HEADER LYASE 11-APR-12 4ELX
TITLE STRUCTURE OF APO E.COLI. 1,4-DIHYDROXY-2- NAPHTHOYL COA SYNTHASES WITH
TITLE 2 CL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1,4-DIHYDROXY-2-NAPHTHOYL-COA SYNTHASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: DHNA-COA SYNTHASE;
COMPND 5 EC: 4.1.3.36;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: MENB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DIHYDROXYNAPHTHOIC ACID SYNTHETASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.R.SUN,H.G.SONG,J.LI,M.JIANG,Y.LI,J.H.ZHOU,Z.H.GUO
REVDAT 3 20-MAR-24 4ELX 1 REMARK
REVDAT 2 03-JUL-13 4ELX 1 JRNL
REVDAT 1 06-JUN-12 4ELX 0
JRNL AUTH Y.R.SUN,H.G.SONG,J.LI,M.JIANG,Y.LI,J.H.ZHOU,Z.H.GUO
JRNL TITL ACTIVE SITE BINDING AND CATALYTIC ROLE OF BICARBONATE IN
JRNL TITL 2 1,4-DIHYDROXY-2-NAPHTHOYL COENZYME A SYNTHASES FROM VITAMIN
JRNL TITL 3 K BIOSYNTHETIC PATHWAYS
JRNL REF BIOCHEMISTRY V. 51 4580 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 22606952
JRNL DOI 10.1021/BI300486J
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
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) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 80858
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4051
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 37.3941 - 6.7198 0.99 2870 158 0.1806 0.1964
REMARK 3 2 6.7198 - 5.3386 1.00 2786 130 0.1849 0.2271
REMARK 3 3 5.3386 - 4.6652 1.00 2729 146 0.1361 0.1669
REMARK 3 4 4.6652 - 4.2393 1.00 2701 153 0.1230 0.1716
REMARK 3 5 4.2393 - 3.9358 0.99 2713 121 0.1324 0.1619
REMARK 3 6 3.9358 - 3.7040 1.00 2702 126 0.1457 0.2256
REMARK 3 7 3.7040 - 3.5187 1.00 2664 154 0.1615 0.1790
REMARK 3 8 3.5187 - 3.3656 0.99 2670 147 0.1729 0.2180
REMARK 3 9 3.3656 - 3.2361 1.00 2675 140 0.1714 0.2500
REMARK 3 10 3.2361 - 3.1245 0.99 2645 151 0.1871 0.2785
REMARK 3 11 3.1245 - 3.0268 0.99 2659 133 0.1739 0.2198
REMARK 3 12 3.0268 - 2.9403 0.99 2624 166 0.1923 0.2684
REMARK 3 13 2.9403 - 2.8630 1.00 2659 131 0.1858 0.3068
REMARK 3 14 2.8630 - 2.7931 0.99 2648 142 0.1961 0.2770
REMARK 3 15 2.7931 - 2.7297 0.99 2655 124 0.1791 0.2316
REMARK 3 16 2.7297 - 2.6716 0.99 2635 157 0.1754 0.2609
REMARK 3 17 2.6716 - 2.6182 0.99 2661 120 0.1743 0.2745
REMARK 3 18 2.6182 - 2.5688 1.00 2628 141 0.1756 0.2478
REMARK 3 19 2.5688 - 2.5229 0.99 2655 128 0.1830 0.2985
REMARK 3 20 2.5229 - 2.4801 0.99 2611 150 0.1838 0.2390
REMARK 3 21 2.4801 - 2.4401 1.00 2651 155 0.1772 0.2576
REMARK 3 22 2.4401 - 2.4026 0.99 2632 135 0.1788 0.2711
REMARK 3 23 2.4026 - 2.3673 0.99 2629 144 0.1773 0.2854
REMARK 3 24 2.3673 - 2.3339 0.99 2637 136 0.1802 0.2705
REMARK 3 25 2.3339 - 2.3024 0.99 2633 136 0.1789 0.2574
REMARK 3 26 2.3024 - 2.2725 0.99 2614 151 0.1900 0.3115
REMARK 3 27 2.2725 - 2.2441 1.00 2655 134 0.1836 0.2688
REMARK 3 28 2.2441 - 2.2171 1.00 2652 137 0.1829 0.2706
REMARK 3 29 2.2171 - 2.1913 0.81 2114 105 0.2241 0.3023
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.11
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 39.25
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.510
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.97
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.87760
REMARK 3 B22 (A**2) : -4.27210
REMARK 3 B33 (A**2) : 2.39450
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
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 : 0.007 12202
REMARK 3 ANGLE : 1.032 16483
REMARK 3 CHIRALITY : 0.070 1785
REMARK 3 PLANARITY : 0.004 2186
REMARK 3 DIHEDRAL : 13.927 4452
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 32
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 4:65 )
REMARK 3 ORIGIN FOR THE GROUP (A): 49.7596 165.9559 14.5073
REMARK 3 T TENSOR
REMARK 3 T11: 0.2397 T22: 0.1569
REMARK 3 T33: 0.2428 T12: 0.0055
REMARK 3 T13: 0.0297 T23: 0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 0.1761 L22: 0.1282
REMARK 3 L33: 0.3788 L12: -0.0066
REMARK 3 L13: 0.0775 L23: -0.0045
REMARK 3 S TENSOR
REMARK 3 S11: -0.0446 S12: 0.0735 S13: 0.2860
REMARK 3 S21: -0.1202 S22: 0.0356 S23: -0.0627
REMARK 3 S31: -0.3643 S32: -0.0489 S33: -0.0321
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 122:122 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.322 154.680 12.865
REMARK 3 T TENSOR
REMARK 3 T11: 0.2253 T22: 0.1934
REMARK 3 T33: 0.2249 T12: -0.0002
REMARK 3 T13: 0.0093 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 0.1999 L22: 0.1800
REMARK 3 L33: 0.0303 L12: -0.0036
REMARK 3 L13: 0.0807 L23: -0.0219
REMARK 3 S TENSOR
REMARK 3 S11: 0.0745 S12: -0.1055 S13: 0.0890
REMARK 3 S21: 0.0874 S22: -0.0269 S23: 0.0400
REMARK 3 S31: -0.1008 S32: -0.0971 S33: 0.0001
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 169:258 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.7216 147.3037 15.2544
REMARK 3 T TENSOR
REMARK 3 T11: 0.1079 T22: 0.1654
REMARK 3 T33: 0.1285 T12: 0.0171
REMARK 3 T13: 0.0177 T23: -0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 0.1094 L22: 0.2895
REMARK 3 L33: 0.0303 L12: -0.0034
REMARK 3 L13: 0.0506 L23: 0.0785
REMARK 3 S TENSOR
REMARK 3 S11: 0.0121 S12: -0.0217 S13: -0.0542
REMARK 3 S21: -0.0787 S22: -0.0213 S23: -0.0678
REMARK 3 S31: -0.0330 S32: 0.0307 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN A AND RESID 259:285 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4062 144.2694 -12.8335
REMARK 3 T TENSOR
REMARK 3 T11: 0.5759 T22: 0.2511
REMARK 3 T33: 0.2318 T12: 0.0410
REMARK 3 T13: -0.1514 T23: 0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 0.0515 L22: 0.0116
REMARK 3 L33: 0.0189 L12: 0.0045
REMARK 3 L13: 0.0181 L23: 0.0120
REMARK 3 S TENSOR
REMARK 3 S11: 0.1526 S12: 0.1329 S13: -0.1348
REMARK 3 S21: 0.0002 S22: -0.0778 S23: 0.0644
REMARK 3 S31: -0.0393 S32: 0.0145 S33: -0.0071
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN B AND RESID 5:86 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.7094 117.4894 44.3845
REMARK 3 T TENSOR
REMARK 3 T11: 0.2428 T22: 0.2034
REMARK 3 T33: 0.2139 T12: 0.0191
REMARK 3 T13: 0.0216 T23: 0.0253
REMARK 3 L TENSOR
REMARK 3 L11: 0.0661 L22: 0.1100
REMARK 3 L33: 0.2171 L12: -0.0203
REMARK 3 L13: -0.0007 L23: -0.1609
REMARK 3 S TENSOR
REMARK 3 S11: -0.0698 S12: -0.0529 S13: -0.1016
REMARK 3 S21: 0.1032 S22: 0.0706 S23: 0.0622
REMARK 3 S31: -0.0372 S32: -0.0101 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN B AND RESID 198:198 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.872 132.700 24.309
REMARK 3 T TENSOR
REMARK 3 T11: 0.1536 T22: 0.1753
REMARK 3 T33: 0.1390 T12: 0.0201
REMARK 3 T13: 0.0198 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.0671 L22: 0.1522
REMARK 3 L33: 0.0716 L12: -0.0355
REMARK 3 L13: -0.0613 L23: -0.0695
REMARK 3 S TENSOR
REMARK 3 S11: 0.0007 S12: -0.1117 S13: -0.0084
REMARK 3 S21: 0.0914 S22: -0.0093 S23: 0.0983
REMARK 3 S31: -0.0879 S32: -0.0274 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ( CHAIN B AND RESID 207:259 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.1782 115.0265 28.1615
REMARK 3 T TENSOR
REMARK 3 T11: 0.1676 T22: 0.1820
REMARK 3 T33: 0.2249 T12: 0.0051
REMARK 3 T13: 0.0160 T23: -0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 0.0249 L22: 0.0271
