HEADER LYASE 11-JUN-09 2WKJ
TITLE CRYSTAL STRUCTURE OF THE E192N MUTANT OF E. COLI N-ACETYLNEURAMINIC
TITLE 2 ACID LYASE IN COMPLEX WITH PYRUVATE AT 1.45A RESOLUTION IN SPACE
TITLE 3 GROUP P212121
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N-ACETYLNEURAMINATE LYASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 2-296;
COMPND 5 SYNONYM: N-ACETYLNEURAMINIC ACID, N-ACETYLNEURAMINIC ACID ALDOLASE,
COMPND 6 N-ACETYLNEURAMINATE PYRUVATE-LYASE, SIALIC ACID LYASE, SIALATE LYASE,
COMPND 7 SIALIC ACID ALDOLASE, NALASE;
COMPND 8 EC: 4.1.3.3;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES;
COMPND 11 OTHER_DETAILS: SCHIFF BASE BETWEEN K165 AND PYRUVATE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: EP-MAX 10B COMPETENT CELLS;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PKKK223-3
KEYWDS DIRECTED EVOLUTION, SIALIC ACID MIMETICS, LYASE, ALDOLASE, SCHIFF
KEYWDS 2 BASE, CARBOHYDRATE METABOLISM, N-ACETYLNEURAMINIC ACID LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.CAMPEOTTO,S.B.CARR,C.H.TRINH,A.S.NELSON,A.BERRY,S.E.V.PHILLIPS,
AUTHOR 2 A.R.PEARSON
REVDAT 6 13-DEC-23 2WKJ 1 REMARK
REVDAT 5 29-NOV-23 2WKJ 1 REMARK
REVDAT 4 15-NOV-23 2WKJ 1 REMARK LINK ATOM
REVDAT 3 19-DEC-18 2WKJ 1 JRNL REMARK LINK
REVDAT 2 13-JUL-11 2WKJ 1 VERSN
REVDAT 1 01-DEC-09 2WKJ 0
JRNL AUTH I.CAMPEOTTO,S.B.CARR,C.H.TRINH,A.S.NELSON,A.BERRY,
JRNL AUTH 2 S.E.PHILLIPS,A.R.PEARSON
JRNL TITL STRUCTURE OF AN ESCHERICHIA COLI N-ACETYL-D-NEURAMINIC ACID
JRNL TITL 2 LYASE MUTANT, E192N, IN COMPLEX WITH PYRUVATE AT 1.45
JRNL TITL 3 ANGSTROM RESOLUTION.
JRNL REF ACTA CRYSTALLOGR. SECT. F V. 65 1088 2009
JRNL REF 2 STRUCT. BIOL. CRYST. COMMUN.
JRNL REFN ESSN 1744-3091
JRNL PMID 19923724
JRNL DOI 10.1107/S1744309109037403
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0066
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 87.33
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 202361
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 10718
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 13091
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.63
REMARK 3 BIN R VALUE (WORKING SET) : 0.2770
REMARK 3 BIN FREE R VALUE SET COUNT : 699
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9188
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 1307
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 14.33
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.94000
REMARK 3 B22 (A**2) : 1.13000
REMARK 3 B33 (A**2) : -0.18000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.064
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.065
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.040
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.266
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9553 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 8830 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12960 ; 1.346 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 20516 ; 1.268 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1235 ; 5.592 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 423 ;38.548 ;24.846
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1668 ;12.148 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 49 ;20.164 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1470 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10718 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1841 ; 0.000 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5971 ; 0.592 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2477 ; 0.199 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9597 ; 0.984 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3582 ; 1.879 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3340 ; 2.899 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 32
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -1 A 6
REMARK 3 ORIGIN FOR THE GROUP (A): 28.0410 -10.5670 21.0650
REMARK 3 T TENSOR
REMARK 3 T11: 0.3284 T22: 0.7746
REMARK 3 T33: 0.7399 T12: -0.1050
REMARK 3 T13: -0.0378 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 22.3476 L22: 3.0358
REMARK 3 L33: 0.1395 L12: 8.1919
REMARK 3 L13: -1.7527 L23: -0.6454
REMARK 3 S TENSOR
REMARK 3 S11: 0.6532 S12: -2.5146 S13: -2.2481
REMARK 3 S21: 0.2022 S22: -0.8544 S23: -0.9489
REMARK 3 S31: -0.0686 S32: 0.1963 S33: 0.2012
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 7 A 33
REMARK 3 ORIGIN FOR THE GROUP (A): 4.4880 -20.0520 31.5370
REMARK 3 T TENSOR
REMARK 3 T11: 0.1511 T22: 0.0744
REMARK 3 T33: 0.0252 T12: 0.0015
REMARK 3 T13: 0.0036 T23: 0.0369
REMARK 3 L TENSOR
REMARK 3 L11: 2.0519 L22: 1.3519
REMARK 3 L33: 0.8724 L12: -0.2162
REMARK 3 L13: 0.0383 L23: -0.3293
REMARK 3 S TENSOR
REMARK 3 S11: -0.0533 S12: -0.1702 S13: -0.1302
REMARK 3 S21: 0.1178 S22: 0.0462 S23: 0.0881
REMARK 3 S31: 0.0698 S32: -0.0406 S33: 0.0071
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 34 A 75
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6580 -14.7740 31.1820
REMARK 3 T TENSOR
REMARK 3 T11: 0.1283 T22: 0.0902
REMARK 3 T33: 0.0101 T12: 0.0004
REMARK 3 T13: -0.0003 T23: 0.0283
REMARK 3 L TENSOR
REMARK 3 L11: 1.1432 L22: 1.0270
REMARK 3 L33: 0.9338 L12: 0.0102
REMARK 3 L13: 0.0556 L23: 0.0793
REMARK 3 S TENSOR
