HEADER HYDROLASE/DNA 28-FEB-17 5V07
TITLE CRYSTAL STRUCTURE OF HUMAN EXONUCLEASE 1 EXO1 (D173A) IN COMPLEX WITH
TITLE 2 5' RECESSED-END DNA (RV)
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 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: DNA (5'-D(*CP*GP*CP*TP*AP*GP*TP*CP*GP*AP*CP*AP*T)-3');
COMPND 11 CHAIN: A;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: DNA (5'-D(P*TP*CP*GP*AP*CP*TP*AP*GP*CP*G)-3');
COMPND 15 CHAIN: B;
COMPND 16 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 5V07 1 LINK
REVDAT 5 04-DEC-19 5V07 1 REMARK
REVDAT 4 13-SEP-17 5V07 1 REMARK
REVDAT 3 21-JUN-17 5V07 1 JRNL
REVDAT 2 07-JUN-17 5V07 1 JRNL
REVDAT 1 24-MAY-17 5V07 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. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.92
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 80.5
REMARK 3 NUMBER OF REFLECTIONS : 22817
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1855
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 36.9240 - 5.0188 0.95 2093 187 0.1499 0.2026
REMARK 3 2 5.0188 - 3.9851 0.98 2031 178 0.1412 0.1755
REMARK 3 3 3.9851 - 3.4818 0.99 2006 178 0.1599 0.2132
REMARK 3 4 3.4818 - 3.1636 1.00 2005 179 0.1849 0.2133
REMARK 3 5 3.1636 - 2.9370 1.00 1996 176 0.2066 0.2427
REMARK 3 6 2.9370 - 2.7639 1.00 1988 176 0.2325 0.2554
REMARK 3 7 2.7639 - 2.6255 1.00 1969 174 0.2344 0.2992
REMARK 3 8 2.6255 - 2.5112 0.95 1886 165 0.2480 0.3037
REMARK 3 9 2.5112 - 2.4146 0.80 1575 137 0.2379 0.3087
REMARK 3 10 2.4146 - 2.3313 0.64 1250 109 0.2524 0.2915
REMARK 3 11 2.3313 - 2.2584 0.49 953 89 0.2433 0.3434
REMARK 3 12 2.2584 - 2.1938 0.35 690 61 0.2218 0.2475
REMARK 3 13 2.1938 - 2.1361 0.27 520 46 0.2263 0.2906
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.590
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 : 0.012 3298
REMARK 3 ANGLE : 1.036 4510
REMARK 3 CHIRALITY : 0.043 508
REMARK 3 PLANARITY : 0.004 500
REMARK 3 DIHEDRAL : 19.042 1268
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): 13.7362 11.6587 -19.8194
REMARK 3 T TENSOR
REMARK 3 T11: 0.7214 T22: 0.5326
REMARK 3 T33: 0.8705 T12: 0.1117
REMARK 3 T13: -0.1335 T23: 0.2194
REMARK 3 L TENSOR
REMARK 3 L11: 8.0314 L22: 6.9136
REMARK 3 L33: 3.1943 L12: -0.7444
REMARK 3 L13: -2.0366 L23: 4.4674
REMARK 3 S TENSOR
REMARK 3 S11: 1.2246 S12: 0.1733 S13: 0.2801
REMARK 3 S21: -1.0371 S22: 1.1028 S23: 1.0276
REMARK 3 S31: -0.3001 S32: -1.0885 S33: -2.0466
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 5:9)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9772 1.2472 -7.9216
REMARK 3 T TENSOR
REMARK 3 T11: 0.8569 T22: 0.8236
REMARK 3 T33: 1.1315 T12: -0.0027
REMARK 3 T13: 0.0367 T23: 0.3917
REMARK 3 L TENSOR
REMARK 3 L11: 5.8498 L22: 3.3940
REMARK 3 L33: 2.8628 L12: -3.0625
REMARK 3 L13: 0.0000 L23: -2.2601
REMARK 3 S TENSOR
REMARK 3 S11: 0.6036 S12: -0.5272 S13: -0.4540
REMARK 3 S21: 1.3146 S22: 0.2920 S23: 1.5949
REMARK 3 S31: -0.1942 S32: -1.1041 S33: -0.8916
