HEADER LYASE 27-DEC-11 4ADM
TITLE CRYSTAL STRUCTURE OF RV1098C IN COMPLEX WITH MESO-TARTRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FUMARATE HYDRATASE CLASS II;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 1-473;
COMPND 5 SYNONYM: FUMARASE C;
COMPND 6 EC: 4.2.1.2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PDEST17
KEYWDS LYASE, TRICARBOXYLIC ACID CYCLE, FUMARASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.E.MECHALY,A.HAOUZ,I.MIRAS,P.WEBER,W.SHEPARD,S.COLE,P.M.ALZARI,
AUTHOR 2 M.BELLINZONI
REVDAT 3 20-DEC-23 4ADM 1 REMARK
REVDAT 2 06-JUN-12 4ADM 1 JRNL
REVDAT 1 25-APR-12 4ADM 0
JRNL AUTH A.E.MECHALY,A.HAOUZ,I.MIRAS,N.BARILONE,P.WEBER,W.SHEPARD,
JRNL AUTH 2 P.M.ALZARI,M.BELLINZONI
JRNL TITL CONFORMATIONAL CHANGES UPON LIGAND BINDING IN THE ESSENTIAL
JRNL TITL 2 CLASS II FUMARASE RV1098C FROM MYCOBACTERIUM TUBERCULOSIS.
JRNL REF FEBS LETT. V. 586 1606 2012
JRNL REFN ISSN 0014-5793
JRNL PMID 22561013
JRNL DOI 10.1016/J.FEBSLET.2012.04.034
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.1
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 276381
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 13967
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.69
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.51
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 20499
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2089
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 19491
REMARK 3 BIN R VALUE (WORKING SET) : 0.2081
REMARK 3 BIN FREE R VALUE : 0.2259
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.92
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1008
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13321
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 1689
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.04
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.98960
REMARK 3 B22 (A**2) : -0.72540
REMARK 3 B33 (A**2) : -0.26420
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.54850
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.186
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.073
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.073
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.071
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.071
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 13553 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 18438 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 6337 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 345 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 2022 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 13553 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1895 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : 4 ; 1.000 ; HARMONIC
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 18514 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.97
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.46
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.39
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 25
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESSEQ 9:99
REMARK 3 ORIGIN FOR THE GROUP (A): 81.5270 11.4239 42.0977
REMARK 3 T TENSOR
REMARK 3 T11: -0.0672 T22: 0.0206
REMARK 3 T33: -0.0004 T12: -0.0526
REMARK 3 T13: -0.0326 T23: -0.0250
REMARK 3 L TENSOR
REMARK 3 L11: 1.2359 L22: 0.6817
REMARK 3 L33: 1.7499 L12: -0.2197
REMARK 3 L13: 0.1880 L23: 0.4572
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: -0.1007 S13: 0.1987
REMARK 3 S21: -0.0122 S22: 0.0307 S23: -0.1840
REMARK 3 S31: -0.2071 S32: 0.2628 S33: -0.0293
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESSEQ 100:221
REMARK 3 ORIGIN FOR THE GROUP (A): 55.6641 11.4759 48.4834
REMARK 3 T TENSOR
REMARK 3 T11: -0.0347 T22: -0.0089
REMARK 3 T33: -0.0735 T12: 0.0183
REMARK 3 T13: -0.0373 T23: -0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 0.9776 L22: 0.2691
REMARK 3 L33: 0.3643 L12: -0.2126
REMARK 3 L13: 0.0758 L23: 0.0225
REMARK 3 S TENSOR
REMARK 3 S11: -0.0361 S12: -0.1501 S13: 0.1315
REMARK 3 S21: 0.0527 S22: 0.0417 S23: -0.0130
REMARK 3 S31: -0.0852 S32: 0.0164 S33: -0.0056
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND RESSEQ 222:259
REMARK 3 ORIGIN FOR THE GROUP (A): 72.2157 0.9349 57.4679
REMARK 3 T TENSOR
REMARK 3 T11: -0.0260 T22: 0.0794
REMARK 3 T33: -0.0677 T12: 0.0370
REMARK 3 T13: -0.0465 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 1.0550 L22: 0.9117
REMARK 3 L33: 1.2153 L12: -0.6560
REMARK 3 L13: -0.5742 L23: 1.3088
REMARK 3 S TENSOR
REMARK 3 S11: -0.0034 S12: -0.0859 S13: -0.1074
REMARK 3 S21: 0.0275 S22: 0.0538 S23: -0.0489
REMARK 3 S31: 0.0823 S32: 0.1656 S33: -0.0504
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND RESSEQ 260:393
REMARK 3 ORIGIN FOR THE GROUP (A): 49.8194 11.4980 41.0434
REMARK 3 T TENSOR
REMARK 3 T11: -0.0185 T22: -0.0160
REMARK 3 T33: -0.0476 T12: 0.0152
REMARK 3 T13: -0.0335 T23: -0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 0.9489 L22: 0.2407
REMARK 3 L33: 0.4672 L12: -0.2008
REMARK 3 L13: 0.1341 L23: -0.0172
REMARK 3 S TENSOR
REMARK 3 S11: -0.0084 S12: -0.0507 S13: 0.0800
REMARK 3 S21: 0.0081 S22: 0.0074 S23: 0.0025
REMARK 3 S31: -0.0648 S32: 0.0109 S33: 0.0010
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND RESSEQ 394:423
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5510 15.7777 44.1731
REMARK 3 T TENSOR
REMARK 3 T11: -0.1006 T22: 0.1026
REMARK 3 T33: 0.0277 T12: 0.1208
REMARK 3 T13: -0.0104 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 1.6660 L22: 1.9475
REMARK 3 L33: 1.2300 L12: 1.0283
REMARK 3 L13: 0.1090 L23: 0.0379
REMARK 3 S TENSOR
REMARK 3 S11: -0.0823 S12: -0.2153 S13: 0.0638