REMARK 3 S11: -0.0218 S12: -0.1717 S13: -0.0241
REMARK 3 S21: 0.0870 S22: 0.0016 S23: -0.0080
REMARK 3 S31: 0.0666 S32: 0.0517 S33: 0.0202
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 76 A 145
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8760 -0.2480 25.2510
REMARK 3 T TENSOR
REMARK 3 T11: 0.1108 T22: 0.0761
REMARK 3 T33: 0.0061 T12: -0.0112
REMARK 3 T13: -0.0097 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 0.4917 L22: 0.4871
REMARK 3 L33: 0.4715 L12: -0.0878
REMARK 3 L13: -0.1034 L23: 0.1679
REMARK 3 S TENSOR
REMARK 3 S11: -0.0032 S12: -0.0558 S13: 0.0408
REMARK 3 S21: 0.0139 S22: 0.0072 S23: -0.0363
REMARK 3 S31: -0.0568 S32: 0.0723 S33: -0.0040
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 146 A 214
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3260 -8.8190 11.6890
REMARK 3 T TENSOR
REMARK 3 T11: 0.1165 T22: 0.0696
REMARK 3 T33: 0.0036 T12: -0.0180
REMARK 3 T13: -0.0036 T23: 0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.4434 L22: 0.4544
REMARK 3 L33: 0.5177 L12: 0.0077
REMARK 3 L13: -0.2477 L23: -0.0290
REMARK 3 S TENSOR
REMARK 3 S11: 0.0039 S12: -0.0467 S13: -0.0077
REMARK 3 S21: 0.0016 S22: -0.0149 S23: -0.0277
REMARK 3 S31: -0.0398 S32: 0.0993 S33: 0.0110
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 215 A 236
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3030 -27.1540 9.5020
REMARK 3 T TENSOR
REMARK 3 T11: 0.1421 T22: 0.1038
REMARK 3 T33: 0.0453 T12: 0.0394
REMARK 3 T13: 0.0341 T23: 0.0244
REMARK 3 L TENSOR
REMARK 3 L11: 3.9926 L22: 2.4239
REMARK 3 L33: 3.8924 L12: -1.0512
REMARK 3 L13: 1.2384 L23: -0.3269
REMARK 3 S TENSOR
REMARK 3 S11: -0.0835 S12: 0.2179 S13: -0.2659
REMARK 3 S21: -0.1151 S22: -0.0311 S23: -0.0732
REMARK 3 S31: 0.2748 S32: 0.5119 S33: 0.1146
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 237 A 277
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8910 -22.6630 20.0820
REMARK 3 T TENSOR
REMARK 3 T11: 0.1303 T22: 0.0336
REMARK 3 T33: 0.0479 T12: -0.0160
REMARK 3 T13: 0.0067 T23: 0.0298
REMARK 3 L TENSOR
REMARK 3 L11: 1.0514 L22: 0.3447
REMARK 3 L33: 1.3914 L12: -0.0374
REMARK 3 L13: -0.3708 L23: 0.1382
REMARK 3 S TENSOR
REMARK 3 S11: -0.0433 S12: -0.0462 S13: -0.1239
REMARK 3 S21: 0.0247 S22: -0.0224 S23: 0.0360
REMARK 3 S31: 0.0862 S32: -0.0579 S33: 0.0657
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 278 A 296
REMARK 3 ORIGIN FOR THE GROUP (A): -0.0130 -31.9990 18.1480
REMARK 3 T TENSOR
REMARK 3 T11: 0.1613 T22: 0.0135
REMARK 3 T33: 0.1110 T12: -0.0241
REMARK 3 T13: 0.0714 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 7.6420 L22: 6.8020
REMARK 3 L33: 3.1351 L12: -0.5661
REMARK 3 L13: 1.1033 L23: -1.7172
REMARK 3 S TENSOR
REMARK 3 S11: -0.1637 S12: -0.0022 S13: -0.4852
REMARK 3 S21: -0.1905 S22: -0.0243 S23: -0.4705
REMARK 3 S31: 0.3724 S32: 0.0446 S33: 0.1880
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -1 B 16
REMARK 3 ORIGIN FOR THE GROUP (A): -13.9370 17.8840 -18.3860
REMARK 3 T TENSOR
REMARK 3 T11: 0.2011 T22: 0.1537
REMARK 3 T33: 0.0940 T12: 0.0505
REMARK 3 T13: -0.0050 T23: 0.0753
REMARK 3 L TENSOR
REMARK 3 L11: 0.5422 L22: 1.6722
REMARK 3 L33: 2.4050 L12: 0.2109
REMARK 3 L13: 0.6381 L23: 1.5281
REMARK 3 S TENSOR
REMARK 3 S11: -0.0040 S12: 0.1324 S13: 0.1689
REMARK 3 S21: -0.1682 S22: -0.0470 S23: -0.0804
REMARK 3 S31: -0.3992 S32: -0.1408 S33: 0.0509
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 17 B 37
REMARK 3 ORIGIN FOR THE GROUP (A): -21.6080 5.8250 -28.0220
REMARK 3 T TENSOR
REMARK 3 T11: 0.0980 T22: 0.2053
REMARK 3 T33: 0.0525 T12: 0.0146
REMARK 3 T13: -0.0266 T23: 0.0624
REMARK 3 L TENSOR
REMARK 3 L11: 1.4795 L22: 3.6663
REMARK 3 L33: 1.7624 L12: -0.2029
REMARK 3 L13: -0.5431 L23: 0.6469
REMARK 3 S TENSOR
REMARK 3 S11: 0.0422 S12: 0.2199 S13: 0.1172
REMARK 3 S21: -0.0828 S22: 0.0444 S23: 0.2949
REMARK 3 S31: 0.0124 S32: -0.2640 S33: -0.0867
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 38 B 115
REMARK 3 ORIGIN FOR THE GROUP (A): -6.5810 11.7640 -24.0990
REMARK 3 T TENSOR
REMARK 3 T11: 0.1018 T22: 0.0935
REMARK 3 T33: 0.0292 T12: 0.0227
REMARK 3 T13: 0.0021 T23: 0.0484
REMARK 3 L TENSOR
REMARK 3 L11: 1.1176 L22: 0.4336
REMARK 3 L33: 0.7333 L12: -0.2777
REMARK 3 L13: 0.1082 L23: -0.1099
REMARK 3 S TENSOR
REMARK 3 S11: 0.0244 S12: 0.1364 S13: 0.1070
REMARK 3 S21: -0.0534 S22: 0.0023 S23: -0.0234
REMARK 3 S31: -0.0900 S32: -0.0514 S33: -0.0267
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 116 B 132
REMARK 3 ORIGIN FOR THE GROUP (A): 5.0180 18.0840 -19.8830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1160 T22: 0.0796
REMARK 3 T33: 0.0904 T12: -0.0114
REMARK 3 T13: 0.0188 T23: 0.0479
REMARK 3 L TENSOR
REMARK 3 L11: 2.6257 L22: 2.6803
REMARK 3 L33: 4.2904 L12: -2.0605
REMARK 3 L13: 1.8265 L23: -1.7439
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: 0.1743 S13: 0.3614
REMARK 3 S21: -0.0248 S22: 0.0007 S23: -0.1995
REMARK 3 S31: -0.2675 S32: 0.2220 S33: -0.0049
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 133 B 223
REMARK 3 ORIGIN FOR THE GROUP (A): -10.0820 17.6870 -7.3470
REMARK 3 T TENSOR
REMARK 3 T11: 0.1205 T22: 0.0580
REMARK 3 T33: 0.0521 T12: 0.0239
REMARK 3 T13: -0.0037 T23: 0.0336
REMARK 3 L TENSOR
REMARK 3 L11: 0.5544 L22: 0.6229
REMARK 3 L33: 0.7487 L12: 0.2552
REMARK 3 L13: -0.2136 L23: 0.0860