REMARK 3 L33: 0.1895 L12: -0.0180
REMARK 3 L13: -0.0137 L23: -0.0399
REMARK 3 S TENSOR
REMARK 3 S11: -0.0802 S12: -0.0362 S13: -0.1429
REMARK 3 S21: -0.1431 S22: -0.0108 S23: 0.0361
REMARK 3 S31: 0.1019 S32: -0.0518 S33: -0.0002
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ( CHAIN B AND RESID 260:285 )
REMARK 3 ORIGIN FOR THE GROUP (A): 52.5729 101.8892 21.1016
REMARK 3 T TENSOR
REMARK 3 T11: 0.7230 T22: 0.2178
REMARK 3 T33: 0.5365 T12: 0.2877
REMARK 3 T13: 0.0066 T23: 0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 0.1749 L22: 0.1555
REMARK 3 L33: 0.1355 L12: 0.1543
REMARK 3 L13: 0.0076 L23: -0.0280
REMARK 3 S TENSOR
REMARK 3 S11: 0.0514 S12: 0.0097 S13: -0.1400
REMARK 3 S21: 0.1964 S22: -0.0398 S23: -0.1025
REMARK 3 S31: 0.0528 S32: 0.0354 S33: 0.0582
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: ( CHAIN C AND RESID 4:17 )
REMARK 3 ORIGIN FOR THE GROUP (A): 67.5890 109.3102 6.4959
REMARK 3 T TENSOR
REMARK 3 T11: 0.2124 T22: 0.3299
REMARK 3 T33: 0.5966 T12: 0.2061
REMARK 3 T13: 0.0472 T23: -0.1499
REMARK 3 L TENSOR
REMARK 3 L11: 0.0291 L22: 0.0286
REMARK 3 L33: 0.0179 L12: -0.0279
REMARK 3 L13: 0.0200 L23: -0.0098
REMARK 3 S TENSOR
REMARK 3 S11: -0.0266 S12: -0.0478 S13: -0.0531
REMARK 3 S21: 0.0254 S22: 0.0560 S23: -0.0203
REMARK 3 S31: -0.0088 S32: 0.0231 S33: 0.0134
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: ( CHAIN C AND RESID 18:49 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.5178 119.1564 -7.0084
REMARK 3 T TENSOR
REMARK 3 T11: 0.3706 T22: 0.2586
REMARK 3 T33: 0.2673 T12: 0.0578
REMARK 3 T13: 0.1070 T23: -0.0448
REMARK 3 L TENSOR
REMARK 3 L11: 0.0650 L22: 0.0297
REMARK 3 L33: 0.0521 L12: 0.0259
REMARK 3 L13: 0.0101 L23: 0.0359
REMARK 3 S TENSOR
REMARK 3 S11: -0.0443 S12: 0.1755 S13: -0.1213
REMARK 3 S21: -0.1843 S22: 0.0008 S23: -0.1885
REMARK 3 S31: 0.0164 S32: 0.1388 S33: -0.0332
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: ( CHAIN C AND RESID 50:65 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.8597 117.5370 -4.7771
REMARK 3 T TENSOR
REMARK 3 T11: 0.2553 T22: 0.3165
REMARK 3 T33: 0.3088 T12: 0.0439
REMARK 3 T13: -0.0042 T23: -0.1175
REMARK 3 L TENSOR
REMARK 3 L11: 0.0162 L22: 0.0068
REMARK 3 L33: 0.0116 L12: -0.0057
REMARK 3 L13: 0.0033 L23: 0.0069
REMARK 3 S TENSOR
REMARK 3 S11: -0.0277 S12: 0.0024 S13: -0.2690
REMARK 3 S21: -0.0324 S22: 0.0499 S23: 0.0788
REMARK 3 S31: -0.0285 S32: 0.0697 S33: 0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: ( CHAIN C AND RESID 66:86 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.8992 120.1377 -0.1765
REMARK 3 T TENSOR
REMARK 3 T11: 0.2514 T22: 0.1417
REMARK 3 T33: 0.1948 T12: 0.1019
REMARK 3 T13: 0.0943 T23: -0.0516
REMARK 3 L TENSOR
REMARK 3 L11: 0.2407 L22: 0.0874
REMARK 3 L33: 0.1640 L12: -0.0743
REMARK 3 L13: 0.0078 L23: -0.0777
REMARK 3 S TENSOR
REMARK 3 S11: 0.0619 S12: 0.1596 S13: -0.1972
REMARK 3 S21: -0.1260 S22: 0.0256 S23: 0.0332
REMARK 3 S31: -0.0521 S32: -0.0310 S33: 0.0797
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: ( CHAIN C AND RESID 87:117 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.1464 126.6905 -1.8384
REMARK 3 T TENSOR
REMARK 3 T11: 0.3069 T22: 0.2603
REMARK 3 T33: 0.2800 T12: 0.0703
REMARK 3 T13: -0.0197 T23: -0.0378
REMARK 3 L TENSOR
REMARK 3 L11: 0.0824 L22: 0.0457
REMARK 3 L33: 0.0184 L12: 0.0082
REMARK 3 L13: 0.0243 L23: 0.0239
REMARK 3 S TENSOR
REMARK 3 S11: -0.0838 S12: 0.1718 S13: 0.2398
REMARK 3 S21: -0.3088 S22: -0.1103 S23: 0.0613
REMARK 3 S31: -0.1426 S32: -0.0047 S33: -0.0010
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: ( CHAIN C AND RESID 118:159 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.3381 129.7909 3.5921
REMARK 3 T TENSOR
REMARK 3 T11: 0.1856 T22: 0.2073
REMARK 3 T33: 0.2451 T12: 0.0705
REMARK 3 T13: 0.0498 T23: -0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 0.0341 L22: 0.0260
REMARK 3 L33: 0.0906 L12: 0.0067
REMARK 3 L13: -0.0328 L23: 0.0266
REMARK 3 S TENSOR
REMARK 3 S11: 0.0302 S12: 0.0502 S13: 0.0353
REMARK 3 S21: -0.0935 S22: 0.0459 S23: -0.0533
REMARK 3 S31: -0.0412 S32: 0.1423 S33: 0.0064
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: ( CHAIN C AND RESID 160:206 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.6498 137.8607 9.0488
REMARK 3 T TENSOR
REMARK 3 T11: 0.1434 T22: 0.1844
REMARK 3 T33: 0.2143 T12: 0.0427
REMARK 3 T13: 0.0188 T23: -0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 0.0225 L22: 0.0498
REMARK 3 L33: 0.0475 L12: -0.0255
REMARK 3 L13: -0.0375 L23: 0.0096
REMARK 3 S TENSOR
REMARK 3 S11: -0.0727 S12: -0.0398 S13: -0.1841
REMARK 3 S21: -0.0714 S22: 0.0741 S23: -0.0600
REMARK 3 S31: -0.0480 S32: -0.0328 S33: -0.0015
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: ( CHAIN C AND RESID 207:222 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.9150 117.1219 9.0473
REMARK 3 T TENSOR
REMARK 3 T11: 0.1111 T22: 0.2457
REMARK 3 T33: 0.3142 T12: 0.1485
REMARK 3 T13: 0.1309 T23: 0.0520
REMARK 3 L TENSOR
REMARK 3 L11: 0.0066 L22: 0.0104
REMARK 3 L33: 0.0901 L12: 0.0073
REMARK 3 L13: -0.0255 L23: -0.0266
REMARK 3 S TENSOR
REMARK 3 S11: -0.0361 S12: -0.0460 S13: -0.0918
REMARK 3 S21: 0.0085 S22: 0.0136 S23: -0.0632
REMARK 3 S31: 0.0258 S32: 0.1119 S33: -0.0610
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: ( CHAIN C AND RESID 223:241 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.4985 117.6825 16.1548
REMARK 3 T TENSOR
REMARK 3 T11: 0.0911 T22: 0.1323
REMARK 3 T33: 0.1860 T12: 0.0865
REMARK 3 T13: 0.0334 T23: 0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 0.0179 L22: 0.0607
REMARK 3 L33: 0.0841 L12: -0.0116
REMARK 3 L13: 0.0262 L23: 0.0109
REMARK 3 S TENSOR
REMARK 3 S11: -0.0499 S12: -0.0853 S13: -0.0373
REMARK 3 S21: -0.1107 S22: -0.0065 S23: -0.0094
REMARK 3 S31: -0.0235 S32: 0.0247 S33: -0.0171
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: ( CHAIN C AND RESID 242:260 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.0081 113.3845 15.9527
REMARK 3 T TENSOR
REMARK 3 T11: 0.2651 T22: 0.1425
REMARK 3 T33: 0.2776 T12: 0.0339
REMARK 3 T13: -0.0579 T23: -0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 0.0133 L22: 0.0124
REMARK 3 L33: 0.0291 L12: 0.0080
REMARK 3 L13: 0.0043 L23: 0.0174
REMARK 3 S TENSOR
REMARK 3 S11: 0.1116 S12: -0.0295 S13: -0.0841
REMARK 3 S21: -0.0698 S22: 0.1001 S23: 0.0553
REMARK 3 S31: 0.2507 S32: 0.0135 S33: 0.0000
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: ( CHAIN D AND RESID 4:65 )
REMARK 3 ORIGIN FOR THE GROUP (A): 53.4505 125.3526 48.9225
REMARK 3 T TENSOR
REMARK 3 T11: 0.2984 T22: 0.3051
REMARK 3 T33: 0.1971 T12: 0.0279
REMARK 3 T13: -0.0816 T23: 0.0681
REMARK 3 L TENSOR
REMARK 3 L11: 0.1700 L22: 0.1842
REMARK 3 L33: 0.1301 L12: -0.0344
REMARK 3 L13: -0.0496 L23: 0.0990
REMARK 3 S TENSOR
REMARK 3 S11: -0.0158 S12: -0.3423 S13: -0.1326
REMARK 3 S21: 0.4439 S22: -0.0462 S23: -0.1152
REMARK 3 S31: 0.1610 S32: 0.0769 S33: -0.0159
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: ( CHAIN D AND RESID 66:285 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.6604 132.3266 35.3867
REMARK 3 T TENSOR
REMARK 3 T11: 0.1497 T22: 0.1823
REMARK 3 T33: 0.1453 T12: 0.0335
