HEADER TRANSFERASE/ANTIBIOTIC 07-FEB-18 6CCL
TITLE CRYSTAL STRUCTURE OF E.COLI PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE
TITLE 2 (PPAT/COAD) IN COMPLEX WITH 1-BENZYL-1H-IMIDAZO[4,5-B]PYRIDINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DEPHOSPHO-COA PYROPHOSPHORYLASE,PANTETHEINE-PHOSPHATE
COMPND 5 ADENYLYLTRANSFERASE,PPAT;
COMPND 6 EC: 2.7.7.3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: COAD, KDTB, YICA, B3634, JW3609;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PPAT COAD FBDD PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE GRAM-NEGATIVE
KEYWDS 2 ANTIBACTERIAL ANTIBIOTIC, TRANSFERASE, TRANSFERASE-ANTIBIOTIC
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MAMO,B.A.APPLETON
REVDAT 3 13-MAR-24 6CCL 1 REMARK
REVDAT 2 09-MAY-18 6CCL 1 JRNL
REVDAT 1 14-MAR-18 6CCL 0
JRNL AUTH R.J.MOREAU,C.K.SKEPPER,B.A.APPLETON,A.BLECHSCHMIDT,
JRNL AUTH 2 C.J.BALIBAR,B.M.BENTON,J.E.DRUMM,B.Y.FENG,M.GENG,C.LI,
JRNL AUTH 3 M.K.LINDVALL,A.LINGEL,Y.LU,M.MAMO,W.MERGO,V.POLYAKOV,
JRNL AUTH 4 T.M.SMITH,K.TAKEOKA,K.UEHARA,L.WANG,J.R.WEI,A.H.WEISS,L.XIE,
JRNL AUTH 5 W.XU,Q.ZHANG,J.DE VICENTE
JRNL TITL FRAGMENT-BASED DRUG DISCOVERY OF INHIBITORS OF
JRNL TITL 2 PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE FROM GRAM-NEGATIVE
JRNL TITL 3 BACTERIA.
JRNL REF J. MED. CHEM. V. 61 3309 2018
JRNL REFN ISSN 1520-4804
JRNL PMID 29498517
JRNL DOI 10.1021/ACS.JMEDCHEM.7B01691
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.7
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) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 39696
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.850
REMARK 3 FREE R VALUE TEST SET COUNT : 1927
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) : 1.77
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.82
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.03
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2751
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2079
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2625
REMARK 3 BIN R VALUE (WORKING SET) : 0.2062
REMARK 3 BIN FREE R VALUE : 0.2442
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.58
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 126
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2490
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 321
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.200
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.101
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.101
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.095
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.098
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 : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2721 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3712 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 932 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 60 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 443 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2721 ; 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 : 353 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : 11 ; 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 : 3630 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.93
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.13
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.36
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|2 - A|37 }
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7649 -13.1083 46.1513
REMARK 3 T TENSOR
REMARK 3 T11: -0.0314 T22: -0.0375
REMARK 3 T33: -0.0077 T12: -0.0033
