HEADER HYDROLASE/DNA/RNA 28-MAR-18 6CVP
TITLE HUMAN APRATAXIN (APTX) R199H BOUND TO RNA-DNA, AMP AND ZN PRODUCT
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APRATAXIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: APRATAXIN CATALYTIC DOMAIN;
COMPND 5 SYNONYM: FORKHEAD-ASSOCIATED DOMAIN HISTIDINE TRIAD-LIKE PROTEIN,FHA-
COMPND 6 HIT;
COMPND 7 EC: 3.1.11.7,3.1.12.2;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: DNA/RNA (5'-R(P*G)-D(P*TP*TP*AP*TP*GP*AP*TP*TP*C)-3');
COMPND 12 CHAIN: D, G;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: DNA (5'-D(*GP*AP*AP*TP*CP*AP*TP*AP*AP*C)-3');
COMPND 16 CHAIN: E, H;
COMPND 17 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: APTX, AXA1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 18 ORGANISM_TAXID: 9606
KEYWDS PROTEIN-DNA COMPLEX, DNA REPAIR, 5'-DNA END PROCESSING, HISTIDINE
KEYWDS 2 TRIAD DOMAIN, HIT DOMAIN, ZINC-FINGER, 5'-DNA END RECOGNITION,
KEYWDS 3 HYDROLASE, HYDROLASE-DNA-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.SCHELLENBERG,R.S.WILLIAMS,P.S.TUMBALE
REVDAT 5 04-OCT-23 6CVP 1 LINK
REVDAT 4 18-DEC-19 6CVP 1 REMARK
REVDAT 3 20-FEB-19 6CVP 1 REMARK
REVDAT 2 25-JUL-18 6CVP 1 JRNL
REVDAT 1 04-JUL-18 6CVP 0
JRNL AUTH P.TUMBALE,M.J.SCHELLENBERG,G.A.MUELLER,E.FAIRWEATHER,
JRNL AUTH 2 M.WATSON,J.N.LITTLE,J.KRAHN,I.WADDELL,R.E.LONDON,
JRNL AUTH 3 R.S.WILLIAMS
JRNL TITL MECHANISM OF APTX NICKED DNA SENSING AND PLEIOTROPIC
JRNL TITL 2 INACTIVATION IN NEURODEGENERATIVE DISEASE.
JRNL REF EMBO J. V. 37 2018
JRNL REFN ESSN 1460-2075
JRNL PMID 29934293
JRNL DOI 10.15252/EMBJ.201798875
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 73.7
REMARK 3 NUMBER OF REFLECTIONS : 56543
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 2847
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 27.6268 - 5.4127 0.95 3501 154 0.1504 0.1813
REMARK 3 2 5.4127 - 4.3014 0.96 3441 206 0.1219 0.1693
REMARK 3 3 4.3014 - 3.7592 0.96 3522 185 0.1336 0.1706
REMARK 3 4 3.7592 - 3.4162 0.96 3514 181 0.1379 0.2086
REMARK 3 5 3.4162 - 3.1717 0.96 3487 175 0.1577 0.2111
REMARK 3 6 3.1717 - 2.9849 0.95 3448 185 0.1764 0.2140
REMARK 3 7 2.9849 - 2.8356 0.95 3452 163 0.2042 0.2534
REMARK 3 8 2.8356 - 2.7123 0.95 3500 172 0.2041 0.2519
REMARK 3 9 2.7123 - 2.6080 0.92 3307 219 0.1964 0.2532
REMARK 3 10 2.6080 - 2.5180 0.88 3239 138 0.1852 0.2268
REMARK 3 11 2.5180 - 2.4393 0.82 3001 155 0.1933 0.2572
REMARK 3 12 2.4393 - 2.3697 0.75 2723 147 0.1934 0.2562
REMARK 3 13 2.3697 - 2.3073 0.69 2479 146 0.1864 0.2584
REMARK 3 14 2.3073 - 2.2510 0.63 2294 140 0.1950 0.2388
REMARK 3 15 2.2510 - 2.1999 0.59 2098 113 0.1941 0.2308
REMARK 3 16 2.1999 - 2.1531 0.52 1912 107 0.2115 0.3034
REMARK 3 17 2.1531 - 2.1100 0.46 1682 90 0.2141 0.2392