REMARK 3 T13: -0.0292 T23: 0.0193
REMARK 3 L TENSOR
REMARK 3 L11: 0.2193 L22: 0.3725
REMARK 3 L33: 0.5193 L12: 0.0939
REMARK 3 L13: 0.0760 L23: 0.0453
REMARK 3 S TENSOR
REMARK 3 S11: -0.0100 S12: -0.1396 S13: -0.0620
REMARK 3 S21: 0.1329 S22: 0.0021 S23: -0.0680
REMARK 3 S31: 0.0148 S32: 0.0554 S33: 0.0272
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: ( CHAIN E AND RESID 5:49 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.6474 114.8695 -9.0087
REMARK 3 T TENSOR
REMARK 3 T11: 0.3530 T22: 0.3052
REMARK 3 T33: 0.2855 T12: -0.0145
REMARK 3 T13: -0.0575 T23: -0.0770
REMARK 3 L TENSOR
REMARK 3 L11: 0.0801 L22: 0.0509
REMARK 3 L33: 0.0343 L12: 0.0520
REMARK 3 L13: 0.0011 L23: 0.0289
REMARK 3 S TENSOR
REMARK 3 S11: 0.0155 S12: 0.2398 S13: -0.1272
REMARK 3 S21: -0.3734 S22: -0.0453 S23: 0.1675
REMARK 3 S31: 0.1188 S32: -0.1541 S33: -0.0000
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: ( CHAIN E AND RESID 50:65 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.6171 115.1637 -5.7409
REMARK 3 T TENSOR
REMARK 3 T11: 0.2797 T22: 0.2834
REMARK 3 T33: 0.2488 T12: -0.0107
REMARK 3 T13: 0.0120 T23: -0.1008
REMARK 3 L TENSOR
REMARK 3 L11: 0.0090 L22: 0.0053
REMARK 3 L33: 0.0088 L12: -0.0028
REMARK 3 L13: 0.0102 L23: -0.0039
REMARK 3 S TENSOR
REMARK 3 S11: 0.0779 S12: 0.2488 S13: -0.0235
REMARK 3 S21: -0.0192 S22: -0.0633 S23: -0.0618
REMARK 3 S31: 0.0542 S32: 0.0499 S33: -0.0000
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: ( CHAIN E AND RESID 66:86 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.5119 116.7671 -3.5727
REMARK 3 T TENSOR
REMARK 3 T11: 0.3179 T22: 0.2345
REMARK 3 T33: 0.2494 T12: -0.0097
REMARK 3 T13: -0.0513 T23: -0.0875
REMARK 3 L TENSOR
REMARK 3 L11: 0.1245 L22: 0.1236
REMARK 3 L33: 0.0708 L12: -0.0150
REMARK 3 L13: 0.0236 L23: -0.0200
REMARK 3 S TENSOR
REMARK 3 S11: 0.0816 S12: 0.2037 S13: -0.0695
REMARK 3 S21: -0.1175 S22: -0.0897 S23: -0.0438
REMARK 3 S31: 0.1290 S32: 0.0416 S33: 0.0005
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: ( CHAIN E AND RESID 87:140 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.1884 117.2774 4.2583
REMARK 3 T TENSOR
REMARK 3 T11: 0.2492 T22: 0.1872
REMARK 3 T33: 0.2005 T12: 0.0066
REMARK 3 T13: -0.0285 T23: -0.0662
REMARK 3 L TENSOR
REMARK 3 L11: 0.0410 L22: 0.0378
REMARK 3 L33: 0.0578 L12: 0.0261
REMARK 3 L13: -0.0082 L23: 0.0213
REMARK 3 S TENSOR
REMARK 3 S11: -0.0343 S12: -0.0618 S13: -0.0575
REMARK 3 S21: -0.0296 S22: 0.0883 S23: 0.0357
REMARK 3 S31: 0.2212 S32: -0.0581 S33: 0.0012
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: ( CHAIN E AND RESID 141:158 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2843 116.3077 8.8849
REMARK 3 T TENSOR
REMARK 3 T11: 0.1717 T22: 0.2069
REMARK 3 T33: 0.2214 T12: -0.0703
REMARK 3 T13: -0.0387 T23: -0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 0.0743 L22: 0.0066
REMARK 3 L33: 0.0975 L12: -0.0219
REMARK 3 L13: -0.0855 L23: 0.0279
REMARK 3 S TENSOR
REMARK 3 S11: 0.0094 S12: 0.1329 S13: -0.0707
REMARK 3 S21: 0.0398 S22: -0.0853 S23: -0.0553
REMARK 3 S31: 0.0750 S32: -0.1878 S33: -0.0088
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: ( CHAIN E AND RESID 159:206 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4964 119.4551 16.1104
REMARK 3 T TENSOR
REMARK 3 T11: 0.1852 T22: 0.2604
REMARK 3 T33: 0.1987 T12: 0.0205
REMARK 3 T13: -0.0279 T23: -0.0337
REMARK 3 L TENSOR
REMARK 3 L11: 0.0234 L22: 0.0410
REMARK 3 L33: 0.0794 L12: 0.0368
REMARK 3 L13: 0.0325 L23: 0.0223
REMARK 3 S TENSOR
REMARK 3 S11: -0.0027 S12: 0.1261 S13: -0.1359
REMARK 3 S21: 0.0270 S22: -0.0928 S23: -0.0337
REMARK 3 S31: 0.0748 S32: 0.0633 S33: -0.0004
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: ( CHAIN E AND RESID 207:241 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.6728 130.0654 -2.1286
REMARK 3 T TENSOR
REMARK 3 T11: 0.2242 T22: 0.1817
REMARK 3 T33: 0.1781 T12: 0.0097
REMARK 3 T13: -0.0550 T23: -0.0296
REMARK 3 L TENSOR
REMARK 3 L11: 0.1021 L22: 0.0707
REMARK 3 L33: 0.0967 L12: -0.0068
REMARK 3 L13: -0.1159 L23: 0.0150
REMARK 3 S TENSOR
REMARK 3 S11: -0.0038 S12: -0.0774 S13: -0.0421
REMARK 3 S21: -0.1606 S22: -0.0314 S23: 0.0138
REMARK 3 S31: -0.1198 S32: -0.1179 S33: 0.0002
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: ( CHAIN E AND RESID 253:253 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.281 140.542 -1.624
REMARK 3 T TENSOR
REMARK 3 T11: 0.2926 T22: 0.2064
REMARK 3 T33: 0.1804 T12: 0.0561
REMARK 3 T13: -0.0176 T23: -0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 0.0005 L22: 0.0074
REMARK 3 L33: 0.0080 L12: -0.0088
REMARK 3 L13: 0.0011 L23: -0.0041
REMARK 3 S TENSOR
REMARK 3 S11: 0.0819 S12: 0.1410 S13: -0.0792
REMARK 3 S21: -0.1505 S22: -0.0688 S23: 0.0174
REMARK 3 S31: 0.0076 S32: -0.0104 S33: 0.0000
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: ( CHAIN E AND RESID 260:285 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.0640 150.5727 -9.2943
REMARK 3 T TENSOR
REMARK 3 T11: 0.7549 T22: 0.3860
REMARK 3 T33: 0.4454 T12: -0.0621
REMARK 3 T13: 0.2802 T23: 0.0707
REMARK 3 L TENSOR
REMARK 3 L11: 0.0761 L22: 0.2499
REMARK 3 L33: 0.2317 L12: 0.1197
REMARK 3 L13: -0.0183 L23: -0.1491
REMARK 3 S TENSOR
REMARK 3 S11: 0.0301 S12: 0.0958 S13: 0.1039
REMARK 3 S21: -0.1271 S22: 0.1131 S23: -0.0516
REMARK 3 S31: -0.0471 S32: 0.0702 S33: 0.1819
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: ( CHAIN F AND RESID 4:86 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.4694 160.4977 17.0184
REMARK 3 T TENSOR
REMARK 3 T11: 0.2351 T22: -0.1735
REMARK 3 T33: 0.2759 T12: 0.3302
REMARK 3 T13: -0.0896 T23: 0.0700
REMARK 3 L TENSOR
REMARK 3 L11: 0.3669 L22: 0.0501
REMARK 3 L33: 0.2873 L12: 0.0581
REMARK 3 L13: -0.0359 L23: 0.0047
REMARK 3 S TENSOR
REMARK 3 S11: 0.0201 S12: 0.0053 S13: 0.4293
REMARK 3 S21: 0.0436 S22: 0.0417 S23: 0.2914
REMARK 3 S31: -0.3625 S32: -0.0951 S33: 0.0579
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: ( CHAIN F AND RESID 87:168 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7011 148.7334 10.2757
REMARK 3 T TENSOR
REMARK 3 T11: 0.2098 T22: 0.2432
REMARK 3 T33: 0.2438 T12: 0.0604
REMARK 3 T13: -0.0425 T23: -0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0568 L22: 0.0984
REMARK 3 L33: 0.0665 L12: 0.0421
REMARK 3 L13: 0.0505 L23: -0.0043
REMARK 3 S TENSOR
REMARK 3 S11: -0.0645 S12: 0.1318 S13: 0.0597
REMARK 3 S21: -0.1106 S22: 0.0279 S23: -0.0152
REMARK 3 S31: -0.1524 S32: -0.0239 S33: -0.0013
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: ( CHAIN F AND RESID 169:285 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9015 144.9867 25.2941
REMARK 3 T TENSOR
REMARK 3 T11: 0.1737 T22: 0.1835
REMARK 3 T33: 0.1515 T12: 0.0639
REMARK 3 T13: -0.0094 T23: -0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 0.2379 L22: 0.5675
REMARK 3 L33: 0.2356 L12: -0.1239
REMARK 3 L13: -0.2320 L23: -0.0631
REMARK 3 S TENSOR
REMARK 3 S11: 0.0166 S12: -0.0538 S13: -0.0153
REMARK 3 S21: 0.1475 S22: 0.0075 S23: 0.0670
REMARK 3 S31: -0.0401 S32: -0.0435 S33: 0.0429
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 4ELX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-MAY-12.