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 10:13)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2421 -18.0193 -5.9807
REMARK 3 T TENSOR
REMARK 3 T11: 1.4933 T22: 0.8092
REMARK 3 T33: 1.3977 T12: -0.3865
REMARK 3 T13: -0.4477 T23: 0.3597
REMARK 3 L TENSOR
REMARK 3 L11: 2.7225 L22: 2.8310
REMARK 3 L33: 3.5033 L12: -0.1240
REMARK 3 L13: -2.8443 L23: 1.3524
REMARK 3 S TENSOR
REMARK 3 S11: -0.3238 S12: 0.7989 S13: -1.2232
REMARK 3 S21: -1.1123 S22: 1.3818 S23: 2.1866
REMARK 3 S31: 1.0168 S32: -1.8547 S33: -0.7535
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESID 1:4)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7141 -2.6070 -7.6455
REMARK 3 T TENSOR
REMARK 3 T11: 0.5311 T22: 0.4780
REMARK 3 T33: 0.5507 T12: 0.0273
REMARK 3 T13: -0.0068 T23: 0.0849
REMARK 3 L TENSOR
REMARK 3 L11: 6.8012 L22: 6.9413
REMARK 3 L33: 5.6708 L12: -2.4390
REMARK 3 L13: -0.6496 L23: -4.9855
REMARK 3 S TENSOR
REMARK 3 S11: 0.6010 S12: -0.0977 S13: -0.2039
REMARK 3 S21: 0.4709 S22: 0.5833 S23: 0.8087
REMARK 3 S31: -0.7081 S32: -0.2882 S33: -1.1979
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN B AND RESID 5:10)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.4831 8.0246 -17.5979
REMARK 3 T TENSOR
REMARK 3 T11: 0.8411 T22: 0.7304
REMARK 3 T33: 1.5535 T12: 0.1668
REMARK 3 T13: -0.3605 T23: 0.9235
REMARK 3 L TENSOR
REMARK 3 L11: 6.3825 L22: 6.3226
REMARK 3 L33: 1.9146 L12: -5.3319
REMARK 3 L13: 2.4796 L23: -3.0931
REMARK 3 S TENSOR
REMARK 3 S11: 0.8157 S12: 0.8707 S13: -0.6009
REMARK 3 S21: -0.3274 S22: 0.0809 S23: 2.3906
REMARK 3 S31: -0.0826 S32: -0.9549 S33: -0.4965
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN Z AND RESID 2:21)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4270 -5.1778 -20.0197
REMARK 3 T TENSOR
REMARK 3 T11: 0.4790 T22: 0.5090
REMARK 3 T33: 0.4141 T12: -0.0329
REMARK 3 T13: -0.0184 T23: -0.0848
REMARK 3 L TENSOR
REMARK 3 L11: 4.3865 L22: 2.5422
REMARK 3 L33: 5.7709 L12: -1.8150
REMARK 3 L13: 3.1496 L23: -2.8927
REMARK 3 S TENSOR
REMARK 3 S11: 0.2995 S12: 0.7271 S13: -0.3120
REMARK 3 S21: -1.2899 S22: -0.2624 S23: 0.8295
REMARK 3 S31: 0.5463 S32: 0.1269 S33: 0.0174
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN Z AND RESID 22:39)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6522 -12.7126 -6.3411
REMARK 3 T TENSOR
REMARK 3 T11: 0.5806 T22: 0.3073
REMARK 3 T33: 0.4326 T12: 0.0634
REMARK 3 T13: -0.1322 T23: -0.0515
REMARK 3 L TENSOR
REMARK 3 L11: 7.4025 L22: 3.6674
REMARK 3 L33: 5.5661 L12: -1.1698
REMARK 3 L13: -3.4668 L23: 1.2767
REMARK 3 S TENSOR
REMARK 3 S11: 0.4697 S12: 0.5610 S13: -0.4476
REMARK 3 S21: 0.1043 S22: -0.2982 S23: 0.1114
REMARK 3 S31: 0.5032 S32: -0.2732 S33: -0.1127
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN Z AND RESID 40:53)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3291 -16.3393 8.0498
REMARK 3 T TENSOR
REMARK 3 T11: 1.1416 T22: 0.5841
REMARK 3 T33: 0.8169 T12: -0.1588
REMARK 3 T13: 0.0659 T23: 0.0684
