HEADER HYDROLASE/DNA 28-FEB-17 5V05
TITLE CRYSTAL STRUCTURE OF HUMAN EXONUCLEASE 1 EXO1 (WT) IN COMPLEX WITH 5'
TITLE 2 RECESSED-END DNA (RIII)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXONUCLEASE 1;
COMPND 3 CHAIN: Z;
COMPND 4 FRAGMENT: UNP RESIDUES 1-352;
COMPND 5 SYNONYM: HEXO1, EXONUCLEASE I, HEXOI;
COMPND 6 EC: 3.1.-.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DNA (5'-D(*CP*GP*CP*TP*AP*GP*TP*CP*GP*AP*CP*AP*T)-3');
COMPND 10 CHAIN: A;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: DNA (5'-D(P*TP*CP*GP*AP*CP*TP*AP*GP*CP*G)-3');
COMPND 14 CHAIN: B;
COMPND 15 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: EXO1, EXOI, HEX1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 11 ORGANISM_TAXID: 32630;
SOURCE 12 MOL_ID: 3;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 15 ORGANISM_TAXID: 32630
KEYWDS EXONUCLEASE, ENDONUCLEASE, HYDROLASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.SHI,L.S.BEESE
REVDAT 6 04-OCT-23 5V05 1 LINK
REVDAT 5 04-DEC-19 5V05 1 REMARK
REVDAT 4 13-SEP-17 5V05 1 REMARK
REVDAT 3 21-JUN-17 5V05 1 JRNL
REVDAT 2 07-JUN-17 5V05 1 JRNL
REVDAT 1 24-MAY-17 5V05 0
JRNL AUTH Y.SHI,H.W.HELLINGA,L.S.BEESE
JRNL TITL INTERPLAY OF CATALYSIS, FIDELITY, THREADING, AND
JRNL TITL 2 PROCESSIVITY IN THE EXO- AND ENDONUCLEOLYTIC REACTIONS OF
JRNL TITL 3 HUMAN EXONUCLEASE I.
JRNL REF PROC. NATL. ACAD. SCI. V. 114 6010 2017
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 28533382
JRNL DOI 10.1073/PNAS.1704845114
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1839
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 11689
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) : 0.199
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.170
REMARK 3 FREE R VALUE TEST SET COUNT : 955
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 38.9820 - 5.5467 0.92 1563 136 0.1791 0.2445
REMARK 3 2 5.5467 - 4.4045 0.98 1552 135 0.1772 0.2124
REMARK 3 3 4.4045 - 3.8483 0.99 1536 140 0.1870 0.2403
REMARK 3 4 3.8483 - 3.4967 1.00 1532 137 0.2159 0.2526
REMARK 3 5 3.4967 - 3.2462 1.00 1521 129 0.2268 0.2724
REMARK 3 6 3.2462 - 3.0549 1.00 1514 136 0.2611 0.2952
REMARK 3 7 3.0549 - 2.9020 1.00 1516 142 0.2998 0.3654
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) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.400
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 3338
REMARK 3 ANGLE : 0.615 4540
REMARK 3 CHIRALITY : 0.022 512
REMARK 3 PLANARITY : 0.002 504
REMARK 3 DIHEDRAL : 16.231 1276
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 25
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 1:4)
REMARK 3 ORIGIN FOR THE GROUP (A): -23.2731 47.8435 -21.3825
REMARK 3 T TENSOR
REMARK 3 T11: 1.2591 T22: 0.9850
REMARK 3 T33: 1.4090 T12: 0.3616
REMARK 3 T13: -0.1685 T23: 0.4010
REMARK 3 L TENSOR
REMARK 3 L11: 0.7837 L22: 1.0211
REMARK 3 L33: 2.2796 L12: 0.6305
REMARK 3 L13: -0.0422 L23: 1.0525
REMARK 3 S TENSOR
REMARK 3 S11: 1.8298 S12: 0.1794 S13: -0.4709
REMARK 3 S21: -2.2996 S22: -0.2292 S23: 0.1567
REMARK 3 S31: 0.0301 S32: -1.1192 S33: 0.4797
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 5:9)