REMARK 100 THE DEPOSITION ID IS D_1000071783.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81295
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 37.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
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) : NULL
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: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 300MM NACL, 20% PEG 3350, 100MM TRIS,
REMARK 280 PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 38.23500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.96450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 66.93900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 76.96450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.23500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 66.93900
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 36230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -201.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ILE A 2
REMARK 465 TYR A 3
REMARK 465 VAL A 90
REMARK 465 ARG A 91
REMARK 465 GLY A 92
REMARK 465 ASP A 93
REMARK 465 TYR A 94
REMARK 465 GLY A 95
REMARK 465 GLY A 96
REMARK 465 TYR A 97
REMARK 465 LYS A 98
REMARK 465 ASP A 99
REMARK 465 ASP A 100
REMARK 465 SER A 101
REMARK 465 GLY A 102
REMARK 465 VAL A 103
REMARK 465 MET B 1
REMARK 465 ILE B 2
REMARK 465 TYR B 3
REMARK 465 PRO B 4
REMARK 465 ARG B 91
REMARK 465 GLY B 92
REMARK 465 ASP B 93
REMARK 465 TYR B 94
REMARK 465 GLY B 95
REMARK 465 GLY B 96
REMARK 465 TYR B 97
REMARK 465 LYS B 98
REMARK 465 ASP B 99
REMARK 465 ASP B 100
REMARK 465 SER B 101
REMARK 465 GLY B 102
REMARK 465 MET C 1
REMARK 465 ILE C 2
REMARK 465 TYR C 3
REMARK 465 GLN C 88
REMARK 465 LYS C 89
REMARK 465 VAL C 90
REMARK 465 ARG C 91
REMARK 465 GLY C 92
REMARK 465 ASP C 93
REMARK 465 TYR C 94
REMARK 465 GLY C 95
REMARK 465 GLY C 96
REMARK 465 TYR C 97
REMARK 465 LYS C 98
REMARK 465 ASP C 99
REMARK 465 ASP C 100
REMARK 465 SER C 101
REMARK 465 GLY C 102
REMARK 465 GLU C 261
REMARK 465 GLU C 262
REMARK 465 GLY C 263
REMARK 465 GLN C 264
REMARK 465 GLU C 265
REMARK 465 GLY C 266
REMARK 465 ARG C 267
REMARK 465 ASN C 268
REMARK 465 ALA C 269
REMARK 465 PHE C 270
REMARK 465 ASN C 271
REMARK 465 GLN C 272
REMARK 465 LYS C 273
REMARK 465 ARG C 274
REMARK 465 GLN C 275
REMARK 465 PRO C 276
REMARK 465 ASP C 277
REMARK 465 PHE C 278
REMARK 465 SER C 279
REMARK 465 LYS C 280
REMARK 465 PHE C 281
REMARK 465 LYS C 282
REMARK 465 ARG C 283
REMARK 465 ASN C 284
REMARK 465 PRO C 285
REMARK 465 MET D 1
REMARK 465 ILE D 2
REMARK 465 TYR D 3
REMARK 465 LYS D 89
REMARK 465 VAL D 90
REMARK 465 ARG D 91
REMARK 465 GLY D 92
REMARK 465 ASP D 93
REMARK 465 TYR D 94
REMARK 465 GLY D 95
REMARK 465 GLY D 96
REMARK 465 TYR D 97
REMARK 465 LYS D 98
REMARK 465 ASP D 99
REMARK 465 ASP D 100
REMARK 465 SER D 101
REMARK 465 GLY D 102
REMARK 465 VAL D 103
REMARK 465 HIS D 104
REMARK 465 HIS D 105
REMARK 465 MET E 1
REMARK 465 ILE E 2
REMARK 465 TYR E 3
REMARK 465 PRO E 4
REMARK 465 GLN E 88
REMARK 465 LYS E 89
REMARK 465 VAL E 90
REMARK 465 ARG E 91
REMARK 465 GLY E 92
REMARK 465 ASP E 93
REMARK 465 TYR E 94
REMARK 465 GLY E 95
REMARK 465 GLY E 96
REMARK 465 TYR E 97
REMARK 465 LYS E 98
REMARK 465 ASP E 99
REMARK 465 ASP E 100
REMARK 465 SER E 101
REMARK 465 GLY E 102
REMARK 465 MET F 1
REMARK 465 ILE F 2
REMARK 465 TYR F 3
REMARK 465 LYS F 89
REMARK 465 VAL F 90
REMARK 465 ARG F 91
REMARK 465 GLY F 92
REMARK 465 ASP F 93
REMARK 465 TYR F 94
REMARK 465 GLY F 95
REMARK 465 GLY F 96
REMARK 465 TYR F 97
REMARK 465 LYS F 98
REMARK 465 ASP F 99
REMARK 465 ASP F 100
REMARK 465 SER F 101
REMARK 465 GLY F 102
REMARK 465 PHE F 270
REMARK 465 ASN F 271
REMARK 465 GLN F 272
REMARK 465 LYS F 273
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 PRO A 4 CG CD
REMARK 470 ARG A 26 CD NE CZ NH1 NH2
REMARK 470 LYS A 54 CD CE NZ
REMARK 470 ASP A 67 OD1 OD2
REMARK 470 HIS A 105 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 193 CE NZ
REMARK 470 TYR A 258 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 261 CG CD OE1 OE2
REMARK 470 ARG A 267 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 273 CE NZ
REMARK 470 GLN A 275 CD OE1 NE2
REMARK 470 LYS A 282 CE NZ
REMARK 470 GLU B 20 CG CD OE1 OE2
REMARK 470 LYS B 54 CE NZ
REMARK 470 LYS B 80 CE NZ
REMARK 470 LYS B 89 CG CD CE NZ
REMARK 470 VAL B 103 CG1 CG2
REMARK 470 HIS B 105 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 193 CD CE NZ
REMARK 470 GLN B 223 OE1 NE2
REMARK 470 MET B 255 CE
REMARK 470 TYR B 258 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 267 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 273 CG CD CE NZ
REMARK 470 GLN B 275 CG CD OE1 NE2
REMARK 470 LYS B 280 CB CG CD CE NZ
REMARK 470 LYS B 282 CG CD CE NZ
REMARK 470 PRO C 4 CB CG CD
REMARK 470 GLU C 20 CB CG CD OE1 OE2
REMARK 470 ARG C 26 CD NE CZ NH1 NH2
REMARK 470 LYS C 54 CD CE NZ
REMARK 470 LYS C 80 CD CE NZ
REMARK 470 VAL C 103 CG1 CG2
REMARK 470 LYS C 158 CG CD CE NZ
REMARK 470 LYS C 193 CD CE NZ
REMARK 470 MET C 255 CE
REMARK 470 ASP D 5 OD1 OD2
REMARK 470 GLU D 6 CG CD OE1 OE2
REMARK 470 GLU D 14 CG CD OE1 OE2
REMARK 470 GLU D 20 CG CD OE1 OE2
REMARK 470 LYS D 54 CD CE NZ
REMARK 470 ASN D 68 CB CG OD1 ND2
REMARK 470 LYS D 80 CE NZ
