HEADER HYDROLASE 04-OCT-13 4N2B
TITLE CRYSTAL STRUCTURE OF PROTEIN ARGININE DEIMINASE 2 (10 MM CA2+)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN-ARGININE DEIMINASE TYPE-2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PAD-H19, PEPTIDYLARGININE DEIMINASE II, PROTEIN-ARGININE
COMPND 5 DEIMINASE TYPE II;
COMPND 6 EC: 3.5.3.15;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PADI2, KIAA0994, PDI2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DEIMINASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.SLADE,X.ZHANG,P.FANG,C.J.DREYTON,Y.ZHANG,M.L.GROSS,M.GUO,
AUTHOR 2 S.A.COONROD,P.R.THOMPSON
REVDAT 3 20-SEP-23 4N2B 1 REMARK SEQADV LINK
REVDAT 2 06-MAY-15 4N2B 1 JRNL
REVDAT 1 04-FEB-15 4N2B 0
JRNL AUTH D.J.SLADE,P.FANG,C.J.DREYTON,Y.ZHANG,J.FUHRMANN,D.REMPEL,
JRNL AUTH 2 B.D.BAX,S.A.COONROD,H.D.LEWIS,M.GUO,M.L.GROSS,P.R.THOMPSON
JRNL TITL PROTEIN ARGININE DEIMINASE 2 BINDS CALCIUM IN AN ORDERED
JRNL TITL 2 FASHION: IMPLICATIONS FOR INHIBITOR DESIGN.
JRNL REF ACS CHEM.BIOL. V. 10 1043 2015
JRNL REFN ISSN 1554-8929
JRNL PMID 25621824
JRNL DOI 10.1021/CB500933J
REMARK 2
REMARK 2 RESOLUTION. 1.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.2_869
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) : 1.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 3 NUMBER OF REFLECTIONS : 79077
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.530
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 40.4043 - 3.6395 1.00 8510 221 0.1480 0.1776
REMARK 3 2 3.6395 - 2.8890 1.00 8367 217 0.1616 0.1842
REMARK 3 3 2.8890 - 2.5239 1.00 8327 216 0.1697 0.2041
REMARK 3 4 2.5239 - 2.2932 1.00 8280 215 0.1686 0.2129
REMARK 3 5 2.2932 - 2.1288 1.00 8267 215 0.1721 0.2027
REMARK 3 6 2.1288 - 2.0033 1.00 8257 214 0.1717 0.1994
REMARK 3 7 2.0033 - 1.9030 1.00 8259 214 0.1795 0.2173
REMARK 3 8 1.9030 - 1.8202 0.96 7997 207 0.1915 0.2360
REMARK 3 9 1.8202 - 1.7501 0.79 6515 170 0.2022 0.2622
REMARK 3 10 1.7501 - 1.6900 0.52 4298 111 0.2179 0.2321
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.73
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 31.04
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.01
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.18140
REMARK 3 B22 (A**2) : 1.20750
REMARK 3 B33 (A**2) : -0.02610
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.29200
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 5413
REMARK 3 ANGLE : 1.337 7416
REMARK 3 CHIRALITY : 0.114 813
REMARK 3 PLANARITY : 0.009 938
REMARK 3 DIHEDRAL : 14.687 1987
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 17
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 3:96)
REMARK 3 ORIGIN FOR THE GROUP (A): -43.4199 13.8231 -3.4688
REMARK 3 T TENSOR
REMARK 3 T11: 0.1182 T22: 0.0558
REMARK 3 T33: 0.1416 T12: 0.0281
REMARK 3 T13: -0.0196 T23: -0.0460
REMARK 3 L TENSOR
REMARK 3 L11: 2.1196 L22: 1.3895
REMARK 3 L33: 3.2941 L12: -1.1285
REMARK 3 L13: 1.1023 L23: -0.2717
REMARK 3 S TENSOR
REMARK 3 S11: 0.1182 S12: 0.1557 S13: 0.1334
REMARK 3 S21: -0.1333 S22: -0.1010 S23: 0.1270
REMARK 3 S31: -0.2416 S32: 0.0357 S33: -0.0070
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 97:112)
REMARK 3 ORIGIN FOR THE GROUP (A): -55.4298 12.4142 -9.0378
REMARK 3 T TENSOR
REMARK 3 T11: 0.1561 T22: 0.0546
REMARK 3 T33: 0.2646 T12: 0.1511
REMARK 3 T13: -0.1301 T23: -0.0861
REMARK 3 L TENSOR
REMARK 3 L11: 2.6108 L22: 3.3721
REMARK 3 L33: 0.4191 L12: -2.0860
REMARK 3 L13: 0.3693 L23: -0.5695
REMARK 3 S TENSOR
REMARK 3 S11: 0.2400 S12: 0.1950 S13: -0.2242
REMARK 3 S21: -0.2484 S22: -0.0824 S23: 0.1978