REMARK 3 S TENSOR
REMARK 3 S11: 0.0134 S12: 0.0625 S13: 0.1456
REMARK 3 S21: 0.0096 S22: 0.0158 S23: 0.0165
REMARK 3 S31: -0.1234 S32: -0.0320 S33: -0.0292
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 224 B 246
REMARK 3 ORIGIN FOR THE GROUP (A): -26.8870 13.8330 -2.5810
REMARK 3 T TENSOR
REMARK 3 T11: 0.0985 T22: 0.1363
REMARK 3 T33: 0.0721 T12: 0.0537
REMARK 3 T13: 0.0103 T23: 0.0238
REMARK 3 L TENSOR
REMARK 3 L11: 1.6112 L22: 4.1713
REMARK 3 L33: 2.2367 L12: 0.2544
REMARK 3 L13: -0.5241 L23: 1.0213
REMARK 3 S TENSOR
REMARK 3 S11: 0.0856 S12: -0.0095 S13: 0.3029
REMARK 3 S21: 0.0360 S22: 0.0007 S23: 0.2066
REMARK 3 S31: -0.2307 S32: -0.3381 S33: -0.0863
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 247 B 278
REMARK 3 ORIGIN FOR THE GROUP (A): -21.4890 -2.3250 -18.6630
REMARK 3 T TENSOR
REMARK 3 T11: 0.0625 T22: 0.1229
REMARK 3 T33: 0.0204 T12: -0.0107
REMARK 3 T13: -0.0210 T23: 0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 1.8752 L22: 0.6225
REMARK 3 L33: 0.4647 L12: -0.5234
REMARK 3 L13: -0.3378 L23: 0.0343
REMARK 3 S TENSOR
REMARK 3 S11: 0.0149 S12: 0.1390 S13: -0.0832
REMARK 3 S21: 0.0001 S22: -0.0045 S23: 0.0828
REMARK 3 S31: 0.0605 S32: -0.0761 S33: -0.0104
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 279 B 296
REMARK 3 ORIGIN FOR THE GROUP (A): -32.1190 -0.2030 -13.3760
REMARK 3 T TENSOR
REMARK 3 T11: 0.0461 T22: 0.1355
REMARK 3 T33: 0.0340 T12: -0.0147
REMARK 3 T13: -0.0108 T23: 0.0255
REMARK 3 L TENSOR
REMARK 3 L11: 6.2013 L22: 3.9402
REMARK 3 L33: 2.0580 L12: -2.3049
REMARK 3 L13: 0.2212 L23: -0.5927
REMARK 3 S TENSOR
REMARK 3 S11: 0.0097 S12: 0.1492 S13: -0.0067
REMARK 3 S21: 0.0650 S22: -0.0875 S23: 0.0257
REMARK 3 S31: -0.0248 S32: -0.1307 S33: 0.0778
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C -1 C 6
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8360 -27.5390 -16.4710
REMARK 3 T TENSOR
REMARK 3 T11: 0.4544 T22: 0.1471
REMARK 3 T33: 0.2308 T12: 0.0033
REMARK 3 T13: -0.0778 T23: -0.0753
REMARK 3 L TENSOR
REMARK 3 L11: 9.6748 L22: 5.5028
REMARK 3 L33: 0.6138 L12: 6.8016
REMARK 3 L13: -2.3945 L23: -1.6256
REMARK 3 S TENSOR
REMARK 3 S11: -0.5242 S12: 0.5620 S13: -0.8357
REMARK 3 S21: -0.4721 S22: 0.3330 S23: -0.3853
REMARK 3 S31: 0.1977 S32: -0.1373 S33: 0.1913
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 7 C 33
REMARK 3 ORIGIN FOR THE GROUP (A): 19.2830 -4.0950 -26.7130
REMARK 3 T TENSOR
REMARK 3 T11: 0.0752 T22: 0.1049
REMARK 3 T33: 0.0068 T12: 0.0085
REMARK 3 T13: 0.0012 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 0.7227 L22: 2.6876
REMARK 3 L33: 1.4567 L12: 0.3640
REMARK 3 L13: -0.3684 L23: -0.7626
REMARK 3 S TENSOR
REMARK 3 S11: 0.0072 S12: 0.1357 S13: -0.0277
REMARK 3 S21: -0.0443 S22: 0.0245 S23: -0.0768
REMARK 3 S31: 0.0039 S32: 0.0602 S33: -0.0317
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 34 C 75
REMARK 3 ORIGIN FOR THE GROUP (A): 14.1790 -10.4620 -26.1470
REMARK 3 T TENSOR
REMARK 3 T11: 0.0918 T22: 0.0948
REMARK 3 T33: 0.0058 T12: 0.0137
REMARK 3 T13: 0.0050 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 0.9355 L22: 1.4572
REMARK 3 L33: 1.0445 L12: -0.1398
REMARK 3 L13: 0.0269 L23: 0.1018
REMARK 3 S TENSOR
REMARK 3 S11: 0.0001 S12: 0.1514 S13: -0.0323
REMARK 3 S21: -0.0496 S22: 0.0180 S23: -0.0749
REMARK 3 S31: 0.1259 S32: 0.0607 S33: -0.0181
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 76 C 145
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3660 -12.5400 -20.2140
REMARK 3 T TENSOR
REMARK 3 T11: 0.1008 T22: 0.0726
REMARK 3 T33: 0.0152 T12: -0.0098
REMARK 3 T13: -0.0118 T23: -0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.9152 L22: 0.3685
REMARK 3 L33: 0.5022 L12: -0.0417
REMARK 3 L13: 0.1722 L23: -0.2680
REMARK 3 S TENSOR
REMARK 3 S11: -0.0044 S12: 0.0974 S13: -0.0896
REMARK 3 S21: -0.0284 S22: 0.0361 S23: 0.0402
REMARK 3 S31: 0.1029 S32: -0.0654 S33: -0.0316
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 146 C 223
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9760 -17.9250 -7.3600
REMARK 3 T TENSOR
REMARK 3 T11: 0.1192 T22: 0.0391
REMARK 3 T33: 0.0078 T12: 0.0001
REMARK 3 T13: -0.0035 T23: -0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 0.6752 L22: 0.4601
REMARK 3 L33: 0.7629 L12: 0.1660
REMARK 3 L13: 0.1138 L23: -0.2738
REMARK 3 S TENSOR
REMARK 3 S11: 0.0051 S12: 0.0303 S13: -0.0581
REMARK 3 S21: -0.0331 S22: 0.0023 S23: 0.0116
REMARK 3 S31: 0.1200 S32: -0.0120 S33: -0.0074
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 224 C 247
REMARK 3 ORIGIN FOR THE GROUP (A): 26.4550 -12.6130 -3.3180
REMARK 3 T TENSOR
REMARK 3 T11: 0.0964 T22: 0.1009
REMARK 3 T33: 0.0182 T12: 0.0251
REMARK 3 T13: -0.0023 T23: 0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 0.8432 L22: 4.4960
REMARK 3 L33: 1.9413 L12: -0.0796
REMARK 3 L13: -0.1319 L23: -1.0119
REMARK 3 S TENSOR
REMARK 3 S11: -0.0198 S12: -0.0322 S13: -0.0799
REMARK 3 S21: 0.0331 S22: -0.0366 S23: -0.1654
REMARK 3 S31: 0.1278 S32: 0.2727 S33: 0.0564
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 248 C 285
REMARK 3 ORIGIN FOR THE GROUP (A): 22.8240 4.5560 -17.4520
REMARK 3 T TENSOR
REMARK 3 T11: 0.0800 T22: 0.0831
REMARK 3 T33: 0.0200 T12: -0.0062
REMARK 3 T13: 0.0012 T23: 0.0240
REMARK 3 L TENSOR
REMARK 3 L11: 1.6706 L22: 0.7332