REMARK 470 LYS D 193 CE NZ
REMARK 470 GLU D 261 CG CD OE1 OE2
REMARK 470 ARG D 267 NE CZ NH1 NH2
REMARK 470 LYS D 273 CB CG CD CE NZ
REMARK 470 LYS D 280 CG CD CE NZ
REMARK 470 LYS D 282 CG CD CE NZ
REMARK 470 ASP E 5 CB CG OD1 OD2
REMARK 470 GLU E 6 CB CG CD OE1 OE2
REMARK 470 GLU E 14 CG CD OE1 OE2
REMARK 470 GLU E 20 CB CG CD OE1 OE2
REMARK 470 ARG E 26 CZ NH1 NH2
REMARK 470 ARG E 45 CD NE CZ NH1 NH2
REMARK 470 LYS E 54 CD CE NZ
REMARK 470 ASP E 67 OD1 OD2
REMARK 470 LYS E 80 CD CE NZ
REMARK 470 VAL E 103 CG1 CG2
REMARK 470 HIS E 105 CB CG ND1 CD2 CE1 NE2
REMARK 470 ARG E 113 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 158 CG CD CE NZ
REMARK 470 LYS E 193 CD CE NZ
REMARK 470 MET E 255 CE
REMARK 470 ARG E 267 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 273 CE NZ
REMARK 470 GLN E 275 CD OE1 NE2
REMARK 470 LYS E 280 CG CD CE NZ
REMARK 470 LYS E 282 CB CG CD CE NZ
REMARK 470 GLU F 14 CG CD OE1 OE2
REMARK 470 GLU F 20 CG CD OE1 OE2
REMARK 470 ARG F 26 CD NE CZ NH1 NH2
REMARK 470 VAL F 44 CG1 CG2
REMARK 470 ARG F 45 CD NE CZ NH1 NH2
REMARK 470 LYS F 54 CE NZ
REMARK 470 ASP F 67 CG OD1 OD2
REMARK 470 LYS F 80 CD CE NZ
REMARK 470 VAL F 103 N CB CG1 CG2
REMARK 470 HIS F 105 CG ND1 CD2 CE1 NE2
REMARK 470 LYS F 193 CE NZ
REMARK 470 MET F 255 CE
REMARK 470 TYR F 258 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU F 261 CG CD OE1 OE2
REMARK 470 ARG F 267 CG CD NE CZ NH1 NH2
REMARK 470 ALA F 269 O CB
REMARK 470 GLN F 275 CG CD OE1 NE2
REMARK 470 SER F 279 CB OG
REMARK 470 LYS F 280 CB CG CD CE NZ
REMARK 470 LYS F 282 CG CD CE NZ
REMARK 470 ARG F 283 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 O ARG B 283 O HOH B 486 2.08
REMARK 500 O ARG E 283 O HOH E 498 2.13
REMARK 500 NH1 ARG B 113 O HOH B 463 2.14
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 ASN A 40 55.01 -112.02
REMARK 500 CYS A 83 120.77 -174.10
REMARK 500 THR A 155 -12.86 -143.68
REMARK 500 ALA A 168 -68.35 -105.76
REMARK 500 ASN B 40 61.61 -116.32
REMARK 500 CYS B 83 133.92 -174.67
REMARK 500 LYS B 89 35.18 -84.14
REMARK 500 ALA B 168 -66.68 -101.72
REMARK 500 ASN C 40 56.76 -115.69
REMARK 500 CYS C 83 123.34 -173.47
REMARK 500 ALA C 168 -67.25 -100.48
REMARK 500 ASN D 40 56.62 -115.88
REMARK 500 CYS D 83 128.30 -170.24
REMARK 500 ALA D 168 -64.96 -104.35
REMARK 500 ARG D 283 72.83 -101.56
REMARK 500 CYS E 83 127.28 -171.39
REMARK 500 ASP F 5 85.22 -66.30
REMARK 500 ASN F 40 51.65 -113.54
REMARK 500 CYS F 83 125.93 -174.48
REMARK 500 ALA F 168 -68.42 -104.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 304
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ELS RELATED DB: PDB
REMARK 900 RELATED ID: 4ELW RELATED DB: PDB
DBREF 4ELX A 1 285 UNP P0ABU0 MENB_ECOLI 1 285
DBREF 4ELX B 1 285 UNP P0ABU0 MENB_ECOLI 1 285
DBREF 4ELX C 1 285 UNP P0ABU0 MENB_ECOLI 1 285
DBREF 4ELX D 1 285 UNP P0ABU0 MENB_ECOLI 1 285
DBREF 4ELX E 1 285 UNP P0ABU0 MENB_ECOLI 1 285
DBREF 4ELX F 1 285 UNP P0ABU0 MENB_ECOLI 1 285
SEQRES 1 A 285 MET ILE TYR PRO ASP GLU ALA MET LEU TYR ALA PRO VAL
SEQRES 2 A 285 GLU TRP HIS ASP CYS SER GLU GLY PHE GLU ASP ILE ARG
SEQRES 3 A 285 TYR GLU LYS SER THR ASP GLY ILE ALA LYS ILE THR ILE
SEQRES 4 A 285 ASN ARG PRO GLN VAL ARG ASN ALA PHE ARG PRO LEU THR
SEQRES 5 A 285 VAL LYS GLU MET ILE GLN ALA LEU ALA ASP ALA ARG TYR
SEQRES 6 A 285 ASP ASP ASN ILE GLY VAL ILE ILE LEU THR GLY ALA GLY
SEQRES 7 A 285 ASP LYS ALA PHE CYS SER GLY GLY ASP GLN LYS VAL ARG
SEQRES 8 A 285 GLY ASP TYR GLY GLY TYR LYS ASP ASP SER GLY VAL HIS
SEQRES 9 A 285 HIS LEU ASN VAL LEU ASP PHE GLN ARG GLN ILE ARG THR
SEQRES 10 A 285 CYS PRO LYS PRO VAL VAL ALA MET VAL ALA GLY TYR SER
SEQRES 11 A 285 ILE GLY GLY GLY HIS VAL LEU HIS MET MET CYS ASP LEU
SEQRES 12 A 285 THR ILE ALA ALA ASP ASN ALA ILE PHE GLY GLN THR GLY
SEQRES 13 A 285 PRO LYS VAL GLY SER PHE ASP GLY GLY TRP GLY ALA SER
SEQRES 14 A 285 TYR MET ALA ARG ILE VAL GLY GLN LYS LYS ALA ARG GLU
SEQRES 15 A 285 ILE TRP PHE LEU CYS ARG GLN TYR ASP ALA LYS GLN ALA
SEQRES 16 A 285 LEU ASP MET GLY LEU VAL ASN THR VAL VAL PRO LEU ALA
SEQRES 17 A 285 ASP LEU GLU LYS GLU THR VAL ARG TRP CYS ARG GLU MET
SEQRES 18 A 285 LEU GLN ASN SER PRO MET ALA LEU ARG CYS LEU LYS ALA
SEQRES 19 A 285 ALA LEU ASN ALA ASP CYS ASP GLY GLN ALA GLY LEU GLN
SEQRES 20 A 285 GLU LEU ALA GLY ASN ALA THR MET LEU PHE TYR MET THR
SEQRES 21 A 285 GLU GLU GLY GLN GLU GLY ARG ASN ALA PHE ASN GLN LYS
SEQRES 22 A 285 ARG GLN PRO ASP PHE SER LYS PHE LYS ARG ASN PRO
SEQRES 1 B 285 MET ILE TYR PRO ASP GLU ALA MET LEU TYR ALA PRO VAL
SEQRES 2 B 285 GLU TRP HIS ASP CYS SER GLU GLY PHE GLU ASP ILE ARG
SEQRES 3 B 285 TYR GLU LYS SER THR ASP GLY ILE ALA LYS ILE THR ILE
SEQRES 4 B 285 ASN ARG PRO GLN VAL ARG ASN ALA PHE ARG PRO LEU THR
SEQRES 5 B 285 VAL LYS GLU MET ILE GLN ALA LEU ALA ASP ALA ARG TYR
SEQRES 6 B 285 ASP ASP ASN ILE GLY VAL ILE ILE LEU THR GLY ALA GLY
SEQRES 7 B 285 ASP LYS ALA PHE CYS SER GLY GLY ASP GLN LYS VAL ARG
SEQRES 8 B 285 GLY ASP TYR GLY GLY TYR LYS ASP ASP SER GLY VAL HIS
SEQRES 9 B 285 HIS LEU ASN VAL LEU ASP PHE GLN ARG GLN ILE ARG THR
SEQRES 10 B 285 CYS PRO LYS PRO VAL VAL ALA MET VAL ALA GLY TYR SER
SEQRES 11 B 285 ILE GLY GLY GLY HIS VAL LEU HIS MET MET CYS ASP LEU
