HEADER SIGNALING PROTEIN/TRANSFERASE 29-NOV-13 4CHB
TITLE CRYSTAL STRUCTURE OF THE HUMAN KLHL2 KELCH DOMAIN IN COMPLEX WITH A
TITLE 2 WNK4 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KELCH-LIKE PROTEIN 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: KELCH DOMAIN, RESIDUES 294-591;
COMPND 5 SYNONYM: ACTIN-BINDING PROTEIN MAYVEN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: SERINE/THREONINE-PROTEIN KINASE WNK4;
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: RESIDUES 557-567;
COMPND 11 SYNONYM: PROTEIN KINASE LYSINE-DEFICIENT 4, PROTEIN KINASE WITH NO
COMPND 12 LYSINE 4;
COMPND 13 EC: 2.7.11.1;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: R3 PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606
KEYWDS SIGNALING PROTEIN-TRANSFERASE COMPLEX, KLHL3, UBIQUITIN, ADAPTOR
KEYWDS 2 PROTEIN, PROTEIN-BINDING, KELCH REPEAT, WNK SIGNALLING PATHWAY
EXPDTA X-RAY DIFFRACTION
AUTHOR F.J.SORRELL,F.R.SCHUMACHER,T.KURZ,D.R.ALESSI,J.NEWMAN,C.D.O.COOPER,
AUTHOR 2 P.CANNING,J.KOPEC,E.WILLIAMS,T.KROJER,F.VON DELFT,C.H.ARROWSMITH,
AUTHOR 3 A.M.EDWARDS,C.BOUNTRA,A.BULLOCK
REVDAT 8 20-DEC-23 4CHB 1 REMARK
REVDAT 7 29-MAY-19 4CHB 1 REMARK
REVDAT 6 06-MAR-19 4CHB 1 REMARK
REVDAT 5 24-JAN-18 4CHB 1 AUTHOR
REVDAT 4 22-JUL-15 4CHB 1 COMPND
REVDAT 3 28-MAY-14 4CHB 1 JRNL
REVDAT 2 21-MAY-14 4CHB 1 JRNL
REVDAT 1 08-JAN-14 4CHB 0
JRNL AUTH F.SCHUMACHER,F.J.SORRELL,D.R.ALESSI,A.N.BULLOCK,T.KURZ
JRNL TITL STRUCTURAL AND BIOCHEMICAL CHARACTERISATION OF THE KLHL3-WNK
JRNL TITL 2 KINASE INTERACTION IMPORTANT IN BLOOD PRESSURE REGULATION.
JRNL REF BIOCHEM.J. V. 460 237 2014
JRNL REFN ISSN 0264-6021
JRNL PMID 24641320
JRNL DOI 10.1042/BJ20140153
REMARK 2
REMARK 2 RESOLUTION. 1.56 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.52
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 106285
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5337
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 39.5284 - 4.8444 0.99 3644 185 0.1902 0.2320
REMARK 3 2 4.8444 - 3.8462 1.00 3484 178 0.1560 0.1621
REMARK 3 3 3.8462 - 3.3603 1.00 3434 186 0.1721 0.1881
REMARK 3 4 3.3603 - 3.0532 1.00 3417 162 0.1757 0.1685
REMARK 3 5 3.0532 - 2.8344 1.00 3401 189 0.1703 0.1896
REMARK 3 6 2.8344 - 2.6673 1.00 3375 180 0.1782 0.1805
REMARK 3 7 2.6673 - 2.5338 1.00 3364 205 0.1752 0.1966
REMARK 3 8 2.5338 - 2.4235 1.00 3382 184 0.1768 0.1843
REMARK 3 9 2.4235 - 2.3302 1.00 3353 174 0.1731 0.1880
REMARK 3 10 2.3302 - 2.2498 1.00 3380 185 0.1706 0.1914
REMARK 3 11 2.2498 - 2.1795 1.00 3333 193 0.1716 0.1851
REMARK 3 12 2.1795 - 2.1172 1.00 3338 189 0.1682 0.1966
REMARK 3 13 2.1172 - 2.0614 1.00 3343 177 0.1605 0.1803
REMARK 3 14 2.0614 - 2.0112 1.00 3344 195 0.1615 0.1695
REMARK 3 15 2.0112 - 1.9654 1.00 3343 185 0.1561 0.1681
REMARK 3 16 1.9654 - 1.9236 1.00 3379 151 0.1545 0.1705
REMARK 3 17 1.9236 - 1.8851 1.00 3327 191 0.1609 0.1821
REMARK 3 18 1.8851 - 1.8496 1.00 3317 182 0.1768 0.2036
REMARK 3 19 1.8496 - 1.8165 1.00 3340 159 0.1837 0.2145
REMARK 3 20 1.8165 - 1.7857 1.00 3326 163 0.1888 0.2222
REMARK 3 21 1.7857 - 1.7569 1.00 3368 161 0.1831 0.2211
REMARK 3 22 1.7569 - 1.7299 1.00 3327 174 0.1964 0.2180