REMARK 3 L33: 0.6337 L12: 0.0389
REMARK 3 L13: 0.2970 L23: -0.0369
REMARK 3 S TENSOR
REMARK 3 S11: -0.0067 S12: 0.0630 S13: 0.1231
REMARK 3 S21: 0.0164 S22: -0.0247 S23: -0.0691
REMARK 3 S31: -0.0435 S32: 0.0259 S33: 0.0314
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 286 C 296
REMARK 3 ORIGIN FOR THE GROUP (A): 34.6660 -4.0790 -14.4150
REMARK 3 T TENSOR
REMARK 3 T11: 0.0474 T22: 0.0863
REMARK 3 T33: 0.0554 T12: 0.0080
REMARK 3 T13: 0.0015 T23: 0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 7.1838 L22: 5.7144
REMARK 3 L33: 3.9253 L12: -0.2114
REMARK 3 L13: -0.6354 L23: -1.6611
REMARK 3 S TENSOR
REMARK 3 S11: -0.0542 S12: 0.1314 S13: -0.3357
REMARK 3 S21: -0.0682 S22: -0.0323 S23: -0.2855
REMARK 3 S31: 0.1650 S32: 0.1268 S33: 0.0865
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D -1 D 6
REMARK 3 ORIGIN FOR THE GROUP (A): -28.1130 9.9440 21.3260
REMARK 3 T TENSOR
REMARK 3 T11: 0.3154 T22: 0.9869
REMARK 3 T33: 0.7118 T12: -0.1533
REMARK 3 T13: 0.1840 T23: -0.1143
REMARK 3 L TENSOR
REMARK 3 L11: 10.2700 L22: 14.5219
REMARK 3 L33: 3.1665 L12: 9.2772
REMARK 3 L13: 3.3759 L23: 6.6022
REMARK 3 S TENSOR
REMARK 3 S11: 0.7038 S12: -1.9120 S13: 1.4758
REMARK 3 S21: 1.1198 S22: -2.0827 S23: 2.8764
REMARK 3 S31: 0.5314 S32: -0.8507 S33: 1.3789
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 7 D 33
REMARK 3 ORIGIN FOR THE GROUP (A): -4.8330 19.0230 32.2200
REMARK 3 T TENSOR
REMARK 3 T11: 0.2089 T22: 0.0999
REMARK 3 T33: 0.0454 T12: 0.0200
REMARK 3 T13: -0.0141 T23: -0.0619
REMARK 3 L TENSOR
REMARK 3 L11: 1.8174 L22: 1.1441
REMARK 3 L33: 0.7199 L12: 0.2144
REMARK 3 L13: -0.0244 L23: 0.4289
REMARK 3 S TENSOR
REMARK 3 S11: -0.1133 S12: -0.2188 S13: 0.1297
REMARK 3 S21: 0.1520 S22: 0.0575 S23: -0.0268
REMARK 3 S31: -0.1411 S32: -0.0051 S33: 0.0558
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 34 D 75
REMARK 3 ORIGIN FOR THE GROUP (A): -11.1190 13.8030 31.4850
REMARK 3 T TENSOR
REMARK 3 T11: 0.1618 T22: 0.0969
REMARK 3 T33: 0.0316 T12: 0.0171
REMARK 3 T13: -0.0029 T23: -0.0523
REMARK 3 L TENSOR
REMARK 3 L11: 1.4893 L22: 1.1834
REMARK 3 L33: 1.0444 L12: -0.1501
REMARK 3 L13: -0.0426 L23: -0.0969
REMARK 3 S TENSOR
REMARK 3 S11: -0.0523 S12: -0.1408 S13: 0.1084
REMARK 3 S21: 0.1301 S22: -0.0084 S23: 0.0419
REMARK 3 S31: -0.1407 S32: -0.0788 S33: 0.0607
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 76 D 145
REMARK 3 ORIGIN FOR THE GROUP (A): -13.1000 -0.5050 25.1890
REMARK 3 T TENSOR
REMARK 3 T11: 0.1067 T22: 0.0677
REMARK 3 T33: 0.0079 T12: 0.0015
REMARK 3 T13: 0.0142 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 0.5741 L22: 0.5966
REMARK 3 L33: 0.4685 L12: -0.1431
REMARK 3 L13: 0.3239 L23: -0.1328
REMARK 3 S TENSOR
REMARK 3 S11: 0.0177 S12: -0.0944 S13: -0.0138
REMARK 3 S21: 0.0234 S22: -0.0082 S23: 0.0557
REMARK 3 S31: -0.0216 S32: -0.1012 S33: -0.0095
REMARK 3
REMARK 3 TLS GROUP : 29
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 146 D 222
REMARK 3 ORIGIN FOR THE GROUP (A): -18.4370 11.1010 12.4990
REMARK 3 T TENSOR
REMARK 3 T11: 0.1125 T22: 0.0656
REMARK 3 T33: 0.0257 T12: 0.0176
REMARK 3 T13: 0.0073 T23: -0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 0.8732 L22: 0.5312
REMARK 3 L33: 0.6500 L12: 0.1491
REMARK 3 L13: 0.1757 L23: -0.2261
REMARK 3 S TENSOR
REMARK 3 S11: 0.0160 S12: -0.0439 S13: 0.1212
REMARK 3 S21: 0.0406 S22: -0.0067 S23: 0.0860
REMARK 3 S31: -0.0474 S32: -0.1159 S33: -0.0093
REMARK 3
REMARK 3 TLS GROUP : 30
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 223 D 245
REMARK 3 ORIGIN FOR THE GROUP (A): -14.5540 27.0830 8.3840
REMARK 3 T TENSOR
REMARK 3 T11: 0.1529 T22: 0.0273
REMARK 3 T33: 0.0876 T12: 0.0443
REMARK 3 T13: -0.0138 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 5.8831 L22: 2.2886
REMARK 3 L33: 2.4243 L12: -0.0638
REMARK 3 L13: 0.6590 L23: -0.8548
REMARK 3 S TENSOR
REMARK 3 S11: -0.0361 S12: 0.0713 S13: 0.3377
REMARK 3 S21: 0.0291 S22: 0.0187 S23: 0.2346
REMARK 3 S31: -0.3128 S32: -0.1904 S33: 0.0175
REMARK 3
REMARK 3 TLS GROUP : 31
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 246 D 277
REMARK 3 ORIGIN FOR THE GROUP (A): 2.3050 21.1250 24.0710
REMARK 3 T TENSOR
REMARK 3 T11: 0.1680 T22: 0.0506
REMARK 3 T33: 0.0953 T12: -0.0302
REMARK 3 T13: -0.0312 T23: -0.0236
REMARK 3 L TENSOR
REMARK 3 L11: 1.1838 L22: 0.9411
REMARK 3 L33: 1.3467 L12: -1.0499
REMARK 3 L13: 0.4509 L23: -0.3281
REMARK 3 S TENSOR
REMARK 3 S11: -0.0970 S12: 0.0057 S13: 0.2921
REMARK 3 S21: 0.0940 S22: -0.0131 S23: -0.2493
REMARK 3 S31: -0.1022 S32: 0.0959 S33: 0.1101
REMARK 3
REMARK 3 TLS GROUP : 32
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 278 D 295
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1050 31.5190 19.2250
REMARK 3 T TENSOR
REMARK 3 T11: 0.1199 T22: 0.0312
REMARK 3 T33: 0.1658 T12: -0.0361
REMARK 3 T13: -0.0165 T23: 0.0526
REMARK 3 L TENSOR
REMARK 3 L11: 10.9656 L22: 6.3592
REMARK 3 L33: 3.7416 L12: -6.6083
REMARK 3 L13: -0.9777 L23: 0.6997
REMARK 3 S TENSOR
REMARK 3 S11: 0.0036 S12: 0.3471 S13: 0.3687
REMARK 3 S21: -0.0835 S22: -0.2017 S23: -0.2342
REMARK 3 S31: -0.4621 S32: 0.1842 S33: 0.1980
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. RESIDUES 0 AND 1 HAVE BEEN MODELLED WITH CB ONLY.
REMARK 4
REMARK 4 2WKJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JUN-09.