SEQRES 12 B 285 THR ILE ALA ALA ASP ASN ALA ILE PHE GLY GLN THR GLY
SEQRES 13 B 285 PRO LYS VAL GLY SER PHE ASP GLY GLY TRP GLY ALA SER
SEQRES 14 B 285 TYR MET ALA ARG ILE VAL GLY GLN LYS LYS ALA ARG GLU
SEQRES 15 B 285 ILE TRP PHE LEU CYS ARG GLN TYR ASP ALA LYS GLN ALA
SEQRES 16 B 285 LEU ASP MET GLY LEU VAL ASN THR VAL VAL PRO LEU ALA
SEQRES 17 B 285 ASP LEU GLU LYS GLU THR VAL ARG TRP CYS ARG GLU MET
SEQRES 18 B 285 LEU GLN ASN SER PRO MET ALA LEU ARG CYS LEU LYS ALA
SEQRES 19 B 285 ALA LEU ASN ALA ASP CYS ASP GLY GLN ALA GLY LEU GLN
SEQRES 20 B 285 GLU LEU ALA GLY ASN ALA THR MET LEU PHE TYR MET THR
SEQRES 21 B 285 GLU GLU GLY GLN GLU GLY ARG ASN ALA PHE ASN GLN LYS
SEQRES 22 B 285 ARG GLN PRO ASP PHE SER LYS PHE LYS ARG ASN PRO
SEQRES 1 C 285 MET ILE TYR PRO ASP GLU ALA MET LEU TYR ALA PRO VAL
SEQRES 2 C 285 GLU TRP HIS ASP CYS SER GLU GLY PHE GLU ASP ILE ARG
SEQRES 3 C 285 TYR GLU LYS SER THR ASP GLY ILE ALA LYS ILE THR ILE
SEQRES 4 C 285 ASN ARG PRO GLN VAL ARG ASN ALA PHE ARG PRO LEU THR
SEQRES 5 C 285 VAL LYS GLU MET ILE GLN ALA LEU ALA ASP ALA ARG TYR
SEQRES 6 C 285 ASP ASP ASN ILE GLY VAL ILE ILE LEU THR GLY ALA GLY
SEQRES 7 C 285 ASP LYS ALA PHE CYS SER GLY GLY ASP GLN LYS VAL ARG
SEQRES 8 C 285 GLY ASP TYR GLY GLY TYR LYS ASP ASP SER GLY VAL HIS
SEQRES 9 C 285 HIS LEU ASN VAL LEU ASP PHE GLN ARG GLN ILE ARG THR
SEQRES 10 C 285 CYS PRO LYS PRO VAL VAL ALA MET VAL ALA GLY TYR SER
SEQRES 11 C 285 ILE GLY GLY GLY HIS VAL LEU HIS MET MET CYS ASP LEU
SEQRES 12 C 285 THR ILE ALA ALA ASP ASN ALA ILE PHE GLY GLN THR GLY
SEQRES 13 C 285 PRO LYS VAL GLY SER PHE ASP GLY GLY TRP GLY ALA SER
SEQRES 14 C 285 TYR MET ALA ARG ILE VAL GLY GLN LYS LYS ALA ARG GLU
SEQRES 15 C 285 ILE TRP PHE LEU CYS ARG GLN TYR ASP ALA LYS GLN ALA
SEQRES 16 C 285 LEU ASP MET GLY LEU VAL ASN THR VAL VAL PRO LEU ALA
SEQRES 17 C 285 ASP LEU GLU LYS GLU THR VAL ARG TRP CYS ARG GLU MET
SEQRES 18 C 285 LEU GLN ASN SER PRO MET ALA LEU ARG CYS LEU LYS ALA
SEQRES 19 C 285 ALA LEU ASN ALA ASP CYS ASP GLY GLN ALA GLY LEU GLN
SEQRES 20 C 285 GLU LEU ALA GLY ASN ALA THR MET LEU PHE TYR MET THR
SEQRES 21 C 285 GLU GLU GLY GLN GLU GLY ARG ASN ALA PHE ASN GLN LYS
SEQRES 22 C 285 ARG GLN PRO ASP PHE SER LYS PHE LYS ARG ASN PRO
SEQRES 1 D 285 MET ILE TYR PRO ASP GLU ALA MET LEU TYR ALA PRO VAL
SEQRES 2 D 285 GLU TRP HIS ASP CYS SER GLU GLY PHE GLU ASP ILE ARG
SEQRES 3 D 285 TYR GLU LYS SER THR ASP GLY ILE ALA LYS ILE THR ILE
SEQRES 4 D 285 ASN ARG PRO GLN VAL ARG ASN ALA PHE ARG PRO LEU THR
SEQRES 5 D 285 VAL LYS GLU MET ILE GLN ALA LEU ALA ASP ALA ARG TYR
SEQRES 6 D 285 ASP ASP ASN ILE GLY VAL ILE ILE LEU THR GLY ALA GLY
SEQRES 7 D 285 ASP LYS ALA PHE CYS SER GLY GLY ASP GLN LYS VAL ARG
SEQRES 8 D 285 GLY ASP TYR GLY GLY TYR LYS ASP ASP SER GLY VAL HIS
SEQRES 9 D 285 HIS LEU ASN VAL LEU ASP PHE GLN ARG GLN ILE ARG THR
SEQRES 10 D 285 CYS PRO LYS PRO VAL VAL ALA MET VAL ALA GLY TYR SER
SEQRES 11 D 285 ILE GLY GLY GLY HIS VAL LEU HIS MET MET CYS ASP LEU
SEQRES 12 D 285 THR ILE ALA ALA ASP ASN ALA ILE PHE GLY GLN THR GLY
SEQRES 13 D 285 PRO LYS VAL GLY SER PHE ASP GLY GLY TRP GLY ALA SER
SEQRES 14 D 285 TYR MET ALA ARG ILE VAL GLY GLN LYS LYS ALA ARG GLU
SEQRES 15 D 285 ILE TRP PHE LEU CYS ARG GLN TYR ASP ALA LYS GLN ALA
SEQRES 16 D 285 LEU ASP MET GLY LEU VAL ASN THR VAL VAL PRO LEU ALA
SEQRES 17 D 285 ASP LEU GLU LYS GLU THR VAL ARG TRP CYS ARG GLU MET
SEQRES 18 D 285 LEU GLN ASN SER PRO MET ALA LEU ARG CYS LEU LYS ALA
SEQRES 19 D 285 ALA LEU ASN ALA ASP CYS ASP GLY GLN ALA GLY LEU GLN
SEQRES 20 D 285 GLU LEU ALA GLY ASN ALA THR MET LEU PHE TYR MET THR
SEQRES 21 D 285 GLU GLU GLY GLN GLU GLY ARG ASN ALA PHE ASN GLN LYS
SEQRES 22 D 285 ARG GLN PRO ASP PHE SER LYS PHE LYS ARG ASN PRO
SEQRES 1 E 285 MET ILE TYR PRO ASP GLU ALA MET LEU TYR ALA PRO VAL
SEQRES 2 E 285 GLU TRP HIS ASP CYS SER GLU GLY PHE GLU ASP ILE ARG
SEQRES 3 E 285 TYR GLU LYS SER THR ASP GLY ILE ALA LYS ILE THR ILE
SEQRES 4 E 285 ASN ARG PRO GLN VAL ARG ASN ALA PHE ARG PRO LEU THR
SEQRES 5 E 285 VAL LYS GLU MET ILE GLN ALA LEU ALA ASP ALA ARG TYR
SEQRES 6 E 285 ASP ASP ASN ILE GLY VAL ILE ILE LEU THR GLY ALA GLY
SEQRES 7 E 285 ASP LYS ALA PHE CYS SER GLY GLY ASP GLN LYS VAL ARG
SEQRES 8 E 285 GLY ASP TYR GLY GLY TYR LYS ASP ASP SER GLY VAL HIS
SEQRES 9 E 285 HIS LEU ASN VAL LEU ASP PHE GLN ARG GLN ILE ARG THR
SEQRES 10 E 285 CYS PRO LYS PRO VAL VAL ALA MET VAL ALA GLY TYR SER
SEQRES 11 E 285 ILE GLY GLY GLY HIS VAL LEU HIS MET MET CYS ASP LEU
SEQRES 12 E 285 THR ILE ALA ALA ASP ASN ALA ILE PHE GLY GLN THR GLY
SEQRES 13 E 285 PRO LYS VAL GLY SER PHE ASP GLY GLY TRP GLY ALA SER
SEQRES 14 E 285 TYR MET ALA ARG ILE VAL GLY GLN LYS LYS ALA ARG GLU
SEQRES 15 E 285 ILE TRP PHE LEU CYS ARG GLN TYR ASP ALA LYS GLN ALA
SEQRES 16 E 285 LEU ASP MET GLY LEU VAL ASN THR VAL VAL PRO LEU ALA
SEQRES 17 E 285 ASP LEU GLU LYS GLU THR VAL ARG TRP CYS ARG GLU MET
SEQRES 18 E 285 LEU GLN ASN SER PRO MET ALA LEU ARG CYS LEU LYS ALA
SEQRES 19 E 285 ALA LEU ASN ALA ASP CYS ASP GLY GLN ALA GLY LEU GLN
SEQRES 20 E 285 GLU LEU ALA GLY ASN ALA THR MET LEU PHE TYR MET THR
SEQRES 21 E 285 GLU GLU GLY GLN GLU GLY ARG ASN ALA PHE ASN GLN LYS
SEQRES 22 E 285 ARG GLN PRO ASP PHE SER LYS PHE LYS ARG ASN PRO
SEQRES 1 F 285 MET ILE TYR PRO ASP GLU ALA MET LEU TYR ALA PRO VAL