REMARK 3 S31: -0.0163 S32: -0.0370 S33: -0.1107
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 113:163)
REMARK 3 ORIGIN FOR THE GROUP (A): -13.1904 4.4075 17.0977
REMARK 3 T TENSOR
REMARK 3 T11: 0.0675 T22: 0.1145
REMARK 3 T33: 0.0637 T12: 0.0076
REMARK 3 T13: 0.0126 T23: 0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 2.9133 L22: 0.2090
REMARK 3 L33: 0.5467 L12: -0.3029
REMARK 3 L13: 0.9428 L23: 0.0746
REMARK 3 S TENSOR
REMARK 3 S11: -0.1090 S12: -0.3617 S13: 0.2992
REMARK 3 S21: 0.0401 S22: -0.0279 S23: -0.0582
REMARK 3 S31: 0.0097 S32: -0.0588 S33: 0.0695
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 164:193)
REMARK 3 ORIGIN FOR THE GROUP (A): -17.8601 -4.6140 23.2212
REMARK 3 T TENSOR
REMARK 3 T11: 0.0538 T22: 0.2340
REMARK 3 T33: 0.0540 T12: -0.0269
REMARK 3 T13: 0.0289 T23: 0.0254
REMARK 3 L TENSOR
REMARK 3 L11: 2.5503 L22: 1.3987
REMARK 3 L33: 1.3658 L12: -1.0895
REMARK 3 L13: 0.5182 L23: -0.3761
REMARK 3 S TENSOR
REMARK 3 S11: -0.0384 S12: -0.4488 S13: -0.2026
REMARK 3 S21: 0.1208 S22: 0.0077 S23: 0.0184
REMARK 3 S31: 0.0436 S32: -0.0261 S33: 0.0071
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 194:242)
REMARK 3 ORIGIN FOR THE GROUP (A): -23.7851 -8.1982 17.5719
REMARK 3 T TENSOR
REMARK 3 T11: 0.0832 T22: 0.1495
REMARK 3 T33: 0.0740 T12: -0.0182
REMARK 3 T13: 0.0087 T23: 0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 0.1629 L22: 0.5901
REMARK 3 L33: 0.7671 L12: 0.1852
REMARK 3 L13: 0.0142 L23: -0.5322
REMARK 3 S TENSOR
REMARK 3 S11: 0.0300 S12: -0.3401 S13: -0.1992
REMARK 3 S21: 0.0592 S22: -0.0159 S23: 0.0667
REMARK 3 S31: 0.0646 S32: -0.0291 S33: 0.0213
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 243:318)
REMARK 3 ORIGIN FOR THE GROUP (A): -8.7921 -3.3655 16.1191
REMARK 3 T TENSOR
REMARK 3 T11: 0.0520 T22: 0.0703
REMARK 3 T33: 0.0512 T12: -0.0012
REMARK 3 T13: 0.0226 T23: 0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 1.5853 L22: 0.3055
REMARK 3 L33: 0.7830 L12: -0.1884
REMARK 3 L13: 0.8775 L23: 0.0002
REMARK 3 S TENSOR
REMARK 3 S11: -0.0068 S12: -0.0868 S13: -0.1474
REMARK 3 S21: 0.0016 S22: 0.0312 S23: 0.0025
REMARK 3 S31: 0.0714 S32: -0.0301 S33: -0.0222
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 319:346)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.3219 -4.0467 39.4876
REMARK 3 T TENSOR
REMARK 3 T11: 0.2615 T22: 0.1876
REMARK 3 T33: 0.0378 T12: 0.1021
REMARK 3 T13: 0.0070 T23: -0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 6.9268 L22: 5.7649
REMARK 3 L33: 2.1502 L12: -0.1420
REMARK 3 L13: 0.5498 L23: -1.2028
REMARK 3 S TENSOR
REMARK 3 S11: -0.0886 S12: -0.4190 S13: 0.1128
REMARK 3 S21: 0.2851 S22: 0.0975 S23: 0.0309
REMARK 3 S31: -0.4003 S32: -0.2093 S33: -0.0070
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 347:369)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5105 -4.8380 24.5481
REMARK 3 T TENSOR
REMARK 3 T11: 0.0599 T22: 0.1279
REMARK 3 T33: 0.0415 T12: -0.0073
REMARK 3 T13: 0.0002 T23: 0.0538
REMARK 3 L TENSOR
REMARK 3 L11: 1.9994 L22: 2.7522
REMARK 3 L33: 2.0675 L12: -0.9060
REMARK 3 L13: -0.0018 L23: -0.0316
REMARK 3 S TENSOR
REMARK 3 S11: -0.0579 S12: -0.3050 S13: -0.1169
REMARK 3 S21: 0.1403 S22: 0.0063 S23: -0.0880
REMARK 3 S31: 0.1545 S32: -0.0677 S33: 0.0344
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN A AND RESID 370:373)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.0900 -15.8064 18.8723
REMARK 3 T TENSOR
REMARK 3 T11: 0.2625 T22: 0.1154
REMARK 3 T33: 0.2620 T12: -0.0340
REMARK 3 T13: -0.0069 T23: 0.0455
REMARK 3 L TENSOR
REMARK 3 L11: 8.7482 L22: 2.2890
REMARK 3 L33: 6.8582 L12: 1.3481