REMARK 3 ORIGIN FOR THE GROUP (A): -28.7334 36.7318 -10.0349
REMARK 3 T TENSOR
REMARK 3 T11: 1.4228 T22: 1.1427
REMARK 3 T33: 1.5466 T12: 0.0917
REMARK 3 T13: 0.0630 T23: 0.4786
REMARK 3 L TENSOR
REMARK 3 L11: 1.6339 L22: 2.3827
REMARK 3 L33: 0.7577 L12: -1.7841
REMARK 3 L13: -0.1007 L23: -0.4438
REMARK 3 S TENSOR
REMARK 3 S11: 1.8735 S12: -1.2906 S13: -2.4241
REMARK 3 S21: 2.3995 S22: -1.9003 S23: 0.2848
REMARK 3 S31: -0.8767 S32: -0.4679 S33: -0.1940
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 10:13)
REMARK 3 ORIGIN FOR THE GROUP (A): -23.9325 17.7213 -6.8478
REMARK 3 T TENSOR
REMARK 3 T11: 2.3598 T22: 1.0640
REMARK 3 T33: 1.6244 T12: -0.1724
REMARK 3 T13: -0.3273 T23: 0.2287
REMARK 3 L TENSOR
REMARK 3 L11: 6.5112 L22: 2.6250
REMARK 3 L33: 1.5279 L12: -1.7118
REMARK 3 L13: -2.8637 L23: 1.5218
REMARK 3 S TENSOR
REMARK 3 S11: -1.6304 S12: 0.5225 S13: -1.2461
REMARK 3 S21: -0.2655 S22: 0.0443 S23: 2.7140
REMARK 3 S31: -2.6458 S32: -2.1220 S33: -0.3351
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESID 1:4)
REMARK 3 ORIGIN FOR THE GROUP (A): -19.2183 33.7285 -9.1527
REMARK 3 T TENSOR
REMARK 3 T11: 1.4687 T22: 1.5079
REMARK 3 T33: 1.6998 T12: 0.1455
REMARK 3 T13: 0.1228 T23: 0.4940
REMARK 3 L TENSOR
REMARK 3 L11: 2.0263 L22: 2.0305
REMARK 3 L33: 1.9998 L12: -4.3072
REMARK 3 L13: -6.8605 L23: 2.0005
REMARK 3 S TENSOR
REMARK 3 S11: 2.6039 S12: -2.8077 S13: -1.5838
REMARK 3 S21: 2.7041 S22: 3.3988 S23: 1.3453
REMARK 3 S31: 0.5103 S32: 0.4651 S33: 9.5582
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN B AND RESID 5:10)
REMARK 3 ORIGIN FOR THE GROUP (A): -30.6606 43.7202 -19.5714
REMARK 3 T TENSOR
REMARK 3 T11: 1.1857 T22: 1.1092
REMARK 3 T33: 1.6650 T12: 0.1072
REMARK 3 T13: -0.0699 T23: 0.6026
REMARK 3 L TENSOR
REMARK 3 L11: 0.6125 L22: 2.7606
REMARK 3 L33: 1.0238 L12: 0.3294
REMARK 3 L13: 0.6119 L23: -0.6243
REMARK 3 S TENSOR
REMARK 3 S11: 1.3138 S12: 1.5929 S13: 0.0932
REMARK 3 S21: -0.3618 S22: -0.4773 S23: 1.9271
REMARK 3 S31: 0.2000 S32: -0.6722 S33: -0.4840
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN Z AND RESID 2:19)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.7632 32.8962 -20.2435
REMARK 3 T TENSOR
REMARK 3 T11: 0.9317 T22: 0.7180
REMARK 3 T33: 0.7679 T12: 0.0355
REMARK 3 T13: -0.1349 T23: -0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 1.8403 L22: 2.0041
REMARK 3 L33: 1.7813 L12: 0.9626
REMARK 3 L13: 0.5297 L23: -1.3165
REMARK 3 S TENSOR
REMARK 3 S11: -0.1764 S12: 0.0365 S13: -0.1770
REMARK 3 S21: -0.6192 S22: 0.7987 S23: -0.7783
REMARK 3 S31: 0.3162 S32: -0.4133 S33: 0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN Z AND RESID 20:35)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8486 23.0918 -8.8884
REMARK 3 T TENSOR
REMARK 3 T11: 0.9266 T22: 0.8185
REMARK 3 T33: 0.7860 T12: 0.2215
REMARK 3 T13: -0.0954 T23: -0.1808
REMARK 3 L TENSOR
REMARK 3 L11: 3.0276 L22: 2.9241
REMARK 3 L33: 1.7940 L12: 1.6338
REMARK 3 L13: -0.7103 L23: -2.2706
REMARK 3 S TENSOR
REMARK 3 S11: 1.1751 S12: 1.0841 S13: -1.4576
REMARK 3 S21: -0.9802 S22: -0.6634 S23: 0.2217
REMARK 3 S31: -1.3009 S32: -0.4904 S33: 0.0007