REMARK 3 L TENSOR
REMARK 3 L11: 4.4734 L22: 9.1335
REMARK 3 L33: 3.5277 L12: 2.2036
REMARK 3 L13: -2.9367 L23: -5.0319
REMARK 3 S TENSOR
REMARK 3 S11: 0.2401 S12: -0.5347 S13: -0.4527
REMARK 3 S21: -0.1110 S22: 0.0996 S23: 1.3523
REMARK 3 S31: 1.6804 S32: -0.0808 S33: -0.3387
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN Z AND RESID 54:72)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.3659 -20.8165 -5.0859
REMARK 3 T TENSOR
REMARK 3 T11: 1.3030 T22: 0.3119
REMARK 3 T33: 0.5711 T12: 0.0854
REMARK 3 T13: -0.1394 T23: -0.0780
REMARK 3 L TENSOR
REMARK 3 L11: 2.4834 L22: 3.6908
REMARK 3 L33: 3.1300 L12: -0.3018
REMARK 3 L13: -0.6465 L23: 0.9184
REMARK 3 S TENSOR
REMARK 3 S11: 0.3065 S12: 0.1539 S13: -0.5419
REMARK 3 S21: -0.1007 S22: -0.1382 S23: -0.0075
REMARK 3 S31: 1.3457 S32: 0.1207 S33: -0.1198
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN Z AND RESID 73:84)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.8029 -3.8761 1.9228
REMARK 3 T TENSOR
REMARK 3 T11: 0.3964 T22: 0.4614
REMARK 3 T33: 0.3244 T12: -0.0250
REMARK 3 T13: -0.0798 T23: -0.0814
REMARK 3 L TENSOR
REMARK 3 L11: 2.5760 L22: 9.1356
REMARK 3 L33: 2.8199 L12: 0.1053
REMARK 3 L13: 0.3433 L23: -2.5907
REMARK 3 S TENSOR
REMARK 3 S11: 0.0862 S12: -0.2431 S13: 0.0594
REMARK 3 S21: 0.7896 S22: 0.2062 S23: 0.4110
REMARK 3 S31: 0.0047 S32: 0.4189 S33: -0.2974
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN Z AND RESID 85:100)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.8027 3.3665 5.0246
REMARK 3 T TENSOR
REMARK 3 T11: 0.5056 T22: 0.3978
REMARK 3 T33: 0.5833 T12: 0.0498
REMARK 3 T13: 0.0362 T23: -0.0365
REMARK 3 L TENSOR
REMARK 3 L11: 5.6205 L22: 4.0679
REMARK 3 L33: 8.8445 L12: 4.7644
REMARK 3 L13: -4.3134 L23: -4.1179
REMARK 3 S TENSOR
REMARK 3 S11: -0.0021 S12: -0.6712 S13: 1.0729
REMARK 3 S21: 0.5957 S22: 0.1664 S23: 0.5531
REMARK 3 S31: -1.0171 S32: -0.6044 S33: -0.1626
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN Z AND RESID 101:124)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.6631 -8.3291 5.8025
REMARK 3 T TENSOR
REMARK 3 T11: 0.8503 T22: 0.8623
REMARK 3 T33: 1.0739 T12: -0.1396
REMARK 3 T13: 0.1454 T23: 0.1954
REMARK 3 L TENSOR
REMARK 3 L11: 6.1539 L22: 2.1908
REMARK 3 L33: 9.1148 L12: 3.3975
REMARK 3 L13: -3.0999 L23: -1.3675
REMARK 3 S TENSOR
REMARK 3 S11: 0.4298 S12: 0.2378 S13: -0.4278
REMARK 3 S21: 0.6596 S22: 0.3050 S23: 1.3477
REMARK 3 S31: 0.4647 S32: -2.0539 S33: -0.6682
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN Z AND RESID 125:142)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.3046 -16.3763 6.0695
REMARK 3 T TENSOR
REMARK 3 T11: 1.0365 T22: 0.4291
REMARK 3 T33: 0.5184 T12: 0.0964
REMARK 3 T13: -0.1045 T23: 0.0261
REMARK 3 L TENSOR
REMARK 3 L11: 4.3473 L22: 6.6518
REMARK 3 L33: 7.2567 L12: -4.8818
REMARK 3 L13: -5.0426 L23: 4.5754
REMARK 3 S TENSOR
REMARK 3 S11: 0.1100 S12: -0.7675 S13: -0.5860
REMARK 3 S21: 0.4015 S22: 0.2804 S23: -0.3270