REMARK 3 L13: 2.0573 L23: -3.3253
REMARK 3 S TENSOR
REMARK 3 S11: -0.2987 S12: -0.0137 S13: -0.9496
REMARK 3 S21: 0.3357 S22: -0.0246 S23: 0.1273
REMARK 3 S31: 1.2849 S32: 0.0833 S33: 0.3020
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN A AND RESID 381:382)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3469 -16.4149 28.3341
REMARK 3 T TENSOR
REMARK 3 T11: 0.5423 T22: 0.5952
REMARK 3 T33: 0.6271 T12: 0.1573
REMARK 3 T13: -0.1439 T23: 0.1731
REMARK 3 L TENSOR
REMARK 3 L11: 2.3166 L22: 2.0503
REMARK 3 L33: 2.3602 L12: 2.0946
REMARK 3 L13: 1.8870 L23: 2.0650
REMARK 3 S TENSOR
REMARK 3 S11: -0.3316 S12: -1.5120 S13: -1.5240
REMARK 3 S21: 1.1370 S22: 0.7208 S23: 0.3139
REMARK 3 S31: 0.8786 S32: 0.2477 S33: -0.3840
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN A AND RESID 383:402)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3524 -14.1370 20.2252
REMARK 3 T TENSOR
REMARK 3 T11: 0.1136 T22: 0.1705
REMARK 3 T33: 0.1361 T12: -0.0493
REMARK 3 T13: -0.0283 T23: 0.0969
REMARK 3 L TENSOR
REMARK 3 L11: 5.6472 L22: 3.2776
REMARK 3 L33: 4.0725 L12: -1.5202
REMARK 3 L13: -3.6132 L23: 1.1743
REMARK 3 S TENSOR
REMARK 3 S11: -0.1656 S12: 0.1801 S13: -0.6444
REMARK 3 S21: -0.0792 S22: 0.0287 S23: -0.0679
REMARK 3 S31: 0.4673 S32: -0.3915 S33: 0.2096
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN A AND RESID 403:475)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.5066 -3.6651 11.0717
REMARK 3 T TENSOR
REMARK 3 T11: 0.0748 T22: 0.0251
REMARK 3 T33: 0.0691 T12: 0.0016
REMARK 3 T13: 0.0074 T23: 0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 1.5202 L22: 0.5180
REMARK 3 L33: 0.6927 L12: -0.3452
REMARK 3 L13: -0.2755 L23: 0.5235
REMARK 3 S TENSOR
REMARK 3 S11: 0.0370 S12: 0.0781 S13: 0.0159
REMARK 3 S21: -0.0695 S22: -0.0054 S23: 0.0341
REMARK 3 S31: 0.0043 S32: -0.0481 S33: -0.0214
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN A AND RESID 476:514)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.0737 3.8663 22.7794
REMARK 3 T TENSOR
REMARK 3 T11: 0.0898 T22: 0.0062
REMARK 3 T33: 0.0427 T12: -0.0044
REMARK 3 T13: -0.0003 T23: -0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 4.2921 L22: 1.0161
REMARK 3 L33: 1.4609 L12: -1.1306
REMARK 3 L13: 0.6211 L23: -0.1240
REMARK 3 S TENSOR
REMARK 3 S11: -0.0878 S12: 0.0358 S13: 0.0961
REMARK 3 S21: 0.0648 S22: -0.0020 S23: -0.0110
REMARK 3 S31: -0.2046 S32: 0.1280 S33: 0.0155
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN A AND RESID 515:530)
REMARK 3 ORIGIN FOR THE GROUP (A): 46.1952 -12.4228 30.1228
REMARK 3 T TENSOR
REMARK 3 T11: 0.1223 T22: 0.1126
REMARK 3 T33: 0.1218 T12: 0.0349
REMARK 3 T13: -0.0501 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 6.1533 L22: 7.1135
REMARK 3 L33: 6.0865 L12: 5.9533
REMARK 3 L13: -5.5036 L23: -6.5677
REMARK 3 S TENSOR
REMARK 3 S11: -0.1101 S12: -0.0100 S13: -0.3852
REMARK 3 S21: -0.0659 S22: 0.0512 S23: -0.4639
REMARK 3 S31: 0.3615 S32: 0.1051 S33: 0.0573
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN A AND RESID 531:607)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.2513 -2.3152 17.6501
REMARK 3 T TENSOR
REMARK 3 T11: 0.0595 T22: 0.0214
REMARK 3 T33: 0.0590 T12: 0.0008
REMARK 3 T13: 0.0055 T23: -0.0254
REMARK 3 L TENSOR
REMARK 3 L11: 1.1492 L22: 0.4492
REMARK 3 L33: 1.3478 L12: 0.0709
REMARK 3 L13: 0.2126 L23: -0.1865
REMARK 3 S TENSOR
REMARK 3 S11: -0.0400 S12: 0.0772 S13: -0.0405
REMARK 3 S21: 0.0007 S22: 0.0568 S23: -0.0295
REMARK 3 S31: 0.0294 S32: 0.1564 S33: -0.0114
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN A AND RESID 608:644)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.5385 -0.8673 32.4095