REMARK 3 23 1.7299 - 1.7045 1.00 3321 172 0.1971 0.2217
REMARK 3 24 1.7045 - 1.6804 1.00 3331 194 0.2056 0.2623
REMARK 3 25 1.6804 - 1.6577 1.00 3334 170 0.2064 0.2263
REMARK 3 26 1.6577 - 1.6362 1.00 3310 187 0.2111 0.2100
REMARK 3 27 1.6362 - 1.6158 1.00 3338 157 0.2126 0.2233
REMARK 3 28 1.6158 - 1.5963 1.00 3323 172 0.2198 0.2119
REMARK 3 29 1.5963 - 1.5777 1.00 3342 170 0.2329 0.2496
REMARK 3 30 1.5777 - 1.5600 1.00 3330 167 0.2462 0.2627
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.700
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 4804
REMARK 3 ANGLE : 1.035 6554
REMARK 3 CHIRALITY : 0.044 716
REMARK 3 PLANARITY : 0.005 862
REMARK 3 DIHEDRAL : 11.060 1721
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 306:323)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.1648 -43.0647 -9.9340
REMARK 3 T TENSOR
REMARK 3 T11: 0.0711 T22: 0.1438
REMARK 3 T33: 0.0690 T12: 0.0158
REMARK 3 T13: -0.0017 T23: 0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 3.7423 L22: 3.9766
REMARK 3 L33: 2.2656 L12: 1.5955
REMARK 3 L13: -0.2335 L23: 0.5237
REMARK 3 S TENSOR
REMARK 3 S11: -0.1190 S12: -0.0474 S13: 0.0240
REMARK 3 S21: -0.0160 S22: -0.0062 S23: -0.1064
REMARK 3 S31: 0.1395 S32: 0.1430 S33: 0.1300
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 324:331)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9030 -42.5009 -13.1569
REMARK 3 T TENSOR
REMARK 3 T11: 0.1988 T22: 0.2724
REMARK 3 T33: 0.1863 T12: 0.0317
REMARK 3 T13: 0.0682 T23: 0.0409
REMARK 3 L TENSOR
REMARK 3 L11: 2.0356 L22: 7.1095
REMARK 3 L33: 4.2736 L12: -2.8923
REMARK 3 L13: 0.1216 L23: 3.4018
REMARK 3 S TENSOR
REMARK 3 S11: -0.3372 S12: -0.0754 S13: -0.1146
REMARK 3 S21: -0.5100 S22: 0.2847 S23: -0.5353
REMARK 3 S31: 0.2228 S32: 0.3669 S33: 0.0565
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 332:373)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6835 -38.3895 -6.2413
REMARK 3 T TENSOR
REMARK 3 T11: 0.0876 T22: 0.1404
REMARK 3 T33: 0.0517 T12: -0.0012
REMARK 3 T13: 0.0012 T23: -0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 3.0110 L22: 0.1716
REMARK 3 L33: 0.6526 L12: -0.0575
REMARK 3 L13: 0.0644 L23: -0.0431
REMARK 3 S TENSOR
REMARK 3 S11: -0.0335 S12: -0.1636 S13: 0.0259
REMARK 3 S21: 0.0219 S22: 0.0314 S23: -0.0298
REMARK 3 S31: 0.0025 S32: 0.0701 S33: 0.0115
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 374:388)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.6268 -32.0078 -1.0905
REMARK 3 T TENSOR
REMARK 3 T11: 0.1248 T22: 0.2187
REMARK 3 T33: 0.0699 T12: -0.0033
REMARK 3 T13: -0.0107 T23: -0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 4.3618 L22: 1.6656
REMARK 3 L33: 0.8045 L12: -0.7363
REMARK 3 L13: 0.6900 L23: 0.1263
REMARK 3 S TENSOR
REMARK 3 S11: -0.1316 S12: -0.1563 S13: 0.1771
REMARK 3 S21: 0.1566 S22: 0.0393 S23: -0.1347
REMARK 3 S31: -0.2830 S32: 0.1947 S33: 0.1205
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 389:459)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.1764 -28.0323 -15.4506
REMARK 3 T TENSOR
REMARK 3 T11: 0.0742 T22: 0.0743
REMARK 3 T33: 0.0652 T12: 0.0179
REMARK 3 T13: -0.0014 T23: -0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 1.3904 L22: 1.4421