REMARK 3 S31: 1.6659 S32: 0.8994 S33: -0.2283
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN Z AND RESID 143:165)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.1332 -4.8601 -3.5235
REMARK 3 T TENSOR
REMARK 3 T11: 0.4897 T22: 0.4520
REMARK 3 T33: 0.3703 T12: 0.0828
REMARK 3 T13: -0.1017 T23: -0.1055
REMARK 3 L TENSOR
REMARK 3 L11: 7.5399 L22: 4.1007
REMARK 3 L33: 2.1182 L12: 1.8073
REMARK 3 L13: -3.0447 L23: -2.0232
REMARK 3 S TENSOR
REMARK 3 S11: -0.0271 S12: 0.2309 S13: -0.1799
REMARK 3 S21: 0.2214 S22: 0.1142 S23: -0.4988
REMARK 3 S31: 0.5692 S32: 0.5700 S33: -0.1074
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN Z AND RESID 166:184)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.4724 -3.6782 -12.0989
REMARK 3 T TENSOR
REMARK 3 T11: 0.5224 T22: 0.3603
REMARK 3 T33: 0.3665 T12: 0.0235
REMARK 3 T13: -0.0486 T23: -0.1025
REMARK 3 L TENSOR
REMARK 3 L11: 2.2475 L22: 5.7576
REMARK 3 L33: 3.8387 L12: 0.6275
REMARK 3 L13: -0.4551 L23: -0.6612
REMARK 3 S TENSOR
REMARK 3 S11: -0.0754 S12: 0.3734 S13: -0.1519
REMARK 3 S21: -0.3052 S22: 0.0872 S23: -0.2288
REMARK 3 S31: 0.0258 S32: 0.0850 S33: -0.0656
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN Z AND RESID 185:193)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.2821 -16.2727 -15.0950
REMARK 3 T TENSOR
REMARK 3 T11: 0.9630 T22: 0.4922
REMARK 3 T33: 0.6043 T12: -0.1820
REMARK 3 T13: -0.0647 T23: -0.1590
REMARK 3 L TENSOR
REMARK 3 L11: 6.2962 L22: 6.1319
REMARK 3 L33: 4.9153 L12: 1.0152
REMARK 3 L13: -1.0908 L23: -4.7707
REMARK 3 S TENSOR
REMARK 3 S11: 0.0990 S12: -0.1048 S13: -0.6479
REMARK 3 S21: -0.9067 S22: -0.3769 S23: 0.8598
REMARK 3 S31: 1.5044 S32: -0.3329 S33: 0.2019
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN Z AND RESID 194:213)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.7253 3.8135 -23.2374
REMARK 3 T TENSOR
REMARK 3 T11: 0.6511 T22: 0.6388
REMARK 3 T33: 0.3760 T12: 0.0414
REMARK 3 T13: -0.0243 T23: -0.0686
REMARK 3 L TENSOR
REMARK 3 L11: 7.0689 L22: 2.1754
REMARK 3 L33: 6.0664 L12: -0.4867
REMARK 3 L13: -1.8935 L23: -1.7515
REMARK 3 S TENSOR
REMARK 3 S11: 0.5176 S12: 0.8697 S13: 0.3731
REMARK 3 S21: -0.8260 S22: -0.9661 S23: -0.6057
REMARK 3 S31: 0.1260 S32: -0.1747 S33: 0.3460
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN Z AND RESID 214:228)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.9342 10.9198 -11.1907
REMARK 3 T TENSOR
REMARK 3 T11: 0.3211 T22: 0.3119
REMARK 3 T33: 0.3546 T12: -0.0147
REMARK 3 T13: 0.0008 T23: -0.0493
REMARK 3 L TENSOR
REMARK 3 L11: 7.3784 L22: 6.2284
REMARK 3 L33: 2.0625 L12: -2.6286
REMARK 3 L13: -0.7046 L23: 0.7955
REMARK 3 S TENSOR
REMARK 3 S11: 0.3372 S12: 0.3224 S13: 0.0535
REMARK 3 S21: -0.0943 S22: -0.4186 S23: 0.3238
REMARK 3 S31: -0.5028 S32: -0.2794 S33: 0.0564
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN Z AND RESID 229:244)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.6790 15.9073 -18.6910
REMARK 3 T TENSOR
REMARK 3 T11: 0.5334 T22: 0.3428
