK 3 T11: 0.0551 T22: 0.0734
REMARK 3 T33: 0.0907 T12: -0.0031
REMARK 3 T13: -0.0009 T23: 0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 0.5915 L22: 0.6628
REMARK 3 L33: 0.2133 L12: -0.0027
REMARK 3 L13: 0.2237 L23: 0.1229
REMARK 3 S TENSOR
REMARK 3 S11: 0.0333 S12: -0.0446 S13: -0.0734
REMARK 3 S21: 0.0089 S22: 0.0028 S23: 0.1201
REMARK 3 S31: 0.0338 S32: -0.0562 S33: -0.0256
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 4G9G 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 RCSB073905.
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 : 6.3
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 : 96822
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 (%) : 51.4
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 (%): 34.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% PEG8000, 0.2M LIAC, 0.1M NAAC, PH
REMARK 280 6.3, 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 64.78350
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 277
REMARK 465 HIS A 278
REMARK 465 HIS A 279
REMARK 465 MET B 1
REMARK 465 THR B 2
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 GLU A 253 CD
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU A 273 OE2 GLU B 47 2657 1.73
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 GLU A 167 CD GLU A 167 OE1 -0.071
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 35 -154.94 -107.13
REMARK 500 SER A 102 -116.54 65.57
REMARK 500 SER B 35 -154.83 -106.78
REMARK 500 SER B 102 -113.49 64.33
REMARK 500 ASN B 234 79.20 -156.51
REMARK 500 HIS B 276 -176.33 -64.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 HIS B 274 23.2 L L OUTSIDE RANGE
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 713 DISTANCE = 5.67 ANGSTROMS
REMARK 525 HOH A 715 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH A 716 DISTANCE = 8.66 ANGSTROMS
REMARK 525 HOH A 722 DISTANCE = 6.84 ANGSTROMS
REMARK 525 HOH A 728 DISTANCE = 8.52 ANGSTROMS
REMARK 525 HOH A 732 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH A 737 DISTANCE = 7.82 ANGSTROMS
REMARK 525 HOH A 753 DISTANCE = 7.20 ANGSTROMS
REMARK 525 HOH A 754 DISTANCE = 5.01 ANGSTROMS
REMARK 525 HOH A 755 DISTANCE = 6.96 ANGSTROMS
REMARK 525 HOH A 757 DISTANCE = 5.22 ANGSTROMS
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 HOH A 674
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 301 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 165 SG
REMARK 620 2 HOH A 970 O 104.3
REMARK 620 3 HOH A 969 O 89.1 99.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 301 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 165 SG
REMARK 620 2 HOH B 851 O 124.3
REMARK 620 3 HOH B 852 O 97.4 55.8
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 301
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: 4G8D RELATED DB: PDB
REMARK 900 RELATED ID: 4G9E RELATED DB: PDB
DBREF 4G9G A 1 271 UNP D2J2T6 D2J2T6_9RHIZ 1 271
DBREF 4G9G B 1 271 UNP D2J2T6 D2J2T6_9RHIZ 1 271
SEQADV 4G9G GLY A 219 UNP D2J2T6 GLU 219 ENGINEERED MUTATION
SEQADV 4G9G LEU A 272 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9G GLU A 273 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9G HIS A 274 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9G HIS A 275 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9G HIS A 276 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9G HIS A 277 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9G HIS A 278 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9G HIS A 279 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9G GLY B 219 UNP D2J2T6 GLU 219 ENGINEERED MUTATION
SEQADV 4G9G LEU B 272 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9G GLU B 273 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9G HIS B 274 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9G HIS B 275 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9G HIS B 276 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9G HIS B 277 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9G HIS B 278 UNP D2J2T6 EXPRESSION TAG
SEQADV 4G9G 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 SER 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 GLY 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 SER 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 GLY 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
HET NI A 301 1
HET NI B 301 1
HETNAM NI NICKEL (II) ION
FORMUL 3 NI 2(NI 2+)
FORMUL 5 HOH *1055(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 SER 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 GLU A 170 THR A 180 1 11
HELIX 12 12 ASP A 181 SER A 194 1 14
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 GLN A 271 1 18
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 LEU B 91 1 16
HELIX 23 23 SER 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 ASP B 143 GLN B 149 5 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 GLU A 19 N ASN A 4
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 GLY A 100
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 ILE A 243 N ASN A 215
SHEET 1 B 8 ASN B 4 THR B 10 0
SHEET 2 B 8 GLY B 13 GLU B 19 -1 O ILE B 15 N LEU B 8
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 MET B 29 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 GLY B 100
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 HIS B 241 N VAL B 213
LINK SG CYS A 165 NI NI A 301 1555 1555 2.27
LINK SG CYS B 165 NI NI B 301 1555 1555 2.30
LINK NI NI A 301 O HOH A 970 1555 1555 2.58
LINK NI NI B 301 O HOH B 851 1555 1555 2.62
LINK NI NI A 301 O HOH A 969 1555 1555 2.78
LINK NI NI B 301 O HOH B 852 1555 1555 2.79
CISPEP 1 GLU A 167 PRO A 168 0 2.81
CISPEP 2 GLU B 167 PRO B 168 0 -1.58
CISPEP 3 HIS B 276 HIS B 277 0 -0.46
SITE 1 AC1 4 CYS A 165 VAL A 177 HOH A 969 HOH A 970
SITE 1 AC2 5 CYS B 165 VAL B 177 HOH B 601 HOH B 851
SITE 2 AC2 5 HOH B 852
CRYST1 42.378 129.567 44.728 90.00 111.02 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 0.023597 0.000000 0.009068 0.00000
SCALE2 0.000000 0.007718 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023951 0.00000
TER 2220 HIS A 276
TER 4425 HIS B 277
MASTER 669 0 2 34 16 0 3 6 5280 2 8 44
END |