REMARK 100 THE DEPOSITION ID IS D_1290039649.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9699
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 213226
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 63.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.38000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1NAL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS HCL, PH 8.2, 200MM AMMONIUM
REMARK 280 ACETATE, 18% PEG 3350
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 39.16450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.15450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.02450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.15450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.16450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.02450
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: 9660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.4 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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLU 192 TO ASN
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLU 192 TO ASN
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, GLU 192 TO ASN
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, GLU 192 TO ASN
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 -6
REMARK 465 GLU A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 MET B -6
REMARK 465 GLU B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 MET C -6
REMARK 465 GLU C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 MET D -6
REMARK 465 GLU D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
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 HIS A 0 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 1 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 296 CG CD NE CZ NH1 NH2
REMARK 470 HIS B 0 CG ND1 CD2 CE1 NE2
REMARK 470 HIS B 1 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 296 CG CD NE CZ NH1 NH2
REMARK 470 HIS C 0 CG ND1 CD2 CE1 NE2
REMARK 470 HIS C 1 CG ND1 CD2 CE1 NE2
REMARK 470 ARG C 296 CG CD NE CZ NH1 NH2
REMARK 470 HIS D 0 CG ND1 CD2 CE1 NE2
REMARK 470 HIS D 1 CG ND1 CD2 CE1 NE2
REMARK 470 ARG D 296 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 NH2 ARG C 28 O HOH C 2041 1.62
REMARK 500 O HOH A 2026 O HOH A 2047 1.72
REMARK 500 CE MET C 9 CD1 ILE C 77 1.95
REMARK 500 O HOH A 2067 O HOH A 2068 1.99
REMARK 500 O HOH C 2080 O HOH C 2131 2.01
REMARK 500 O HOH A 2045 O HOH A 2124 2.02
REMARK 500 O HOH C 2079 O HOH C 2080 2.05
REMARK 500 OD1 ASP B 150 O HOH B 2215 2.06
REMARK 500 O HOH C 2259 O HOH C 2274 2.10
REMARK 500 OE1 GLN D 37 O HOH D 2040 2.10
REMARK 500 O HOH D 2064 O HOH D 2105 2.13
REMARK 500 OD2 ASP B 150 O HOH B 2215 2.19
REMARK 500 CG GLN A 18 O HOH A 2022 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 NH2 ARG B 123 OE2 GLU D 226 4555 2.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP B 244 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP C 244 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP C 244 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR A 110 -74.24 70.53
REMARK 500 MET A 213 34.95 -151.68
REMARK 500 PRO A 268 35.41 -84.92
REMARK 500 TYR B 110 -74.25 70.04
REMARK 500 MET B 213 40.50 -153.45
REMARK 500 PRO B 268 35.55 -83.40
REMARK 500 ASN C 4 1.11 -67.68
REMARK 500 TYR C 110 -75.65 71.27
REMARK 500 MET C 213 39.11 -155.06
REMARK 500 PRO C 268 35.72 -88.09
REMARK 500 ASN D 4 0.85 -64.91
REMARK 500 TYR D 110 -75.04 71.87
REMARK 500 MET D 213 39.01 -155.89
REMARK 500 PRO D 268 42.13 -86.82
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 = 5.96 ANGSTROMS
REMARK 525 HOH A2021 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A2035 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH A2102 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH B2034 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH B2038 DISTANCE = 6.19 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 POLYETHYLENE GLYCOL 400 (1PE): PARTIAL PEG400 PRESENT
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1PE A 1297
REMARK 610 1PE C 1297
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 9-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 9-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "DA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1297
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR C 1298
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR D 1297
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF RESIDUES 1297 TO
REMARK 800 1297
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NAL RELATED DB: PDB
REMARK 900 THE THREE-DIMENSIONAL STRUCTURE OF N- ACETYLNEURAMINATE LYASE FROM
REMARK 900 ESCHERICHIA COLI
REMARK 900 RELATED ID: 1HL2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF N-ACETYLNEURAMINATE LYASE FROM E. COLI MUTANT