REMARK 3 T33: 0.5571 T12: 0.1527
REMARK 3 T13: -0.1189 T23: 0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 7.3744 L22: 6.1941
REMARK 3 L33: 6.0821 L12: 1.9599
REMARK 3 L13: -2.0178 L23: -1.5117
REMARK 3 S TENSOR
REMARK 3 S11: 0.4254 S12: 0.9990 S13: 0.0178
REMARK 3 S21: -0.2271 S22: 0.0072 S23: 0.6475
REMARK 3 S31: -1.0667 S32: -0.4870 S33: -0.4398
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN Z AND RESID 245:270)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.6771 24.6310 -15.6477
REMARK 3 T TENSOR
REMARK 3 T11: 0.7933 T22: 0.4872
REMARK 3 T33: 0.7106 T12: 0.0222
REMARK 3 T13: 0.0245 T23: 0.0342
REMARK 3 L TENSOR
REMARK 3 L11: 2.9589 L22: 2.5304
REMARK 3 L33: 7.4507 L12: 0.4445
REMARK 3 L13: 4.2557 L23: -1.0061
REMARK 3 S TENSOR
REMARK 3 S11: -0.5331 S12: 0.0883 S13: 1.0917
REMARK 3 S21: -0.2356 S22: -0.1134 S23: 0.1875
REMARK 3 S31: -1.5592 S32: 0.2430 S33: 0.5789
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN Z AND RESID 271:287)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.2814 12.8257 -4.0673
REMARK 3 T TENSOR
REMARK 3 T11: 0.4420 T22: 0.4259
REMARK 3 T33: 0.3549 T12: -0.0543
REMARK 3 T13: 0.0169 T23: -0.1603
REMARK 3 L TENSOR
REMARK 3 L11: 4.2521 L22: 5.9937
REMARK 3 L33: 4.2580 L12: -3.2730
REMARK 3 L13: 2.8154 L23: -4.5056
REMARK 3 S TENSOR
REMARK 3 S11: -0.4035 S12: -0.6299 S13: 0.3841
REMARK 3 S21: 0.6739 S22: 0.6084 S23: -0.1267
REMARK 3 S31: -0.8100 S32: 0.0628 S33: -0.1431
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN Z AND RESID 288:298)
REMARK 3 ORIGIN FOR THE GROUP (A): 46.7486 -2.1371 1.8771
REMARK 3 T TENSOR
REMARK 3 T11: 0.4582 T22: 0.8087
REMARK 3 T33: 0.5798 T12: 0.1377
REMARK 3 T13: -0.0644 T23: -0.1087
REMARK 3 L TENSOR
REMARK 3 L11: 7.7152 L22: 5.0295
REMARK 3 L33: 4.4566 L12: -5.1018
REMARK 3 L13: 3.9597 L23: -4.5398
REMARK 3 S TENSOR
REMARK 3 S11: -0.1421 S12: 0.0060 S13: -0.1449
REMARK 3 S21: -0.3268 S22: -0.3378 S23: -1.1233
REMARK 3 S31: 0.4435 S32: 1.8277 S33: 0.4844
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN Z AND RESID 299:309)
REMARK 3 ORIGIN FOR THE GROUP (A): 44.7970 14.5690 -1.5693
REMARK 3 T TENSOR
REMARK 3 T11: 0.7330 T22: 0.8391
REMARK 3 T33: 0.8488 T12: -0.2702
REMARK 3 T13: -0.0285 T23: -0.2352
REMARK 3 L TENSOR
REMARK 3 L11: 3.2775 L22: 3.7555
REMARK 3 L33: 5.1779 L12: -2.6210
REMARK 3 L13: -4.0482 L23: 2.7463
REMARK 3 S TENSOR
REMARK 3 S11: 0.4439 S12: -0.6049 S13: 1.1846
REMARK 3 S21: -0.2652 S22: 0.4745 S23: -1.0632
REMARK 3 S31: -2.3087 S32: 2.6115 S33: -0.7022
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN Z AND RESID 310:329)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.6374 0.4954 9.0371
REMARK 3 T TENSOR
REMARK 3 T11: 0.5751 T22: 0.6028
REMARK 3 T33: 0.3588 T12: -0.0034
REMARK 3 T13: -0.1181 T23: -0.0830
REMARK 3 L TENSOR
REMARK 3 L11: 3.2855 L22: 2.8841
REMARK 3 L33: 6.2102 L12: -2.6823
REMARK 3 L13: 2.2279 L23: -3.7013
REMARK 3 S TENSOR
REMARK 3 S11: -0.3702 S12: -0.7082 S13: 0.1552
