HEADER HYDROLASE 07-JAN-11 3Q93
TITLE CRYSTAL STRUCTURE OF HUMAN 8-OXO-DGTPASE (MTH1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 7,8-DIHYDRO-8-OXOGUANINE TRIPHOSPHATASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 8-OXO-DGTPASE, NUCLEOSIDE DIPHOSPHATE-LINKED MOIETY X MOTIF
COMPND 5 1, NUDIX MOTIF 1;
COMPND 6 EC: 3.6.1.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MTH1, NUDT1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) R3 PRARE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, NUDIX,
KEYWDS 2 MUTT-LIKE, HYDROLASE, MAGNESIUM BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR L.TRESAUGUES,M.I.SIPONEN,C.H.ARROWSMITH,H.BERGLUND,C.BOUNTRA,
AUTHOR 2 R.COLLINS,A.M.EDWARDS,T.EKBLAD,S.FLODIN,A.FLORES,S.GRASLUND,
AUTHOR 3 M.HAMMARSTROM,I.JOHANSSON,T.KARLBERG,S.KOL,T.KOTENYOVA,
AUTHOR 4 E.KOUZNETSOVA,M.MOCHE,T.NYMAN,C.PERSSON,H.SCHULER,P.SCHUTZ,
AUTHOR 5 A.G.THORSELL,S.VAN DER BERG,E.WAHLBERG,J.WEIGELT,M.WELIN,P.NORDLUND,
AUTHOR 6 STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 2 13-SEP-23 3Q93 1 REMARK SEQADV
REVDAT 1 02-MAR-11 3Q93 0
JRNL AUTH L.TRESAUGUES,M.I.SIPONEN,C.H.ARROWSMITH,H.BERGLUND,
JRNL AUTH 2 C.BOUNTRA,R.COLLINS,A.M.EDWARDS,T.EKBLAD,S.FLODIN,A.FLORES,
JRNL AUTH 3 S.GRASLUND,M.HAMMARSTROM,I.JOHANSSON,T.KARLBERG,S.KOL,
JRNL AUTH 4 T.KOTENYOVA,E.KOUZNETSOVA,M.MOCHE,T.NYMAN,C.PERSSON,
JRNL AUTH 5 H.SCHULER,P.SCHUTZ,A.G.THORSELL,S.VAN DER BERG,E.WAHLBERG,
JRNL AUTH 6 J.WEIGELT,M.WELIN,P.NORDLUND
JRNL TITL CRYSTAL STRUCTURE OF HUMAN 8-OXO-DGTPASE (MTH1)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.96
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 31318
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1587
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 33.9636 - 3.8763 1.00 3180 172 0.1815 0.1678
REMARK 3 2 3.8763 - 3.0774 1.00 3000 175 0.1829 0.2410
REMARK 3 3 3.0774 - 2.6885 0.99 2997 170 0.2037 0.2832
REMARK 3 4 2.6885 - 2.4428 0.99 2983 145 0.2055 0.2450
REMARK 3 5 2.4428 - 2.2677 0.99 2944 168 0.2087 0.2429
REMARK 3 6 2.2677 - 2.1341 0.99 2963 153 0.2043 0.2339
REMARK 3 7 2.1341 - 2.0272 0.98 2947 142 0.2137 0.2421
REMARK 3 8 2.0272 - 1.9390 0.99 2911 166 0.2363 0.2973
REMARK 3 9 1.9390 - 1.8643 0.99 2916 150 0.2642 0.3163
REMARK 3 10 1.8643 - 1.8000 0.98 2890 146 0.3088 0.3617
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 : 47.08
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.850
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.69570
REMARK 3 B22 (A**2) : -5.90600
REMARK 3 B33 (A**2) : 13.60170
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
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 : 0.007 2640
REMARK 3 ANGLE : 1.066 3574
REMARK 3 CHIRALITY : 0.066 368
REMARK 3 PLANARITY : 0.005 463
REMARK 3 DIHEDRAL : 12.921 981
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 3:12)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.1580 5.6408 11.9594