REMARK 3 18 2.1100 - 2.0702 0.37 1330 69 0.2226 0.2437
REMARK 3 19 2.0702 - 2.0333 0.27 996 61 0.2437 0.2976
REMARK 3 20 2.0333 - 1.9988 0.21 770 41 0.2420 0.2807
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.690
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.77
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 : 0.011 4011
REMARK 3 ANGLE : 0.983 5585
REMARK 3 CHIRALITY : 0.057 606
REMARK 3 PLANARITY : 0.007 552
REMARK 3 DIHEDRAL : 17.787 2233
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 165 THROUGH 192 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0278 21.4862 0.2627
REMARK 3 T TENSOR
REMARK 3 T11: 0.6123 T22: 0.1896
REMARK 3 T33: 0.2353 T12: -0.0225
REMARK 3 T13: 0.0335 T23: 0.0593
REMARK 3 L TENSOR
REMARK 3 L11: 1.5332 L22: 0.0612
REMARK 3 L33: 1.7099 L12: 0.2152
REMARK 3 L13: 0.3092 L23: -0.1703
REMARK 3 S TENSOR
REMARK 3 S11: 0.0375 S12: 0.4288 S13: 0.3247
REMARK 3 S21: -0.3029 S22: -0.0549 S23: -0.0305
REMARK 3 S31: -0.4496 S32: 0.2247 S33: 0.1623
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 193 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6178 17.0432 4.2868
REMARK 3 T TENSOR
REMARK 3 T11: 0.4244 T22: 0.0080
REMARK 3 T33: 0.1692 T12: 0.2119
REMARK 3 T13: -0.0061 T23: -0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 0.0616 L22: 0.9795
REMARK 3 L33: 0.5784 L12: 0.0134
REMARK 3 L13: 0.1847 L23: -0.0309
REMARK 3 S TENSOR
REMARK 3 S11: -0.1758 S12: -0.0496 S13: 0.1433
REMARK 3 S21: 0.0331 S22: 0.0124 S23: -0.1196
REMARK 3 S31: -0.7545 S32: -0.2515 S33: -0.1851
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 218 THROUGH 239 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3203 19.0178 -3.3932
REMARK 3 T TENSOR
REMARK 3 T11: 0.6235 T22: 0.2976
REMARK 3 T33: 0.1403 T12: 0.2966
REMARK 3 T13: -0.2145 T23: 0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 0.2259 L22: 0.2288
REMARK 3 L33: 0.2098 L12: -0.0665
REMARK 3 L13: 0.1565 L23: -0.1303
REMARK 3 S TENSOR
REMARK 3 S11: -0.1173 S12: 0.0083 S13: 0.1526
REMARK 3 S21: -0.1317 S22: 0.0240 S23: 0.0728
REMARK 3 S31: -0.1329 S32: -0.1430 S33: -0.1509
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 240 THROUGH 275 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1310 8.4423 5.0225
REMARK 3 T TENSOR
REMARK 3 T11: 0.2088 T22: 0.1654
REMARK 3 T33: 0.1806 T12: 0.0722
REMARK 3 T13: -0.0197 T23: 0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 1.6170 L22: 1.4362
REMARK 3 L33: 0.9047 L12: -0.0652
REMARK 3 L13: 0.2199 L23: -0.2659
REMARK 3 S TENSOR
REMARK 3 S11: -0.0587 S12: 0.0765 S13: -0.1308
REMARK 3 S21: -0.0464 S22: 0.0149 S23: 0.0816
REMARK 3 S31: -0.2215 S32: -0.1627 S33: 0.0367