REMARK 900 L142R IN COMPLEX WITH B-HYDROXYPYRUVATE
REMARK 900 RELATED ID: 1FDZ RELATED DB: PDB
REMARK 900 N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH PYRUVATE VIA BOROHYDRIDE
REMARK 900 REDUCTION
REMARK 900 RELATED ID: 1FDY RELATED DB: PDB
REMARK 900 N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 N-TERMINAL TAG RESIDUES HHEAT IN ALL CHAINS.P0A6L4 3
REMARK 999 RESIDUES DIFFER FROM P0A6L4 AS AN ALTERNATE LOCI WAS USED
REMARK 999 FOR THIS CLONE. THESE RESIDUES ARE 84 (THR IN P0A6L4 SER
REMARK 999 HERE), 70 (GLY IN P0A6L4 ALA HERE) AND 282 (GLN IN P0A6L4
REMARK 999 AND LEU HERE)
DBREF 2WKJ A -6 1 PDB 2WKJ 2WKJ -6 1
DBREF 2WKJ A 2 296 UNP P0A6L4 NANA_ECOLI 2 296
DBREF 2WKJ B -6 1 PDB 2WKJ 2WKJ -6 1
DBREF 2WKJ B 2 296 UNP P0A6L4 NANA_ECOLI 2 296
DBREF 2WKJ C -6 1 PDB 2WKJ 2WKJ -6 1
DBREF 2WKJ C 2 296 UNP P0A6L4 NANA_ECOLI 2 296
DBREF 2WKJ D -6 1 PDB 2WKJ 2WKJ -6 1
DBREF 2WKJ D 2 296 UNP P0A6L4 NANA_ECOLI 2 296
SEQADV 2WKJ ASN A 192 UNP P0A6L4 GLU 192 ENGINEERED MUTATION
SEQADV 2WKJ ASN B 192 UNP P0A6L4 GLU 192 ENGINEERED MUTATION
SEQADV 2WKJ ASN C 192 UNP P0A6L4 GLU 192 ENGINEERED MUTATION
SEQADV 2WKJ ASN D 192 UNP P0A6L4 GLU 192 ENGINEERED MUTATION
SEQRES 1 A 303 MET GLU HIS HIS HIS HIS HIS HIS ALA THR ASN LEU ARG
SEQRES 2 A 303 GLY VAL MET ALA ALA LEU LEU THR PRO PHE ASP GLN GLN
SEQRES 3 A 303 GLN ALA LEU ASP LYS ALA SER LEU ARG ARG LEU VAL GLN
SEQRES 4 A 303 PHE ASN ILE GLN GLN GLY ILE ASP GLY LEU TYR VAL GLY
SEQRES 5 A 303 GLY SER THR GLY GLU ALA PHE VAL GLN SER LEU SER GLU
SEQRES 6 A 303 ARG GLU GLN VAL LEU GLU ILE VAL ALA GLU GLU ALA LYS
SEQRES 7 A 303 GLY LYS ILE LYS LEU ILE ALA HIS VAL GLY CYS VAL SER
SEQRES 8 A 303 THR ALA GLU SER GLN GLN LEU ALA ALA SER ALA LYS ARG
SEQRES 9 A 303 TYR GLY PHE ASP ALA VAL SER ALA VAL THR PRO PHE TYR
SEQRES 10 A 303 TYR PRO PHE SER PHE GLU GLU HIS CYS ASP HIS TYR ARG
SEQRES 11 A 303 ALA ILE ILE ASP SER ALA ASP GLY LEU PRO MET VAL VAL
SEQRES 12 A 303 TYR ASN ILE PRO ALA LEU SER GLY VAL LYS LEU THR LEU
SEQRES 13 A 303 ASP GLN ILE ASN THR LEU VAL THR LEU PRO GLY VAL GLY
SEQRES 14 A 303 ALA LEU KPI GLN THR SER GLY ASP LEU TYR GLN MET GLU
SEQRES 15 A 303 GLN ILE ARG ARG GLU HIS PRO ASP LEU VAL LEU TYR ASN
SEQRES 16 A 303 GLY TYR ASP ASN ILE PHE ALA SER GLY LEU LEU ALA GLY
SEQRES 17 A 303 ALA ASP GLY GLY ILE GLY SER THR TYR ASN ILE MET GLY
SEQRES 18 A 303 TRP ARG TYR GLN GLY ILE VAL LYS ALA LEU LYS GLU GLY
SEQRES 19 A 303 ASP ILE GLN THR ALA GLN LYS LEU GLN THR GLU CYS ASN
SEQRES 20 A 303 LYS VAL ILE ASP LEU LEU ILE LYS THR GLY VAL PHE ARG
SEQRES 21 A 303 GLY LEU LYS THR VAL LEU HIS TYR MET ASP VAL VAL SER
SEQRES 22 A 303 VAL PRO LEU CYS ARG LYS PRO PHE GLY PRO VAL ASP GLU
SEQRES 23 A 303 LYS TYR LEU PRO GLU LEU LYS ALA LEU ALA GLN GLN LEU
SEQRES 24 A 303 MET GLN GLU ARG
SEQRES 1 B 303 MET GLU HIS HIS HIS HIS HIS HIS ALA THR ASN LEU ARG
SEQRES 2 B 303 GLY VAL MET ALA ALA LEU LEU THR PRO PHE ASP GLN GLN
SEQRES 3 B 303 GLN ALA LEU ASP LYS ALA SER LEU ARG ARG LEU VAL GLN
SEQRES 4 B 303 PHE ASN ILE GLN GLN GLY ILE ASP GLY LEU TYR VAL GLY
SEQRES 5 B 303 GLY SER THR GLY GLU ALA PHE VAL GLN SER LEU SER GLU
SEQRES 6 B 303 ARG GLU GLN VAL LEU GLU ILE VAL ALA GLU GLU ALA LYS
SEQRES 7 B 303 GLY LYS ILE LYS LEU ILE ALA HIS VAL GLY CYS VAL SER
SEQRES 8 B 303 THR ALA GLU SER GLN GLN LEU ALA ALA SER ALA LYS ARG
SEQRES 9 B 303 TYR GLY PHE ASP ALA VAL SER ALA VAL THR PRO PHE TYR
SEQRES 10 B 303 TYR PRO PHE SER PHE GLU GLU HIS CYS ASP HIS TYR ARG
SEQRES 11 B 303 ALA ILE ILE ASP SER ALA ASP GLY LEU PRO MET VAL VAL
SEQRES 12 B 303 TYR ASN ILE PRO ALA LEU SER GLY VAL LYS LEU THR LEU
SEQRES 13 B 303 ASP GLN ILE ASN THR LEU VAL THR LEU PRO GLY VAL GLY
SEQRES 14 B 303 ALA LEU KPI GLN THR SER GLY ASP LEU TYR GLN MET GLU
SEQRES 15 B 303 GLN ILE ARG ARG GLU HIS PRO ASP LEU VAL LEU TYR ASN
SEQRES 16 B 303 GLY TYR ASP ASN ILE PHE ALA SER GLY LEU LEU ALA GLY
SEQRES 17 B 303 ALA ASP GLY GLY ILE GLY SER THR TYR ASN ILE MET GLY
SEQRES 18 B 303 TRP ARG TYR GLN GLY ILE VAL LYS ALA LEU LYS GLU GLY
SEQRES 19 B 303 ASP ILE GLN THR ALA GLN LYS LEU GLN THR GLU CYS ASN
SEQRES 20 B 303 LYS VAL ILE ASP LEU LEU ILE LYS THR GLY VAL PHE ARG
SEQRES 21 B 303 GLY LEU LYS THR VAL LEU HIS TYR MET ASP VAL VAL SER
SEQRES 22 B 303 VAL PRO LEU CYS ARG LYS PRO PHE GLY PRO VAL ASP GLU
SEQRES 23 B 303 LYS TYR LEU PRO GLU LEU LYS ALA LEU ALA GLN GLN LEU
SEQRES 24 B 303 MET GLN GLU ARG
SEQRES 1 C 303 MET GLU HIS HIS HIS HIS HIS HIS ALA THR ASN LEU ARG
SEQRES 2 C 303 GLY VAL MET ALA ALA LEU LEU THR PRO PHE ASP GLN GLN
SEQRES 3 C 303 GLN ALA LEU ASP LYS ALA SER LEU ARG ARG LEU VAL GLN
SEQRES 4 C 303 PHE ASN ILE GLN GLN GLY ILE ASP GLY LEU TYR VAL GLY
SEQRES 5 C 303 GLY SER THR GLY GLU ALA PHE VAL GLN SER LEU SER GLU
SEQRES 6 C 303 ARG GLU GLN VAL LEU GLU ILE VAL ALA GLU GLU ALA LYS