REMARK 3 S21: -0.0732 S22: 0.0214 S23: 0.2021
REMARK 3 S31: -0.0948 S32: -0.2406 S33: 0.0609
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND RESSEQ 424:467
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3468 15.8817 46.9824
REMARK 3 T TENSOR
REMARK 3 T11: -0.0966 T22: 0.1129
REMARK 3 T33: 0.0092 T12: 0.1035
REMARK 3 T13: 0.0202 T23: 0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 2.9529 L22: 1.8697
REMARK 3 L33: 3.0011 L12: -1.1493
REMARK 3 L13: 0.4099 L23: 0.3372
REMARK 3 S TENSOR
REMARK 3 S11: -0.0567 S12: -0.2296 S13: -0.0674
REMARK 3 S21: 0.0407 S22: 0.0106 S23: 0.2628
REMARK 3 S31: -0.1281 S32: -0.3324 S33: 0.0461
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND RESSEQ 9:44
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2997 -9.8262 32.0103
REMARK 3 T TENSOR
REMARK 3 T11: -0.1100 T22: 0.0236
REMARK 3 T33: 0.1025 T12: -0.0626
REMARK 3 T13: -0.0665 T23: 0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 2.1417 L22: 1.9267
REMARK 3 L33: 1.2032 L12: -1.2715
REMARK 3 L13: -1.0381 L23: -0.4543
REMARK 3 S TENSOR
REMARK 3 S11: 0.0076 S12: 0.1522 S13: -0.2050
REMARK 3 S21: -0.0991 S22: 0.0910 S23: 0.5684
REMARK 3 S31: 0.2306 S32: -0.3914 S33: -0.0987
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND RESSEQ 45:144
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7114 -9.6881 47.4486
REMARK 3 T TENSOR
REMARK 3 T11: -0.0734 T22: 0.0622
REMARK 3 T33: 0.0630 T12: -0.0229
REMARK 3 T13: 0.0211 T23: 0.0761
REMARK 3 L TENSOR
REMARK 3 L11: 1.0427 L22: 0.6234
REMARK 3 L33: 1.3659 L12: -0.1164
REMARK 3 L13: 0.1605 L23: -0.3769
REMARK 3 S TENSOR
REMARK 3 S11: -0.0479 S12: -0.2228 S13: -0.2954
REMARK 3 S21: 0.1039 S22: 0.0439 S23: 0.2173
REMARK 3 S31: 0.1446 S32: -0.2590 S33: 0.0039
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN B AND RESSEQ 145:259
REMARK 3 ORIGIN FOR THE GROUP (A): 47.3184 -10.2616 52.6119
REMARK 3 T TENSOR
REMARK 3 T11: -0.0471 T22: 0.0119
REMARK 3 T33: -0.0611 T12: 0.0302
REMARK 3 T13: -0.0214 T23: 0.0540
REMARK 3 L TENSOR
REMARK 3 L11: 1.1568 L22: 0.3506
REMARK 3 L33: 0.3954 L12: -0.2565
REMARK 3 L13: 0.0057 L23: -0.0271
REMARK 3 S TENSOR
REMARK 3 S11: -0.0519 S12: -0.2703 S13: -0.1726
REMARK 3 S21: 0.0806 S22: 0.0749 S23: 0.0647
REMARK 3 S31: 0.0538 S32: -0.0391 S33: -0.0230
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN B AND RESSEQ 260:393
REMARK 3 ORIGIN FOR THE GROUP (A): 48.2235 -11.6719 40.8389
REMARK 3 T TENSOR
REMARK 3 T11: -0.0059 T22: -0.0015
REMARK 3 T33: -0.0091 T12: 0.0110
REMARK 3 T13: -0.0311 T23: 0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 0.8676 L22: 0.4107
REMARK 3 L33: 0.4235 L12: -0.2458
REMARK 3 L13: 0.0040 L23: 0.0121
REMARK 3 S TENSOR
REMARK 3 S11: -0.0120 S12: -0.0801 S13: -0.1447
REMARK 3 S21: 0.0266 S22: 0.0305 S23: 0.0633
REMARK 3 S31: 0.0760 S32: -0.0336 S33: -0.0185
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND RESSEQ 394:423
REMARK 3 ORIGIN FOR THE GROUP (A): 85.4686 -15.8004 43.9675
REMARK 3 T TENSOR
REMARK 3 T11: -0.0791 T22: 0.0829
REMARK 3 T33: -0.0352 T12: 0.1017
REMARK 3 T13: -0.0364 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 1.9522 L22: 1.3429
REMARK 3 L33: 0.8629 L12: 0.5364
REMARK 3 L13: 0.4092 L23: 0.1270
REMARK 3 S TENSOR
REMARK 3 S11: -0.0703 S12: -0.1463 S13: -0.1233
REMARK 3 S21: -0.0664 S22: 0.0630 S23: -0.1365
REMARK 3 S31: 0.0633 S32: 0.1815 S33: 0.0073
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN B AND RESSEQ 424:466
REMARK 3 ORIGIN FOR THE GROUP (A): 93.2209 -15.8452 46.3350
REMARK 3 T TENSOR
REMARK 3 T11: -0.0890 T22: 0.1080
REMARK 3 T33: -0.0100 T12: 0.0992
REMARK 3 T13: -0.0765 T23: -0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 3.0207 L22: 1.8366
REMARK 3 L33: 2.3276 L12: -1.0843
REMARK 3 L13: -0.4972 L23: -0.4592
REMARK 3 S TENSOR
REMARK 3 S11: -0.0290 S12: -0.2189 S13: -0.1055
REMARK 3 S21: 0.0226 S22: 0.0297 S23: -0.2349
REMARK 3 S31: 0.2215 S32: 0.2990 S33: -0.0007
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN C AND RESSEQ 10:23
REMARK 3 ORIGIN FOR THE GROUP (A): 56.4053 43.2287 34.6769
REMARK 3 T TENSOR
REMARK 3 T11: 0.3334 T22: -0.0917
REMARK 3 T33: 0.0381 T12: -0.1932
REMARK 3 T13: -0.1407 T23: -0.0801
REMARK 3 L TENSOR
REMARK 3 L11: 0.4248 L22: 1.9006
REMARK 3 L33: 0.2017 L12: -0.2471
REMARK 3 L13: -0.5559 L23: 0.7078
REMARK 3 S TENSOR
REMARK 3 S11: 0.0015 S12: -0.0647 S13: 0.0652
REMARK 3 S21: 0.0819 S22: -0.0120 S23: 0.1277
REMARK 3 S31: -0.1009 S32: -0.0976 S33: 0.0105
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN C AND RESSEQ 24:48
REMARK 3 ORIGIN FOR THE GROUP (A): 57.7903 30.3479 31.6615
REMARK 3 T TENSOR
REMARK 3 T11: -0.0202 T22: -0.0942
REMARK 3 T33: -0.0821 T12: -0.0329
REMARK 3 T13: -0.0600 T23: -0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 1.2750 L22: 2.5572
REMARK 3 L33: 7.2062 L12: 0.5876
REMARK 3 L13: -1.0625 L23: -2.9479
REMARK 3 S TENSOR
REMARK 3 S11: 0.1166 S12: -0.0539 S13: 0.1366
REMARK 3 S21: 0.2915 S22: -0.1678 S23: -0.0087
REMARK 3 S31: -0.7057 S32: 0.5005 S33: 0.0512
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN C AND RESSEQ 49:137
REMARK 3 ORIGIN FOR THE GROUP (A): 55.9475 32.8844 17.2890
REMARK 3 T TENSOR
REMARK 3 T11: 0.0653 T22: -0.0872
REMARK 3 T33: -0.0107 T12: -0.0441
REMARK 3 T13: -0.0337 T23: 0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 0.5244 L22: 1.0739
REMARK 3 L33: 3.1465 L12: 0.0417
REMARK 3 L13: 0.0343 L23: -0.3208
REMARK 3 S TENSOR
REMARK 3 S11: -0.0466 S12: 0.0371 S13: 0.1461
REMARK 3 S21: -0.0877 S22: 0.0483 S23: -0.0878
REMARK 3 S31: -0.4352 S32: 0.1858 S33: -0.0017
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN C AND RESSEQ 138:232
REMARK 3 ORIGIN FOR THE GROUP (A): 60.8613 -1.0759 15.0239
REMARK 3 T TENSOR