REMARK 3 T TENSOR
REMARK 3 T11: 0.0925 T22: 0.0593
REMARK 3 T33: 0.0248 T12: 0.0062
REMARK 3 T13: -0.0074 T23: -0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 1.4848 L22: 3.7638
REMARK 3 L33: 1.2882 L12: -0.3691
REMARK 3 L13: -0.0852 L23: -0.6457
REMARK 3 S TENSOR
REMARK 3 S11: -0.0097 S12: -0.1682 S13: -0.0639
REMARK 3 S21: -0.0409 S22: 0.0732 S23: 0.0950
REMARK 3 S31: -0.0386 S32: 0.0286 S33: -0.0575
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN A AND RESID 645:668)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9342 3.2855 20.1947
REMARK 3 T TENSOR
REMARK 3 T11: 0.0692 T22: 0.0835
REMARK 3 T33: 0.0877 T12: 0.0317
REMARK 3 T13: 0.0302 T23: -0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 3.4656 L22: 2.5583
REMARK 3 L33: 2.9751 L12: -1.5125
REMARK 3 L13: 2.5670 L23: -2.2338
REMARK 3 S TENSOR
REMARK 3 S11: -0.0024 S12: 0.0596 S13: 0.0739
REMARK 3 S21: -0.0636 S22: -0.0440 S23: -0.0885
REMARK 3 S31: 0.1316 S32: 0.1370 S33: 0.0390
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 4N2B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1000082662.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-03
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9787
REMARK 200 MONOCHROMATOR : DIAMOND(111)
REMARK 200 OPTICS : BERYLLIUM LENSES
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 : 79078
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.690
REMARK 200 RESOLUTION RANGE LOW (A) : 40.393
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.52300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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 4N25
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-20% MPD, 50 MM MES, PH 5.6, 0.12 M
REMARK 280 SODIUM ACETATE, VAPOR DIFFUSION, SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 101.33250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.77450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 101.33250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.77450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -212.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1375 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -20
REMARK 465 GLY A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 SER A -8
REMARK 465 SER A -7
REMARK 465 GLY A -6
REMARK 465 HIS A -5
REMARK 465 ILE A -4
REMARK 465 GLU A -3
REMARK 465 GLY A -2
REMARK 465 ARG A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 LEU A 2
REMARK 465 GLN A 340
REMARK 465 TYR A 341
REMARK 465 LEU A 342
REMARK 465 ASN A 343
REMARK 465 ARG A 344
REMARK 465 GLY A 345
REMARK 465 ASP A 374
REMARK 465 GLY A 375
REMARK 465 ASN A 376
REMARK 465 LEU A 377
REMARK 465 LYS A 378
REMARK 465 ASP A 379
REMARK 465 PHE A 380
REMARK 465 SER A 669
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 ARG A 3 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 43 CE NZ
REMARK 470 TRP A 49 CE3 CZ2 CZ3 CH2
REMARK 470 ASP A 55 CG OD1 OD2
REMARK 470 GLU A 100 CG CD OE1 OE2
REMARK 470 GLU A 101 CG CD OE1 OE2
REMARK 470 LEU A 162 CG CD1 CD2
REMARK 470 LYS A 175 CE NZ
REMARK 470 LYS A 240 CG CD CE NZ
REMARK 470 GLN A 278 CG CD OE1 NE2
REMARK 470 LYS A 315 CG CD CE NZ
REMARK 470 ARG A 373 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 396 CG CD OE1 OE2
REMARK 470 LYS A 485 CG CD CE NZ
REMARK 470 ARG A 525 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 574 CE NZ
REMARK 470 GLU A 644 CG CD OE1 OE2
REMARK 470 ARG A 668 CG CD NE CZ NH1 NH2
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 OD1 ASN A 420 O HOH A 1054 2.05