REMARK 3 S21: 1.1714 S22: 0.2858 S23: -0.9318
REMARK 3 S31: 0.0024 S32: 0.5467 S33: 0.0531
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (CHAIN Z AND RESID 330:345)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.2521 -10.6516 14.2321
REMARK 3 T TENSOR
REMARK 3 T11: 0.9728 T22: 0.8892
REMARK 3 T33: 0.6022 T12: -0.0020
REMARK 3 T13: -0.0857 T23: 0.0411
REMARK 3 L TENSOR
REMARK 3 L11: 2.0623 L22: 7.6307
REMARK 3 L33: 6.5439 L12: 0.4652
REMARK 3 L13: 2.2583 L23: -3.1031
REMARK 3 S TENSOR
REMARK 3 S11: 0.2560 S12: -1.2682 S13: -0.2864
REMARK 3 S21: 1.1444 S22: -0.2715 S23: 0.1160
REMARK 3 S31: 0.6801 S32: 0.8764 S33: 0.0372
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 5V07 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_1000226690.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-FEB-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
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 : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22902
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
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 (%) : 80.3
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 25.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.30800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.830
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 (%): 53.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
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 89.53350
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 36.91850
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 36.91850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 134.30025
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 36.91850
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 36.91850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 44.76675
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 36.91850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 36.91850
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 134.30025
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 36.91850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 36.91850
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 44.76675
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 89.53350
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: 4190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 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 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 ALA Z 346
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 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 -0.122
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 DC A 8 O4' - C1' - N1 ANGL. DEV. = 3.4 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 TYR Z 149 -122.97 -130.79
REMARK 500 LEU Z 227 114.53 -166.47
REMARK 500 ASP Z 303 31.86 -92.89
REMARK 500 ASP Z 340 32.88 -140.04