REMARK 3 T11: 0.0113 T22: -0.0083
REMARK 3 T33: -0.0572 T12: 0.0167
REMARK 3 T13: -0.0218 T23: -0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 0.4369 L22: 0.7154
REMARK 3 L33: 0.2207 L12: -0.2142
REMARK 3 L13: 0.0393 L23: -0.0847
REMARK 3 S TENSOR
REMARK 3 S11: 0.0191 S12: 0.1282 S13: 0.0062
REMARK 3 S21: -0.1296 S22: -0.0056 S23: -0.0678
REMARK 3 S31: 0.0146 S32: 0.0608 S33: -0.0135
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN C AND RESSEQ 233:260
REMARK 3 ORIGIN FOR THE GROUP (A): 48.4284 23.5466 6.2155
REMARK 3 T TENSOR
REMARK 3 T11: 0.0739 T22: -0.0240
REMARK 3 T33: -0.0518 T12: 0.0144
REMARK 3 T13: -0.0620 T23: 0.0458
REMARK 3 L TENSOR
REMARK 3 L11: 1.2704 L22: 1.7747
REMARK 3 L33: 0.4079 L12: -0.3743
REMARK 3 L13: -0.9053 L23: -0.2380
REMARK 3 S TENSOR
REMARK 3 S11: -0.0962 S12: 0.0721 S13: 0.2258
REMARK 3 S21: -0.1062 S22: 0.0763 S23: -0.0075
REMARK 3 S31: 0.0216 S32: -0.0634 S33: 0.0199
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN C AND RESSEQ 261:399
REMARK 3 ORIGIN FOR THE GROUP (A): 62.8810 0.5740 25.3487
REMARK 3 T TENSOR
REMARK 3 T11: -0.0471 T22: -0.0438
REMARK 3 T33: -0.0790 T12: 0.0100
REMARK 3 T13: -0.0275 T23: -0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.6507 L22: 0.4287
REMARK 3 L33: 0.4155 L12: -0.1666
REMARK 3 L13: 0.0532 L23: -0.0185
REMARK 3 S TENSOR
REMARK 3 S11: -0.0021 S12: 0.0208 S13: 0.0023
REMARK 3 S21: -0.0488 S22: 0.0219 S23: -0.0523
REMARK 3 S31: -0.0131 S32: 0.0729 S33: -0.0198
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN C AND RESSEQ 400:465
REMARK 3 ORIGIN FOR THE GROUP (A): 74.0335 -40.3315 19.1834
REMARK 3 T TENSOR
REMARK 3 T11: 0.1155 T22: -0.1308
REMARK 3 T33: 0.0576 T12: 0.0283
REMARK 3 T13: -0.0577 T23: -0.0501
REMARK 3 L TENSOR
REMARK 3 L11: 1.4207 L22: 6.6738
REMARK 3 L33: 7.8935 L12: -0.2047
REMARK 3 L13: 0.0745 L23: -2.7289
REMARK 3 S TENSOR
REMARK 3 S11: 0.0585 S12: -0.1608 S13: -0.2092
REMARK 3 S21: -0.3871 S22: 0.1396 S23: -0.4981
REMARK 3 S31: 1.0507 S32: -0.0403 S33: -0.1981
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN D AND RESSEQ 10:48
REMARK 3 ORIGIN FOR THE GROUP (A): 39.2592 -32.9268 32.2450
REMARK 3 T TENSOR
REMARK 3 T11: 0.0922 T22: -0.0740
REMARK 3 T33: 0.0272 T12: -0.0814
REMARK 3 T13: -0.0417 T23: 0.0584
REMARK 3 L TENSOR
REMARK 3 L11: 2.1191 L22: 2.3149
REMARK 3 L33: 4.9579 L12: -0.1598
REMARK 3 L13: 0.1636 L23: 1.5037
REMARK 3 S TENSOR
REMARK 3 S11: -0.0032 S12: -0.1161 S13: -0.2887
REMARK 3 S21: 0.2314 S22: 0.0355 S23: 0.2009
REMARK 3 S31: 0.8822 S32: -0.4543 S33: -0.0322
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN D AND RESSEQ 49:137
REMARK 3 ORIGIN FOR THE GROUP (A): 42.0600 -32.5281 17.0001
REMARK 3 T TENSOR
REMARK 3 T11: 0.0637 T22: -0.1243
REMARK 3 T33: 0.0337 T12: -0.0498
REMARK 3 T13: -0.0813 T23: -0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 0.5373 L22: 1.1492
REMARK 3 L33: 3.6268 L12: 0.0936
REMARK 3 L13: 0.1002 L23: 0.1363
REMARK 3 S TENSOR
REMARK 3 S11: -0.0233 S12: 0.0624 S13: -0.1716
REMARK 3 S21: -0.1603 S22: 0.0566 S23: 0.2038
REMARK 3 S31: 0.5307 S32: -0.1909 S33: -0.0333
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN D AND RESSEQ 138:232
REMARK 3 ORIGIN FOR THE GROUP (A): 37.1329 1.3910 15.0514
REMARK 3 T TENSOR
REMARK 3 T11: 0.0012 T22: -0.0196
REMARK 3 T33: -0.0493 T12: 0.0109
REMARK 3 T13: -0.0559 T23: 0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.5418 L22: 1.0709
REMARK 3 L33: 0.2707 L12: -0.3734
REMARK 3 L13: 0.0362 L23: 0.2120
REMARK 3 S TENSOR
REMARK 3 S11: 0.0181 S12: 0.0913 S13: -0.0671
REMARK 3 S21: -0.1087 S22: -0.0033 S23: 0.1625
REMARK 3 S31: 0.0128 S32: -0.0433 S33: -0.0148
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN D AND RESSEQ 233:260
REMARK 3 ORIGIN FOR THE GROUP (A): 49.5536 -23.1405 5.9515
REMARK 3 T TENSOR
REMARK 3 T11: 0.0620 T22: -0.0383
REMARK 3 T33: -0.0466 T12: 0.0130
REMARK 3 T13: -0.0440 T23: -0.0522
REMARK 3 L TENSOR
REMARK 3 L11: 2.4244 L22: 2.0907
REMARK 3 L33: 1.7035 L12: -1.4720
REMARK 3 L13: 1.2857 L23: -0.3689
REMARK 3 S TENSOR
REMARK 3 S11: 0.0234 S12: 0.1724 S13: -0.1450
REMARK 3 S21: -0.0884 S22: -0.0793 S23: -0.0560
REMARK 3 S31: 0.0395 S32: 0.0749 S33: 0.0559
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN D AND RESSEQ 261:399
REMARK 3 ORIGIN FOR THE GROUP (A): 35.1302 -0.3640 25.3594
REMARK 3 T TENSOR
REMARK 3 T11: -0.0452 T22: -0.0390
REMARK 3 T33: -0.0490 T12: 0.0089
REMARK 3 T13: -0.0443 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.6887 L22: 0.5083
REMARK 3 L33: 0.4491 L12: -0.2122
REMARK 3 L13: 0.0368 L23: 0.0301
REMARK 3 S TENSOR
REMARK 3 S11: -0.0024 S12: -0.0023 S13: -0.0357
REMARK 3 S21: -0.0307 S22: 0.0167 S23: 0.0988
REMARK 3 S31: 0.0090 S32: -0.0781 S33: -0.0143
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN D AND RESSEQ 400:465
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8634 40.8556 19.8015
REMARK 3 T TENSOR
REMARK 3 T11: 0.1000 T22: -0.1211
REMARK 3 T33: 0.1002 T12: 0.0393
REMARK 3 T13: -0.0650 T23: 0.0452
REMARK 3 L TENSOR
REMARK 3 L11: 0.9204 L22: 7.5702
REMARK 3 L33: 6.4008 L12: -0.6914
REMARK 3 L13: -0.0508 L23: 2.3693
REMARK 3 S TENSOR
REMARK 3 S11: 0.0415 S12: -0.0767 S13: 0.2337
REMARK 3 S21: -0.3531 S22: 0.0910 S23: 0.4951
REMARK 3 S31: -0.8743 S32: -0.0082 S33: -0.1324
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.
REMARK 3 ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY.
REMARK 4
REMARK 4 4ADM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-DEC-11.
REMARK 100 THE DEPOSITION ID IS D_1290050809.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 287
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 277914