REMARK 3 T TENSOR
REMARK 3 T11: 0.1763 T22: 0.1893
REMARK 3 T33: 0.1797 T12: -0.0033
REMARK 3 T13: -0.0075 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 3.7016 L22: 8.6255
REMARK 3 L33: 3.9524 L12: 0.7783
REMARK 3 L13: -0.4605 L23: -4.9026
REMARK 3 S TENSOR
REMARK 3 S11: 0.2581 S12: 0.0502 S13: -0.5524
REMARK 3 S21: 0.0249 S22: -0.3230 S23: 0.1577
REMARK 3 S31: 0.0432 S32: 0.2671 S33: -0.0615
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 13:33)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.0908 19.0664 14.1031
REMARK 3 T TENSOR
REMARK 3 T11: 0.1750 T22: 0.1411
REMARK 3 T33: 0.0868 T12: -0.0009
REMARK 3 T13: 0.0364 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 3.9136 L22: 5.1968
REMARK 3 L33: 9.2121 L12: -0.0583
REMARK 3 L13: -2.6008 L23: -1.9739
REMARK 3 S TENSOR
REMARK 3 S11: 0.0131 S12: 0.1932 S13: 0.0513
REMARK 3 S21: 0.2385 S22: 0.1389 S23: 0.1313
REMARK 3 S31: -0.0525 S32: -0.4483 S33: -0.0764
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 34:54)
REMARK 3 ORIGIN FOR THE GROUP (A): -11.2724 8.3532 9.1532
REMARK 3 T TENSOR
REMARK 3 T11: 0.1785 T22: 0.2288
REMARK 3 T33: 0.2090 T12: -0.0056
REMARK 3 T13: 0.0044 T23: -0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 5.8155 L22: 2.8188
REMARK 3 L33: 0.1125 L12: 3.3846
REMARK 3 L13: 0.6012 L23: 0.6024
REMARK 3 S TENSOR
REMARK 3 S11: 0.1893 S12: 0.2974 S13: 0.0913
REMARK 3 S21: 0.1316 S22: -0.2415 S23: 0.3838
REMARK 3 S31: 0.0427 S32: -0.1854 S33: 0.0127
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 55:69)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.3613 12.7979 3.9887
REMARK 3 T TENSOR
REMARK 3 T11: 0.1486 T22: 0.1931
REMARK 3 T33: 0.2123 T12: -0.0479
REMARK 3 T13: -0.0119 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 7.3668 L22: 7.3702
REMARK 3 L33: 4.2140 L12: -6.1690
REMARK 3 L13: -0.0486 L23: 1.0445
REMARK 3 S TENSOR
REMARK 3 S11: 0.2991 S12: 0.6619 S13: -0.1162
REMARK 3 S21: -0.4341 S22: -0.4063 S23: 0.5825
REMARK 3 S31: 0.0368 S32: -0.0680 S33: 0.1161
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 70:86)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4462 0.9117 16.7453
REMARK 3 T TENSOR
REMARK 3 T11: 0.1839 T22: 0.1648
REMARK 3 T33: 0.1258 T12: -0.0115
REMARK 3 T13: 0.0183 T23: -0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 2.9870 L22: 5.5784
REMARK 3 L33: 9.8949 L12: -1.1221
REMARK 3 L13: 3.1107 L23: -6.9091
REMARK 3 S TENSOR
REMARK 3 S11: 0.0997 S12: -0.1949 S13: -0.4119
REMARK 3 S21: 0.2082 S22: 0.0678 S23: 0.1988
REMARK 3 S31: -0.0606 S32: -0.3087 S33: -0.0831
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 87:108)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.9612 22.4704 9.3621
REMARK 3 T TENSOR
REMARK 3 T11: 0.2314 T22: 0.1738
REMARK 3 T33: 0.2487 T12: 0.0276
REMARK 3 T13: 0.0320 T23: 0.0678
REMARK 3 L TENSOR
REMARK 3 L11: 3.5251 L22: 3.9035