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 ASP Z 171 OD2 80.8
REMARK 620 3 HOH Z 524 O 94.1 173.4
REMARK 620 4 HOH Z 563 O 174.0 99.0 86.5
REMARK 620 5 HOH Z 583 O 90.2 92.6 91.6 83.8
REMARK 620 6 DC B 2 OP1 95.4 92.7 83.6 90.6 172.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 101 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP Z 152 OD1
REMARK 620 2 HOH Z 505 O 93.0
REMARK 620 3 HOH Z 534 O 99.8 85.8
REMARK 620 4 HOH Z 539 O 92.4 171.7 87.1
REMARK 620 5 DT B 1 O3' 172.5 87.3 87.7 88.1
REMARK 620 6 DC B 2 OP1 107.7 92.3 152.6 92.0 64.9
REMARK 620 N 1 2 3 4 5
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 97.3
REMARK 620 3 ILE Z 233 O 91.7 77.3
REMARK 620 4 DT A 4 OP2 153.4 107.3 84.0
REMARK 620 5 HOH A 115 O 106.8 90.0 158.8 83.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 102 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH Z 510 O
REMARK 620 2 HOH Z 601 O 99.0
REMARK 620 3 DT B 1 OP1 82.3 171.9
REMARK 620 4 HOH B 205 O 174.0 86.9 91.9
REMARK 620 5 HOH B 212 O 90.2 97.2 90.8 88.4
REMARK 620 6 HOH B 213 O 99.8 79.5 92.4 81.8 169.8
REMARK 620 N 1 2 3 4 5
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 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 102
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: 5V05 RELATED DB: PDB
REMARK 900 RELATED ID: 5V06 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 5V07 Z 1 352 UNP Q9UQ84 EXO1_HUMAN 1 352
DBREF 5V07 A 1 13 PDB 5V07 5V07 1 13
DBREF 5V07 B 1 10 PDB 5V07 5V07 1 10
SEQADV 5V07 ALA Z 173 UNP Q9UQ84 ASP 173 ENGINEERED MUTATION
SEQRES 1 Z 352 MET GLY ILE GLN GLY LEU LEU GLN PHE ILE LYS GLU ALA
SEQRES 2 Z 352 SER GLU PRO ILE HIS VAL ARG LYS TYR LYS GLY GLN VAL
SEQRES 3 Z 352 VAL ALA VAL ASP THR TYR CYS TRP LEU HIS LYS GLY ALA
SEQRES 4 Z 352 ILE ALA CYS ALA GLU LYS LEU ALA LYS GLY GLU PRO THR
SEQRES 5 Z 352 ASP ARG TYR VAL GLY PHE CYS MET LYS PHE VAL ASN MET
SEQRES 6 Z 352 LEU LEU SER HIS GLY ILE LYS PRO ILE LEU VAL PHE ASP
SEQRES 7 Z 352 GLY CYS THR LEU PRO SER LYS LYS GLU VAL GLU ARG SER
SEQRES 8 Z 352 ARG ARG GLU ARG ARG GLN ALA ASN LEU LEU LYS GLY LYS
SEQRES 9 Z 352 GLN LEU LEU ARG GLU GLY LYS VAL SER GLU ALA ARG GLU
SEQRES 10 Z 352 CYS PHE THR ARG SER ILE ASN ILE THR HIS ALA MET ALA
SEQRES 11 Z 352 HIS LYS VAL ILE LYS ALA ALA ARG SER GLN GLY VAL ASP
SEQRES 12 Z 352 CYS LEU VAL ALA PRO TYR GLU ALA ASP ALA GLN LEU ALA
SEQRES 13 Z 352 TYR LEU ASN LYS ALA GLY ILE VAL GLN ALA ILE ILE THR
SEQRES 14 Z 352 GLU ASP SER ALA LEU LEU ALA PHE GLY CYS LYS LYS VAL
SEQRES 15 Z 352 ILE LEU LYS MET ASP GLN PHE GLY ASN GLY LEU GLU ILE
SEQRES 16 Z 352 ASP GLN ALA ARG LEU GLY MET CYS ARG GLN LEU GLY ASP
SEQRES 17 Z 352 VAL PHE THR GLU GLU LYS PHE ARG TYR MET CYS ILE LEU
SEQRES 18 Z 352 SER GLY CYS ASP TYR LEU SER SER LEU ARG GLY ILE GLY
SEQRES 19 Z 352 LEU ALA LYS ALA CYS LYS VAL LEU ARG LEU ALA ASN ASN
SEQRES 20 Z 352 PRO ASP ILE VAL LYS VAL ILE LYS LYS ILE GLY HIS TYR
SEQRES 21 Z 352 LEU LYS MET ASN ILE THR VAL PRO GLU ASP TYR ILE ASN