REMARK 3 L33: 1.4239 L12: 0.0317
REMARK 3 L13: 0.0797 L23: -0.0536
REMARK 3 S TENSOR
REMARK 3 S11: -0.0163 S12: -0.1686 S13: 0.1236
REMARK 3 S21: 0.1139 S22: 0.0008 S23: -0.0501
REMARK 3 S31: -0.1832 S32: -0.0268 S33: 0.0211
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 460:524)
REMARK 3 ORIGIN FOR THE GROUP (A): -12.0183 -31.0053 -29.3302
REMARK 3 T TENSOR
REMARK 3 T11: 0.0786 T22: 0.0748
REMARK 3 T33: 0.0656 T12: 0.0078
REMARK 3 T13: 0.0127 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 1.2860 L22: 1.4118
REMARK 3 L33: 1.1652 L12: -0.3469
REMARK 3 L13: -0.4489 L23: 0.2759
REMARK 3 S TENSOR
REMARK 3 S11: 0.0382 S12: 0.0652 S13: 0.1273
REMARK 3 S21: -0.1063 S22: -0.0250 S23: -0.1005
REMARK 3 S31: -0.1210 S32: -0.0217 S33: -0.0090
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 525:578)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4997 -43.9151 -25.4034
REMARK 3 T TENSOR
REMARK 3 T11: 0.1064 T22: 0.1545
REMARK 3 T33: 0.1257 T12: 0.0429
REMARK 3 T13: 0.0351 T23: 0.0405
REMARK 3 L TENSOR
REMARK 3 L11: 1.5258 L22: 0.5541
REMARK 3 L33: 1.0088 L12: 0.4032
REMARK 3 L13: -0.2623 L23: 0.1002
REMARK 3 S TENSOR
REMARK 3 S11: -0.1553 S12: -0.2799 S13: -0.3266
REMARK 3 S21: -0.0643 S22: -0.0411 S23: -0.1813
REMARK 3 S31: 0.2576 S32: 0.3375 S33: 0.1066
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 579:591)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9694 -40.7837 -13.8357
REMARK 3 T TENSOR
REMARK 3 T11: 0.0969 T22: 0.2194
REMARK 3 T33: 0.1021 T12: 0.0487
REMARK 3 T13: -0.0013 T23: 0.0554
REMARK 3 L TENSOR
REMARK 3 L11: 6.4862 L22: 4.9742
REMARK 3 L33: 3.2875 L12: 3.3200
REMARK 3 L13: 0.9874 L23: 1.6875
REMARK 3 S TENSOR
REMARK 3 S11: 0.1488 S12: -0.2586 S13: -0.0699
REMARK 3 S21: 0.0406 S22: -0.3079 S23: -0.2893
REMARK 3 S31: 0.0408 S32: -0.0149 S33: 0.1408
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 306:323)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1817 -54.5698 11.7132
REMARK 3 T TENSOR
REMARK 3 T11: 0.1934 T22: 0.0983
REMARK 3 T33: 0.0619 T12: 0.0051
REMARK 3 T13: 0.0189 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 3.6216 L22: 2.9907
REMARK 3 L33: 1.7920 L12: 1.1252
REMARK 3 L13: 0.6315 L23: -0.1621
REMARK 3 S TENSOR
REMARK 3 S11: -0.0787 S12: 0.0092 S13: -0.1236
REMARK 3 S21: -0.0604 S22: -0.0482 S23: -0.0799
REMARK 3 S31: 0.2631 S32: 0.1385 S33: 0.1328
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 324:335)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.8754 -66.0694 13.8105
REMARK 3 T TENSOR
REMARK 3 T11: 0.1992 T22: 0.1282
REMARK 3 T33: 0.1320 T12: -0.0021
REMARK 3 T13: 0.0141 T23: 0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 7.0872 L22: 7.3650
REMARK 3 L33: 9.0035 L12: -1.9014
REMARK 3 L13: -1.1780 L23: -1.6546
REMARK 3 S TENSOR
REMARK 3 S11: 0.1209 S12: -0.4186 S13: -0.3018
REMARK 3 S21: 0.1213 S22: 0.0419 S23: 0.2854
REMARK 3 S31: 0.1866 S32: 0.2099 S33: -0.1561
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN B AND RESID 336:376)
REMARK 3 ORIGIN FOR THE GROUP (A): -20.8337 -48.4167 7.1624
REMARK 3 T TENSOR
REMARK 3 T11: 0.1482 T22: 0.0952
REMARK 3 T33: 0.0476 T12: -0.0085