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN Z AND RESID 36:51)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.5222 21.5348 4.8002
REMARK 3 T TENSOR
REMARK 3 T11: 1.1678 T22: 1.2304
REMARK 3 T33: 1.2416 T12: -0.0020
REMARK 3 T13: 0.0362 T23: 0.2190
REMARK 3 L TENSOR
REMARK 3 L11: 0.6022 L22: 0.2841
REMARK 3 L33: 0.9705 L12: 0.0881
REMARK 3 L13: 0.6990 L23: 0.0687
REMARK 3 S TENSOR
REMARK 3 S11: 0.3694 S12: -0.9449 S13: -0.0654
REMARK 3 S21: 0.0678 S22: 1.3169 S23: 2.9986
REMARK 3 S31: 1.7587 S32: -0.6288 S33: 0.0214
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN Z AND RESID 52:72)
REMARK 3 ORIGIN FOR THE GROUP (A): -8.2030 15.9139 -3.6338
REMARK 3 T TENSOR
REMARK 3 T11: 1.2502 T22: 0.6788
REMARK 3 T33: 0.8809 T12: 0.1168
REMARK 3 T13: -0.0897 T23: 0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 1.7672 L22: 1.9896
REMARK 3 L33: 2.0194 L12: -1.2864
REMARK 3 L13: 1.7513 L23: -0.7023
REMARK 3 S TENSOR
REMARK 3 S11: -0.4557 S12: -0.0041 S13: -2.0051
REMARK 3 S21: -0.9493 S22: 0.6691 S23: 0.6575
REMARK 3 S31: 2.0412 S32: 0.3472 S33: 0.0068
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN Z AND RESID 73:79)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1116 26.9930 -0.0751
REMARK 3 T TENSOR
REMARK 3 T11: 0.9413 T22: 1.0375
REMARK 3 T33: 0.5551 T12: 0.1862
REMARK 3 T13: -0.0291 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 6.3045 L22: 4.6397
REMARK 3 L33: 0.2847 L12: 4.8997
REMARK 3 L13: -0.9207 L23: -0.3792
REMARK 3 S TENSOR
REMARK 3 S11: 0.0482 S12: -0.9478 S13: -1.9190
REMARK 3 S21: 0.8062 S22: -0.0942 S23: -0.4864
REMARK 3 S31: -0.7458 S32: -0.5597 S33: -0.0544
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN Z AND RESID 80:85)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.0308 42.7875 4.8916
REMARK 3 T TENSOR
REMARK 3 T11: 1.3354 T22: 0.8612
REMARK 3 T33: 1.3440 T12: 0.0258
REMARK 3 T13: 0.2260 T23: 0.1955
REMARK 3 L TENSOR
REMARK 3 L11: 0.3355 L22: 0.0804
REMARK 3 L33: 0.1296 L12: 0.0279
REMARK 3 L13: -0.1960 L23: -0.0641
REMARK 3 S TENSOR
REMARK 3 S11: -0.5663 S12: -1.6192 S13: -0.0029
REMARK 3 S21: 1.8535 S22: 1.9050 S23: 1.9441
REMARK 3 S31: -1.0310 S32: -1.3694 S33: 0.0018
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN Z AND RESID 86:97)
REMARK 3 ORIGIN FOR THE GROUP (A): -20.7868 40.2026 6.1287
REMARK 3 T TENSOR
REMARK 3 T11: 1.3913 T22: 1.3470
REMARK 3 T33: 1.6965 T12: 0.1467
REMARK 3 T13: 0.0397 T23: 0.1489
REMARK 3 L TENSOR
REMARK 3 L11: 0.6621 L22: 0.0323
REMARK 3 L33: 0.4832 L12: 0.0044
REMARK 3 L13: -0.1154 L23: -0.1257
REMARK 3 S TENSOR
REMARK 3 S11: 2.7075 S12: 0.6636 S13: -1.0393
REMARK 3 S21: 1.5409 S22: 0.1955 S23: 1.7646
REMARK 3 S31: 0.6516 S32: -0.0545 S33: 0.0375
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN Z AND RESID 98:115)
REMARK 3 ORIGIN FOR THE GROUP (A): -36.0183 27.4441 5.0934
REMARK 3 T TENSOR
REMARK 3 T11: 1.1317 T22: 1.2282
REMARK 3 T33: 2.5259 T12: -0.0333
REMARK 3 T13: 0.0106 T23: 0.5883
REMARK 3 L TENSOR
REMARK 3 L11: 1.5064 L22: 0.5813
REMARK 3 L33: 4.3115 L12: 0.9515
REMARK 3 L13: -2.5480 L23: -1.5931
REMARK 3 S TENSOR