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 39.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.54000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3NO9
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 94.47000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.24500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 94.47000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 48.24500
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 29830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -153.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -21
REMARK 465 SER A -20
REMARK 465 TYR A -19
REMARK 465 TYR 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 LEU A -11
REMARK 465 GLU A -10
REMARK 465 SER A -9
REMARK 465 THR A -8
REMARK 465 SER A -7
REMARK 465 LEU A -6
REMARK 465 TYR A -5
REMARK 465 LYS A -4
REMARK 465 LYS A -3
REMARK 465 ALA A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 VAL A 3
REMARK 465 ASP A 4
REMARK 465 ALA A 5
REMARK 465 ASP A 6
REMARK 465 SER A 7
REMARK 465 ALA A 8
REMARK 465 GLN A 315
REMARK 465 PRO A 316
REMARK 465 GLY A 317
REMARK 465 SER A 318
REMARK 465 SER A 319
REMARK 465 ILE A 320
REMARK 465 MET A 321
REMARK 465 PRO A 322
REMARK 465 GLY A 323
REMARK 465 GLN A 468
REMARK 465 LEU A 469
REMARK 465 ASP A 470
REMARK 465 SER A 471
REMARK 465 ASP A 472
REMARK 465 ARG A 473
REMARK 465 MET B -21
REMARK 465 SER B -20
REMARK 465 TYR B -19
REMARK 465 TYR B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 LEU B -11
REMARK 465 GLU B -10
REMARK 465 SER B -9
REMARK 465 THR B -8
REMARK 465 SER B -7
REMARK 465 LEU B -6
REMARK 465 TYR B -5
REMARK 465 LYS B -4
REMARK 465 LYS B -3
REMARK 465 ALA B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 VAL B 3
REMARK 465 ASP B 4
REMARK 465 ALA B 5
REMARK 465 ASP B 6
REMARK 465 SER B 7
REMARK 465 ALA B 8
REMARK 465 PRO B 316
REMARK 465 GLY B 317
REMARK 465 SER B 318
REMARK 465 SER B 319
REMARK 465 ILE B 320
REMARK 465 MET B 321
REMARK 465 PRO B 322
REMARK 465 GLY B 323
REMARK 465 LYS B 324
REMARK 465 GLU B 467
REMARK 465 GLN B 468
REMARK 465 LEU B 469
REMARK 465 ASP B 470
REMARK 465 SER B 471
REMARK 465 ASP B 472
REMARK 465 ARG B 473
REMARK 465 MET C -21
REMARK 465 SER C -20
REMARK 465 TYR C -19
REMARK 465 TYR C -18
REMARK 465 HIS C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 LEU C -11
REMARK 465 GLU C -10
REMARK 465 SER C -9
REMARK 465 THR C -8
REMARK 465 SER C -7
REMARK 465 LEU C -6
REMARK 465 TYR C -5
REMARK 465 LYS C -4
REMARK 465 LYS C -3
REMARK 465 ALA C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 VAL C 3
REMARK 465 ASP C 4
REMARK 465 ALA C 5
REMARK 465 ASP C 6
REMARK 465 SER C 7
REMARK 465 ALA C 8
REMARK 465 ASN C 9
REMARK 465 ALA C 466
REMARK 465 GLU C 467
REMARK 465 GLN C 468
REMARK 465 LEU C 469
REMARK 465 ASP C 470
REMARK 465 SER C 471
REMARK 465 ASP C 472
REMARK 465 ARG C 473
REMARK 465 MET D -21
REMARK 465 SER D -20
REMARK 465 TYR D -19
REMARK 465 TYR D -18
REMARK 465 HIS D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 LEU D -11
REMARK 465 GLU D -10
REMARK 465 SER D -9
REMARK 465 THR D -8
REMARK 465 SER D -7
REMARK 465 LEU D -6
REMARK 465 TYR D -5
REMARK 465 LYS D -4
REMARK 465 LYS D -3
REMARK 465 ALA D -2
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 VAL D 3
REMARK 465 ASP D 4
REMARK 465 ALA D 5
REMARK 465 ASP D 6
REMARK 465 SER D 7
REMARK 465 ALA D 8
REMARK 465 ASN D 9
REMARK 465 ASP D 15
REMARK 465 THR D 16
REMARK 465 MET D 17
REMARK 465 GLY D 18
REMARK 465 GLU D 19
REMARK 465 ALA D 466
REMARK 465 GLU D 467
REMARK 465 GLN D 468
REMARK 465 LEU D 469
REMARK 465 ASP D 470
REMARK 465 SER D 471
REMARK 465 ASP D 472
REMARK 465 ARG D 473
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 ASN A 9 CG OD1 ND2
REMARK 470 LYS A 324 CG CD CE NZ
REMARK 470 GLU A 467 CG CD OE1 OE2
REMARK 470 ASN B 9 CG OD1 ND2
REMARK 470 TYR C 10 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG C 11 CG CD NE CZ NH1 NH2
REMARK 470 ILE C 12 CG1 CG2 CD1
REMARK 470 MET C 17 CG SD CE
REMARK 470 GLU C 19 CG CD OE1 OE2
REMARK 470 ARG C 21 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 25 CG CD CE NZ
REMARK 470 GLU C 396 CG CD OE1 OE2
REMARK 470 TYR C 418 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU C 419 CG CD OE1 OE2
REMARK 470 ASP C 447 CG OD1 OD2
REMARK 470 ARG C 448 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 11 CG CD NE CZ NH1 NH2
REMARK 470 ILE D 12 CG1 CG2 CD1
REMARK 470 HIS D 14 CG ND1 CD2 CE1 NE2
REMARK 470 ARG D 21 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 74 CG CD OE1 OE2
REMARK 470 GLU D 396 CG CD OE1 OE2
REMARK 470 GLU D 419 CG CD OE1 OE2
REMARK 470 ASP D 447 CG OD1 OD2
REMARK 470 ARG D 448 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 OE1 GLN D 165 NH1 ARG D 381 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 2333 O HOH A 2333 2656 1.88
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 ARG A 29 -150.51 -128.47
REMARK 500 HIS A 158 -56.87 -127.33
REMARK 500 ALA A 191 -158.77 -121.60
REMARK 500 THR A 229 -130.88 48.50
REMARK 500 PHE A 356 -120.75 50.20
REMARK 500 VAL A 360 43.60 -104.52
REMARK 500 CYS A 387 -64.85 -129.77
REMARK 500 LEU A 449 107.94 -161.06
REMARK 500 ARG B 29 -150.88 -128.80
REMARK 500 HIS B 158 -57.77 -126.29
REMARK 500 ALA B 191 -157.83 -121.56
REMARK 500 THR B 229 -131.48 49.02
REMARK 500 PHE B 356 -121.70 50.64
REMARK 500 VAL B 360 44.74 -103.89
REMARK 500 CYS B 387 -65.82 -129.15
REMARK 500 LEU B 449 107.87 -160.31
REMARK 500 ARG C 29 -158.36 -127.29
REMARK 500 HIS C 158 -50.47 -128.11
REMARK 500 THR C 229 -139.02 49.80
REMARK 500 PHE C 356 -119.09 51.10
REMARK 500 CYS C 387 -70.22 -129.46
REMARK 500 ARG D 29 -157.28 -127.48
REMARK 500 HIS D 158 -50.22 -127.87
REMARK 500 THR D 229 -139.44 48.84
REMARK 500 PHE D 356 -118.98 49.41