REMARK 500 O HOH A 1164 O HOH A 1316 2.15
REMARK 500 O HOH A 1205 O HOH A 1312 2.16
REMARK 500 OE2 GLU A 323 O HOH A 1049 2.18
REMARK 500 O ILE A 513 O HOH A 1499 2.18
REMARK 500 O HOH A 1383 O HOH A 1561 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1327 O HOH A 1334 2555 2.10
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 SER A 72 140.43 -176.63
REMARK 500 ARG A 233 19.84 57.23
REMARK 500 ALA A 277 171.29 175.89
REMARK 500 ASP A 279 -3.93 75.10
REMARK 500 PHE A 399 -60.48 -127.40
REMARK 500 GLN A 455 -26.16 71.83
REMARK 500 ALA A 458 67.65 33.82
REMARK 500 ASP A 595 -123.10 43.89
REMARK 500 HIS A 639 -4.68 67.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 89 SER A 90 149.23
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 CA A 704 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 123 OD1
REMARK 620 2 ASP A 125 OD1 87.9
REMARK 620 3 ASP A 127 OD1 83.6 88.8
REMARK 620 4 VAL A 129 O 84.0 171.6 92.5
REMARK 620 5 GLU A 131 OE1 100.9 91.4 175.5 87.9
REMARK 620 6 HOH A 954 O 166.3 91.3 82.7 97.2 92.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 705 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 154 OD1
REMARK 620 2 ASP A 156 OD1 81.9
REMARK 620 3 GLU A 158 OE2 160.9 95.8
REMARK 620 4 ASP A 166 OD2 107.9 86.9 90.8
REMARK 620 5 ASP A 177 OD1 89.6 166.1 95.8 85.3
REMARK 620 6 ASP A 180 OD2 87.9 87.2 73.0 162.2 103.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 709 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 156 OD2
REMARK 620 2 GLU A 158 OE2 82.7
REMARK 620 3 ASP A 180 OD2 88.7 70.5
REMARK 620 4 ASP A 180 OD1 110.9 119.4 52.1
REMARK 620 5 ASP A 389 OD1 84.9 156.4 129.2 83.8
REMARK 620 6 HOH A 850 O 91.6 77.9 148.1 152.4 82.5
REMARK 620 7 HOH A 857 O 171.0 90.6 94.7 77.7 99.3 81.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 706 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 166 O
REMARK 620 2 ASP A 169 OD1 83.6
REMARK 620 3 LYS A 171 O 166.9 83.5
REMARK 620 4 HOH A 826 O 84.4 74.4 89.3
REMARK 620 5 HOH A 844 O 105.4 142.7 86.7 141.4
REMARK 620 6 HOH A 886 O 84.5 144.2 104.4 70.9 73.0
REMARK 620 7 HOH A 900 O 85.0 71.0 93.6 144.7 73.9 141.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 707 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 350 OE1
REMARK 620 2 GLU A 354 OE1 137.1
REMARK 620 3 PHE A 408 O 82.9 103.2
REMARK 620 4 LEU A 411 O 143.7 78.5 81.0
REMARK 620 5 GLU A 412 OE2 74.7 143.8 96.6 75.1
REMARK 620 6 HOH A 819 O 64.9 73.5 83.9 144.0 139.3
REMARK 620 7 HOH A 952 O 93.6 81.6 175.2 100.1 79.2 97.7
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 709
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4N20 RELATED DB: PDB
REMARK 900 RELATED ID: 4N22 RELATED DB: PDB
REMARK 900 RELATED ID: 4N24 RELATED DB: PDB
REMARK 900 RELATED ID: 4N25 RELATED DB: PDB
REMARK 900 RELATED ID: 4N26 RELATED DB: PDB
REMARK 900 RELATED ID: 4N28 RELATED DB: PDB
REMARK 900 RELATED ID: 4N2A RELATED DB: PDB
REMARK 900 RELATED ID: 4N2C RELATED DB: PDB
REMARK 900 RELATED ID: 4N2D RELATED DB: PDB
REMARK 900 RELATED ID: 4N2E RELATED DB: PDB
REMARK 900 RELATED ID: 4N2F RELATED DB: PDB
REMARK 900 RELATED ID: 4N2G RELATED DB: PDB
REMARK 900 RELATED ID: 4N2H RELATED DB: PDB
REMARK 900 RELATED ID: 4N2I RELATED DB: PDB
REMARK 900 RELATED ID: 4N2K RELATED DB: PDB
REMARK 900 RELATED ID: 4N2L RELATED DB: PDB
REMARK 900 RELATED ID: 4N2M RELATED DB: PDB
REMARK 900 RELATED ID: 4N2N RELATED DB: PDB
DBREF 4N2B A 1 665 UNP Q9Y2J8 PADI2_HUMAN 1 665