REMARK 3 T13: -0.0020 T23: 0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 1.2021 L22: 2.5377
REMARK 3 L33: 1.3102 L12: 0.4866
REMARK 3 L13: -0.1153 L23: 0.6275
REMARK 3 S TENSOR
REMARK 3 S11: -0.0103 S12: 0.0978 S13: -0.0363
REMARK 3 S21: -0.2094 S22: -0.0045 S23: 0.0540
REMARK 3 S31: 0.1111 S32: -0.0287 S33: -0.0024
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN B AND RESID 377:388)
REMARK 3 ORIGIN FOR THE GROUP (A): -25.5455 -48.3631 2.3912
REMARK 3 T TENSOR
REMARK 3 T11: 0.1835 T22: 0.1212
REMARK 3 T33: 0.0728 T12: -0.0183
REMARK 3 T13: -0.0159 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 1.8047 L22: 4.2924
REMARK 3 L33: 2.3292 L12: -0.9153
REMARK 3 L13: 0.0375 L23: 2.2301
REMARK 3 S TENSOR
REMARK 3 S11: 0.1147 S12: 0.1152 S13: -0.1369
REMARK 3 S21: -0.3594 S22: -0.0913 S23: 0.1035
REMARK 3 S31: 0.0204 S32: -0.2341 S33: 0.0104
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN B AND RESID 389:458)
REMARK 3 ORIGIN FOR THE GROUP (A): -28.7225 -39.2252 17.0527
REMARK 3 T TENSOR
REMARK 3 T11: 0.0809 T22: 0.0615
REMARK 3 T33: 0.0580 T12: 0.0102
REMARK 3 T13: -0.0085 T23: 0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 1.8600 L22: 1.5305
REMARK 3 L33: 1.7560 L12: -0.1055
REMARK 3 L13: -0.0559 L23: -0.0650
REMARK 3 S TENSOR
REMARK 3 S11: -0.0138 S12: 0.1383 S13: -0.0030
REMARK 3 S21: -0.1622 S22: 0.0184 S23: 0.0893
REMARK 3 S31: -0.0252 S32: -0.0997 S33: 0.0066
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN B AND RESID 459:463)
REMARK 3 ORIGIN FOR THE GROUP (A): -18.1333 -32.3620 29.6408
REMARK 3 T TENSOR
REMARK 3 T11: 0.2424 T22: 0.1493
REMARK 3 T33: 0.1555 T12: -0.0359
REMARK 3 T13: -0.0562 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 4.5716 L22: 3.6699
REMARK 3 L33: 0.4826 L12: 4.0951
REMARK 3 L13: -1.4816 L23: -1.3312
REMARK 3 S TENSOR
REMARK 3 S11: -0.0231 S12: -0.4218 S13: 0.6180
REMARK 3 S21: 0.4825 S22: -0.3226 S23: 0.0855
REMARK 3 S31: -0.6684 S32: 0.3577 S33: 0.3507
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN B AND RESID 464:542)
REMARK 3 ORIGIN FOR THE GROUP (A): -24.1014 -46.2956 30.5575
REMARK 3 T TENSOR
REMARK 3 T11: 0.0761 T22: 0.0663
REMARK 3 T33: 0.0577 T12: 0.0070
REMARK 3 T13: 0.0085 T23: 0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 0.7837 L22: 1.3545
REMARK 3 L33: 1.0618 L12: -0.2457
REMARK 3 L13: 0.0496 L23: -0.5784
REMARK 3 S TENSOR
REMARK 3 S11: -0.0553 S12: -0.1337 S13: -0.0813
REMARK 3 S21: 0.0680 S22: 0.0375 S23: 0.0668
REMARK 3 S31: 0.0003 S32: -0.0169 S33: 0.0179
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN B AND RESID 543:591)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.0248 -57.0460 23.3921
REMARK 3 T TENSOR
REMARK 3 T11: 0.2040 T22: 0.1301
REMARK 3 T33: 0.1256 T12: 0.0414
REMARK 3 T13: 0.0634 T23: 0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 0.4020 L22: 1.0722
REMARK 3 L33: 1.5802 L12: 0.4790
REMARK 3 L13: -0.3113 L23: -0.1051
REMARK 3 S TENSOR
REMARK 3 S11: -0.1072 S12: -0.0465 S13: -0.2318
REMARK 3 S21: -0.4148 S22: -0.1009 S23: -0.2896
REMARK 3 S31: 0.4194 S32: 0.3388 S33: -0.0032
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 4CHB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-NOV-13.