REMARK 500 CYS D 387 -70.14 -130.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2020 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH A2209 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH B2030 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH B2084 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH B2130 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH C2054 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH C2107 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH C2160 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH D2356 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH D2357 DISTANCE = 7.46 ANGSTROMS
REMARK 525 HOH D2359 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH D2360 DISTANCE = 8.56 ANGSTROMS
REMARK 525 HOH D2361 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH D2362 DISTANCE = 7.12 ANGSTROMS
REMARK 525 HOH D2363 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH D2365 DISTANCE = 7.79 ANGSTROMS
REMARK 525 HOH D2366 DISTANCE = 7.71 ANGSTROMS
REMARK 525 HOH D2368 DISTANCE = 7.66 ANGSTROMS
REMARK 525 HOH D2369 DISTANCE = 9.28 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT D 1466
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT C 1466
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1468
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ADL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF RV1098C IN COMPLEX WITH MALATE
REMARK 900 RELATED ID: 4APA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS FUMARASE ( RV1098C)
REMARK 900 S318A IN APO FORM
REMARK 900 RELATED ID: 4APB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS FUMARASE ( RV1098C)
REMARK 900 S318C IN COMPLEX WITH FUMARATE
DBREF 4ADM A 1 473 UNP O53446 FUMC_MYCTU 1 473
DBREF 4ADM B 1 473 UNP O53446 FUMC_MYCTU 1 473
DBREF 4ADM C 1 473 UNP O53446 FUMC_MYCTU 1 473
DBREF 4ADM D 1 473 UNP O53446 FUMC_MYCTU 1 473
SEQADV 4ADM MET A -21 UNP O53446 EXPRESSION TAG
SEQADV 4ADM SER A -20 UNP O53446 EXPRESSION TAG
SEQADV 4ADM TYR A -19 UNP O53446 EXPRESSION TAG
SEQADV 4ADM TYR A -18 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS A -17 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS A -16 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS A -15 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS A -14 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS A -13 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS A -12 UNP O53446 EXPRESSION TAG
SEQADV 4ADM LEU A -11 UNP O53446 EXPRESSION TAG
SEQADV 4ADM GLU A -10 UNP O53446 EXPRESSION TAG
SEQADV 4ADM SER A -9 UNP O53446 EXPRESSION TAG
SEQADV 4ADM THR A -8 UNP O53446 EXPRESSION TAG
SEQADV 4ADM SER A -7 UNP O53446 EXPRESSION TAG
SEQADV 4ADM LEU A -6 UNP O53446 EXPRESSION TAG
SEQADV 4ADM TYR A -5 UNP O53446 EXPRESSION TAG
SEQADV 4ADM LYS A -4 UNP O53446 EXPRESSION TAG
SEQADV 4ADM LYS A -3 UNP O53446 EXPRESSION TAG
SEQADV 4ADM ALA A -2 UNP O53446 EXPRESSION TAG
SEQADV 4ADM GLY A -1 UNP O53446 EXPRESSION TAG
SEQADV 4ADM SER A 0 UNP O53446 EXPRESSION TAG
SEQADV 4ADM MET B -21 UNP O53446 EXPRESSION TAG
SEQADV 4ADM SER B -20 UNP O53446 EXPRESSION TAG
SEQADV 4ADM TYR B -19 UNP O53446 EXPRESSION TAG
SEQADV 4ADM TYR B -18 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS B -17 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS B -16 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS B -15 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS B -14 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS B -13 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS B -12 UNP O53446 EXPRESSION TAG
SEQADV 4ADM LEU B -11 UNP O53446 EXPRESSION TAG
SEQADV 4ADM GLU B -10 UNP O53446 EXPRESSION TAG
SEQADV 4ADM SER B -9 UNP O53446 EXPRESSION TAG
SEQADV 4ADM THR B -8 UNP O53446 EXPRESSION TAG
SEQADV 4ADM SER B -7 UNP O53446 EXPRESSION TAG
SEQADV 4ADM LEU B -6 UNP O53446 EXPRESSION TAG
SEQADV 4ADM TYR B -5 UNP O53446 EXPRESSION TAG
SEQADV 4ADM LYS B -4 UNP O53446 EXPRESSION TAG
SEQADV 4ADM LYS B -3 UNP O53446 EXPRESSION TAG
SEQADV 4ADM ALA B -2 UNP O53446 EXPRESSION TAG
SEQADV 4ADM GLY B -1 UNP O53446 EXPRESSION TAG
SEQADV 4ADM SER B 0 UNP O53446 EXPRESSION TAG
SEQADV 4ADM MET C -21 UNP O53446 EXPRESSION TAG
SEQADV 4ADM SER C -20 UNP O53446 EXPRESSION TAG
SEQADV 4ADM TYR C -19 UNP O53446 EXPRESSION TAG
SEQADV 4ADM TYR C -18 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS C -17 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS C -16 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS C -15 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS C -14 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS C -13 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS C -12 UNP O53446 EXPRESSION TAG
SEQADV 4ADM LEU C -11 UNP O53446 EXPRESSION TAG
SEQADV 4ADM GLU C -10 UNP O53446 EXPRESSION TAG
SEQADV 4ADM SER C -9 UNP O53446 EXPRESSION TAG
SEQADV 4ADM THR C -8 UNP O53446 EXPRESSION TAG
SEQADV 4ADM SER C -7 UNP O53446 EXPRESSION TAG
SEQADV 4ADM LEU C -6 UNP O53446 EXPRESSION TAG
SEQADV 4ADM TYR C -5 UNP O53446 EXPRESSION TAG
SEQADV 4ADM LYS C -4 UNP O53446 EXPRESSION TAG
SEQADV 4ADM LYS C -3 UNP O53446 EXPRESSION TAG
SEQADV 4ADM ALA C -2 UNP O53446 EXPRESSION TAG
SEQADV 4ADM GLY C -1 UNP O53446 EXPRESSION TAG
SEQADV 4ADM SER C 0 UNP O53446 EXPRESSION TAG
SEQADV 4ADM MET D -21 UNP O53446 EXPRESSION TAG
SEQADV 4ADM SER D -20 UNP O53446 EXPRESSION TAG
SEQADV 4ADM TYR D -19 UNP O53446 EXPRESSION TAG
SEQADV 4ADM TYR D -18 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS D -17 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS D -16 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS D -15 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS D -14 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS D -13 UNP O53446 EXPRESSION TAG