SEQADV 4N2B MET A -20 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B GLY A -19 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B HIS A -18 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B HIS A -17 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B HIS A -16 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B HIS A -15 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B HIS A -14 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B HIS A -13 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B HIS A -12 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B HIS A -11 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B HIS A -10 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B HIS A -9 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B SER A -8 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B SER A -7 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B GLY A -6 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B HIS A -5 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B ILE A -4 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B GLU A -3 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B GLY A -2 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B ARG A -1 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B HIS A 0 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B SER A 666 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B ARG A 667 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B ARG A 668 UNP Q9Y2J8 EXPRESSION TAG
SEQADV 4N2B SER A 669 UNP Q9Y2J8 EXPRESSION TAG
SEQRES 1 A 690 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 A 690 SER GLY HIS ILE GLU GLY ARG HIS MET LEU ARG GLU ARG
SEQRES 3 A 690 THR VAL ARG LEU GLN TYR GLY SER ARG VAL GLU ALA VAL
SEQRES 4 A 690 TYR VAL LEU GLY THR TYR LEU TRP THR ASP VAL TYR SER
SEQRES 5 A 690 ALA ALA PRO ALA GLY ALA GLN THR PHE SER LEU LYS HIS
SEQRES 6 A 690 SER GLU HIS VAL TRP VAL GLU VAL VAL ARG ASP GLY GLU
SEQRES 7 A 690 ALA GLU GLU VAL ALA THR ASN GLY LYS GLN ARG TRP LEU
SEQRES 8 A 690 LEU SER PRO SER THR THR LEU ARG VAL THR MET SER GLN
SEQRES 9 A 690 ALA SER THR GLU ALA SER SER ASP LYS VAL THR VAL ASN
SEQRES 10 A 690 TYR TYR ASP GLU GLU GLY SER ILE PRO ILE ASP GLN ALA
SEQRES 11 A 690 GLY LEU PHE LEU THR ALA ILE GLU ILE SER LEU ASP VAL
SEQRES 12 A 690 ASP ALA ASP ARG ASP GLY VAL VAL GLU LYS ASN ASN PRO
SEQRES 13 A 690 LYS LYS ALA SER TRP THR TRP GLY PRO GLU GLY GLN GLY
SEQRES 14 A 690 ALA ILE LEU LEU VAL ASN CYS ASP ARG GLU THR PRO TRP
SEQRES 15 A 690 LEU PRO LYS GLU ASP CYS ARG ASP GLU LYS VAL TYR SER
SEQRES 16 A 690 LYS GLU ASP LEU LYS ASP MET SER GLN MET ILE LEU ARG
SEQRES 17 A 690 THR LYS GLY PRO ASP ARG LEU PRO ALA GLY TYR GLU ILE
SEQRES 18 A 690 VAL LEU TYR ILE SER MET SER ASP SER ASP LYS VAL GLY
SEQRES 19 A 690 VAL PHE TYR VAL GLU ASN PRO PHE PHE GLY GLN ARG TYR
SEQRES 20 A 690 ILE HIS ILE LEU GLY ARG ARG LYS LEU TYR HIS VAL VAL
SEQRES 21 A 690 LYS TYR THR GLY GLY SER ALA GLU LEU LEU PHE PHE VAL
SEQRES 22 A 690 GLU GLY LEU CYS PHE PRO ASP GLU GLY PHE SER GLY LEU
SEQRES 23 A 690 VAL SER ILE HIS VAL SER LEU LEU GLU TYR MET ALA GLN
SEQRES 24 A 690 ASP ILE PRO LEU THR PRO ILE PHE THR ASP THR VAL ILE
SEQRES 25 A 690 PHE ARG ILE ALA PRO TRP ILE MET THR PRO ASN ILE LEU
SEQRES 26 A 690 PRO PRO VAL SER VAL PHE VAL CYS CYS MET LYS ASP ASN
SEQRES 27 A 690 TYR LEU PHE LEU LYS GLU VAL LYS ASN LEU VAL GLU LYS
SEQRES 28 A 690 THR ASN CYS GLU LEU LYS VAL CYS PHE GLN TYR LEU ASN
SEQRES 29 A 690 ARG GLY ASP ARG TRP ILE GLN ASP GLU ILE GLU PHE GLY
SEQRES 30 A 690 TYR ILE GLU ALA PRO HIS LYS GLY PHE PRO VAL VAL LEU
SEQRES 31 A 690 ASP SER PRO ARG ASP GLY ASN LEU LYS ASP PHE PRO VAL