REMARK 100 THE DEPOSITION ID IS D_1290059110.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 114962
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.520
REMARK 200 RESOLUTION RANGE LOW (A) : 39.590
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.52
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 1.10000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
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 2XN4
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING-DROP VAPOUR-DIFFUSION, 2.5 M
REMARK 280 AMMONIUM SULPHATE, 0.1 M HEPES, 2 % PEG 400 (PH 7.2), 293 K,
REMARK 280 VAPOR DIFFUSION, SITTING DROP
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 53.32500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 58.85000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 58.85000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 79.98750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 58.85000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 58.85000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 26.66250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 58.85000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.85000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 79.98750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 58.85000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.85000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 26.66250
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 53.32500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 SER A 292
REMARK 465 MET A 293
REMARK 465 SER A 294
REMARK 465 VAL A 295
REMARK 465 ARG A 296
REMARK 465 THR A 297
REMARK 465 ARG A 298
REMARK 465 LEU A 299
REMARK 465 ARG A 300
REMARK 465 THR A 301
REMARK 465 PRO A 302
REMARK 465 MET A 303
REMARK 465 ASN A 304
REMARK 465 LEU A 305
REMARK 465 ARG A 592
REMARK 465 LEU A 593
REMARK 465 SER B 292
REMARK 465 MET B 293
REMARK 465 SER B 294
REMARK 465 VAL B 295
REMARK 465 ARG B 296
REMARK 465 THR B 297
REMARK 465 ARG B 298
REMARK 465 LEU B 299
REMARK 465 ARG B 300
REMARK 465 THR B 301
REMARK 465 PRO B 302
REMARK 465 MET B 303
REMARK 465 ASN B 304
REMARK 465 LEU B 305
REMARK 465 ARG B 592
REMARK 465 LEU B 593
REMARK 465 GLN C 567
REMARK 465 GLN D 567
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 318 CG CD CE NZ
REMARK 470 LYS A 329 CG CD CE NZ
REMARK 470 LYS A 377 CE NZ
REMARK 470 ARG A 387 CZ NH1 NH2
REMARK 470 LYS A 423 CD CE NZ
REMARK 470 ASN A 542 CG OD1 ND2
REMARK 470 LYS A 591 CG CD CE NZ
REMARK 470 LYS B 318 CE NZ
REMARK 470 LYS B 329 CG CD CE NZ
REMARK 470 LYS B 377 CE NZ
REMARK 470 ARG B 387 CZ NH1 NH2
REMARK 470 LYS B 423 CD CE NZ
REMARK 470 ARG B 460 CD NE CZ NH1 NH2
REMARK 470 ASN B 542 CG OD1 ND2
REMARK 470 SER B 554 OG
REMARK 470 LYS B 591 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 2007 O HOH B 2008 1.94
REMARK 500 O HOH A 2138 O HOH A 2139 2.02
REMARK 500 O3 SO4 B 1592 O HOH A 2051 2.12
REMARK 500 O HOH A 2064 O HOH C 2003 2.15
REMARK 500 O HOH B 2115 O HOH B 2116 2.17
REMARK 500 O HOH A 2093 O HOH A 2094 2.17
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 CYS A 468 CA - CB - SG ANGL. DEV. = 6.9 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 ALA A 316 53.20 -152.84
REMARK 500 VAL A 336 -165.89 -116.85
REMARK 500 SER A 364 -54.97 -125.50
REMARK 500 SER A 411 -51.67 -120.66
REMARK 500 ILE A 479 -169.90 -109.90