REMARK 3 L33: 0.3520 L12: 0.0801
REMARK 3 L13: 0.9997 L23: 0.7567
REMARK 3 S TENSOR
REMARK 3 S11: 0.0512 S12: 0.1643 S13: 0.5067
REMARK 3 S21: -0.2133 S22: -0.0111 S23: 0.5206
REMARK 3 S31: -0.1368 S32: -0.1851 S33: -0.1053
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 109:131)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4445 14.3967 10.8005
REMARK 3 T TENSOR
REMARK 3 T11: 0.1345 T22: 0.1345
REMARK 3 T33: 0.1383 T12: -0.0162
REMARK 3 T13: -0.0025 T23: 0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 3.3775 L22: 5.4206
REMARK 3 L33: 2.8377 L12: -0.2969
REMARK 3 L13: -0.6771 L23: 0.4499
REMARK 3 S TENSOR
REMARK 3 S11: 0.0139 S12: 0.1360 S13: 0.2139
REMARK 3 S21: 0.0414 S22: -0.0515 S23: -0.3274
REMARK 3 S31: -0.1028 S32: 0.0282 S33: 0.0378
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 132:156)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0137 2.2244 12.9706
REMARK 3 T TENSOR
REMARK 3 T11: 0.1416 T22: 0.1079
REMARK 3 T33: 0.1119 T12: 0.0065
REMARK 3 T13: 0.0118 T23: -0.0278
REMARK 3 L TENSOR
REMARK 3 L11: 6.1839 L22: 4.2219
REMARK 3 L33: 2.3117 L12: -0.6854
REMARK 3 L13: 2.6957 L23: -1.6483
REMARK 3 S TENSOR
REMARK 3 S11: 0.1242 S12: 0.1941 S13: -0.4402
REMARK 3 S21: 0.0288 S22: -0.0971 S23: -0.0810
REMARK 3 S31: 0.4260 S32: 0.3151 S33: -0.0816
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 3:12)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.5606 -6.6848 10.6896
REMARK 3 T TENSOR
REMARK 3 T11: 0.1658 T22: 0.2667
REMARK 3 T33: 0.5420 T12: -0.0203
REMARK 3 T13: -0.0928 T23: -0.1453
REMARK 3 L TENSOR
REMARK 3 L11: 5.6885 L22: 9.0313
REMARK 3 L33: 4.8305 L12: -0.4083
REMARK 3 L13: -2.7385 L23: 5.8414
REMARK 3 S TENSOR
REMARK 3 S11: 0.2690 S12: -0.0297 S13: -0.9371
REMARK 3 S21: 0.6810 S22: -0.7253 S23: 0.4696
REMARK 3 S31: 0.4500 S32: -0.3171 S33: 0.3212
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 13:31)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.6552 -19.4117 7.2631
REMARK 3 T TENSOR
REMARK 3 T11: 0.1409 T22: 0.2155
REMARK 3 T33: 1.7255 T12: 0.0570
REMARK 3 T13: -0.2100 T23: -0.3101
REMARK 3 L TENSOR
REMARK 3 L11: 2.1351 L22: 1.8034
REMARK 3 L33: 3.3439 L12: 0.9167
REMARK 3 L13: -3.0635 L23: -0.4138
REMARK 3 S TENSOR
REMARK 3 S11: -0.2834 S12: 1.6646 S13: -4.2141
REMARK 3 S21: 0.0966 S22: -0.3102 S23: -0.7936
REMARK 3 S31: 0.1356 S32: -0.5197 S33: 0.1933
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN B AND RESID 32:51)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.4266 -8.6994 6.8769
REMARK 3 T TENSOR
REMARK 3 T11: 0.1644 T22: 0.3097
REMARK 3 T33: 0.8203 T12: 0.0252
REMARK 3 T13: -0.1141 T23: -0.2397
REMARK 3 L TENSOR
REMARK 3 L11: 2.6141 L22: 4.2747
REMARK 3 L33: 0.5401 L12: -1.6006
REMARK 3 L13: -0.8476 L23: 0.5792
REMARK 3 S TENSOR
REMARK 3 S11: 0.3185 S12: 0.7461 S13: -1.8328
REMARK 3 S21: 0.2303 S22: -0.1860 S23: -0.1099