SEQRES 2 F 285 GLU TRP HIS ASP CYS SER GLU GLY PHE GLU ASP ILE ARG
SEQRES 3 F 285 TYR GLU LYS SER THR ASP GLY ILE ALA LYS ILE THR ILE
SEQRES 4 F 285 ASN ARG PRO GLN VAL ARG ASN ALA PHE ARG PRO LEU THR
SEQRES 5 F 285 VAL LYS GLU MET ILE GLN ALA LEU ALA ASP ALA ARG TYR
SEQRES 6 F 285 ASP ASP ASN ILE GLY VAL ILE ILE LEU THR GLY ALA GLY
SEQRES 7 F 285 ASP LYS ALA PHE CYS SER GLY GLY ASP GLN LYS VAL ARG
SEQRES 8 F 285 GLY ASP TYR GLY GLY TYR LYS ASP ASP SER GLY VAL HIS
SEQRES 9 F 285 HIS LEU ASN VAL LEU ASP PHE GLN ARG GLN ILE ARG THR
SEQRES 10 F 285 CYS PRO LYS PRO VAL VAL ALA MET VAL ALA GLY TYR SER
SEQRES 11 F 285 ILE GLY GLY GLY HIS VAL LEU HIS MET MET CYS ASP LEU
SEQRES 12 F 285 THR ILE ALA ALA ASP ASN ALA ILE PHE GLY GLN THR GLY
SEQRES 13 F 285 PRO LYS VAL GLY SER PHE ASP GLY GLY TRP GLY ALA SER
SEQRES 14 F 285 TYR MET ALA ARG ILE VAL GLY GLN LYS LYS ALA ARG GLU
SEQRES 15 F 285 ILE TRP PHE LEU CYS ARG GLN TYR ASP ALA LYS GLN ALA
SEQRES 16 F 285 LEU ASP MET GLY LEU VAL ASN THR VAL VAL PRO LEU ALA
SEQRES 17 F 285 ASP LEU GLU LYS GLU THR VAL ARG TRP CYS ARG GLU MET
SEQRES 18 F 285 LEU GLN ASN SER PRO MET ALA LEU ARG CYS LEU LYS ALA
SEQRES 19 F 285 ALA LEU ASN ALA ASP CYS ASP GLY GLN ALA GLY LEU GLN
SEQRES 20 F 285 GLU LEU ALA GLY ASN ALA THR MET LEU PHE TYR MET THR
SEQRES 21 F 285 GLU GLU GLY GLN GLU GLY ARG ASN ALA PHE ASN GLN LYS
SEQRES 22 F 285 ARG GLN PRO ASP PHE SER LYS PHE LYS ARG ASN PRO
HET GOL A 301 6
HET CL A 302 1
HET GOL B 301 6
HET CL B 302 1
HET PEG B 303 7
HET EDO B 304 4
HET GOL C 301 6
HET CL C 302 1
HET PEG C 303 7
HET PO4 C 304 5
HET GOL D 301 6
HET CL D 302 1
HET PEG D 303 7
HET GOL E 301 6
HET EDO E 302 4
HET GOL F 301 6
HET CL F 302 1
HET CL F 303 1
HET GOL F 304 6
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PO4 PHOSPHATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 7 GOL 7(C3 H8 O3)
FORMUL 8 CL 6(CL 1-)
FORMUL 11 PEG 3(C4 H10 O3)
FORMUL 12 EDO 2(C2 H6 O2)
FORMUL 16 PO4 O4 P 3-
FORMUL 26 HOH *638(H2 O)
HELIX 1 1 ASP A 5 TYR A 10 1 6
HELIX 2 2 ARG A 41 ARG A 45 5 5
HELIX 3 3 ARG A 49 ASP A 66 1 18
HELIX 4 4 ASN A 107 CYS A 118 1 12
HELIX 5 5 GLY A 132 CYS A 141 1 10
HELIX 6 6 THR A 155 GLY A 160 5 6
HELIX 7 7 ALA A 168 GLY A 176 1 9
HELIX 8 8 GLY A 176 CYS A 187 1 12
HELIX 9 9 ALA A 192 MET A 198 1 7
HELIX 10 10 PRO A 206 ALA A 208 5 3
HELIX 11 11 ASP A 209 GLN A 223 1 15
HELIX 12 12 SER A 225 ASP A 239 1 15
HELIX 13 13 ASP A 241 TYR A 258 1 18
HELIX 14 14 MET A 259 THR A 260 5 2
HELIX 15 15 GLU A 261 GLY A 263 5 3
HELIX 16 16 GLN A 264 GLN A 272 1 9
HELIX 17 17 GLU B 6 TYR B 10 1 5
HELIX 18 18 ARG B 41 ARG B 45 5 5
HELIX 19 19 ARG B 49 ASP B 66 1 18
HELIX 20 20 ASN B 107 CYS B 118 1 12
HELIX 21 21 GLY B 132 CYS B 141 1 10
HELIX 22 22 THR B 155 GLY B 160 5 6
HELIX 23 23 ALA B 168 GLY B 176 1 9
HELIX 24 24 GLY B 176 CYS B 187 1 12
HELIX 25 25 ALA B 192 MET B 198 1 7
HELIX 26 26 PRO B 206 ALA B 208 5 3
HELIX 27 27 ASP B 209 GLN B 223 1 15
HELIX 28 28 SER B 225 ASP B 239 1 15
HELIX 29 29 ASP B 241 MET B 259 1 19
HELIX 30 30 GLN B 264 GLN B 272 1 9
HELIX 31 31 ASP C 5 TYR C 10 1 6
HELIX 32 32 ARG C 41 ARG C 45 5 5
HELIX 33 33 ARG C 49 ASP C 66 1 18
HELIX 34 34 ASN C 107 CYS C 118 1 12
HELIX 35 35 GLY C 132 CYS C 141 1 10
HELIX 36 36 THR C 155 GLY C 160 5 6
HELIX 37 37 GLY C 165 GLY C 176 1 12
HELIX 38 38 GLY C 176 CYS C 187 1 12
HELIX 39 39 ALA C 192 MET C 198 1 7
HELIX 40 40 PRO C 206 ALA C 208 5 3
HELIX 41 41 ASP C 209 GLN C 223 1 15
HELIX 42 42 SER C 225 ASP C 239 1 15
HELIX 43 43 ASP C 241 MET C 259 1 19
HELIX 44 44 ASP D 5 TYR D 10 1 6
HELIX 45 45 ARG D 41 ARG D 45 5 5
HELIX 46 46 ARG D 49 ASP D 66 1 18
HELIX 47 47 ASN D 107 CYS D 118 1 12
HELIX 48 48 GLY D 132 CYS D 141 1 10
HELIX 49 49 THR D 155 GLY D 160 5 6
HELIX 50 50 GLY D 165 GLY D 176 1 12
HELIX 51 51 GLY D 176 CYS D 187 1 12
HELIX 52 52 ASP D 191 MET D 198 1 8
HELIX 53 53 PRO D 206 ALA D 208 5 3
HELIX 54 54 ASP D 209 GLN D 223 1 15
HELIX 55 55 SER D 225 ALA D 238 1 14
HELIX 56 56 ASP D 241 MET D 259 1 19
HELIX 57 57 THR D 260 GLN D 272 1 13
HELIX 58 58 ASP D 277 PHE D 281 5 5
HELIX 59 59 GLU E 6 TYR E 10 1 5
HELIX 60 60 ARG E 41 ARG E 45 5 5
HELIX 61 61 ARG E 49 ASP E 66 1 18
HELIX 62 62 ASN E 107 CYS E 118 1 12
HELIX 63 63 GLY E 132 CYS E 141 1 10
HELIX 64 64 VAL E 159 TRP E 166 5 8
HELIX 65 65 GLY E 167 GLY E 176 1 10
HELIX 66 66 GLY E 176 CYS E 187 1 12
HELIX 67 67 ALA E 192 GLY E 199 1 8
HELIX 68 68 PRO E 206 ALA E 208 5 3
HELIX 69 69 ASP E 209 GLN E 223 1 15
HELIX 70 70 SER E 225 ALA E 238 1 14
HELIX 71 71 ASP E 241 TYR E 258 1 18
HELIX 72 72 THR E 260 GLN E 272 1 13
HELIX 73 73 ASP F 5 TYR F 10 1 6
HELIX 74 74 ARG F 41 ARG F 45 5 5
HELIX 75 75 ARG F 49 ASP F 66 1 18
HELIX 76 76 ASN F 107 CYS F 118 1 12
HELIX 77 77 GLY F 132 CYS F 141 1 10
HELIX 78 78 THR F 155 GLY F 160 5 6
HELIX 79 79 ALA F 168 GLY F 176 1 9
HELIX 80 80 GLY F 176 CYS F 187 1 12
HELIX 81 81 ALA F 192 MET F 198 1 7
HELIX 82 82 PRO F 206 ALA F 208 5 3
HELIX 83 83 ASP F 209 GLN F 223 1 15
HELIX 84 84 SER F 225 ALA F 238 1 14
HELIX 85 85 ASP F 241 MET F 259 1 19
HELIX 86 86 THR F 260 ALA F 269 1 10
SHEET 1 A 7 HIS A 16 ASP A 17 0
SHEET 2 A 7 ILE A 25 LYS A 29 -1 O LYS A 29 N HIS A 16
SHEET 3 A 7 ILE A 34 ILE A 39 -1 O LYS A 36 N GLU A 28