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 276 THROUGH 314 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.3821 12.5657 13.0629
REMARK 3 T TENSOR
REMARK 3 T11: 0.1351 T22: 0.3757
REMARK 3 T33: 0.2571 T12: 0.3622
REMARK 3 T13: -0.0223 T23: 0.0368
REMARK 3 L TENSOR
REMARK 3 L11: 1.3756 L22: 1.5444
REMARK 3 L33: 1.2820 L12: -1.1574
REMARK 3 L13: 0.3266 L23: -0.2657
REMARK 3 S TENSOR
REMARK 3 S11: -0.0748 S12: -0.2346 S13: 0.1411
REMARK 3 S21: 0.0565 S22: 0.0021 S23: 0.3352
REMARK 3 S31: -0.7410 S32: -0.9057 S33: -0.1081
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 315 THROUGH 340 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8678 -7.1343 10.6264
REMARK 3 T TENSOR
REMARK 3 T11: 0.2138 T22: 0.2738
REMARK 3 T33: 0.3172 T12: 0.0158
REMARK 3 T13: -0.0076 T23: 0.0691
REMARK 3 L TENSOR
REMARK 3 L11: 1.1955 L22: 0.8218
REMARK 3 L33: 2.8775 L12: 0.2910
REMARK 3 L13: -0.2789 L23: 0.3579
REMARK 3 S TENSOR
REMARK 3 S11: -0.0509 S12: -0.1445 S13: -0.2443
REMARK 3 S21: 0.1143 S22: 0.1217 S23: 0.3280
REMARK 3 S31: 0.5692 S32: -0.2760 S33: -0.0525
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 10 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.2054 2.5473 23.7489
REMARK 3 T TENSOR
REMARK 3 T11: 0.2678 T22: 0.2576
REMARK 3 T33: 0.3468 T12: -0.0089
REMARK 3 T13: -0.0880 T23: 0.0629
REMARK 3 L TENSOR
REMARK 3 L11: 0.4936 L22: 2.2233
REMARK 3 L33: 1.0317 L12: 0.1384
REMARK 3 L13: 0.2205 L23: -1.3435
REMARK 3 S TENSOR
REMARK 3 S11: 0.2506 S12: -0.2058 S13: -0.2006
REMARK 3 S21: 0.2150 S22: -0.2928 S23: -0.2000
REMARK 3 S31: 0.2054 S32: 0.1239 S33: 0.0400
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 10 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.7794 2.8771 24.6809
REMARK 3 T TENSOR
REMARK 3 T11: 0.2821 T22: 0.1914
REMARK 3 T33: 0.3645 T12: -0.0375
REMARK 3 T13: -0.0337 T23: 0.0297
REMARK 3 L TENSOR
REMARK 3 L11: 0.9204 L22: 3.1989
REMARK 3 L33: 0.2343 L12: 1.7008
REMARK 3 L13: -0.1397 L23: -0.2063
REMARK 3 S TENSOR
REMARK 3 S11: 0.2882 S12: -0.3018 S13: -0.0205
REMARK 3 S21: 0.4439 S22: -0.3188 S23: 0.4808
REMARK 3 S31: 0.2211 S32: 0.1180 S33: -0.0639
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 164 THROUGH 176 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4375 14.6928 33.1680
REMARK 3 T TENSOR
REMARK 3 T11: 0.2025 T22: 0.3207
REMARK 3 T33: 0.1837 T12: 0.0139
REMARK 3 T13: 0.0030 T23: -0.0452
REMARK 3 L TENSOR
REMARK 3 L11: 2.3069 L22: 1.7943
REMARK 3 L33: 2.7447 L12: 0.3762
REMARK 3 L13: 1.3593 L23: 0.3121
REMARK 3 S TENSOR
REMARK 3 S11: 0.1012 S12: 0.1879 S13: -0.2067
REMARK 3 S21: -0.2739 S22: -0.0300 S23: -0.0497
REMARK 3 S31: 0.1483 S32: 0.4142 S33: -0.0154
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 177 THROUGH 192 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9150 16.2570 42.5070