SEQADV 4ADM HIS D -12 UNP O53446 EXPRESSION TAG
SEQADV 4ADM LEU D -11 UNP O53446 EXPRESSION TAG
SEQADV 4ADM GLU D -10 UNP O53446 EXPRESSION TAG
SEQADV 4ADM SER D -9 UNP O53446 EXPRESSION TAG
SEQADV 4ADM THR D -8 UNP O53446 EXPRESSION TAG
SEQADV 4ADM SER D -7 UNP O53446 EXPRESSION TAG
SEQADV 4ADM LEU D -6 UNP O53446 EXPRESSION TAG
SEQADV 4ADM TYR D -5 UNP O53446 EXPRESSION TAG
SEQADV 4ADM LYS D -4 UNP O53446 EXPRESSION TAG
SEQADV 4ADM LYS D -3 UNP O53446 EXPRESSION TAG
SEQADV 4ADM ALA D -2 UNP O53446 EXPRESSION TAG
SEQADV 4ADM GLY D -1 UNP O53446 EXPRESSION TAG
SEQADV 4ADM SER D 0 UNP O53446 EXPRESSION TAG
SEQRES 1 A 495 MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER
SEQRES 2 A 495 THR SER LEU TYR LYS LYS ALA GLY SER MET ALA VAL ASP
SEQRES 3 A 495 ALA ASP SER ALA ASN TYR ARG ILE GLU HIS ASP THR MET
SEQRES 4 A 495 GLY GLU VAL ARG VAL PRO ALA LYS ALA LEU TRP ARG ALA
SEQRES 5 A 495 GLN THR GLN ARG ALA VAL GLU ASN PHE PRO ILE SER GLY
SEQRES 6 A 495 ARG GLY LEU GLU ARG THR GLN ILE ARG ALA LEU GLY LEU
SEQRES 7 A 495 LEU LYS GLY ALA CYS ALA GLN VAL ASN SER ASP LEU GLY
SEQRES 8 A 495 LEU LEU ALA PRO GLU LYS ALA ASP ALA ILE ILE ALA ALA
SEQRES 9 A 495 ALA ALA GLU ILE ALA ASP GLY GLN HIS ASP ASP GLN PHE
SEQRES 10 A 495 PRO ILE ASP VAL PHE GLN THR GLY SER GLY THR SER SER
SEQRES 11 A 495 ASN MET ASN THR ASN GLU VAL ILE ALA SER ILE ALA ALA
SEQRES 12 A 495 LYS GLY GLY VAL THR LEU HIS PRO ASN ASP ASP VAL ASN
SEQRES 13 A 495 MET SER GLN SER SER ASN ASP THR PHE PRO THR ALA THR
SEQRES 14 A 495 HIS ILE ALA ALA THR GLU ALA ALA VAL ALA HIS LEU ILE
SEQRES 15 A 495 PRO ALA LEU GLN GLN LEU HIS ASP ALA LEU ALA ALA LYS
SEQRES 16 A 495 ALA LEU ASP TRP HIS THR VAL VAL LYS SER GLY ARG THR
SEQRES 17 A 495 HIS LEU MET ASP ALA VAL PRO VAL THR LEU GLY GLN GLU
SEQRES 18 A 495 PHE SER GLY TYR ALA ARG GLN ILE GLU ALA GLY ILE GLU
SEQRES 19 A 495 ARG VAL ARG ALA CYS LEU PRO ARG LEU GLY GLU LEU ALA
SEQRES 20 A 495 ILE GLY GLY THR ALA VAL GLY THR GLY LEU ASN ALA PRO
SEQRES 21 A 495 ASP ASP PHE GLY VAL ARG VAL VAL ALA VAL LEU VAL ALA
SEQRES 22 A 495 GLN THR GLY LEU SER GLU LEU ARG THR ALA ALA ASN SER
SEQRES 23 A 495 PHE GLU ALA GLN ALA ALA ARG ASP GLY LEU VAL GLU ALA
SEQRES 24 A 495 SER GLY ALA LEU ARG THR ILE ALA VAL SER LEU THR LYS
SEQRES 25 A 495 ILE ALA ASN ASP ILE ARG TRP MET GLY SER GLY PRO LEU
SEQRES 26 A 495 THR GLY LEU ALA GLU ILE GLN LEU PRO ASP LEU GLN PRO
SEQRES 27 A 495 GLY SER SER ILE MET PRO GLY LYS VAL ASN PRO VAL LEU
SEQRES 28 A 495 PRO GLU ALA VAL THR GLN VAL ALA ALA GLN VAL ILE GLY
SEQRES 29 A 495 ASN ASP ALA ALA ILE ALA TRP GLY GLY ALA ASN GLY ALA
SEQRES 30 A 495 PHE GLU LEU ASN VAL TYR ILE PRO MET MET ALA ARG ASN
SEQRES 31 A 495 ILE LEU GLU SER PHE LYS LEU LEU THR ASN VAL SER ARG
SEQRES 32 A 495 LEU PHE ALA GLN ARG CYS ILE ALA GLY LEU THR ALA ASN
SEQRES 33 A 495 VAL GLU HIS LEU ARG ARG LEU ALA GLU SER SER PRO SER
SEQRES 34 A 495 ILE VAL THR PRO LEU ASN SER ALA ILE GLY TYR GLU GLU
SEQRES 35 A 495 ALA ALA ALA VAL ALA LYS GLN ALA LEU LYS GLU ARG LYS
SEQRES 36 A 495 THR ILE ARG GLN THR VAL ILE ASP ARG GLY LEU ILE GLY
SEQRES 37 A 495 ASP ARG LEU SER ILE GLU ASP LEU ASP ARG ARG LEU ASP
SEQRES 38 A 495 VAL LEU ALA MET ALA LYS ALA GLU GLN LEU ASP SER ASP
SEQRES 39 A 495 ARG
SEQRES 1 B 495 MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER
SEQRES 2 B 495 THR SER LEU TYR LYS LYS ALA GLY SER MET ALA VAL ASP
SEQRES 3 B 495 ALA ASP SER ALA ASN TYR ARG ILE GLU HIS ASP THR MET
SEQRES 4 B 495 GLY GLU VAL ARG VAL PRO ALA LYS ALA LEU TRP ARG ALA
SEQRES 5 B 495 GLN THR GLN ARG ALA VAL GLU ASN PHE PRO ILE SER GLY
SEQRES 6 B 495 ARG GLY LEU GLU ARG THR GLN ILE ARG ALA LEU GLY LEU
SEQRES 7 B 495 LEU LYS GLY ALA CYS ALA GLN VAL ASN SER ASP LEU GLY
SEQRES 8 B 495 LEU LEU ALA PRO GLU LYS ALA ASP ALA ILE ILE ALA ALA
SEQRES 9 B 495 ALA ALA GLU ILE ALA ASP GLY GLN HIS ASP ASP GLN PHE
SEQRES 10 B 495 PRO ILE ASP VAL PHE GLN THR GLY SER GLY THR SER SER
SEQRES 11 B 495 ASN MET ASN THR ASN GLU VAL ILE ALA SER ILE ALA ALA
SEQRES 12 B 495 LYS GLY GLY VAL THR LEU HIS PRO ASN ASP ASP VAL ASN
SEQRES 13 B 495 MET SER GLN SER SER ASN ASP THR PHE PRO THR ALA THR
SEQRES 14 B 495 HIS ILE ALA ALA THR GLU ALA ALA VAL ALA HIS LEU ILE
SEQRES 15 B 495 PRO ALA LEU GLN GLN LEU HIS ASP ALA LEU ALA ALA LYS
SEQRES 16 B 495 ALA LEU ASP TRP HIS THR VAL VAL LYS SER GLY ARG THR
SEQRES 17 B 495 HIS LEU MET ASP ALA VAL PRO VAL THR LEU GLY GLN GLU
SEQRES 18 B 495 PHE SER GLY TYR ALA ARG GLN ILE GLU ALA GLY ILE GLU
SEQRES 19 B 495 ARG VAL ARG ALA CYS LEU PRO ARG LEU GLY GLU LEU ALA
SEQRES 20 B 495 ILE GLY GLY THR ALA VAL GLY THR GLY LEU ASN ALA PRO
SEQRES 21 B 495 ASP ASP PHE GLY VAL ARG VAL VAL ALA VAL LEU VAL ALA
SEQRES 22 B 495 GLN THR GLY LEU SER GLU LEU ARG THR ALA ALA ASN SER
SEQRES 23 B 495 PHE GLU ALA GLN ALA ALA ARG ASP GLY LEU VAL GLU ALA
SEQRES 24 B 495 SER GLY ALA LEU ARG THR ILE ALA VAL SER LEU THR LYS
SEQRES 25 B 495 ILE ALA ASN ASP ILE ARG TRP MET GLY SER GLY PRO LEU
SEQRES 26 B 495 THR GLY LEU ALA GLU ILE GLN LEU PRO ASP LEU GLN PRO
SEQRES 27 B 495 GLY SER SER ILE MET PRO GLY LYS VAL ASN PRO VAL LEU
SEQRES 28 B 495 PRO GLU ALA VAL THR GLN VAL ALA ALA GLN VAL ILE GLY
SEQRES 29 B 495 ASN ASP ALA ALA ILE ALA TRP GLY GLY ALA ASN GLY ALA
SEQRES 30 B 495 PHE GLU LEU ASN VAL TYR ILE PRO MET MET ALA ARG ASN
SEQRES 31 B 495 ILE LEU GLU SER PHE LYS LEU LEU THR ASN VAL SER ARG
SEQRES 32 B 495 LEU PHE ALA GLN ARG CYS ILE ALA GLY LEU THR ALA ASN
SEQRES 33 B 495 VAL GLU HIS LEU ARG ARG LEU ALA GLU SER SER PRO SER
SEQRES 34 B 495 ILE VAL THR PRO LEU ASN SER ALA ILE GLY TYR GLU GLU
SEQRES 35 B 495 ALA ALA ALA VAL ALA LYS GLN ALA LEU LYS GLU ARG LYS