SEQRES 32 A 690 LYS GLU LEU LEU GLY PRO ASP PHE GLY TYR VAL THR ARG
SEQRES 33 A 690 GLU PRO LEU PHE GLU SER VAL THR SER LEU ASP SER PHE
SEQRES 34 A 690 GLY ASN LEU GLU VAL SER PRO PRO VAL THR VAL ASN GLY
SEQRES 35 A 690 LYS THR TYR PRO LEU GLY ARG ILE LEU ILE GLY SER SER
SEQRES 36 A 690 PHE PRO LEU SER GLY GLY ARG ARG MET THR LYS VAL VAL
SEQRES 37 A 690 ARG ASP PHE LEU LYS ALA GLN GLN VAL GLN ALA PRO VAL
SEQRES 38 A 690 GLU LEU TYR SER ASP TRP LEU THR VAL GLY HIS VAL ASP
SEQRES 39 A 690 GLU PHE MET SER PHE VAL PRO ILE PRO GLY THR LYS LYS
SEQRES 40 A 690 PHE LEU LEU LEU MET ALA SER THR SER ALA CYS TYR LYS
SEQRES 41 A 690 LEU PHE ARG GLU LYS GLN LYS ASP GLY HIS GLY GLU ALA
SEQRES 42 A 690 ILE MET PHE LYS GLY LEU GLY GLY MET SER SER LYS ARG
SEQRES 43 A 690 ILE THR ILE ASN LYS ILE LEU SER ASN GLU SER LEU VAL
SEQRES 44 A 690 GLN GLU ASN LEU TYR PHE GLN ARG CYS LEU ASP TRP ASN
SEQRES 45 A 690 ARG ASP ILE LEU LYS LYS GLU LEU GLY LEU THR GLU GLN
SEQRES 46 A 690 ASP ILE ILE ASP LEU PRO ALA LEU PHE LYS MET ASP GLU
SEQRES 47 A 690 ASP HIS ARG ALA ARG ALA PHE PHE PRO ASN MET VAL ASN
SEQRES 48 A 690 MET ILE VAL LEU ASP LYS ASP LEU GLY ILE PRO LYS PRO
SEQRES 49 A 690 PHE GLY PRO GLN VAL GLU GLU GLU CYS CYS LEU GLU MET
SEQRES 50 A 690 HIS VAL ARG GLY LEU LEU GLU PRO LEU GLY LEU GLU CYS
SEQRES 51 A 690 THR PHE ILE ASP ASP ILE SER ALA TYR HIS LYS PHE LEU
SEQRES 52 A 690 GLY GLU VAL HIS CYS GLY THR ASN VAL ARG ARG LYS PRO
SEQRES 53 A 690 PHE THR PHE LYS TRP TRP HIS MET VAL PRO SER ARG ARG
SEQRES 54 A 690 SER
HET MPD A 701 8
HET MPD A 702 8
HET MPD A 703 8
HET CA A 704 1
HET CA A 705 1
HET CA A 706 1
HET CA A 707 1
HET MPD A 708 8
HET CA A 709 1
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM CA CALCIUM ION
FORMUL 2 MPD 4(C6 H14 O2)
FORMUL 5 CA 5(CA 2+)
FORMUL 11 HOH *762(H2 O)
HELIX 1 1 GLU A 165 ASP A 169 5 5
HELIX 2 2 SER A 174 MET A 181 5 8
HELIX 3 3 MET A 206 ASP A 210 5 5
HELIX 4 4 ASN A 317 LYS A 330 1 14
HELIX 5 5 ARG A 347 GLU A 352 1 6
HELIX 6 6 PRO A 381 LEU A 386 5 6
HELIX 7 7 THR A 403 GLY A 409 5 7
HELIX 8 8 THR A 444 GLN A 455 1 12
HELIX 9 9 HIS A 471 GLU A 474 5 4
HELIX 10 10 THR A 494 ASP A 507 1 14
HELIX 11 11 LEU A 518 ARG A 525 5 8
HELIX 12 12 THR A 527 SER A 533 1 7
HELIX 13 13 ASN A 534 GLY A 560 1 27
HELIX 14 14 THR A 562 GLN A 564 5 3
HELIX 15 15 CYS A 613 GLU A 623 1 11
HELIX 16 16 PRO A 624 GLY A 626 5 3
HELIX 17 17 ILE A 635 HIS A 639 5 5
HELIX 18 18 LYS A 659 MET A 663 5 5
SHEET 1 A 5 GLU A 4 THR A 6 0
SHEET 2 A 5 TYR A 24 THR A 27 1 O TYR A 24 N ARG A 5
SHEET 3 A 5 THR A 75 MET A 81 -1 O LEU A 77 N THR A 27
SHEET 4 A 5 VAL A 48 ARG A 54 -1 N TRP A 49 O THR A 80
SHEET 5 A 5 GLU A 57 VAL A 61 -1 O GLU A 57 N ARG A 54
SHEET 1 B 5 VAL A 15 VAL A 20 0
SHEET 2 B 5 ASP A 107 VAL A 122 1 O PHE A 112 N VAL A 15
SHEET 3 B 5 ASP A 91 TYR A 98 -1 N VAL A 95 O ALA A 109
SHEET 4 B 5 THR A 39 HIS A 44 -1 N LYS A 43 O THR A 94
SHEET 5 B 5 TRP A 69 LEU A 70 -1 O TRP A 69 N PHE A 40
SHEET 1 C 6 VAL A 15 VAL A 20 0
SHEET 2 C 6 ASP A 107 VAL A 122 1 O PHE A 112 N VAL A 15
SHEET 3 C 6 SER A 182 GLY A 190 -1 O ARG A 187 N SER A 119
SHEET 4 C 6 GLY A 244 GLY A 254 -1 O VAL A 252 N SER A 182
SHEET 5 C 6 VAL A 212 GLU A 218 -1 N GLY A 213 O GLU A 253
SHEET 6 C 6 ARG A 225 LEU A 230 -1 O ILE A 227 N TYR A 216
SHEET 1 D 5 ALA A 149 LEU A 151 0
SHEET 2 D 5 THR A 283 ILE A 294 1 O ARG A 293 N LEU A 151
SHEET 3 D 5 LEU A 265 GLU A 274 -1 N VAL A 266 O PHE A 292
SHEET 4 D 5 TYR A 198 TYR A 203 -1 N GLU A 199 O LEU A 273
SHEET 5 D 5 TYR A 236 VAL A 239 -1 O VAL A 239 N ILE A 200
SHEET 1 E 4 ILE A 298 MET A 299 0
SHEET 2 E 4 ILE A 353 GLU A 359 -1 O TYR A 357 N ILE A 298