REMARK 3 T TENSOR
REMARK 3 T11: 0.1182 T22: 0.3624
REMARK 3 T33: 0.3067 T12: -0.0515
REMARK 3 T13: 0.0141 T23: -0.0218
REMARK 3 L TENSOR
REMARK 3 L11: 2.3384 L22: 1.8534
REMARK 3 L33: 1.1758 L12: 0.5669
REMARK 3 L13: -0.5947 L23: -0.3127
REMARK 3 S TENSOR
REMARK 3 S11: 0.0225 S12: 0.2539 S13: -0.0279
REMARK 3 S21: -0.0959 S22: 0.0519 S23: -0.3153
REMARK 3 S31: -0.0540 S32: 0.4650 S33: 0.1238
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 193 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6675 17.3977 44.5072
REMARK 3 T TENSOR
REMARK 3 T11: 0.1446 T22: 0.1593
REMARK 3 T33: 0.1974 T12: -0.0491
REMARK 3 T13: -0.0261 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 1.0837 L22: 1.1780
REMARK 3 L33: 1.5667 L12: -0.0308
REMARK 3 L13: 0.1275 L23: 0.1269
REMARK 3 S TENSOR
REMARK 3 S11: 0.0209 S12: 0.1064 S13: -0.1293
REMARK 3 S21: -0.1301 S22: 0.0152 S23: -0.0388
REMARK 3 S31: -0.1827 S32: 0.1864 S33: -0.0354
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 218 THROUGH 239 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.1946 13.3451 53.6384
REMARK 3 T TENSOR
REMARK 3 T11: 0.1255 T22: 0.2254
REMARK 3 T33: 0.1703 T12: 0.0093
REMARK 3 T13: -0.0019 T23: 0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 2.0475 L22: 4.9102
REMARK 3 L33: 1.5898 L12: 1.5363
REMARK 3 L13: 0.1095 L23: 0.0811
REMARK 3 S TENSOR
REMARK 3 S11: 0.0232 S12: -0.0517 S13: -0.1156
REMARK 3 S21: 0.1036 S22: 0.1356 S23: -0.1301
REMARK 3 S31: -0.0175 S32: 0.2474 S33: -0.1217
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 240 THROUGH 286 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8521 24.7417 48.3883
REMARK 3 T TENSOR
REMARK 3 T11: 0.1640 T22: 0.1476
REMARK 3 T33: 0.1605 T12: -0.0039
REMARK 3 T13: 0.0077 T23: -0.0239
REMARK 3 L TENSOR
REMARK 3 L11: 1.0960 L22: 1.2711
REMARK 3 L33: 1.4325 L12: -0.6077
REMARK 3 L13: 0.1193 L23: -0.1195
REMARK 3 S TENSOR
REMARK 3 S11: -0.0139 S12: -0.0827 S13: 0.0978
REMARK 3 S21: 0.0637 S22: 0.0658 S23: -0.0318
REMARK 3 S31: -0.3707 S32: 0.0367 S33: -0.0484
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 287 THROUGH 314 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6831 12.2307 54.1882
REMARK 3 T TENSOR
REMARK 3 T11: 0.1890 T22: 0.2883
REMARK 3 T33: 0.3579 T12: 0.0306
REMARK 3 T13: 0.0850 T23: 0.0525
REMARK 3 L TENSOR
REMARK 3 L11: 1.7750 L22: 1.8927
REMARK 3 L33: 0.6461 L12: -0.9764
REMARK 3 L13: 0.4708 L23: -0.4030
REMARK 3 S TENSOR
REMARK 3 S11: -0.0350 S12: -0.4364 S13: -0.4761
REMARK 3 S21: 0.2468 S22: 0.1750 S23: 0.5552
REMARK 3 S31: -0.0061 S32: -0.4402 S33: -0.0245
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 315 THROUGH 328 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.5793 33.7147 54.8703