SEQRES 22 Z 352 GLY PHE ILE ARG ALA ASN ASN THR PHE LEU TYR GLN LEU
SEQRES 23 Z 352 VAL PHE ASP PRO ILE LYS ARG LYS LEU ILE PRO LEU ASN
SEQRES 24 Z 352 ALA TYR GLU ASP ASP VAL ASP PRO GLU THR LEU SER TYR
SEQRES 25 Z 352 ALA GLY GLN TYR VAL ASP ASP SER ILE ALA LEU GLN ILE
SEQRES 26 Z 352 ALA LEU GLY ASN LYS ASP ILE ASN THR PHE GLU GLN ILE
SEQRES 27 Z 352 ASP ASP TYR ASN PRO ASP THR ALA MET PRO ALA HIS SER
SEQRES 28 Z 352 ARG
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
HET MN B 101 1
HET MN B 102 1
HETNAM MN MANGANESE (II) ION
HETNAM NA SODIUM ION
FORMUL 4 MN 4(MN 2+)
FORMUL 6 NA NA 1+
FORMUL 9 HOH *132(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 ALA Z 41 1 11
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 ARG Z 108 1 24
HELIX 8 AA8 LYS Z 111 ARG Z 121 1 11
HELIX 9 AA9 THR Z 126 GLN Z 140 1 15
HELIX 10 AB1 GLU Z 150 ALA Z 161 1 12
HELIX 11 AB2 ASP Z 171 GLY Z 178 5 8
HELIX 12 AB3 ALA Z 198 GLY Z 207 5 10
HELIX 13 AB4 THR Z 211 SER Z 222 1 12
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 GLY Z 192 N ILE Z 17
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 ILE Z 168 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 ILE Z 74 N VAL Z 29
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 LYS Z 294 N ASP Z 289
LINK SG CYS Z 80 MN MN Z 402 1555 1555 2.42
LINK OD2 ASP Z 152 MN MN Z 401 1555 1555 2.10
LINK OD1 ASP Z 152 MN MN B 101 1555 1555 2.10
LINK OD2 ASP Z 171 MN MN Z 401 1555 1555 2.21
LINK O SER Z 222 NA NA Z 403 1555 1555 2.53
LINK OG SER Z 229 NA NA Z 403 1555 1555 2.58
LINK O ILE Z 233 NA NA Z 403 1555 1555 2.46
LINK MN MN Z 401 O HOH Z 524 1555 1555 2.31
LINK MN MN Z 401 O HOH Z 563 1555 1555 2.20
LINK MN MN Z 401 O HOH Z 583 1555 1555 2.23
LINK MN MN Z 401 OP1 DC B 2 1555 1555 2.09
LINK NA NA Z 403 OP2 DT A 4 1555 1555 2.52
LINK NA NA Z 403 O HOH A 115 1555 1555 2.33
LINK O HOH Z 505 MN MN B 101 1555 1555 2.24
LINK O HOH Z 510 MN MN B 102 1555 1555 2.15
LINK O HOH Z 534 MN MN B 101 1555 1555 2.15
LINK O HOH Z 539 MN MN B 101 1555 1555 2.29
LINK O HOH Z 601 MN MN B 102 1555 1555 2.23
LINK O3' DT B 1 MN MN B 101 1555 1555 2.41
LINK OP1 DT B 1 MN MN B 102 1555 1555 2.36
LINK OP1 DC B 2 MN MN B 101 1555 1555 2.23
LINK MN MN B 102 O HOH B 205 1555 1555 2.16
LINK MN MN B 102 O HOH B 212 1555 1555 2.14
LINK MN MN B 102 O HOH B 213 1555 1555 2.22
SITE 1 AC1 7 DC B 2 MN B 101 ASP Z 152 ASP Z 171
SITE 2 AC1 7 HOH Z 524 HOH Z 563 HOH Z 583
SITE 1 AC2 1 CYS Z 80
SITE 1 AC3 5 DT A 4 HOH A 115 SER Z 222 SER Z 229
SITE 2 AC3 5 ILE Z 233
SITE 1 AC4 7 DT B 1 DC B 2 ASP Z 152 MN Z 401
SITE 2 AC4 7 HOH Z 505 HOH Z 534 HOH Z 539
SITE 1 AC5 6 DT B 1 HOH B 205 HOH B 212 HOH B 213
SITE 2 AC5 6 HOH Z 510 HOH Z 601
CRYST1 73.837 73.837 179.067 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 0.013543 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013543 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005585 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