REMARK 500 VAL A 526 -166.47 -116.25
REMARK 500 ALA B 316 53.16 -152.37
REMARK 500 VAL B 336 -167.56 -116.61
REMARK 500 SER B 364 -55.35 -125.09
REMARK 500 SER B 411 -51.30 -121.20
REMARK 500 SER B 411 -57.88 -120.81
REMARK 500 VAL B 526 -165.24 -116.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 12P A 1595
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1592
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1592
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1593
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1594
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 12P A 1595
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1596
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1593
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1594
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1595
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1567
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1567
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CH9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN KLHL3 KELCH DOMAIN IN COMPLEX WITH A
REMARK 900 WNK4 PEPTIDE
DBREF 4CHB A 294 591 UNP O95198 KLHL2_HUMAN 294 591
DBREF 4CHB B 294 591 UNP O95198 KLHL2_HUMAN 294 591
DBREF 4CHB C 557 567 UNP Q96J92 WNK4_HUMAN 557 567
DBREF 4CHB D 557 567 UNP Q96J92 WNK4_HUMAN 557 567
SEQADV 4CHB SER A 292 UNP O95198 EXPRESSION TAG
SEQADV 4CHB MET A 293 UNP O95198 EXPRESSION TAG
SEQADV 4CHB ARG A 592 UNP O95198 EXPRESSION TAG
SEQADV 4CHB LEU A 593 UNP O95198 EXPRESSION TAG
SEQADV 4CHB VAL A 457 UNP O95198 GLY 457 CONFLICT
SEQADV 4CHB SER B 292 UNP O95198 EXPRESSION TAG
SEQADV 4CHB MET B 293 UNP O95198 EXPRESSION TAG
SEQADV 4CHB ARG B 592 UNP O95198 EXPRESSION TAG
SEQADV 4CHB LEU B 593 UNP O95198 EXPRESSION TAG
SEQADV 4CHB VAL B 457 UNP O95198 GLY 457 CONFLICT
SEQRES 1 A 302 SER MET SER VAL ARG THR ARG LEU ARG THR PRO MET ASN
SEQRES 2 A 302 LEU PRO LYS LEU MET VAL VAL VAL GLY GLY GLN ALA PRO
SEQRES 3 A 302 LYS ALA ILE ARG SER VAL GLU CYS TYR ASP PHE LYS GLU
SEQRES 4 A 302 GLU ARG TRP HIS GLN VAL ALA GLU LEU PRO SER ARG ARG
SEQRES 5 A 302 CYS ARG ALA GLY MET VAL TYR MET ALA GLY LEU VAL PHE
SEQRES 6 A 302 ALA VAL GLY GLY PHE ASN GLY SER LEU ARG VAL ARG THR
SEQRES 7 A 302 VAL ASP SER TYR ASP PRO VAL LYS ASP GLN TRP THR SER
SEQRES 8 A 302 VAL ALA ASN MET ARG ASP ARG ARG SER THR LEU GLY ALA
SEQRES 9 A 302 ALA VAL LEU ASN GLY LEU LEU TYR ALA VAL GLY GLY PHE
SEQRES 10 A 302 ASP GLY SER THR GLY LEU SER SER VAL GLU ALA TYR ASN
SEQRES 11 A 302 ILE LYS SER ASN GLU TRP PHE HIS VAL ALA PRO MET ASN
SEQRES 12 A 302 THR ARG ARG SER SER VAL GLY VAL GLY VAL VAL GLY GLY
SEQRES 13 A 302 LEU LEU TYR ALA VAL GLY GLY TYR ASP VAL ALA SER ARG
SEQRES 14 A 302 GLN CYS LEU SER THR VAL GLU CYS TYR ASN ALA THR THR
SEQRES 15 A 302 ASN GLU TRP THR TYR ILE ALA GLU MET SER THR ARG ARG
SEQRES 16 A 302 SER GLY ALA GLY VAL GLY VAL LEU ASN ASN LEU LEU TYR
SEQRES 17 A 302 ALA VAL GLY GLY HIS ASP GLY PRO LEU VAL ARG LYS SER
SEQRES 18 A 302 VAL GLU VAL TYR ASP PRO THR THR ASN ALA TRP ARG GLN
SEQRES 19 A 302 VAL ALA ASP MET ASN MET CYS ARG ARG ASN ALA GLY VAL
SEQRES 20 A 302 CYS ALA VAL ASN GLY LEU LEU TYR VAL VAL GLY GLY ASP
SEQRES 21 A 302 ASP GLY SER CYS ASN LEU ALA SER VAL GLU TYR TYR ASN
SEQRES 22 A 302 PRO THR THR ASP LYS TRP THR VAL VAL SER SER CYS MET
SEQRES 23 A 302 SER THR GLY ARG SER TYR ALA GLY VAL THR VAL ILE ASP