REMARK 3 T TENSOR
REMARK 3 T11: 0.2791 T22: 0.3247
REMARK 3 T33: 0.3215 T12: 0.0641
REMARK 3 T13: -0.0045 T23: -0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 1.1000 L22: 1.2210
REMARK 3 L33: 2.5765 L12: -0.8100
REMARK 3 L13: 0.6307 L23: -0.9022
REMARK 3 S TENSOR
REMARK 3 S11: -0.0929 S12: -0.2542 S13: 0.2049
REMARK 3 S21: 0.1157 S22: 0.0902 S23: 0.0118
REMARK 3 S31: -0.1677 S32: 0.1808 S33: 0.0757
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 329 THROUGH 340 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1054 40.0568 52.1513
REMARK 3 T TENSOR
REMARK 3 T11: 0.4764 T22: 0.3684
REMARK 3 T33: 0.3241 T12: -0.1287
REMARK 3 T13: -0.0020 T23: -0.0323
REMARK 3 L TENSOR
REMARK 3 L11: 0.5678 L22: 2.7483
REMARK 3 L33: 7.7850 L12: 0.8281
REMARK 3 L13: 1.7244 L23: 0.9951
REMARK 3 S TENSOR
REMARK 3 S11: 0.1920 S12: -0.2514 S13: 0.2829
REMARK 3 S21: 0.1465 S22: -0.1474 S23: -0.4745
REMARK 3 S31: -0.4302 S32: 0.6812 S33: 0.0755
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 1 THROUGH 10 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.7941 32.8004 30.7544
REMARK 3 T TENSOR
REMARK 3 T11: 0.3441 T22: 0.2122
REMARK 3 T33: 0.2869 T12: 0.0108
REMARK 3 T13: -0.1025 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 1.5877 L22: 2.2691
REMARK 3 L33: 1.1472 L12: -1.6966
REMARK 3 L13: 0.0624 L23: -0.0722
REMARK 3 S TENSOR
REMARK 3 S11: -0.0368 S12: 0.3587 S13: 0.3574
REMARK 3 S21: -0.1357 S22: -0.2412 S23: 0.1944
REMARK 3 S31: -0.4402 S32: -0.2425 S33: 0.1987
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 10 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.1774 31.3012 31.0507
REMARK 3 T TENSOR
REMARK 3 T11: 0.3921 T22: 0.2274
REMARK 3 T33: 0.2804 T12: 0.0419
REMARK 3 T13: -0.0454 T23: -0.0387
REMARK 3 L TENSOR
REMARK 3 L11: 1.0429 L22: 2.3221
REMARK 3 L33: 1.3317 L12: -0.7184
REMARK 3 L13: -0.6675 L23: 1.2957
REMARK 3 S TENSOR
REMARK 3 S11: -0.2157 S12: 0.1163 S13: 0.1852
REMARK 3 S21: 0.2454 S22: -0.1517 S23: 0.2901
REMARK 3 S31: -0.3186 S32: -0.3234 S33: 0.2986
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 6CVP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1000232821.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAY-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 1.000
REMARK 200 MONOCHROMATOR : 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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39638
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 97.2
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.47500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 4NDF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, 20% W/V POLYETHYLENE