REMARK 3 S11: -0.0381 S12: 1.3401 S13: 1.5281
REMARK 3 S21: 0.0086 S22: 1.5784 S23: -0.0695
REMARK 3 S31: 0.5882 S32: -2.1362 S33: 0.0244
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN Z AND RESID 116:124)
REMARK 3 ORIGIN FOR THE GROUP (A): -26.7140 27.6990 1.1204
REMARK 3 T TENSOR
REMARK 3 T11: 1.1698 T22: 1.0707
REMARK 3 T33: 1.7271 T12: -0.1122
REMARK 3 T13: -0.1842 T23: 0.3462
REMARK 3 L TENSOR
REMARK 3 L11: 0.4004 L22: 0.4256
REMARK 3 L33: 0.5851 L12: -0.3151
REMARK 3 L13: -0.4672 L23: 0.2693
REMARK 3 S TENSOR
REMARK 3 S11: 0.7638 S12: -0.2615 S13: -0.2624
REMARK 3 S21: 0.0886 S22: 0.5310 S23: 3.1810
REMARK 3 S31: -0.6701 S32: -1.4870 S33: 0.0065
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN Z AND RESID 125:149)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.4431 23.7605 5.5384
REMARK 3 T TENSOR
REMARK 3 T11: 1.1170 T22: 0.6036
REMARK 3 T33: 0.7570 T12: 0.2347
REMARK 3 T13: -0.1918 T23: 0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 1.7773 L22: 2.2331
REMARK 3 L33: 2.0848 L12: 0.5533
REMARK 3 L13: 0.5089 L23: 0.2285
REMARK 3 S TENSOR
REMARK 3 S11: 0.4758 S12: -0.5893 S13: 0.0397
REMARK 3 S21: 1.7397 S22: -0.2596 S23: -1.1490
REMARK 3 S31: 0.5258 S32: 0.9343 S33: 0.0344
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN Z AND RESID 150:185)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0859 32.9292 -9.6316
REMARK 3 T TENSOR
REMARK 3 T11: 0.7797 T22: 0.6377
REMARK 3 T33: 0.7901 T12: 0.0477
REMARK 3 T13: -0.0843 T23: -0.1591
REMARK 3 L TENSOR
REMARK 3 L11: 2.2215 L22: 2.4202
REMARK 3 L33: 2.9156 L12: 1.3726
REMARK 3 L13: -2.5441 L23: -2.0663
REMARK 3 S TENSOR
REMARK 3 S11: -0.2237 S12: 0.5456 S13: -0.1786
REMARK 3 S21: 0.0193 S22: -0.1641 S23: -0.0589
REMARK 3 S31: -0.7443 S32: 0.7299 S33: 0.0000
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN Z AND RESID 186:212)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8957 33.7321 -21.3272
REMARK 3 T TENSOR
REMARK 3 T11: 0.9549 T22: 0.8137
REMARK 3 T33: 0.7478 T12: 0.0711
REMARK 3 T13: -0.0440 T23: -0.1938
REMARK 3 L TENSOR
REMARK 3 L11: 4.4261 L22: 2.6372
REMARK 3 L33: 3.5497 L12: -1.7472
REMARK 3 L13: 1.3694 L23: 1.9439
REMARK 3 S TENSOR
REMARK 3 S11: 0.5233 S12: 0.6200 S13: -0.1721
REMARK 3 S21: -0.2656 S22: 0.0167 S23: -1.0241
REMARK 3 S31: 0.1407 S32: -0.2624 S33: 0.0000
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN Z AND RESID 213:224)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.7167 47.8463 -14.4660
REMARK 3 T TENSOR
REMARK 3 T11: 0.7875 T22: 0.6562
REMARK 3 T33: 0.7625 T12: -0.0125
REMARK 3 T13: -0.0127 T23: -0.0702
REMARK 3 L TENSOR
REMARK 3 L11: 0.4895 L22: 1.2976
REMARK 3 L33: 0.7466 L12: -0.4328
REMARK 3 L13: 0.4613 L23: -0.2316
REMARK 3 S TENSOR
REMARK 3 S11: 0.6403 S12: 0.3838 S13: 0.5966
REMARK 3 S21: -0.0275 S22: -0.2350 S23: 0.6690
REMARK 3 S31: -2.1345 S32: -0.4296 S33: 0.0002
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN Z AND RESID 225:242)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.3157 50.6966 -14.9828
REMARK 3 T TENSOR
REMARK 3 T11: 0.9632 T22: 0.6124
REMARK 3 T33: 0.8840 T12: 0.1938