SEQRES 24 A 302 LYS ARG LEU
SEQRES 1 B 302 SER MET SER VAL ARG THR ARG LEU ARG THR PRO MET ASN
SEQRES 2 B 302 LEU PRO LYS LEU MET VAL VAL VAL GLY GLY GLN ALA PRO
SEQRES 3 B 302 LYS ALA ILE ARG SER VAL GLU CYS TYR ASP PHE LYS GLU
SEQRES 4 B 302 GLU ARG TRP HIS GLN VAL ALA GLU LEU PRO SER ARG ARG
SEQRES 5 B 302 CYS ARG ALA GLY MET VAL TYR MET ALA GLY LEU VAL PHE
SEQRES 6 B 302 ALA VAL GLY GLY PHE ASN GLY SER LEU ARG VAL ARG THR
SEQRES 7 B 302 VAL ASP SER TYR ASP PRO VAL LYS ASP GLN TRP THR SER
SEQRES 8 B 302 VAL ALA ASN MET ARG ASP ARG ARG SER THR LEU GLY ALA
SEQRES 9 B 302 ALA VAL LEU ASN GLY LEU LEU TYR ALA VAL GLY GLY PHE
SEQRES 10 B 302 ASP GLY SER THR GLY LEU SER SER VAL GLU ALA TYR ASN
SEQRES 11 B 302 ILE LYS SER ASN GLU TRP PHE HIS VAL ALA PRO MET ASN
SEQRES 12 B 302 THR ARG ARG SER SER VAL GLY VAL GLY VAL VAL GLY GLY
SEQRES 13 B 302 LEU LEU TYR ALA VAL GLY GLY TYR ASP VAL ALA SER ARG
SEQRES 14 B 302 GLN CYS LEU SER THR VAL GLU CYS TYR ASN ALA THR THR
SEQRES 15 B 302 ASN GLU TRP THR TYR ILE ALA GLU MET SER THR ARG ARG
SEQRES 16 B 302 SER GLY ALA GLY VAL GLY VAL LEU ASN ASN LEU LEU TYR
SEQRES 17 B 302 ALA VAL GLY GLY HIS ASP GLY PRO LEU VAL ARG LYS SER
SEQRES 18 B 302 VAL GLU VAL TYR ASP PRO THR THR ASN ALA TRP ARG GLN
SEQRES 19 B 302 VAL ALA ASP MET ASN MET CYS ARG ARG ASN ALA GLY VAL
SEQRES 20 B 302 CYS ALA VAL ASN GLY LEU LEU TYR VAL VAL GLY GLY ASP
SEQRES 21 B 302 ASP GLY SER CYS ASN LEU ALA SER VAL GLU TYR TYR ASN
SEQRES 22 B 302 PRO THR THR ASP LYS TRP THR VAL VAL SER SER CYS MET
SEQRES 23 B 302 SER THR GLY ARG SER TYR ALA GLY VAL THR VAL ILE ASP
SEQRES 24 B 302 LYS ARG LEU
SEQRES 1 C 11 GLU PRO GLU GLU PRO GLU ALA ASP GLN HIS GLN
SEQRES 1 D 11 GLU PRO GLU GLU PRO GLU ALA ASP GLN HIS GLN
HET EDO A1592 4
HET SO4 A1593 5
HET EDO A1594 4
HET 12P A1595 28
HET SO4 A1596 5
HET SO4 B1592 5
HET EDO B1593 4
HET EDO B1594 4
HET SO4 B1595 5
HET EDO C1567 4
HET EDO D1567 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SO4 SULFATE ION
HETNAM 12P DODECAETHYLENE GLYCOL
HETSYN EDO ETHYLENE GLYCOL
HETSYN 12P POLYETHYLENE GLYCOL PEG400
FORMUL 5 EDO 6(C2 H6 O2)
FORMUL 6 SO4 4(O4 S 2-)
FORMUL 8 12P C24 H50 O13
FORMUL 16 HOH *296(H2 O)
HELIX 1 1 PRO C 561 GLN C 565 5 5
HELIX 2 2 PRO D 561 GLN D 565 5 5
SHEET 1 AA 4 ARG A 332 GLN A 335 0
SHEET 2 AA 4 VAL A 323 ASP A 327 -1 O CYS A 325 N HIS A 334
SHEET 3 AA 4 LYS A 307 VAL A 312 -1 O MET A 309 N TYR A 326
SHEET 4 AA 4 GLY A 585 ASP A 590 -1 O GLY A 585 N VAL A 312
SHEET 1 AB 4 GLY A 347 MET A 351 0
SHEET 2 AB 4 LEU A 354 VAL A 358 -1 O LEU A 354 N MET A 351
SHEET 3 AB 4 VAL A 370 ASP A 374 -1 O ASP A 371 N ALA A 357
SHEET 4 AB 4 GLN A 379 VAL A 383 -1 O GLN A 379 N ASP A 374
SHEET 1 AC 4 GLY A 394 LEU A 398 0
SHEET 2 AC 4 LEU A 401 VAL A 405 -1 O LEU A 401 N LEU A 398
SHEET 3 AC 4 VAL A 417 ASN A 421 -1 O GLU A 418 N ALA A 404
SHEET 4 AC 4 GLU A 426 VAL A 430 -1 O GLU A 426 N ASN A 421
SHEET 1 AD 4 GLY A 441 VAL A 445 0
SHEET 2 AD 4 LEU A 448 VAL A 452 -1 O LEU A 448 N VAL A 445
SHEET 3 AD 4 VAL A 466 ASN A 470 -1 O GLU A 467 N ALA A 451
SHEET 4 AD 4 GLU A 475 TYR A 478 -1 O GLU A 475 N ASN A 470
SHEET 1 AE 2 TYR A 455 ASP A 456 0
SHEET 2 AE 2 GLN A 461 CYS A 462 -1 O GLN A 461 N ASP A 456
SHEET 1 AF 4 GLY A 490 LEU A 494 0
SHEET 2 AF 4 LEU A 497 VAL A 501 -1 O LEU A 497 N LEU A 494
SHEET 3 AF 4 VAL A 513 TYR A 516 -1 O GLU A 514 N ALA A 500
SHEET 4 AF 4 TRP A 523 GLN A 525 -1 O ARG A 524 N VAL A 515