REMARK 3 S31: -0.1536 S32: -0.0195 S33: 0.0483
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN B AND RESID 52:69)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.2976 -10.6147 0.6893
REMARK 3 T TENSOR
REMARK 3 T11: 0.0725 T22: 0.6090
REMARK 3 T33: 0.9127 T12: 0.0701
REMARK 3 T13: -0.0939 T23: -0.5843
REMARK 3 L TENSOR
REMARK 3 L11: 4.9523 L22: 4.7491
REMARK 3 L33: 3.1447 L12: -1.9667
REMARK 3 L13: -3.3827 L23: -0.1051
REMARK 3 S TENSOR
REMARK 3 S11: 0.0628 S12: 1.9546 S13: -2.3411
REMARK 3 S21: -0.1338 S22: -0.5313 S23: -0.5047
REMARK 3 S31: -0.0640 S32: -0.3909 S33: 0.0734
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN B AND RESID 70:88)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9101 -4.7564 15.7470
REMARK 3 T TENSOR
REMARK 3 T11: 0.2052 T22: 0.2003
REMARK 3 T33: 0.3510 T12: -0.0505
REMARK 3 T13: -0.1234 T23: 0.0342
REMARK 3 L TENSOR
REMARK 3 L11: 9.5561 L22: 0.8228
REMARK 3 L33: 8.5793 L12: -0.3250
REMARK 3 L13: -6.9808 L23: 0.6446
REMARK 3 S TENSOR
REMARK 3 S11: 0.2328 S12: -0.3652 S13: -1.1243
REMARK 3 S21: 0.1716 S22: -0.3414 S23: -0.4860
REMARK 3 S31: -0.3430 S32: 0.7718 S33: 0.0934
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN B AND RESID 89:107)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.7074 -21.3978 0.7551
REMARK 3 T TENSOR
REMARK 3 T11: 0.0862 T22: 0.5193
REMARK 3 T33: 1.9862 T12: 0.0934
REMARK 3 T13: 0.0711 T23: -0.7744
REMARK 3 L TENSOR
REMARK 3 L11: 9.7689 L22: 5.5502
REMARK 3 L33: 2.8929 L12: -0.7258
REMARK 3 L13: -0.9836 L23: 1.0638
REMARK 3 S TENSOR
REMARK 3 S11: 0.0184 S12: 1.6764 S13: -4.5899
REMARK 3 S21: 0.1010 S22: -0.7373 S23: 0.0111
REMARK 3 S31: 0.9507 S32: -0.8651 S33: 0.5895
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN B AND RESID 108:130)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1632 -14.1480 7.9517
REMARK 3 T TENSOR
REMARK 3 T11: 0.2136 T22: 0.2945
REMARK 3 T33: 1.0479 T12: 0.0307
REMARK 3 T13: -0.0973 T23: -0.3196
REMARK 3 L TENSOR
REMARK 3 L11: 7.9516 L22: 1.3929
REMARK 3 L33: 1.3313 L12: 0.7541
REMARK 3 L13: -0.3755 L23: 0.2653
REMARK 3 S TENSOR
REMARK 3 S11: 0.1581 S12: 0.8587 S13: -2.3739
REMARK 3 S21: 0.0428 S22: -0.1924 S23: -0.1191
REMARK 3 S31: 0.2252 S32: -0.0511 S33: -0.0484
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN B AND RESID 131:156)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7949 -3.3506 14.4558
REMARK 3 T TENSOR
REMARK 3 T11: 0.2083 T22: 0.1657
REMARK 3 T33: 0.2505 T12: -0.0005
REMARK 3 T13: -0.0632 T23: -0.0333
REMARK 3 L TENSOR
REMARK 3 L11: 9.1717 L22: 3.8197
REMARK 3 L33: 6.9802 L12: -0.1602
REMARK 3 L13: -1.2959 L23: -3.8918
REMARK 3 S TENSOR
REMARK 3 S11: 0.2857 S12: 0.0036 S13: -0.5784
REMARK 3 S21: 0.2096 S22: -0.2258 S23: -0.1671
REMARK 3 S31: -0.2195 S32: -0.0207 S33: -0.1244
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 3Q93 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-11.