REMARK 3 T13: -0.0961 T23: -0.0720
REMARK 3 L TENSOR
REMARK 3 L11: 1.4690 L22: 2.6460
REMARK 3 L33: 0.4443 L12: -0.3866
REMARK 3 L13: 0.8168 L23: -0.2468
REMARK 3 S TENSOR
REMARK 3 S11: 0.8011 S12: -0.3867 S13: -0.1235
REMARK 3 S21: 0.2463 S22: -0.4417 S23: 1.0337
REMARK 3 S31: 0.1351 S32: -0.5485 S33: -0.0003
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN Z AND RESID 243:249)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1598 56.9746 -22.5752
REMARK 3 T TENSOR
REMARK 3 T11: 1.1531 T22: 1.3562
REMARK 3 T33: 1.1364 T12: -0.0844
REMARK 3 T13: 0.0361 T23: 0.2296
REMARK 3 L TENSOR
REMARK 3 L11: 0.6806 L22: 0.7457
REMARK 3 L33: 0.3392 L12: -0.5971
REMARK 3 L13: 0.4133 L23: -0.1975
REMARK 3 S TENSOR
REMARK 3 S11: 0.6701 S12: 1.0610 S13: -0.4961
REMARK 3 S21: -0.9947 S22: 1.2042 S23: -1.2481
REMARK 3 S31: -0.4792 S32: 1.1348 S33: 0.0049
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN Z AND RESID 250:275)
REMARK 3 ORIGIN FOR THE GROUP (A): -11.4050 60.5085 -14.2515
REMARK 3 T TENSOR
REMARK 3 T11: 1.1318 T22: 0.7445
REMARK 3 T33: 0.8232 T12: 0.0602
REMARK 3 T13: -0.0703 T23: -0.0630
REMARK 3 L TENSOR
REMARK 3 L11: 0.4553 L22: 2.1738
REMARK 3 L33: 0.5401 L12: -0.0177
REMARK 3 L13: -0.1561 L23: 0.6531
REMARK 3 S TENSOR
REMARK 3 S11: 0.0699 S12: 0.4118 S13: 1.0579
REMARK 3 S21: 0.3649 S22: -0.3365 S23: 0.2222
REMARK 3 S31: -1.3811 S32: -1.0687 S33: 0.0000
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN Z AND RESID 276:300)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6674 41.8729 -1.0933
REMARK 3 T TENSOR
REMARK 3 T11: 0.8109 T22: 0.7656
REMARK 3 T33: 0.7668 T12: 0.0029
REMARK 3 T13: -0.2711 T23: -0.1074
REMARK 3 L TENSOR
REMARK 3 L11: 0.3246 L22: 0.7602
REMARK 3 L33: 3.9902 L12: -0.2802
REMARK 3 L13: -0.8116 L23: 0.0935
REMARK 3 S TENSOR
REMARK 3 S11: -0.7136 S12: -0.3148 S13: 0.1098
REMARK 3 S21: 0.6043 S22: 0.1915 S23: -0.4575
REMARK 3 S31: -1.0975 S32: 0.7255 S33: -0.0057
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN Z AND RESID 301:309)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0854 53.3122 -1.2463
REMARK 3 T TENSOR
REMARK 3 T11: 1.2713 T22: 1.0450
REMARK 3 T33: 1.0016 T12: -0.1614
REMARK 3 T13: -0.3523 T23: -0.1101
REMARK 3 L TENSOR
REMARK 3 L11: 1.2793 L22: 0.1689
REMARK 3 L33: 0.5370 L12: -0.4489
REMARK 3 L13: 0.7720 L23: -0.2562
REMARK 3 S TENSOR
REMARK 3 S11: 0.9842 S12: 0.7278 S13: 1.3445
REMARK 3 S21: 1.3542 S22: -0.9873 S23: -0.4014
REMARK 3 S31: -1.5138 S32: 1.6439 S33: -0.0445
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN Z AND RESID 310:337)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7821 36.3602 11.6297
REMARK 3 T TENSOR
REMARK 3 T11: 1.0784 T22: 0.9668
REMARK 3 T33: 0.8555 T12: -0.0878
REMARK 3 T13: -0.1510 T23: -0.0452
REMARK 3 L TENSOR
REMARK 3 L11: 0.9682 L22: 1.9623
REMARK 3 L33: 3.2001 L12: -0.3666
REMARK 3 L13: 1.4661 L23: 0.9288
REMARK 3 S TENSOR
REMARK 3 S11: -0.0193 S12: -0.4272 S13: -0.1563
REMARK 3 S21: 0.6664 S22: -0.0464 S23: 0.2039
REMARK 3 S31: -0.1868 S32: -0.0309 S33: -0.0000
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (CHAIN Z AND RESID 338:346)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0950 21.0406 12.0530