SEQRES 36 B 495 THR ILE ARG GLN THR VAL ILE ASP ARG GLY LEU ILE GLY
SEQRES 37 B 495 ASP ARG LEU SER ILE GLU ASP LEU ASP ARG ARG LEU ASP
SEQRES 38 B 495 VAL LEU ALA MET ALA LYS ALA GLU GLN LEU ASP SER ASP
SEQRES 39 B 495 ARG
SEQRES 1 C 495 MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER
SEQRES 2 C 495 THR SER LEU TYR LYS LYS ALA GLY SER MET ALA VAL ASP
SEQRES 3 C 495 ALA ASP SER ALA ASN TYR ARG ILE GLU HIS ASP THR MET
SEQRES 4 C 495 GLY GLU VAL ARG VAL PRO ALA LYS ALA LEU TRP ARG ALA
SEQRES 5 C 495 GLN THR GLN ARG ALA VAL GLU ASN PHE PRO ILE SER GLY
SEQRES 6 C 495 ARG GLY LEU GLU ARG THR GLN ILE ARG ALA LEU GLY LEU
SEQRES 7 C 495 LEU LYS GLY ALA CYS ALA GLN VAL ASN SER ASP LEU GLY
SEQRES 8 C 495 LEU LEU ALA PRO GLU LYS ALA ASP ALA ILE ILE ALA ALA
SEQRES 9 C 495 ALA ALA GLU ILE ALA ASP GLY GLN HIS ASP ASP GLN PHE
SEQRES 10 C 495 PRO ILE ASP VAL PHE GLN THR GLY SER GLY THR SER SER
SEQRES 11 C 495 ASN MET ASN THR ASN GLU VAL ILE ALA SER ILE ALA ALA
SEQRES 12 C 495 LYS GLY GLY VAL THR LEU HIS PRO ASN ASP ASP VAL ASN
SEQRES 13 C 495 MET SER GLN SER SER ASN ASP THR PHE PRO THR ALA THR
SEQRES 14 C 495 HIS ILE ALA ALA THR GLU ALA ALA VAL ALA HIS LEU ILE
SEQRES 15 C 495 PRO ALA LEU GLN GLN LEU HIS ASP ALA LEU ALA ALA LYS
SEQRES 16 C 495 ALA LEU ASP TRP HIS THR VAL VAL LYS SER GLY ARG THR
SEQRES 17 C 495 HIS LEU MET ASP ALA VAL PRO VAL THR LEU GLY GLN GLU
SEQRES 18 C 495 PHE SER GLY TYR ALA ARG GLN ILE GLU ALA GLY ILE GLU
SEQRES 19 C 495 ARG VAL ARG ALA CYS LEU PRO ARG LEU GLY GLU LEU ALA
SEQRES 20 C 495 ILE GLY GLY THR ALA VAL GLY THR GLY LEU ASN ALA PRO
SEQRES 21 C 495 ASP ASP PHE GLY VAL ARG VAL VAL ALA VAL LEU VAL ALA
SEQRES 22 C 495 GLN THR GLY LEU SER GLU LEU ARG THR ALA ALA ASN SER
SEQRES 23 C 495 PHE GLU ALA GLN ALA ALA ARG ASP GLY LEU VAL GLU ALA
SEQRES 24 C 495 SER GLY ALA LEU ARG THR ILE ALA VAL SER LEU THR LYS
SEQRES 25 C 495 ILE ALA ASN ASP ILE ARG TRP MET GLY SER GLY PRO LEU
SEQRES 26 C 495 THR GLY LEU ALA GLU ILE GLN LEU PRO ASP LEU GLN PRO
SEQRES 27 C 495 GLY SER SER ILE MET PRO GLY LYS VAL ASN PRO VAL LEU
SEQRES 28 C 495 PRO GLU ALA VAL THR GLN VAL ALA ALA GLN VAL ILE GLY
SEQRES 29 C 495 ASN ASP ALA ALA ILE ALA TRP GLY GLY ALA ASN GLY ALA
SEQRES 30 C 495 PHE GLU LEU ASN VAL TYR ILE PRO MET MET ALA ARG ASN
SEQRES 31 C 495 ILE LEU GLU SER PHE LYS LEU LEU THR ASN VAL SER ARG
SEQRES 32 C 495 LEU PHE ALA GLN ARG CYS ILE ALA GLY LEU THR ALA ASN
SEQRES 33 C 495 VAL GLU HIS LEU ARG ARG LEU ALA GLU SER SER PRO SER
SEQRES 34 C 495 ILE VAL THR PRO LEU ASN SER ALA ILE GLY TYR GLU GLU
SEQRES 35 C 495 ALA ALA ALA VAL ALA LYS GLN ALA LEU LYS GLU ARG LYS
SEQRES 36 C 495 THR ILE ARG GLN THR VAL ILE ASP ARG GLY LEU ILE GLY
SEQRES 37 C 495 ASP ARG LEU SER ILE GLU ASP LEU ASP ARG ARG LEU ASP
SEQRES 38 C 495 VAL LEU ALA MET ALA LYS ALA GLU GLN LEU ASP SER ASP
SEQRES 39 C 495 ARG
SEQRES 1 D 495 MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER
SEQRES 2 D 495 THR SER LEU TYR LYS LYS ALA GLY SER MET ALA VAL ASP
SEQRES 3 D 495 ALA ASP SER ALA ASN TYR ARG ILE GLU HIS ASP THR MET
SEQRES 4 D 495 GLY GLU VAL ARG VAL PRO ALA LYS ALA LEU TRP ARG ALA
SEQRES 5 D 495 GLN THR GLN ARG ALA VAL GLU ASN PHE PRO ILE SER GLY
SEQRES 6 D 495 ARG GLY LEU GLU ARG THR GLN ILE ARG ALA LEU GLY LEU
SEQRES 7 D 495 LEU LYS GLY ALA CYS ALA GLN VAL ASN SER ASP LEU GLY
SEQRES 8 D 495 LEU LEU ALA PRO GLU LYS ALA ASP ALA ILE ILE ALA ALA
SEQRES 9 D 495 ALA ALA GLU ILE ALA ASP GLY GLN HIS ASP ASP GLN PHE
SEQRES 10 D 495 PRO ILE ASP VAL PHE GLN THR GLY SER GLY THR SER SER
SEQRES 11 D 495 ASN MET ASN THR ASN GLU VAL ILE ALA SER ILE ALA ALA
SEQRES 12 D 495 LYS GLY GLY VAL THR LEU HIS PRO ASN ASP ASP VAL ASN
SEQRES 13 D 495 MET SER GLN SER SER ASN ASP THR PHE PRO THR ALA THR
SEQRES 14 D 495 HIS ILE ALA ALA THR GLU ALA ALA VAL ALA HIS LEU ILE
SEQRES 15 D 495 PRO ALA LEU GLN GLN LEU HIS ASP ALA LEU ALA ALA LYS
SEQRES 16 D 495 ALA LEU ASP TRP HIS THR VAL VAL LYS SER GLY ARG THR
SEQRES 17 D 495 HIS LEU MET ASP ALA VAL PRO VAL THR LEU GLY GLN GLU
SEQRES 18 D 495 PHE SER GLY TYR ALA ARG GLN ILE GLU ALA GLY ILE GLU
SEQRES 19 D 495 ARG VAL ARG ALA CYS LEU PRO ARG LEU GLY GLU LEU ALA
SEQRES 20 D 495 ILE GLY GLY THR ALA VAL GLY THR GLY LEU ASN ALA PRO
SEQRES 21 D 495 ASP ASP PHE GLY VAL ARG VAL VAL ALA VAL LEU VAL ALA
SEQRES 22 D 495 GLN THR GLY LEU SER GLU LEU ARG THR ALA ALA ASN SER
SEQRES 23 D 495 PHE GLU ALA GLN ALA ALA ARG ASP GLY LEU VAL GLU ALA
SEQRES 24 D 495 SER GLY ALA LEU ARG THR ILE ALA VAL SER LEU THR LYS
SEQRES 25 D 495 ILE ALA ASN ASP ILE ARG TRP MET GLY SER GLY PRO LEU
SEQRES 26 D 495 THR GLY LEU ALA GLU ILE GLN LEU PRO ASP LEU GLN PRO
SEQRES 27 D 495 GLY SER SER ILE MET PRO GLY LYS VAL ASN PRO VAL LEU
SEQRES 28 D 495 PRO GLU ALA VAL THR GLN VAL ALA ALA GLN VAL ILE GLY
SEQRES 29 D 495 ASN ASP ALA ALA ILE ALA TRP GLY GLY ALA ASN GLY ALA
SEQRES 30 D 495 PHE GLU LEU ASN VAL TYR ILE PRO MET MET ALA ARG ASN
SEQRES 31 D 495 ILE LEU GLU SER PHE LYS LEU LEU THR ASN VAL SER ARG
SEQRES 32 D 495 LEU PHE ALA GLN ARG CYS ILE ALA GLY LEU THR ALA ASN
SEQRES 33 D 495 VAL GLU HIS LEU ARG ARG LEU ALA GLU SER SER PRO SER
SEQRES 34 D 495 ILE VAL THR PRO LEU ASN SER ALA ILE GLY TYR GLU GLU
SEQRES 35 D 495 ALA ALA ALA VAL ALA LYS GLN ALA LEU LYS GLU ARG LYS
SEQRES 36 D 495 THR ILE ARG GLN THR VAL ILE ASP ARG GLY LEU ILE GLY
SEQRES 37 D 495 ASP ARG LEU SER ILE GLU ASP LEU ASP ARG ARG LEU ASP
SEQRES 38 D 495 VAL LEU ALA MET ALA LYS ALA GLU GLN LEU ASP SER ASP
SEQRES 39 D 495 ARG
HET GOL A1468 6
HET GOL B1467 6
HET SRT C1466 10
HET SRT D1466 10
HETNAM GOL GLYCEROL
HETNAM SRT S,R MESO-TARTARIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 7 SRT 2(C4 H6 O6)
FORMUL 9 HOH *1689(H2 O)
HELIX 1 1 ARG A 29 PHE A 39 1 11