REMARK 3 T13: 0.0004 T23: -0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 1.0380 L22: 0.8511
REMARK 3 L33: 0.5334 L12: 0.3906
REMARK 3 L13: -0.1201 L23: -0.5217
REMARK 3 S TENSOR
REMARK 3 S11: -0.0081 S12: -0.0869 S13: 0.0196
REMARK 3 S21: 0.0465 S22: 0.0457 S23: 0.1171
REMARK 3 S31: -0.0396 S32: -0.0848 S33: -0.0376
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|38 - A|47 }
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3381 -11.6422 28.4281
REMARK 3 T TENSOR
REMARK 3 T11: 0.0661 T22: -0.0400
REMARK 3 T33: 0.0381 T12: -0.0647
REMARK 3 T13: -0.0635 T23: 0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 1.4498 L22: 1.7260
REMARK 3 L33: 1.5417 L12: -0.9442
REMARK 3 L13: 2.9104 L23: 0.0676
REMARK 3 S TENSOR
REMARK 3 S11: -0.0398 S12: 0.0822 S13: -0.0857
REMARK 3 S21: -0.2186 S22: 0.1119 S23: 0.2355
REMARK 3 S31: -0.0604 S32: -0.0022 S33: -0.0721
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { A|48 - A|73 }
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6991 -7.3537 42.3932
REMARK 3 T TENSOR
REMARK 3 T11: -0.0280 T22: -0.0567
REMARK 3 T33: 0.0619 T12: 0.0110
REMARK 3 T13: -0.0026 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 2.4170 L22: 2.3505
REMARK 3 L33: 0.0315 L12: 0.4930
REMARK 3 L13: -0.6193 L23: -0.3230
REMARK 3 S TENSOR
REMARK 3 S11: -0.0024 S12: -0.0076 S13: 0.2765
REMARK 3 S21: 0.0532 S22: 0.0963 S23: 0.4566
REMARK 3 S31: -0.0143 S32: -0.1086 S33: -0.0939
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { A|74 - A|92 }
REMARK 3 ORIGIN FOR THE GROUP (A): 28.2119 -9.0393 41.6011
REMARK 3 T TENSOR
REMARK 3 T11: -0.0088 T22: -0.0579
REMARK 3 T33: -0.0154 T12: -0.0093
REMARK 3 T13: -0.0059 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 1.3216 L22: 3.6806
REMARK 3 L33: 0.8350 L12: 0.1209
REMARK 3 L13: -0.3873 L23: -0.9533
REMARK 3 S TENSOR
REMARK 3 S11: 0.0271 S12: -0.0071 S13: 0.0650
REMARK 3 S21: 0.0251 S22: -0.0636 S23: -0.0206
REMARK 3 S31: -0.0956 S32: -0.0148 S33: 0.0366
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { A|93 - A|109 }
REMARK 3 ORIGIN FOR THE GROUP (A): 33.9329 -17.3196 34.9094
REMARK 3 T TENSOR
REMARK 3 T11: -0.0183 T22: 0.0176
REMARK 3 T33: 0.0007 T12: 0.0247
REMARK 3 T13: -0.0072 T23: -0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 2.0297 L22: 3.7031
REMARK 3 L33: 2.2015 L12: -0.4169
REMARK 3 L13: -0.7837 L23: 0.0828
REMARK 3 S TENSOR
REMARK 3 S11: 0.0189 S12: 0.1835 S13: -0.2770
REMARK 3 S21: -0.0547 S22: -0.0733 S23: 0.0615
REMARK 3 S31: -0.0886 S32: -0.0827 S33: 0.0544
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { A|110 - A|128 }
REMARK 3 ORIGIN FOR THE GROUP (A): 25.9594 -20.6956 43.9808
REMARK 3 T TENSOR
REMARK 3 T11: 0.0023 T22: -0.0210
REMARK 3 T33: 0.0221 T12: 0.0085
REMARK 3 T13: -0.0192 T23: 0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 0.5198 L22: 1.5706
REMARK 3 L33: 0.3002 L12: 0.8956
REMARK 3 L13: -0.2892 L23: -0.0580
REMARK 3 S TENSOR
REMARK 3 S11: 0.0650 S12: 0.0668 S13: -0.1657
REMARK 3 S21: 0.0442 S22: -0.0360 S23: -0.1523
REMARK 3 S31: 0.0395 S32: 0.0550 S33: -0.0290
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: { A|129 - A|138 }
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4947 -24.4960 30.3147
REMARK 3 T TENSOR
REMARK 3 T11: -0.0054 T22: -0.0194
REMARK 3 T33: 0.0010 T12: -0.0281
REMARK 3 T13: 0.0035 T23: 0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 1.9924 L22: 0.5251
REMARK 3 L33: 0.0000 L12: 0.1677
REMARK 3 L13: -0.9276 L23: 1.0934
REMARK 3 S TENSOR
REMARK 3 S11: -0.0087 S12: 0.0628 S13: 0.0273
REMARK 3 S21: -0.0508 S22: 0.0215 S23: -0.0289
REMARK 3 S31: -0.1683 S32: 0.0849 S33: -0.0128