SHEET 3 E 4 GLY A 364 ASP A 370 -1 O LEU A 369 N GLU A 354
SHEET 4 E 4 GLY A 391 THR A 394 1 O GLY A 391 N VAL A 368
SHEET 1 F 3 GLU A 334 CYS A 338 0
SHEET 2 F 3 PRO A 306 CYS A 312 1 N VAL A 309 O GLU A 334
SHEET 3 F 3 GLY A 648 ARG A 653 -1 O ARG A 652 N VAL A 307
SHEET 1 G 3 LEU A 411 VAL A 413 0
SHEET 2 G 3 ILE A 429 SER A 433 -1 O LEU A 430 N GLU A 412
SHEET 3 G 3 VAL A 460 TYR A 463 1 O LEU A 462 N ILE A 431
SHEET 1 H 2 VAL A 417 VAL A 419 0
SHEET 2 H 2 LYS A 422 TYR A 424 -1 O LYS A 422 N VAL A 419
SHEET 1 I 3 MET A 476 PRO A 480 0
SHEET 2 I 3 PHE A 487 SER A 493 -1 O LEU A 490 N SER A 477
SHEET 3 I 3 ILE A 566 PRO A 570 1 O LEU A 569 N MET A 491
SHEET 1 J 2 PHE A 573 MET A 575 0
SHEET 2 J 2 ALA A 581 ALA A 583 -1 O ARG A 582 N LYS A 574
SHEET 1 K 3 ILE A 592 LEU A 594 0
SHEET 2 K 3 ASP A 597 PRO A 601 -1 O ASP A 597 N LEU A 594
SHEET 3 K 3 GLU A 628 ILE A 632 1 O THR A 630 N ILE A 600
SHEET 1 L 2 GLN A 607 VAL A 608 0
SHEET 2 L 2 GLU A 611 CYS A 612 -1 O GLU A 611 N VAL A 608
LINK OD1 ASP A 123 CA CA A 704 1555 1555 2.18
LINK OD1 ASP A 125 CA CA A 704 1555 1555 2.23
LINK OD1 ASP A 127 CA CA A 704 1555 1555 2.25
LINK O VAL A 129 CA CA A 704 1555 1555 2.24
LINK OE1 GLU A 131 CA CA A 704 1555 1555 2.29
LINK OD1 ASN A 154 CA CA A 705 1555 1555 2.30
LINK OD1 ASP A 156 CA CA A 705 1555 1555 2.30
LINK OD2 ASP A 156 CA CA A 709 1555 1555 2.33
LINK OE2 GLU A 158 CA CA A 705 1555 1555 2.49
LINK OE2 GLU A 158 CA CA A 709 1555 1555 2.50
LINK OD2 ASP A 166 CA CA A 705 1555 1555 2.22
LINK O ASP A 166 CA CA A 706 1555 1555 2.31
LINK OD1 ASP A 169 CA CA A 706 1555 1555 2.33
LINK O LYS A 171 CA CA A 706 1555 1555 2.29
LINK OD1 ASP A 177 CA CA A 705 1555 1555 2.30
LINK OD2 ASP A 180 CA CA A 705 1555 1555 2.24
LINK OD2 ASP A 180 CA CA A 709 1555 1555 2.38
LINK OD1 ASP A 180 CA CA A 709 1555 1555 2.61
LINK OE1AGLN A 350 CA CA A 707 1555 1555 2.63
LINK OE1 GLU A 354 CA CA A 707 1555 1555 2.34
LINK OD1 ASP A 389 CA CA A 709 1555 1555 2.35
LINK O PHE A 408 CA CA A 707 1555 1555 2.31
LINK O LEU A 411 CA CA A 707 1555 1555 2.41
LINK OE2 GLU A 412 CA CA A 707 1555 1555 2.45
LINK CA CA A 704 O HOH A 954 1555 1555 2.34
LINK CA CA A 706 O HOH A 826 1555 1555 2.45
LINK CA CA A 706 O HOH A 844 1555 1555 2.39
LINK CA CA A 706 O HOH A 886 1555 1555 2.36
LINK CA CA A 706 O HOH A 900 1555 1555 2.48
LINK CA CA A 707 O HOH A 819 1555 1555 2.48
LINK CA CA A 707 O HOH A 952 1555 1555 2.35
LINK CA CA A 709 O HOH A 850 1555 1555 2.43
LINK CA CA A 709 O HOH A 857 1555 1555 2.50
SITE 1 AC1 9 SER A 433 SER A 434 PRO A 436 GLU A 461
SITE 2 AC1 9 LEU A 462 TRP A 550 HOH A 983 HOH A1311
SITE 3 AC1 9 HOH A1493
SITE 1 AC2 3 GLU A 199 LEU A 282 HOH A1290
SITE 1 AC3 7 TYR A 216 GLU A 218 HIS A 237 VAL A 239
SITE 2 AC3 7 LYS A 240 PHE A 250 HOH A1468
SITE 1 AC4 6 ASP A 123 ASP A 125 ASP A 127 VAL A 129
SITE 2 AC4 6 GLU A 131 HOH A 954
SITE 1 AC5 7 ASN A 154 ASP A 156 GLU A 158 ASP A 166
SITE 2 AC5 7 ASP A 177 ASP A 180 CA A 709
SITE 1 AC6 7 ASP A 166 ASP A 169 LYS A 171 HOH A 826
SITE 2 AC6 7 HOH A 844 HOH A 886 HOH A 900
SITE 1 AC7 7 GLN A 350 GLU A 354 PHE A 408 LEU A 411
SITE 2 AC7 7 GLU A 412 HOH A 819 HOH A 952
SITE 1 AC8 2 MET A 575 HOH A 956
SITE 1 AC9 8 ASP A 156 GLU A 158 ASP A 180 LYS A 363
SITE 2 AC9 8 ASP A 389 CA A 705 HOH A 850 HOH A 857
CRYST1 202.665 51.549 76.217 90.00 105.76 90.00 C 1 2 1 4
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 0.004934 0.000000 0.001393 0.00000
SCALE2 0.000000 0.019399 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013633 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