SEQRES 7 C 303 GLY LYS ILE LYS LEU ILE ALA HIS VAL GLY CYS VAL SER
SEQRES 8 C 303 THR ALA GLU SER GLN GLN LEU ALA ALA SER ALA LYS ARG
SEQRES 9 C 303 TYR GLY PHE ASP ALA VAL SER ALA VAL THR PRO PHE TYR
SEQRES 10 C 303 TYR PRO PHE SER PHE GLU GLU HIS CYS ASP HIS TYR ARG
SEQRES 11 C 303 ALA ILE ILE ASP SER ALA ASP GLY LEU PRO MET VAL VAL
SEQRES 12 C 303 TYR ASN ILE PRO ALA LEU SER GLY VAL LYS LEU THR LEU
SEQRES 13 C 303 ASP GLN ILE ASN THR LEU VAL THR LEU PRO GLY VAL GLY
SEQRES 14 C 303 ALA LEU KPI GLN THR SER GLY ASP LEU TYR GLN MET GLU
SEQRES 15 C 303 GLN ILE ARG ARG GLU HIS PRO ASP LEU VAL LEU TYR ASN
SEQRES 16 C 303 GLY TYR ASP ASN ILE PHE ALA SER GLY LEU LEU ALA GLY
SEQRES 17 C 303 ALA ASP GLY GLY ILE GLY SER THR TYR ASN ILE MET GLY
SEQRES 18 C 303 TRP ARG TYR GLN GLY ILE VAL LYS ALA LEU LYS GLU GLY
SEQRES 19 C 303 ASP ILE GLN THR ALA GLN LYS LEU GLN THR GLU CYS ASN
SEQRES 20 C 303 LYS VAL ILE ASP LEU LEU ILE LYS THR GLY VAL PHE ARG
SEQRES 21 C 303 GLY LEU LYS THR VAL LEU HIS TYR MET ASP VAL VAL SER
SEQRES 22 C 303 VAL PRO LEU CYS ARG LYS PRO PHE GLY PRO VAL ASP GLU
SEQRES 23 C 303 LYS TYR LEU PRO GLU LEU LYS ALA LEU ALA GLN GLN LEU
SEQRES 24 C 303 MET GLN GLU ARG
SEQRES 1 D 303 MET GLU HIS HIS HIS HIS HIS HIS ALA THR ASN LEU ARG
SEQRES 2 D 303 GLY VAL MET ALA ALA LEU LEU THR PRO PHE ASP GLN GLN
SEQRES 3 D 303 GLN ALA LEU ASP LYS ALA SER LEU ARG ARG LEU VAL GLN
SEQRES 4 D 303 PHE ASN ILE GLN GLN GLY ILE ASP GLY LEU TYR VAL GLY
SEQRES 5 D 303 GLY SER THR GLY GLU ALA PHE VAL GLN SER LEU SER GLU
SEQRES 6 D 303 ARG GLU GLN VAL LEU GLU ILE VAL ALA GLU GLU ALA LYS
SEQRES 7 D 303 GLY LYS ILE LYS LEU ILE ALA HIS VAL GLY CYS VAL SER
SEQRES 8 D 303 THR ALA GLU SER GLN GLN LEU ALA ALA SER ALA LYS ARG
SEQRES 9 D 303 TYR GLY PHE ASP ALA VAL SER ALA VAL THR PRO PHE TYR
SEQRES 10 D 303 TYR PRO PHE SER PHE GLU GLU HIS CYS ASP HIS TYR ARG
SEQRES 11 D 303 ALA ILE ILE ASP SER ALA ASP GLY LEU PRO MET VAL VAL
SEQRES 12 D 303 TYR ASN ILE PRO ALA LEU SER GLY VAL LYS LEU THR LEU
SEQRES 13 D 303 ASP GLN ILE ASN THR LEU VAL THR LEU PRO GLY VAL GLY
SEQRES 14 D 303 ALA LEU KPI GLN THR SER GLY ASP LEU TYR GLN MET GLU
SEQRES 15 D 303 GLN ILE ARG ARG GLU HIS PRO ASP LEU VAL LEU TYR ASN
SEQRES 16 D 303 GLY TYR ASP ASN ILE PHE ALA SER GLY LEU LEU ALA GLY
SEQRES 17 D 303 ALA ASP GLY GLY ILE GLY SER THR TYR ASN ILE MET GLY
SEQRES 18 D 303 TRP ARG TYR GLN GLY ILE VAL LYS ALA LEU LYS GLU GLY
SEQRES 19 D 303 ASP ILE GLN THR ALA GLN LYS LEU GLN THR GLU CYS ASN
SEQRES 20 D 303 LYS VAL ILE ASP LEU LEU ILE LYS THR GLY VAL PHE ARG
SEQRES 21 D 303 GLY LEU LYS THR VAL LEU HIS TYR MET ASP VAL VAL SER
SEQRES 22 D 303 VAL PRO LEU CYS ARG LYS PRO PHE GLY PRO VAL ASP GLU
SEQRES 23 D 303 LYS TYR LEU PRO GLU LEU LYS ALA LEU ALA GLN GLN LEU
SEQRES 24 D 303 MET GLN GLU ARG
MODRES 2WKJ KPI A 165 LYS
MODRES 2WKJ KPI B 165 LYS
MODRES 2WKJ KPI C 165 LYS
MODRES 2WKJ KPI D 165 LYS
HET KPI A 165 14
HET KPI B 165 14
HET KPI C 165 14
HET KPI D 165 14
HET 1PE A1297 8
HET 1PE C1297 8
HET PYR C1298 12
HET PYR D1297 6
HETNAM KPI (2S)-2-AMINO-6-[(1-HYDROXY-1-OXO-PROPAN-2-YLIDENE)
HETNAM 2 KPI AMINO]HEXANOIC ACID
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM PYR PYRUVIC ACID
HETSYN 1PE PEG400
FORMUL 1 KPI 4(C9 H16 N2 O4)
FORMUL 5 1PE 2(C10 H22 O6)
FORMUL 7 PYR 2(C3 H4 O3)
FORMUL 9 HOH *1307(H2 O)
HELIX 1 1 HIS A -1 ARG A 6 5 8
HELIX 2 2 ASP A 23 GLN A 37 1 15
HELIX 3 3 GLU A 50 GLN A 54 5 5
HELIX 4 4 SER A 55 LYS A 71 1 17
HELIX 5 5 SER A 84 GLY A 99 1 16
HELIX 6 6 SER A 114 ASP A 130 1 17
HELIX 7 7 ILE A 139 GLY A 144 1 6
HELIX 8 8 THR A 148 THR A 157 1 10
HELIX 9 9 ASP A 170 HIS A 181 1 12
HELIX 10 10 TYR A 190 ASN A 192 5 3
HELIX 11 11 ILE A 193 GLY A 201 1 9
HELIX 12 12 THR A 209 GLY A 227 1 19
HELIX 13 13 ASP A 228 GLY A 250 1 23
HELIX 14 14 GLY A 250 MET A 262 1 13
HELIX 15 15 ASP A 278 LYS A 280 5 3
HELIX 16 16 TYR A 281 ARG A 296 1 16
HELIX 17 17 HIS B -1 ARG B 6 5 8
HELIX 18 18 ASP B 23 GLN B 37 1 15
HELIX 19 19 GLU B 50 GLN B 54 5 5
HELIX 20 20 SER B 55 LYS B 71 1 17
HELIX 21 21 SER B 84 GLY B 99 1 16
HELIX 22 22 SER B 114 ASP B 130 1 17
HELIX 23 23 ILE B 139 GLY B 144 1 6
HELIX 24 24 THR B 148 VAL B 156 1 9
HELIX 25 25 ASP B 170 HIS B 181 1 12
HELIX 26 26 TYR B 190 ASN B 192 5 3
HELIX 27 27 ILE B 193 GLY B 201 1 9
HELIX 28 28 THR B 209 GLY B 227 1 19
HELIX 29 29 ASP B 228 GLY B 250 1 23
HELIX 30 30 GLY B 250 MET B 262 1 13
HELIX 31 31 ASP B 278 LYS B 280 5 3
HELIX 32 32 TYR B 281 ARG B 296 1 16
HELIX 33 33 HIS C -1 ARG C 6 5 8
HELIX 34 34 ASP C 23 GLN C 37 1 15
HELIX 35 35 GLU C 50 GLN C 54 5 5
HELIX 36 36 SER C 55 LYS C 71 1 17
HELIX 37 37 SER C 84 GLY C 99 1 16
HELIX 38 38 SER C 114 ASP C 130 1 17
HELIX 39 39 ILE C 139 GLY C 144 1 6
HELIX 40 40 THR C 148 THR C 157 1 10
HELIX 41 41 ASP C 170 HIS C 181 1 12
HELIX 42 42 TYR C 190 ASN C 192 5 3