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: { A|139 - A|160 }
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4153 -20.7632 37.7007
REMARK 3 T TENSOR
REMARK 3 T11: -0.0528 T22: -0.0075
REMARK 3 T33: 0.0747 T12: -0.0138
REMARK 3 T13: -0.0064 T23: -0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 2.9903 L22: 0.7844
REMARK 3 L33: 0.6919 L12: 0.7289
REMARK 3 L13: -0.5175 L23: 0.4505
REMARK 3 S TENSOR
REMARK 3 S11: -0.0305 S12: 0.0550 S13: 0.4152
REMARK 3 S21: -0.0091 S22: -0.0402 S23: 0.2407
REMARK 3 S31: 0.0429 S32: -0.2794 S33: 0.0707
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: { B|2 - B|15 }
REMARK 3 ORIGIN FOR THE GROUP (A): 42.1382 -23.6421 55.9317
REMARK 3 T TENSOR
REMARK 3 T11: -0.0358 T22: -0.0158
REMARK 3 T33: -0.0305 T12: 0.0191
REMARK 3 T13: 0.0051 T23: 0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 1.4692 L22: 0.0000
REMARK 3 L33: 1.7603 L12: 1.6932
REMARK 3 L13: -0.8693 L23: -0.6105
REMARK 3 S TENSOR
REMARK 3 S11: -0.0042 S12: -0.0764 S13: -0.0621
REMARK 3 S21: -0.0008 S22: -0.0923 S23: -0.0895
REMARK 3 S31: -0.0998 S32: 0.1598 S33: 0.0965
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: { B|16 - B|59 }
REMARK 3 ORIGIN FOR THE GROUP (A): 47.1837 -23.5732 55.6381
REMARK 3 T TENSOR
REMARK 3 T11: -0.0632 T22: 0.0215
REMARK 3 T33: -0.0434 T12: -0.0016
REMARK 3 T13: 0.0025 T23: 0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 3.1811 L22: 0.8509
REMARK 3 L33: 2.0931 L12: -1.1840
REMARK 3 L13: -1.1091 L23: -0.0877
REMARK 3 S TENSOR
REMARK 3 S11: -0.1353 S12: -0.2865 S13: -0.1643
REMARK 3 S21: 0.0348 S22: -0.0207 S23: 0.0918
REMARK 3 S31: 0.0585 S32: 0.3172 S33: 0.1560
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: { B|60 - B|80 }
REMARK 3 ORIGIN FOR THE GROUP (A): 40.2424 -25.2459 61.8990
REMARK 3 T TENSOR
REMARK 3 T11: -0.0233 T22: 0.0968
REMARK 3 T33: -0.0028 T12: -0.0309
REMARK 3 T13: 0.0040 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 1.4523 L22: 0.2839
REMARK 3 L33: 2.5491 L12: 0.4068
REMARK 3 L13: -0.4008 L23: -0.9196
REMARK 3 S TENSOR
REMARK 3 S11: -0.0248 S12: -0.1475 S13: -0.0950
REMARK 3 S21: 0.1604 S22: 0.0494 S23: -0.0997
REMARK 3 S31: 0.0482 S32: -0.0802 S33: -0.0246
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: { B|81 - B|109 }
REMARK 3 ORIGIN FOR THE GROUP (A): 32.3757 -28.7751 50.0970
REMARK 3 T TENSOR
REMARK 3 T11: -0.0326 T22: -0.0618
REMARK 3 T33: -0.0463 T12: 0.0112
REMARK 3 T13: -0.0247 T23: 0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 3.1817 L22: 1.8195
REMARK 3 L33: 2.7314 L12: 0.2706
REMARK 3 L13: 0.4279 L23: 0.7867
REMARK 3 S TENSOR
REMARK 3 S11: 0.0858 S12: 0.2753 S13: -0.2569
REMARK 3 S21: -0.1419 S22: 0.1800 S23: -0.0667
REMARK 3 S31: 0.1354 S32: 0.0945 S33: -0.2658
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: { B|110 - B|128 }
REMARK 3 ORIGIN FOR THE GROUP (A): 37.9164 -22.2836 46.4662
REMARK 3 T TENSOR
REMARK 3 T11: -0.0098 T22: 0.0050
REMARK 3 T33: -0.0320 T12: 0.0106
REMARK 3 T13: -0.0158 T23: 0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 1.8347 L22: 0.7658
REMARK 3 L33: 0.4219 L12: 1.0887
REMARK 3 L13: -0.5692 L23: -0.6849
REMARK 3 S TENSOR
REMARK 3 S11: 0.0967 S12: 0.2193 S13: -0.1319
REMARK 3 S21: -0.0396 S22: -0.0277 S23: -0.0371
REMARK 3 S31: 0.0055 S32: 0.0321 S33: -0.0690
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: { B|129 - B|137 }
REMARK 3 ORIGIN FOR THE GROUP (A): 55.1318 -33.3396 43.3095
REMARK 3 T TENSOR
REMARK 3 T11: 0.0198 T22: 0.0253
REMARK 3 T33: 0.0803 T12: 0.0137
REMARK 3 T13: -0.0001 T23: 0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 1.0497 L22: 1.2157
REMARK 3 L33: 0.5402 L12: 1.3790