REMARK 3 T TENSOR
REMARK 3 T11: 1.0902 T22: 1.5052
REMARK 3 T33: 1.0245 T12: 0.1285
REMARK 3 T13: -0.2113 T23: 0.4123
REMARK 3 L TENSOR
REMARK 3 L11: 5.4993 L22: 2.9944
REMARK 3 L33: 3.6634 L12: -3.6497
REMARK 3 L13: -4.4386 L23: 3.1586
REMARK 3 S TENSOR
REMARK 3 S11: -0.2965 S12: 0.3237 S13: -1.6571
REMARK 3 S21: -0.2589 S22: -1.8265 S23: 0.8825
REMARK 3 S31: -0.3198 S32: 0.5822 S33: -0.2609
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 5V05 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1000226688.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-APR-15
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 : ALS
REMARK 200 BEAMLINE : 12.3.1
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 : DOUBLE CRYSTAL SI(111)
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 : 11702
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.5200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.68500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.690
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 3QEA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM ACETATE, PH 7.0, 10 MM
REMARK 280 POTASSIUM CHLORIDE, 2-4% PEG4000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 91.75600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 36.95300
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 36.95300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 137.63400
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 36.95300
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 36.95300
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 45.87800
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 36.95300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 36.95300
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 137.63400
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 36.95300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 36.95300
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 45.87800
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 91.75600
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Z, A, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH Z 538 LIES ON A SPECIAL POSITION.
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 Z 1
REMARK 465 MET Z 347
REMARK 465 PRO Z 348
REMARK 465 ALA Z 349
REMARK 465 HIS Z 350
REMARK 465 SER Z 351
REMARK 465 ARG Z 352
REMARK 465 GLU Z 353
REMARK 465 ASN Z 354
REMARK 465 TYR Z 356
REMARK 465 PHE Z 357
REMARK 465 GLN Z 358
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 DT B 1 P DT B 1 OP3 -0.128
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLU Z 109 CB - CA - C ANGL. DEV. = -15.5 DEGREES
REMARK 500 GLY Z 110 N - CA - C ANGL. DEV. = 18.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP Z 53 35.02 -152.50
REMARK 500 TYR Z 149 -113.35 -138.49
REMARK 500 VAL Z 209 51.26 -91.21
REMARK 500 ASP Z 340 50.71 -144.40
REMARK 500
REMARK 500 REMARK: NULL
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 MN Z 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP Z 152 OD2