REMARK 100 THE DEPOSITION ID IS D_1000063348.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : SI 111 CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31366
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 33.960
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : 0.10800
REMARK 200 R SYM (I) : 0.10800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.70100
REMARK 200 R SYM FOR SHELL (I) : 0.70100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1IRY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.26 M AMMONIUM SULFATE, 22 % W/V
REMARK 280 PEG4000, 13 % GLYCEROL, PH 7.4, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 29.77200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.33900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.84050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.33900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.77200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.84050
REMARK 290 SMTRY3 4 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 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 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 GLY B 2
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 90 52.82 -141.45
REMARK 500 SER B 90 110.21 -175.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 157
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 158
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 157
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 158
DBREF 3Q93 A 1 156 UNP P36639 8ODP_HUMAN 42 197
DBREF 3Q93 B 1 156 UNP P36639 8ODP_HUMAN 42 197
SEQADV 3Q93 MET A -19 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 GLY A -18 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 SER A -17 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 SER A -16 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 HIS A -15 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 HIS A -14 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 HIS A -13 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 HIS A -12 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 HIS A -11 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 HIS A -10 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 SER A -9 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 SER A -8 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 GLY A -7 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 LEU A -6 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 VAL A -5 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 PRO A -4 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 ARG A -3 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 GLY A -2 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 SER A -1 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 HIS A 0 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 MET B -19 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 GLY B -18 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 SER B -17 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 SER B -16 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 HIS B -15 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 HIS B -14 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 HIS B -13 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 HIS B -12 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 HIS B -11 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 HIS B -10 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 SER B -9 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 SER B -8 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 GLY B -7 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 LEU B -6 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 VAL B -5 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 PRO B -4 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 ARG B -3 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 GLY B -2 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 SER B -1 UNP P36639 EXPRESSION TAG