SHEET 1 AG 2 HIS A 504 ASP A 505 0
SHEET 2 AG 2 LEU A 508 VAL A 509 -1 O LEU A 508 N ASP A 505
SHEET 1 AH 4 GLY A 537 VAL A 541 0
SHEET 2 AH 4 LEU A 544 VAL A 548 -1 O LEU A 544 N VAL A 541
SHEET 3 AH 4 VAL A 560 ASN A 564 -1 O GLU A 561 N VAL A 547
SHEET 4 AH 4 LYS A 569 VAL A 572 -1 O LYS A 569 N ASN A 564
SHEET 1 BA 4 ARG B 332 VAL B 336 0
SHEET 2 BA 4 VAL B 323 ASP B 327 -1 O VAL B 323 N VAL B 336
SHEET 3 BA 4 LYS B 307 VAL B 312 -1 O MET B 309 N TYR B 326
SHEET 4 BA 4 GLY B 585 ASP B 590 -1 O GLY B 585 N VAL B 312
SHEET 1 BB 4 GLY B 347 MET B 351 0
SHEET 2 BB 4 LEU B 354 VAL B 358 -1 O LEU B 354 N MET B 351
SHEET 3 BB 4 VAL B 370 ASP B 374 -1 O ASP B 371 N ALA B 357
SHEET 4 BB 4 GLN B 379 VAL B 383 -1 O GLN B 379 N ASP B 374
SHEET 1 BC 4 GLY B 394 LEU B 398 0
SHEET 2 BC 4 LEU B 401 VAL B 405 -1 O LEU B 401 N LEU B 398
SHEET 3 BC 4 VAL B 417 ASN B 421 -1 O GLU B 418 N ALA B 404
SHEET 4 BC 4 GLU B 426 VAL B 430 -1 O GLU B 426 N ASN B 421
SHEET 1 BD 4 GLY B 441 VAL B 445 0
SHEET 2 BD 4 LEU B 448 VAL B 452 -1 O LEU B 448 N VAL B 445
SHEET 3 BD 4 VAL B 466 ASN B 470 -1 O GLU B 467 N ALA B 451
SHEET 4 BD 4 GLU B 475 TYR B 478 -1 O GLU B 475 N ASN B 470
SHEET 1 BE 2 TYR B 455 ASP B 456 0
SHEET 2 BE 2 GLN B 461 CYS B 462 -1 O GLN B 461 N ASP B 456
SHEET 1 BF 4 GLY B 490 LEU B 494 0
SHEET 2 BF 4 LEU B 497 VAL B 501 -1 O LEU B 497 N LEU B 494
SHEET 3 BF 4 VAL B 513 TYR B 516 -1 O GLU B 514 N ALA B 500
SHEET 4 BF 4 TRP B 523 GLN B 525 -1 O ARG B 524 N VAL B 515
SHEET 1 BG 2 HIS B 504 ASP B 505 0
SHEET 2 BG 2 LEU B 508 VAL B 509 -1 O LEU B 508 N ASP B 505
SHEET 1 BH 4 GLY B 537 VAL B 541 0
SHEET 2 BH 4 LEU B 544 VAL B 548 -1 O LEU B 544 N VAL B 541
SHEET 3 BH 4 VAL B 560 ASN B 564 -1 O GLU B 561 N VAL B 547
SHEET 4 BH 4 LYS B 569 VAL B 572 -1 O LYS B 569 N ASN B 564
CISPEP 1 ALA A 316 PRO A 317 0 0.29
CISPEP 2 ALA B 316 PRO B 317 0 0.45
SITE 1 AC1 7 ARG A 343 ALA A 357 GLY A 359 VAL A 367
SITE 2 AC1 7 THR A 369 ASP A 371 HOH A2023
SITE 1 AC2 9 ARG A 368 ARG A 389 HOH A2035 HOH A2051
SITE 2 AC2 9 HOH A2159 ARG B 368 ARG B 389 HOH B2024
SITE 3 AC2 9 HOH B2134
SITE 1 AC3 4 ARG A 368 ARG A 389 HOH A2036 HOH A2159
SITE 1 AC4 10 PRO A 340 SER A 341 ARG A 343 ASP A 371
SITE 2 AC4 10 SER A 382 HOH A2038 HOH A2039 ASN B 362
SITE 3 AC4 10 SER B 364 LEU B 365
SITE 1 AC5 10 LEU A 497 ASP A 517 ARG A 524 VAL A 526
SITE 2 AC5 10 TYR A 563 ASN B 495 ASP B 517 ARG B 524
SITE 3 AC5 10 VAL B 526 TYR B 563
SITE 1 AC6 6 SER A 341 ARG A 343 ASN A 362 SER B 341
SITE 2 AC6 6 ARG B 343 ASN B 362
SITE 1 AC7 7 ARG B 343 ALA B 357 GLY B 359 VAL B 367
SITE 2 AC7 7 THR B 369 ASP B 371 HOH B2017
SITE 1 AC8 8 ASN A 362 SER A 364 LEU A 365 HOH A2033
SITE 2 AC8 8 PRO B 340 SER B 341 ARG B 343 ASP B 371
SITE 1 AC9 3 ARG B 368 ARG B 389 HOH B2134
SITE 1 BC1 5 LEU A 365 ARG A 366 ARG A 389 ASP A 409
SITE 2 BC1 5 GLU C 557
SITE 1 BC2 6 LEU B 365 ARG B 366 ARG B 389 ASP B 409
SITE 2 BC2 6 GLY B 410 GLU D 557
CRYST1 117.700 117.700 106.650 90.00 90.00 90.00 P 43 21 2 16
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 0.008496 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008496 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009376 0.00000
MTRIX1 1 -0.119900 -0.992800 0.002067 -58.48000 1
MTRIX2 1 -0.992800 0.119900 -0.000210 -51.81000 1
MTRIX3 1 -0.000040 -0.002077 -1.000000 1.65100 1
(ATOM LINES ARE NOT SHOWN.)
END