REMARK 620 2 HOH Z 509 O 77.0
REMARK 620 3 HOH Z 531 O 87.3 81.9
REMARK 620 4 HOH Z 532 O 95.6 156.2 75.1
REMARK 620 5 HOH B 101 O 169.3 104.5 82.5 78.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN Z 402 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP Z 152 OD1
REMARK 620 2 ASP Z 171 OD2 96.5
REMARK 620 3 ASP Z 173 OD1 117.5 75.0
REMARK 620 4 HOH B 107 O 164.6 87.8 77.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA Z 403 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER Z 222 O
REMARK 620 2 SER Z 229 OG 86.6
REMARK 620 3 ILE Z 233 O 94.2 85.5
REMARK 620 4 HOH Z 536 O 87.0 89.3 174.5
REMARK 620 5 DT A 4 OP2 160.0 113.0 91.6 89.1
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN Z 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN Z 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA Z 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5UZV RELATED DB: PDB
REMARK 900 RELATED ID: 5V04 RELATED DB: PDB
REMARK 900 RELATED ID: 5V06 RELATED DB: PDB
REMARK 900 RELATED ID: 5V07 RELATED DB: PDB
REMARK 900 RELATED ID: 5V08 RELATED DB: PDB
REMARK 900 RELATED ID: 5V09 RELATED DB: PDB
REMARK 900 RELATED ID: 5V0A RELATED DB: PDB
REMARK 900 RELATED ID: 5V0B RELATED DB: PDB
REMARK 900 RELATED ID: 5V0C RELATED DB: PDB
REMARK 900 RELATED ID: 5V0D RELATED DB: PDB
REMARK 900 RELATED ID: 5V0E RELATED DB: PDB
DBREF 5V05 Z 1 352 UNP Q9UQ84 EXO1_HUMAN 1 352
DBREF 5V05 A 1 13 PDB 5V05 5V05 1 13
DBREF 5V05 B 1 10 PDB 5V05 5V05 1 10
SEQADV 5V05 GLU Z 353 UNP Q9UQ84 EXPRESSION TAG
SEQADV 5V05 ASN Z 354 UNP Q9UQ84 EXPRESSION TAG
SEQADV 5V05 LEU Z 355 UNP Q9UQ84 EXPRESSION TAG
SEQADV 5V05 TYR Z 356 UNP Q9UQ84 EXPRESSION TAG
SEQADV 5V05 PHE Z 357 UNP Q9UQ84 EXPRESSION TAG
SEQADV 5V05 GLN Z 358 UNP Q9UQ84 EXPRESSION TAG
SEQRES 1 Z 358 MET GLY ILE GLN GLY LEU LEU GLN PHE ILE LYS GLU ALA
SEQRES 2 Z 358 SER GLU PRO ILE HIS VAL ARG LYS TYR LYS GLY GLN VAL
SEQRES 3 Z 358 VAL ALA VAL ASP THR TYR CYS TRP LEU HIS LYS GLY ALA
SEQRES 4 Z 358 ILE ALA CYS ALA GLU LYS LEU ALA LYS GLY GLU PRO THR
SEQRES 5 Z 358 ASP ARG TYR VAL GLY PHE CYS MET LYS PHE VAL ASN MET
SEQRES 6 Z 358 LEU LEU SER HIS GLY ILE LYS PRO ILE LEU VAL PHE ASP
SEQRES 7 Z 358 GLY CYS THR LEU PRO SER LYS LYS GLU VAL GLU ARG SER
SEQRES 8 Z 358 ARG ARG GLU ARG ARG GLN ALA ASN LEU LEU LYS GLY LYS
SEQRES 9 Z 358 GLN LEU LEU ARG GLU GLY LYS VAL SER GLU ALA ARG GLU
SEQRES 10 Z 358 CYS PHE THR ARG SER ILE ASN ILE THR HIS ALA MET ALA
SEQRES 11 Z 358 HIS LYS VAL ILE LYS ALA ALA ARG SER GLN GLY VAL ASP
SEQRES 12 Z 358 CYS LEU VAL ALA PRO TYR GLU ALA ASP ALA GLN LEU ALA
SEQRES 13 Z 358 TYR LEU ASN LYS ALA GLY ILE VAL GLN ALA ILE ILE THR
SEQRES 14 Z 358 GLU ASP SER ASP LEU LEU ALA PHE GLY CYS LYS LYS VAL
SEQRES 15 Z 358 ILE LEU LYS MET ASP GLN PHE GLY ASN GLY LEU GLU ILE
SEQRES 16 Z 358 ASP GLN ALA ARG LEU GLY MET CYS ARG GLN LEU GLY ASP
SEQRES 17 Z 358 VAL PHE THR GLU GLU LYS PHE ARG TYR MET CYS ILE LEU
SEQRES 18 Z 358 SER GLY CYS ASP TYR LEU SER SER LEU ARG GLY ILE GLY
SEQRES 19 Z 358 LEU ALA LYS ALA CYS LYS VAL LEU ARG LEU ALA ASN ASN
SEQRES 20 Z 358 PRO ASP ILE VAL LYS VAL ILE LYS LYS ILE GLY HIS TYR