SHEET 4 A 7 VAL A 71 GLY A 76 1 O ILE A 73 N ALA A 35
SHEET 5 A 7 VAL A 122 VAL A 126 1 O VAL A 123 N ILE A 72
SHEET 6 A 7 LEU A 143 ALA A 147 1 O ILE A 145 N ALA A 124
SHEET 7 A 7 THR A 203 VAL A 205 1 O VAL A 205 N ALA A 146
SHEET 1 B 4 ALA A 81 CYS A 83 0
SHEET 2 B 4 TYR A 129 ILE A 131 1 O TYR A 129 N PHE A 82
SHEET 3 B 4 ILE A 151 GLY A 153 1 O ILE A 151 N SER A 130
SHEET 4 B 4 TYR A 190 ASP A 191 -1 O TYR A 190 N PHE A 152
SHEET 1 C 7 TRP B 15 ASP B 17 0
SHEET 2 C 7 ILE B 25 SER B 30 -1 O LYS B 29 N HIS B 16
SHEET 3 C 7 ILE B 34 ILE B 39 -1 O LYS B 36 N GLU B 28
SHEET 4 C 7 VAL B 71 GLY B 76 1 O ILE B 73 N ALA B 35
SHEET 5 C 7 VAL B 122 VAL B 126 1 O VAL B 123 N ILE B 72
SHEET 6 C 7 LEU B 143 ALA B 147 1 O LEU B 143 N ALA B 124
SHEET 7 C 7 THR B 203 VAL B 205 1 O VAL B 205 N ALA B 146
SHEET 1 D 4 ALA B 81 CYS B 83 0
SHEET 2 D 4 TYR B 129 ILE B 131 1 O ILE B 131 N CYS B 83
SHEET 3 D 4 ILE B 151 GLY B 153 1 O ILE B 151 N SER B 130
SHEET 4 D 4 TYR B 190 ASP B 191 -1 O TYR B 190 N PHE B 152
SHEET 1 E 7 TRP C 15 ASP C 17 0
SHEET 2 E 7 ILE C 25 SER C 30 -1 O LYS C 29 N HIS C 16
SHEET 3 E 7 ILE C 34 ILE C 39 -1 O LYS C 36 N GLU C 28
SHEET 4 E 7 VAL C 71 GLY C 76 1 O ILE C 73 N ILE C 37
SHEET 5 E 7 VAL C 122 VAL C 126 1 O VAL C 123 N ILE C 72
SHEET 6 E 7 LEU C 143 ALA C 147 1 O LEU C 143 N ALA C 124
SHEET 7 E 7 THR C 203 VAL C 205 1 O THR C 203 N ALA C 146
SHEET 1 F 4 ALA C 81 CYS C 83 0
SHEET 2 F 4 TYR C 129 ILE C 131 1 O TYR C 129 N CYS C 83
SHEET 3 F 4 ILE C 151 GLY C 153 1 O ILE C 151 N SER C 130
SHEET 4 F 4 TYR C 190 ASP C 191 -1 O TYR C 190 N PHE C 152
SHEET 1 G 7 TRP D 15 ASP D 17 0
SHEET 2 G 7 ILE D 25 SER D 30 -1 O LYS D 29 N HIS D 16
SHEET 3 G 7 ILE D 34 ILE D 39 -1 O LYS D 36 N GLU D 28
SHEET 4 G 7 VAL D 71 GLY D 76 1 O ILE D 73 N ALA D 35
SHEET 5 G 7 VAL D 122 VAL D 126 1 O VAL D 123 N ILE D 72
SHEET 6 G 7 LEU D 143 ALA D 147 1 O LEU D 143 N ALA D 124
SHEET 7 G 7 THR D 203 VAL D 205 1 O VAL D 205 N ALA D 146
SHEET 1 H 3 ALA D 81 CYS D 83 0
SHEET 2 H 3 TYR D 129 ILE D 131 1 O TYR D 129 N PHE D 82
SHEET 3 H 3 ILE D 151 GLY D 153 1 O ILE D 151 N SER D 130
SHEET 1 I 7 TRP E 15 ASP E 17 0
SHEET 2 I 7 ILE E 25 SER E 30 -1 O LYS E 29 N HIS E 16
SHEET 3 I 7 ILE E 34 ILE E 39 -1 O LYS E 36 N GLU E 28
SHEET 4 I 7 VAL E 71 GLY E 76 1 O ILE E 73 N ALA E 35
SHEET 5 I 7 VAL E 122 VAL E 126 1 O VAL E 123 N ILE E 72
SHEET 6 I 7 LEU E 143 ALA E 147 1 O ILE E 145 N ALA E 124
SHEET 7 I 7 THR E 203 VAL E 205 1 O VAL E 205 N ALA E 146
SHEET 1 J 4 ALA E 81 CYS E 83 0
SHEET 2 J 4 TYR E 129 ILE E 131 1 O TYR E 129 N PHE E 82
SHEET 3 J 4 ILE E 151 GLY E 153 1 O ILE E 151 N SER E 130
SHEET 4 J 4 TYR E 190 ASP E 191 -1 O TYR E 190 N PHE E 152
SHEET 1 K 7 HIS F 16 ASP F 17 0
SHEET 2 K 7 ILE F 25 LYS F 29 -1 O LYS F 29 N HIS F 16
SHEET 3 K 7 ILE F 34 ILE F 39 -1 O THR F 38 N ARG F 26
SHEET 4 K 7 VAL F 71 GLY F 76 1 O ILE F 73 N ALA F 35
SHEET 5 K 7 VAL F 122 VAL F 126 1 O VAL F 123 N ILE F 72
SHEET 6 K 7 LEU F 143 ALA F 147 1 O ALA F 147 N VAL F 126
SHEET 7 K 7 THR F 203 VAL F 205 1 O VAL F 205 N ALA F 146
SHEET 1 L 4 ALA F 81 CYS F 83 0
SHEET 2 L 4 TYR F 129 ILE F 131 1 O TYR F 129 N CYS F 83
SHEET 3 L 4 ILE F 151 GLY F 153 1 O ILE F 151 N SER F 130
SHEET 4 L 4 TYR F 190 ASP F 191 -1 O TYR F 190 N PHE F 152
SITE 1 AC1 6 THR A 203 VAL A 205 GLU A 213 ARG A 216
SITE 2 AC1 6 TRP A 217 ARG C 188
SITE 1 AC2 6 GLY A 132 GLN A 154 THR A 155 GLY A 156
SITE 2 AC2 6 TRP A 184 HOH A 536
SITE 1 AC3 4 GLU B 213 ARG B 216 TRP B 217 ARG E 188
SITE 1 AC4 5 GLY B 132 GLN B 154 THR B 155 GLY B 156
SITE 2 AC4 5 TRP B 184
SITE 1 AC5 10 ARG B 173 ILE B 174 VAL B 175 GLY B 176
SITE 2 AC5 10 HOH B 419 HOH B 502 GLY E 176 ILE F 174
SITE 3 AC5 10 VAL F 175 GLY F 176
SITE 1 AC6 6 THR C 203 VAL C 205 GLU C 213 ARG C 216
SITE 2 AC6 6 TRP C 217 ARG D 188
SITE 1 AC7 7 GLY C 132 GLN C 154 THR C 155 GLY C 156
SITE 2 AC7 7 TRP C 184 HOH C 477 HOH C 482
SITE 1 AC8 9 ARG A 173 ILE A 174 VAL A 175 GLY A 176
SITE 2 AC8 9 ALA C 172 ARG C 173 HOH C 407 ALA D 172
SITE 3 AC8 9 VAL D 175
SITE 1 AC9 7 THR C 75 GLY C 76 GLY C 78 ASP C 79
SITE 2 AC9 7 MET C 125 GLU C 211 HOH C 483
SITE 1 BC1 6 ARG A 188 THR D 203 VAL D 205 GLU D 213
SITE 2 BC1 6 ARG D 216 TRP D 217
SITE 1 BC2 7 GLY D 132 GLN D 154 THR D 155 GLY D 156
SITE 2 BC2 7 TRP D 184 HOH D 484 HOH D 485
SITE 1 BC3 9 GLN B 243 ALA C 238 ASP C 239 HOH C 467
SITE 2 BC3 9 ARG D 173 ASP D 239 CYS D 240 HOH D 404
SITE 3 BC3 9 HOH D 417
SITE 1 BC4 8 TYR E 10 THR E 203 VAL E 205 GLU E 213
SITE 2 BC4 8 ARG E 216 TRP E 217 HOH E 487 ARG F 188
SITE 1 BC5 7 HOH B 519 GLN C 247 GLY E 165 TRP E 166
SITE 2 BC5 7 GLY E 167 ALA E 168 SER E 169
SITE 1 BC6 5 ARG B 188 THR F 203 VAL F 205 GLU F 213
SITE 2 BC6 5 TRP F 217
SITE 1 BC7 5 GLY F 132 GLN F 154 THR F 155 GLY F 156
SITE 2 BC7 5 TRP F 184
SITE 1 BC8 4 HOH B 529 ARG F 173 ASP F 239 HOH F 430
SITE 1 BC9 6 THR F 75 GLY F 76 GLY F 78 ASP F 79
SITE 2 BC9 6 HOH F 414 HOH F 466
CRYST1 76.470 133.878 153.929 90.00 90.00 90.00 P 21 21 21 24
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 0.013077 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007469 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006497 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