REMARK 280 GLYCOL 3350, PH 6.5, VAPOR DIFFUSION, 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 19.75350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.15700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.55250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.15700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.75350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 60.55250
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G, H
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 GLY A 161
REMARK 465 SER A 162
REMARK 465 HIS A 163
REMARK 465 MET A 164
REMARK 465 THR A 341
REMARK 465 GLN A 342
REMARK 465 GLY B 161
REMARK 465 THR B 341
REMARK 465 GLN B 342
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 HIS A 258 108.75 77.24
REMARK 500 HIS B 258 108.22 77.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 670 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH B 720 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH B 721 DISTANCE = 6.36 ANGSTROMS
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 ZN A 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 319 SG
REMARK 620 2 CYS A 322 SG 116.9
REMARK 620 3 HIS A 335 NE2 101.2 107.3
REMARK 620 4 HIS A 339 NE2 105.7 119.3 104.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 403 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 255 OG
REMARK 620 2 HOH B 660 O 91.3
REMARK 620 3 HOH B 669 O 96.2 100.5
REMARK 620 4 HOH B 711 O 167.8 77.7 91.2
REMARK 620 5 HOH G 118 O 92.2 167.1 91.5 97.4
REMARK 620 6 HOH G 121 O 81.3 88.9 170.4 93.0 79.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 319 SG
REMARK 620 2 CYS B 322 SG 119.9
REMARK 620 3 HIS B 335 NE2 104.9 103.9
REMARK 620 4 HIS B 339 NE2 99.8 123.3 102.6
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NDF RELATED DB: PDB
REMARK 900 CONTAINS WILDTYOE APTX
DBREF 6CVP A 165 342 UNP Q7Z2E3 APTX_HUMAN 179 356
DBREF 6CVP D 1 10 PDB 6CVP 6CVP 1 10
DBREF 6CVP E 1 10 PDB 6CVP 6CVP 1 10
DBREF 6CVP B 165 342 UNP Q7Z2E3 APTX_HUMAN 179 356
DBREF 6CVP G 1 10 PDB 6CVP 6CVP 1 10
DBREF 6CVP H 1 10 PDB 6CVP 6CVP 1 10
SEQADV 6CVP GLY A 161 UNP Q7Z2E3 EXPRESSION TAG
SEQADV 6CVP SER A 162 UNP Q7Z2E3 EXPRESSION TAG
SEQADV 6CVP HIS A 163 UNP Q7Z2E3 EXPRESSION TAG
SEQADV 6CVP MET A 164 UNP Q7Z2E3 EXPRESSION TAG
SEQADV 6CVP HIS A 199 UNP Q7Z2E3 ARG 213 ENGINEERED MUTATION
SEQADV 6CVP GLY B 161 UNP Q7Z2E3 EXPRESSION TAG
SEQADV 6CVP SER B 162 UNP Q7Z2E3 EXPRESSION TAG
SEQADV 6CVP HIS B 163 UNP Q7Z2E3 EXPRESSION TAG
SEQADV 6CVP MET B 164 UNP Q7Z2E3 EXPRESSION TAG
SEQADV 6CVP HIS B 199 UNP Q7Z2E3 ARG 213 ENGINEERED MUTATION
SEQRES 1 A 182 GLY SER HIS MET GLY HIS TRP SER GLN GLY LEU LYS ILE
SEQRES 2 A 182 SER MET GLN ASP PRO LYS MET GLN VAL TYR LYS ASP GLU