SEQRES 21 Z 358 LEU LYS MET ASN ILE THR VAL PRO GLU ASP TYR ILE ASN
SEQRES 22 Z 358 GLY PHE ILE ARG ALA ASN ASN THR PHE LEU TYR GLN LEU
SEQRES 23 Z 358 VAL PHE ASP PRO ILE LYS ARG LYS LEU ILE PRO LEU ASN
SEQRES 24 Z 358 ALA TYR GLU ASP ASP VAL ASP PRO GLU THR LEU SER TYR
SEQRES 25 Z 358 ALA GLY GLN TYR VAL ASP ASP SER ILE ALA LEU GLN ILE
SEQRES 26 Z 358 ALA LEU GLY ASN LYS ASP ILE ASN THR PHE GLU GLN ILE
SEQRES 27 Z 358 ASP ASP TYR ASN PRO ASP THR ALA MET PRO ALA HIS SER
SEQRES 28 Z 358 ARG GLU ASN LEU TYR PHE GLN
SEQRES 1 A 13 DC DG DC DT DA DG DT DC DG DA DC DA DT
SEQRES 1 B 10 DT DC DG DA DC DT DA DG DC DG
HET MN Z 401 1
HET MN Z 402 1
HET NA Z 403 1
HETNAM MN MANGANESE (II) ION
HETNAM NA SODIUM ION
FORMUL 4 MN 2(MN 2+)
FORMUL 6 NA NA 1+
FORMUL 7 HOH *54(H2 O)
HELIX 1 AA1 GLY Z 5 ILE Z 10 1 6
HELIX 2 AA2 ARG Z 20 LYS Z 23 5 4
HELIX 3 AA3 THR Z 31 CYS Z 42 1 12
HELIX 4 AA4 CYS Z 42 GLY Z 49 1 8
HELIX 5 AA5 ASP Z 53 HIS Z 69 1 17
HELIX 6 AA6 LEU Z 82 SER Z 84 5 3
HELIX 7 AA7 LYS Z 85 GLU Z 109 1 25
HELIX 8 AA8 VAL Z 112 THR Z 120 1 9
HELIX 9 AA9 THR Z 126 SER Z 139 1 14
HELIX 10 AB1 GLU Z 150 ALA Z 161 1 12
HELIX 11 AB2 SER Z 172 PHE Z 177 1 6
HELIX 12 AB3 ALA Z 198 CYS Z 203 5 6
HELIX 13 AB4 THR Z 211 GLY Z 223 1 13
HELIX 14 AB5 GLY Z 234 ALA Z 245 1 12
HELIX 15 AB6 ASP Z 249 LYS Z 256 1 8
HELIX 16 AB7 LYS Z 256 LYS Z 262 1 7
HELIX 17 AB8 PRO Z 268 GLN Z 285 1 18
HELIX 18 AB9 ASP Z 306 GLY Z 314 5 9
HELIX 19 AC1 ASP Z 318 LEU Z 327 1 10
SHEET 1 AA1 7 SER Z 14 HIS Z 18 0
SHEET 2 AA1 7 ASN Z 191 ASP Z 196 -1 O GLU Z 194 N GLU Z 15
SHEET 3 AA1 7 LYS Z 181 LEU Z 184 -1 N LEU Z 184 O LEU Z 193
SHEET 4 AA1 7 ALA Z 166 THR Z 169 1 N ILE Z 167 O ILE Z 183
SHEET 5 AA1 7 VAL Z 26 ASP Z 30 1 N ASP Z 30 O ILE Z 168
SHEET 6 AA1 7 LYS Z 72 PHE Z 77 1 O LYS Z 72 N VAL Z 27
SHEET 7 AA1 7 ASP Z 143 VAL Z 146 1 O LEU Z 145 N LEU Z 75
SHEET 1 AA2 2 LEU Z 286 ASP Z 289 0
SHEET 2 AA2 2 LYS Z 294 PRO Z 297 -1 O ILE Z 296 N VAL Z 287
LINK OD2 ASP Z 152 MN MN Z 401 1555 1555 2.17
LINK OD1 ASP Z 152 MN MN Z 402 1555 1555 2.16
LINK OD2 ASP Z 171 MN MN Z 402 1555 1555 2.16
LINK OD1 ASP Z 173 MN MN Z 402 1555 1555 2.15
LINK O SER Z 222 NA NA Z 403 1555 1555 2.41
LINK OG SER Z 229 NA NA Z 403 1555 1555 2.43
LINK O ILE Z 233 NA NA Z 403 1555 1555 2.46
LINK MN MN Z 401 O HOH Z 509 1555 1555 2.20
LINK MN MN Z 401 O HOH Z 531 1555 1555 2.19
LINK MN MN Z 401 O HOH Z 532 1555 1555 2.19
LINK MN MN Z 401 O HOH B 101 1555 1555 2.18
LINK MN MN Z 402 O HOH B 107 1555 1555 2.19
LINK NA NA Z 403 O HOH Z 536 1555 1555 2.42
LINK NA NA Z 403 OP2 DT A 4 1555 1555 2.49
SITE 1 AC1 6 HOH B 101 ASP Z 152 MN Z 402 HOH Z 509
SITE 2 AC1 6 HOH Z 531 HOH Z 532
SITE 1 AC2 5 HOH B 107 ASP Z 152 ASP Z 171 ASP Z 173
SITE 2 AC2 5 MN Z 401
SITE 1 AC3 5 DT A 4 SER Z 222 SER Z 229 ILE Z 233
SITE 2 AC3 5 HOH Z 536
CRYST1 73.906 73.906 183.512 90.00 90.00 90.00 P 43 21 2 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 0.013531 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013531 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005449 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