REMARK 3 L13: -1.7835 L23: -0.6780
REMARK 3 S TENSOR
REMARK 3 S11: 0.0068 S12: -0.0152 S13: -0.0690
REMARK 3 S21: 0.1020 S22: -0.0477 S23: 0.1078
REMARK 3 S31: 0.0775 S32: 0.0374 S33: 0.0409
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: { B|138 - B|159 }
REMARK 3 ORIGIN FOR THE GROUP (A): 60.7152 -26.5554 46.4942
REMARK 3 T TENSOR
REMARK 3 T11: -0.0869 T22: 0.0039
REMARK 3 T33: -0.0505 T12: 0.0104
REMARK 3 T13: 0.0097 T23: 0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 4.3704 L22: 0.6034
REMARK 3 L33: 0.7896 L12: -0.8065
REMARK 3 L13: -0.1133 L23: 0.7330
REMARK 3 S TENSOR
REMARK 3 S11: 0.0175 S12: -0.4309 S13: -0.1850
REMARK 3 S21: -0.0344 S22: -0.0091 S23: 0.0312
REMARK 3 S31: 0.0503 S32: 0.1157 S33: -0.0084
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: { A|201 }
REMARK 3 ORIGIN FOR THE GROUP (A): 26.6678 -10.2687 32.0301
REMARK 3 T TENSOR
REMARK 3 T11: 0.0295 T22: -0.0375
REMARK 3 T33: 0.0089 T12: -0.0504
REMARK 3 T13: 0.0498 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0.0406 L22: 0.1913
REMARK 3 L33: 0.0000 L12: -0.1426
REMARK 3 L13: 0.0924 L23: -0.2419
REMARK 3 S TENSOR
REMARK 3 S11: -0.0053 S12: -0.0162 S13: -0.0027
REMARK 3 S21: 0.0052 S22: 0.0001 S23: 0.0115
REMARK 3 S31: 0.0044 S32: -0.0058 S33: 0.0052
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6CCL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1000232526.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9774
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.31
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39709
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
REMARK 200 RESOLUTION RANGE LOW (A) : 36.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 0.67100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3 M AMMONIUM SULFATE, 0.2 M
REMARK 280 POTASSIUM THIOCYANATE, 0.2 M POTASSIUM BROMIDE, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,X+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 67.52500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 67.52500
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 67.52500
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 67.52500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 67.52500
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 67.52500
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 67.52500
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 67.52500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 67.52500
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 67.52500
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 67.52500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 67.52500
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 67.52500
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 67.52500
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 67.52500
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 67.52500
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 67.52500
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 67.52500
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 67.52500
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 67.52500
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 67.52500
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 67.52500
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 67.52500
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 67.52500
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 67.52500
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 67.52500
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 67.52500