SEQADV 3Q93 HIS B 0 UNP P36639 EXPRESSION TAG
SEQRES 1 A 176 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 176 LEU VAL PRO ARG GLY SER HIS MET GLY ALA SER ARG LEU
SEQRES 3 A 176 TYR THR LEU VAL LEU VAL LEU GLN PRO GLN ARG VAL LEU
SEQRES 4 A 176 LEU GLY MET LYS LYS ARG GLY PHE GLY ALA GLY ARG TRP
SEQRES 5 A 176 ASN GLY PHE GLY GLY LYS VAL GLN GLU GLY GLU THR ILE
SEQRES 6 A 176 GLU ASP GLY ALA ARG ARG GLU LEU GLN GLU GLU SER GLY
SEQRES 7 A 176 LEU THR VAL ASP ALA LEU HIS LYS VAL GLY GLN ILE VAL
SEQRES 8 A 176 PHE GLU PHE VAL GLY GLU PRO GLU LEU MET ASP VAL HIS
SEQRES 9 A 176 VAL PHE CYS THR ASP SER ILE GLN GLY THR PRO VAL GLU
SEQRES 10 A 176 SER ASP GLU MET ARG PRO CYS TRP PHE GLN LEU ASP GLN
SEQRES 11 A 176 ILE PRO PHE LYS ASP MET TRP PRO ASP ASP SER TYR TRP
SEQRES 12 A 176 PHE PRO LEU LEU LEU GLN LYS LYS LYS PHE HIS GLY TYR
SEQRES 13 A 176 PHE LYS PHE GLN GLY GLN ASP THR ILE LEU ASP TYR THR
SEQRES 14 A 176 LEU ARG GLU VAL ASP THR VAL
SEQRES 1 B 176 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 176 LEU VAL PRO ARG GLY SER HIS MET GLY ALA SER ARG LEU
SEQRES 3 B 176 TYR THR LEU VAL LEU VAL LEU GLN PRO GLN ARG VAL LEU
SEQRES 4 B 176 LEU GLY MET LYS LYS ARG GLY PHE GLY ALA GLY ARG TRP
SEQRES 5 B 176 ASN GLY PHE GLY GLY LYS VAL GLN GLU GLY GLU THR ILE
SEQRES 6 B 176 GLU ASP GLY ALA ARG ARG GLU LEU GLN GLU GLU SER GLY
SEQRES 7 B 176 LEU THR VAL ASP ALA LEU HIS LYS VAL GLY GLN ILE VAL
SEQRES 8 B 176 PHE GLU PHE VAL GLY GLU PRO GLU LEU MET ASP VAL HIS
SEQRES 9 B 176 VAL PHE CYS THR ASP SER ILE GLN GLY THR PRO VAL GLU
SEQRES 10 B 176 SER ASP GLU MET ARG PRO CYS TRP PHE GLN LEU ASP GLN
SEQRES 11 B 176 ILE PRO PHE LYS ASP MET TRP PRO ASP ASP SER TYR TRP
SEQRES 12 B 176 PHE PRO LEU LEU LEU GLN LYS LYS LYS PHE HIS GLY TYR
SEQRES 13 B 176 PHE LYS PHE GLN GLY GLN ASP THR ILE LEU ASP TYR THR
SEQRES 14 B 176 LEU ARG GLU VAL ASP THR VAL
HET SO4 A 157 5
HET SO4 A 158 5
HET SO4 A 159 5
HET IMD A 160 5
HET GOL A 161 6
HET GOL A 162 6
HET SO4 B 157 5
HET SO4 B 158 5
HETNAM SO4 SULFATE ION
HETNAM IMD IMIDAZOLE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 SO4 5(O4 S 2-)
FORMUL 6 IMD C3 H5 N2 1+
FORMUL 7 GOL 2(C3 H8 O3)
FORMUL 11 HOH *215(H2 O)
HELIX 1 1 THR A 44 GLY A 58 1 15
HELIX 2 2 PRO A 112 MET A 116 5 5
HELIX 3 3 TRP A 117 PRO A 118 5 2
HELIX 4 4 ASP A 119 GLN A 129 1 11
HELIX 5 5 THR B 44 GLY B 58 1 15
HELIX 6 6 ASP B 109 ILE B 111 5 3
HELIX 7 7 PRO B 112 MET B 116 5 5
HELIX 8 8 TRP B 117 PRO B 118 5 2
HELIX 9 9 ASP B 119 GLN B 129 1 11
SITE 1 AC1 7 ALA A 63 HIS A 65 THR A 88 ASP A 89
SITE 2 AC1 7 SER A 90 HOH A 233 HOH A 301
SITE 1 AC2 3 HIS A 65 LYS A 66 HOH A 238
SITE 1 AC3 4 ARG A 17 TRP A 105 HOH A 276 LYS B 132
SITE 1 AC4 6 ASN A 33 PHE A 72 TRP A 117 ASP A 119
SITE 2 AC4 6 HOH A 191 HOH A 277
SITE 1 AC5 8 LYS A 23 LYS A 24 GLY A 30 HOH A 181
SITE 2 AC5 8 HOH A 240 HOH A 245 HOH A 288 HOH A 298
SITE 1 AC6 7 LYS A 24 GLU A 97 TYR A 136 LYS A 138
SITE 2 AC6 7 ASP A 147 TYR B 122 TYR B 148
SITE 1 AC7 4 HOH A 225 HIS B 134 ARG B 151 HOH B 214
SITE 1 AC8 6 HOH A 302 ARG B 151 VAL B 153 ASP B 154
SITE 2 AC8 6 THR B 155 HOH B 166
CRYST1 59.544 67.681 82.678 90.00 90.00 90.00 P 21 21 21 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 0.016794 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014775 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012095 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