HELIX 43 43 ILE C 193 GLY C 201 1 9
HELIX 44 44 THR C 209 GLU C 226 1 18
HELIX 45 45 ASP C 228 GLY C 250 1 23
HELIX 46 46 GLY C 250 MET C 262 1 13
HELIX 47 47 ASP C 278 LYS C 280 5 3
HELIX 48 48 TYR C 281 ARG C 296 1 16
HELIX 49 49 HIS D -1 ARG D 6 5 8
HELIX 50 50 ASP D 23 GLY D 38 1 16
HELIX 51 51 GLU D 50 GLN D 54 5 5
HELIX 52 52 SER D 55 LYS D 71 1 17
HELIX 53 53 SER D 84 TYR D 98 1 15
HELIX 54 54 SER D 114 ALA D 129 1 16
HELIX 55 55 ILE D 139 GLY D 144 1 6
HELIX 56 56 THR D 148 THR D 157 1 10
HELIX 57 57 ASP D 170 HIS D 181 1 12
HELIX 58 58 TYR D 190 ASN D 192 5 3
HELIX 59 59 ILE D 193 GLY D 201 1 9
HELIX 60 60 THR D 209 GLY D 227 1 19
HELIX 61 61 ASP D 228 GLY D 250 1 23
HELIX 62 62 GLY D 250 MET D 262 1 13
HELIX 63 63 ASP D 278 LYS D 280 5 3
HELIX 64 64 TYR D 281 ARG D 296 1 16
SHEET 1 AA10 VAL A 8 ALA A 11 0
SHEET 2 AA10 GLY A 204 GLY A 207 1 O GLY A 205 N MET A 9
SHEET 3 AA10 VAL A 185 ASN A 188 1 O ASN A 188 N ILE A 206
SHEET 4 AA10 VAL A 161 LEU A 164 1 O GLY A 162 N VAL A 185
SHEET 5 AA10 MET A 134 TYR A 137 1 O MET A 134 N GLY A 162
SHEET 6 AA10 ALA A 102 VAL A 106 1 O VAL A 103 N VAL A 135
SHEET 7 AA10 LYS A 75 HIS A 79 1 O ALA A 78 N SER A 104
SHEET 8 AA10 GLY A 41 VAL A 44 1 O LEU A 42 N ILE A 77
SHEET 9 AA10 VAL A 8 ALA A 11 1 O ALA A 10 N TYR A 43
SHEET 10 AA10 VAL A 8 ALA A 11 0
SHEET 1 BA10 VAL B 8 ALA B 11 0
SHEET 2 BA10 GLY B 204 GLY B 207 1 O GLY B 205 N MET B 9
SHEET 3 BA10 VAL B 185 ASN B 188 1 O ASN B 188 N ILE B 206
SHEET 4 BA10 VAL B 161 LEU B 164 1 O GLY B 162 N VAL B 185
SHEET 5 BA10 MET B 134 TYR B 137 1 O MET B 134 N GLY B 162
SHEET 6 BA10 ALA B 102 VAL B 106 1 O VAL B 103 N VAL B 135
SHEET 7 BA10 LYS B 75 HIS B 79 1 O ALA B 78 N SER B 104
SHEET 8 BA10 GLY B 41 VAL B 44 1 O LEU B 42 N ILE B 77
SHEET 9 BA10 VAL B 8 ALA B 11 1 O ALA B 10 N TYR B 43
SHEET 10 BA10 VAL B 8 ALA B 11 0
SHEET 1 CA22 VAL C 8 ALA C 11 0
SHEET 2 CA22 GLY C 204 GLY C 207 1 O GLY C 205 N MET C 9
SHEET 3 CA22 VAL C 185 ASN C 188 1 O ASN C 188 N ILE C 206
SHEET 4 CA22 VAL C 161 LEU C 164 1 O GLY C 162 N VAL C 185
SHEET 5 CA22 MET C 134 TYR C 137 1 O MET C 134 N GLY C 162
SHEET 6 CA22 ALA C 102 VAL C 106 1 O VAL C 103 N VAL C 135
SHEET 7 CA22 LYS C 75 HIS C 79 1 O ALA C 78 N SER C 104
SHEET 8 CA22 GLY C 41 VAL C 44 1 O LEU C 42 N ILE C 77
SHEET 9 CA22 GLY C 41 VAL C 44 0
SHEET 10 CA22 VAL C 8 ALA C 11 1 O ALA C 10 N TYR C 43
SHEET 11 CA22 LYS C 75 HIS C 79 0
SHEET 12 CA22 GLY C 41 VAL C 44 1 O LEU C 42 N ILE C 77
SHEET 13 CA22 ALA C 102 VAL C 106 0
SHEET 14 CA22 LYS C 75 HIS C 79 1 O ALA C 78 N SER C 104
SHEET 15 CA22 MET C 134 TYR C 137 0
SHEET 16 CA22 ALA C 102 VAL C 106 1 O VAL C 103 N VAL C 135
SHEET 17 CA22 VAL C 161 LEU C 164 0
SHEET 18 CA22 MET C 134 TYR C 137 1 O MET C 134 N GLY C 162
SHEET 19 CA22 VAL C 185 ASN C 188 0
SHEET 20 CA22 VAL C 161 LEU C 164 1 O GLY C 162 N VAL C 185
SHEET 21 CA22 GLY C 204 GLY C 207 0
SHEET 22 CA22 VAL C 8 ALA C 11 1 O MET C 9 N GLY C 207
SHEET 1 DA16 VAL D 8 ALA D 11 0
SHEET 2 DA16 GLY D 204 GLY D 207 1 O GLY D 205 N MET D 9
SHEET 3 DA16 GLY D 41 VAL D 44 0
SHEET 4 DA16 VAL D 8 ALA D 11 1 O ALA D 10 N TYR D 43
SHEET 5 DA16 LYS D 75 HIS D 79 0
SHEET 6 DA16 GLY D 41 VAL D 44 1 O LEU D 42 N ILE D 77
SHEET 7 DA16 ALA D 102 VAL D 106 0
SHEET 8 DA16 LYS D 75 HIS D 79 1 O ALA D 78 N SER D 104
SHEET 9 DA16 MET D 134 TYR D 137 0
SHEET 10 DA16 ALA D 102 VAL D 106 1 O VAL D 103 N VAL D 135
SHEET 11 DA16 VAL D 161 LEU D 164 0
SHEET 12 DA16 MET D 134 TYR D 137 1 O MET D 134 N GLY D 162
SHEET 13 DA16 VAL D 185 ASN D 188 0
SHEET 14 DA16 VAL D 161 LEU D 164 1 O GLY D 162 N VAL D 185
SHEET 15 DA16 GLY D 204 GLY D 207 0
SHEET 16 DA16 VAL D 8 ALA D 11 1 O MET D 9 N GLY D 207
LINK C LEU A 164 N KPI A 165 1555 1555 1.32
LINK C KPI A 165 N GLN A 166 1555 1555 1.33
LINK C LEU B 164 N KPI B 165 1555 1555 1.33
LINK C KPI B 165 N GLN B 166 1555 1555 1.33
LINK C LEU C 164 N KPI C 165 1555 1555 1.34
LINK C KPI C 165 N GLN C 166 1555 1555 1.32
LINK C LEU D 164 N KPI D 165 1555 1555 1.32
LINK C KPI D 165 N GLN D 166 1555 1555 1.32
CISPEP 1 LYS A 272 PRO A 273 0 16.64
CISPEP 2 LYS B 272 PRO B 273 0 17.44
CISPEP 3 LYS C 272 PRO C 273 0 19.30
CISPEP 4 LYS D 272 PRO D 273 0 17.36
SITE 1 AC1 6 LEU A 282 PRO A 283 LYS A 286 GLN C 36
SITE 2 AC1 6 GLN C 37 GLY C 38
SITE 1 AC2 8 GLY C 189 TYR C 190 ASP C 191 ASN C 192
SITE 2 AC2 8 SER C 208 THR C 209 HOH C2339 HOH C2340
SITE 1 AC3 7 GLY D 189 TYR D 190 ASP D 191 ASN D 192
SITE 2 AC3 7 ILE D 243 HOH D2274 HOH D2275
SITE 1 AC4 3 GLN C 36 GLN C 37 GLY C 38
CRYST1 78.329 108.049 148.309 90.00 90.00 90.00 P 21 21 21 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 0.012767 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009255 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006743 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