HELIX 2 2 GLU A 47 LEU A 68 1 22
HELIX 3 3 ALA A 72 ASP A 88 1 17
HELIX 4 4 HIS A 91 PHE A 95 5 5
HELIX 5 5 GLY A 105 GLY A 123 1 19
HELIX 6 6 SER A 138 HIS A 158 1 21
HELIX 7 7 HIS A 158 TRP A 177 1 20
HELIX 8 8 LEU A 196 GLY A 222 1 27
HELIX 9 9 ASP A 240 GLY A 254 1 15
HELIX 10 10 PHE A 265 ALA A 270 1 6
HELIX 11 11 ARG A 271 GLY A 299 1 29
HELIX 12 12 PRO A 327 ASN A 353 1 27
HELIX 13 13 TYR A 361 CYS A 387 1 27
HELIX 14 14 ILE A 388 LEU A 391 5 4
HELIX 15 15 ASN A 394 SER A 405 1 12
HELIX 16 16 PRO A 406 PRO A 411 5 6
HELIX 17 17 LEU A 412 GLY A 417 1 6
HELIX 18 18 GLY A 417 ARG A 432 1 16
HELIX 19 19 THR A 434 ARG A 442 1 9
HELIX 20 20 SER A 450 LEU A 458 1 9
HELIX 21 21 ASP A 459 ALA A 464 1 6
HELIX 22 22 ARG B 29 PHE B 39 1 11
HELIX 23 23 GLU B 47 LEU B 68 1 22
HELIX 24 24 ALA B 72 ASP B 88 1 17
HELIX 25 25 HIS B 91 PHE B 95 5 5
HELIX 26 26 GLY B 105 GLY B 123 1 19
HELIX 27 27 SER B 138 HIS B 158 1 21
HELIX 28 28 HIS B 158 TRP B 177 1 20
HELIX 29 29 LEU B 196 GLY B 222 1 27
HELIX 30 30 ASP B 240 GLY B 254 1 15
HELIX 31 31 PHE B 265 ALA B 270 1 6
HELIX 32 32 ARG B 271 GLY B 299 1 29
HELIX 33 33 PRO B 327 ASN B 353 1 27
HELIX 34 34 TYR B 361 CYS B 387 1 27
HELIX 35 35 ILE B 388 LEU B 391 5 4
HELIX 36 36 ASN B 394 SER B 405 1 12
HELIX 37 37 PRO B 406 PRO B 411 5 6
HELIX 38 38 LEU B 412 GLY B 417 1 6
HELIX 39 39 GLY B 417 ARG B 432 1 16
HELIX 40 40 THR B 434 ARG B 442 1 9
HELIX 41 41 SER B 450 LEU B 458 1 9
HELIX 42 42 ASP B 459 ALA B 464 1 6
HELIX 43 43 ARG C 29 PHE C 39 1 11
HELIX 44 44 GLU C 47 LEU C 68 1 22
HELIX 45 45 ALA C 72 ASP C 88 1 17
HELIX 46 46 HIS C 91 PHE C 95 5 5
HELIX 47 47 GLY C 105 GLY C 123 1 19
HELIX 48 48 HIS C 128 ASN C 134 1 7
HELIX 49 49 SER C 138 HIS C 158 1 21
HELIX 50 50 HIS C 158 TRP C 177 1 20
HELIX 51 51 LEU C 196 GLY C 222 1 27
HELIX 52 52 ASP C 240 GLY C 254 1 15
HELIX 53 53 PHE C 265 ALA C 270 1 6
HELIX 54 54 ARG C 271 GLY C 299 1 29
HELIX 55 55 PRO C 327 ASN C 353 1 27
HELIX 56 56 TYR C 361 CYS C 387 1 27
HELIX 57 57 ILE C 388 LEU C 391 5 4
HELIX 58 58 ASN C 394 SER C 404 1 11
HELIX 59 59 SER C 405 VAL C 409 5 5
HELIX 60 60 VAL C 409 PRO C 411 5 3
HELIX 61 61 LEU C 412 GLY C 417 1 6
HELIX 62 62 GLY C 417 ARG C 432 1 16
HELIX 63 63 THR C 434 ARG C 442 1 9
HELIX 64 64 SER C 450 LEU C 458 1 9
HELIX 65 65 ASP C 459 ALA C 464 1 6
HELIX 66 66 ARG D 29 PHE D 39 1 11
HELIX 67 67 GLU D 47 LEU D 68 1 22
HELIX 68 68 ALA D 72 ASP D 88 1 17
HELIX 69 69 HIS D 91 PHE D 95 5 5
HELIX 70 70 GLY D 105 GLY D 123 1 19
HELIX 71 71 HIS D 128 ASN D 134 1 7
HELIX 72 72 SER D 138 HIS D 158 1 21
HELIX 73 73 HIS D 158 TRP D 177 1 20
HELIX 74 74 LEU D 196 GLY D 222 1 27
HELIX 75 75 ASP D 240 GLY D 254 1 15
HELIX 76 76 PHE D 265 ALA D 270 1 6
HELIX 77 77 ARG D 271 GLY D 299 1 29
HELIX 78 78 PRO D 327 ASN D 353 1 27
HELIX 79 79 TYR D 361 CYS D 387 1 27
HELIX 80 80 ILE D 388 LEU D 391 5 4
HELIX 81 81 ASN D 394 SER D 404 1 11
HELIX 82 82 SER D 405 VAL D 409 5 5
HELIX 83 83 VAL D 409 PRO D 411 5 3
HELIX 84 84 LEU D 412 GLY D 417 1 6
HELIX 85 85 GLY D 417 ARG D 432 1 16
HELIX 86 86 THR D 434 ARG D 442 1 9
HELIX 87 87 SER D 450 LEU D 458 1 9
HELIX 88 88 ASP D 459 ALA D 464 1 6
SHEET 1 AA 2 TYR A 10 ASP A 15 0
SHEET 2 AA 2 GLY A 18 PRO A 23 -1 O GLY A 18 N ASP A 15
SHEET 1 AB 2 VAL A 181 THR A 186 0
SHEET 2 AB 2 MET A 189 THR A 195 -1 O MET A 189 N THR A 186
SHEET 1 AC 2 GLU A 223 LEU A 224 0
SHEET 2 AC 2 ARG A 259 THR A 260 1 O ARG A 259 N LEU A 224
SHEET 1 AD 2 ILE A 309 GLN A 310 0
SHEET 2 AD 2 THR A 392 ALA A 393 -1 O THR A 392 N GLN A 310
SHEET 1 BA 2 TYR B 10 ASP B 15 0
SHEET 2 BA 2 GLY B 18 PRO B 23 -1 O GLY B 18 N ASP B 15
SHEET 1 BB 2 VAL B 181 THR B 186 0
SHEET 2 BB 2 MET B 189 THR B 195 -1 O MET B 189 N THR B 186
SHEET 1 BC 2 GLU B 223 LEU B 224 0
SHEET 2 BC 2 ARG B 259 THR B 260 1 O ARG B 259 N LEU B 224
SHEET 1 BD 2 ILE B 309 GLN B 310 0
SHEET 2 BD 2 THR B 392 ALA B 393 -1 O THR B 392 N GLN B 310
SHEET 1 CA 2 ARG C 11 HIS C 14 0
SHEET 2 CA 2 GLU C 19 VAL C 22 -1 O VAL C 20 N GLU C 13
SHEET 1 CB 2 VAL C 181 THR C 186 0
SHEET 2 CB 2 MET C 189 THR C 195 -1 O MET C 189 N THR C 186
SHEET 1 CC 2 GLU C 223 LEU C 224 0
SHEET 2 CC 2 ARG C 259 THR C 260 1 O ARG C 259 N LEU C 224
SHEET 1 CD 2 ILE C 309 GLN C 310 0
SHEET 2 CD 2 THR C 392 ALA C 393 -1 O THR C 392 N GLN C 310
SHEET 1 DA 2 ARG D 11 GLU D 13 0
SHEET 2 DA 2 ARG D 21 PRO D 23 -1 O VAL D 22 N ILE D 12
SHEET 1 DB 2 VAL D 181 THR D 186 0
SHEET 2 DB 2 MET D 189 THR D 195 -1 O MET D 189 N THR D 186
SHEET 1 DC 2 GLU D 223 LEU D 224 0
SHEET 2 DC 2 ARG D 259 THR D 260 1 O ARG D 259 N LEU D 224
SHEET 1 DD 2 ILE D 309 GLN D 310 0
SHEET 2 DD 2 THR D 392 ALA D 393 -1 O THR D 392 N GLN D 310
CISPEP 1 GLY A 301 PRO A 302 0 8.11
CISPEP 2 GLY B 301 PRO B 302 0 7.59
CISPEP 3 GLY C 301 PRO C 302 0 9.73
CISPEP 4 GLY D 301 PRO D 302 0 8.85
SITE 1 AC1 14 THR A 186 HIS A 187 SER B 104 THR B 106
SITE 2 AC1 14 SER B 138 SER B 139 ASN B 140 GLY D 317
SITE 3 AC1 14 SER D 318 SER D 319 ILE D 320 MET D 321
SITE 4 AC1 14 LYS D 324 ASN D 326
SITE 1 AC2 14 SER A 104 THR A 106 SER A 138 SER A 139
SITE 2 AC2 14 ASN A 140 THR B 186 HIS B 187 GLY C 317
SITE 3 AC2 14 SER C 318 SER C 319 ILE C 320 MET C 321
SITE 4 AC2 14 LYS C 324 ASN C 326
SITE 1 AC3 9 SER B 404 PRO B 406 ALA B 428 LEU B 429
SITE 2 AC3 9 LYS B 433 HOH B2356 HOH B2375 HOH B2411
SITE 3 AC3 9 LEU C 303
SITE 1 AC4 8 SER A 404 SER A 405 PRO A 406 ALA A 428
SITE 2 AC4 8 LYS A 433 HOH A2454 HOH A2517 LEU D 303
CRYST1 188.940 96.490 139.650 90.00 112.44 90.00 C 1 2 1 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.005293 0.000000 0.002186 0.00000
SCALE2 0.000000 0.010364 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007747 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