SEQRES 3 A 182 GLN VAL VAL VAL ILE LYS ASP LYS TYR PRO LYS ALA HIS
SEQRES 4 A 182 TYR HIS TRP LEU VAL LEU PRO TRP THR SER ILE SER SER
SEQRES 5 A 182 LEU LYS ALA VAL ALA ARG GLU HIS LEU GLU LEU LEU LYS
SEQRES 6 A 182 HIS MET HIS THR VAL GLY GLU LYS VAL ILE VAL ASP PHE
SEQRES 7 A 182 ALA GLY SER SER LYS LEU ARG PHE ARG LEU GLY TYR HIS
SEQRES 8 A 182 ALA ILE PRO SER MET SER HIS VAL HIS LEU HIS VAL ILE
SEQRES 9 A 182 SER GLN ASP PHE ASP SER PRO CYS LEU LYS ASN LYS LYS
SEQRES 10 A 182 HIS TRP ASN SER PHE ASN THR GLU TYR PHE LEU GLU SER
SEQRES 11 A 182 GLN ALA VAL ILE GLU MET VAL GLN GLU ALA GLY ARG VAL
SEQRES 12 A 182 THR VAL ARG ASP GLY MET PRO GLU LEU LEU LYS LEU PRO
SEQRES 13 A 182 LEU ARG CYS HIS GLU CYS GLN GLN LEU LEU PRO SER ILE
SEQRES 14 A 182 PRO GLN LEU LYS GLU HIS LEU ARG LYS HIS TRP THR GLN
SEQRES 1 D 10 G DT DT DA DT DG DA DT DT DC
SEQRES 1 E 10 DG DA DA DT DC DA DT DA DA DC
SEQRES 1 B 182 GLY SER HIS MET GLY HIS TRP SER GLN GLY LEU LYS ILE
SEQRES 2 B 182 SER MET GLN ASP PRO LYS MET GLN VAL TYR LYS ASP GLU
SEQRES 3 B 182 GLN VAL VAL VAL ILE LYS ASP LYS TYR PRO LYS ALA HIS
SEQRES 4 B 182 TYR HIS TRP LEU VAL LEU PRO TRP THR SER ILE SER SER
SEQRES 5 B 182 LEU LYS ALA VAL ALA ARG GLU HIS LEU GLU LEU LEU LYS
SEQRES 6 B 182 HIS MET HIS THR VAL GLY GLU LYS VAL ILE VAL ASP PHE
SEQRES 7 B 182 ALA GLY SER SER LYS LEU ARG PHE ARG LEU GLY TYR HIS
SEQRES 8 B 182 ALA ILE PRO SER MET SER HIS VAL HIS LEU HIS VAL ILE
SEQRES 9 B 182 SER GLN ASP PHE ASP SER PRO CYS LEU LYS ASN LYS LYS
SEQRES 10 B 182 HIS TRP ASN SER PHE ASN THR GLU TYR PHE LEU GLU SER
SEQRES 11 B 182 GLN ALA VAL ILE GLU MET VAL GLN GLU ALA GLY ARG VAL
SEQRES 12 B 182 THR VAL ARG ASP GLY MET PRO GLU LEU LEU LYS LEU PRO
SEQRES 13 B 182 LEU ARG CYS HIS GLU CYS GLN GLN LEU LEU PRO SER ILE
SEQRES 14 B 182 PRO GLN LEU LYS GLU HIS LEU ARG LYS HIS TRP THR GLN
SEQRES 1 G 10 G DT DT DA DT DG DA DT DT DC
SEQRES 1 H 10 DG DA DA DT DC DA DT DA DA DC
HET AMP A 401 23
HET ZN A 402 1
HET AMP B 401 23
HET ZN B 402 1
HET NA B 403 1
HETNAM AMP ADENOSINE MONOPHOSPHATE
HETNAM ZN ZINC ION
HETNAM NA SODIUM ION
FORMUL 7 AMP 2(C10 H14 N5 O7 P)
FORMUL 8 ZN 2(ZN 2+)
FORMUL 11 NA NA 1+
FORMUL 12 HOH *509(H2 O)
HELIX 1 AA1 HIS A 166 SER A 168 5 3
HELIX 2 AA2 GLN A 169 ASP A 177 1 9
HELIX 3 AA3 SER A 212 VAL A 216 5 5
HELIX 4 AA4 ALA A 217 GLU A 219 5 3
HELIX 5 AA5 HIS A 220 GLY A 240 1 21
HELIX 6 AA6 ASN A 275 THR A 284 1 10
HELIX 7 AA7 SER A 290 GLY A 301 1 12
HELIX 8 AA8 GLY A 308 LEU A 313 1 6
HELIX 9 AA9 SER A 328 ARG A 337 1 10
HELIX 10 AB1 LYS A 338 TRP A 340 5 3
HELIX 11 AB2 GLY B 165 SER B 168 5 4
HELIX 12 AB3 GLN B 169 GLN B 176 1 8
HELIX 13 AB4 ASP B 177 LYS B 179 5 3
HELIX 14 AB5 SER B 212 VAL B 216 5 5
HELIX 15 AB6 ALA B 217 GLU B 219 5 3
HELIX 16 AB7 HIS B 220 GLY B 240 1 21
HELIX 17 AB8 SER B 241 LYS B 243 5 3
HELIX 18 AB9 ASN B 275 THR B 284 1 10
HELIX 19 AC1 SER B 290 GLY B 301 1 12
HELIX 20 AC2 GLY B 308 LEU B 313 1 6
HELIX 21 AC3 SER B 328 ARG B 337 1 10
HELIX 22 AC4 LYS B 338 TRP B 340 5 3
SHEET 1 AA1 6 GLN A 181 LYS A 184 0
SHEET 2 AA1 6 VAL A 188 LYS A 192 -1 O VAL A 190 N TYR A 183
SHEET 3 AA1 6 HIS A 201 PRO A 206 -1 O LEU A 205 N VAL A 189
SHEET 4 AA1 6 LEU A 261 SER A 265 -1 O VAL A 263 N TRP A 202
SHEET 5 AA1 6 PHE A 246 HIS A 251 -1 N GLY A 249 O HIS A 262
SHEET 6 AA1 6 PHE A 287 GLU A 289 -1 O LEU A 288 N TYR A 250
SHEET 1 AA2 2 LEU A 317 ARG A 318 0
SHEET 2 AA2 2 LEU A 325 LEU A 326 -1 O LEU A 326 N LEU A 317
SHEET 1 AA3 6 GLN B 181 LYS B 184 0
SHEET 2 AA3 6 VAL B 188 LYS B 192 -1 O VAL B 190 N TYR B 183
SHEET 3 AA3 6 HIS B 201 PRO B 206 -1 O LEU B 203 N ILE B 191
SHEET 4 AA3 6 LEU B 261 SER B 265 -1 O VAL B 263 N TRP B 202
SHEET 5 AA3 6 PHE B 246 HIS B 251 -1 N GLY B 249 O HIS B 262
SHEET 6 AA3 6 PHE B 287 GLU B 289 -1 O LEU B 288 N TYR B 250
SHEET 1 AA4 2 LEU B 317 ARG B 318 0
SHEET 2 AA4 2 LEU B 325 LEU B 326 -1 O LEU B 326 N LEU B 317
LINK SG CYS A 319 ZN ZN A 402 1555 1555 2.32
LINK SG CYS A 322 ZN ZN A 402 1555 1555 2.24
LINK NE2 HIS A 335 ZN ZN A 402 1555 1555 1.98
LINK NE2 HIS A 339 ZN ZN A 402 1555 1555 2.08
LINK OG SER B 255 NA NA B 403 1555 1555 2.39
LINK SG CYS B 319 ZN ZN B 402 1555 1555 2.27
LINK SG CYS B 322 ZN ZN B 402 1555 1555 2.28
LINK NE2 HIS B 335 ZN ZN B 402 1555 1555 1.97
LINK NE2 HIS B 339 ZN ZN B 402 1555 1555 2.08
LINK NA NA B 403 O HOH B 660 1555 1555 2.22
LINK NA NA B 403 O HOH B 669 1555 1555 2.40
LINK NA NA B 403 O HOH B 711 1555 1555 2.37
LINK NA NA B 403 O HOH G 118 1555 1555 2.37
LINK NA NA B 403 O HOH G 121 1555 1555 2.81
SITE 1 AC1 19 GLY A 170 LEU A 171 SER A 174 LYS A 192
SITE 2 AC1 19 ASP A 193 LYS A 194 TYR A 195 LYS A 197
SITE 3 AC1 19 LEU A 203 HIS A 251 PRO A 254 SER A 255
SITE 4 AC1 19 MET A 256 HIS A 260 HIS A 262 HOH A 523
SITE 5 AC1 19 HOH A 543 G D 1 HOH D 101
SITE 1 AC2 4 CYS A 319 CYS A 322 HIS A 335 HIS A 339
SITE 1 AC3 19 LEU B 171 SER B 174 LYS B 192 ASP B 193
SITE 2 AC3 19 LYS B 194 TYR B 195 LYS B 197 LEU B 203
SITE 3 AC3 19 HIS B 251 PRO B 254 SER B 255 MET B 256
SITE 4 AC3 19 HIS B 260 HIS B 262 HOH B 503 HOH B 542
SITE 5 AC3 19 HOH B 610 G G 1 HOH G 106
SITE 1 AC4 4 CYS B 319 CYS B 322 HIS B 335 HIS B 339
SITE 1 AC5 6 SER B 255 HOH B 660 HOH B 669 HOH B 711
SITE 2 AC5 6 HOH G 118 HOH G 121
CRYST1 39.507 121.105 122.314 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 0.025312 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008257 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008176 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