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 67.52500
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 67.52500
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 67.52500
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 67.52500
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 67.52500
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 67.52500
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 67.52500
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 67.52500
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 67.52500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -454.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 24-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 76750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 143840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1395.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 5 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 6 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 7 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 8 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT1 9 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 9 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 9 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 10 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 11 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT3 12 1.000000 0.000000 0.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 13 1.000000 0.000000 0.000000 -67.52500
REMARK 350 BIOMT2 13 0.000000 1.000000 0.000000 67.52500
REMARK 350 BIOMT3 13 0.000000 0.000000 1.000000 -67.52500
REMARK 350 BIOMT1 14 -1.000000 0.000000 0.000000 67.52500
REMARK 350 BIOMT2 14 0.000000 -1.000000 0.000000 -67.52500
REMARK 350 BIOMT3 14 0.000000 0.000000 1.000000 -67.52500
REMARK 350 BIOMT1 15 -1.000000 0.000000 0.000000 67.52500
REMARK 350 BIOMT2 15 0.000000 1.000000 0.000000 67.52500
REMARK 350 BIOMT3 15 0.000000 0.000000 -1.000000 67.52500
REMARK 350 BIOMT1 16 1.000000 0.000000 0.000000 -67.52500
REMARK 350 BIOMT2 16 0.000000 -1.000000 0.000000 -67.52500
REMARK 350 BIOMT3 16 0.000000 0.000000 -1.000000 67.52500
REMARK 350 BIOMT1 17 0.000000 0.000000 1.000000 -67.52500
REMARK 350 BIOMT2 17 1.000000 0.000000 0.000000 -67.52500
REMARK 350 BIOMT3 17 0.000000 1.000000 0.000000 67.52500
REMARK 350 BIOMT1 18 0.000000 0.000000 1.000000 -67.52500
REMARK 350 BIOMT2 18 -1.000000 0.000000 0.000000 67.52500
REMARK 350 BIOMT3 18 0.000000 -1.000000 0.000000 -67.52500
REMARK 350 BIOMT1 19 0.000000 0.000000 -1.000000 67.52500
REMARK 350 BIOMT2 19 -1.000000 0.000000 0.000000 67.52500
REMARK 350 BIOMT3 19 0.000000 1.000000 0.000000 67.52500
REMARK 350 BIOMT1 20 0.000000 0.000000 -1.000000 67.52500
REMARK 350 BIOMT2 20 1.000000 0.000000 0.000000 -67.52500
REMARK 350 BIOMT3 20 0.000000 -1.000000 0.000000 -67.52500
REMARK 350 BIOMT1 21 0.000000 1.000000 0.000000 67.52500
REMARK 350 BIOMT2 21 0.000000 0.000000 1.000000 -67.52500
REMARK 350 BIOMT3 21 1.000000 0.000000 0.000000 -67.52500
REMARK 350 BIOMT1 22 0.000000 -1.000000 0.000000 -67.52500
REMARK 350 BIOMT2 22 0.000000 0.000000 1.000000 -67.52500
REMARK 350 BIOMT3 22 -1.000000 0.000000 0.000000 67.52500
REMARK 350 BIOMT1 23 0.000000 1.000000 0.000000 67.52500
REMARK 350 BIOMT2 23 0.000000 0.000000 -1.000000 67.52500
REMARK 350 BIOMT3 23 -1.000000 0.000000 0.000000 67.52500
REMARK 350 BIOMT1 24 0.000000 -1.000000 0.000000 -67.52500
REMARK 350 BIOMT2 24 0.000000 0.000000 -1.000000 67.52500
REMARK 350 BIOMT3 24 1.000000 0.000000 0.000000 -67.52500
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASP A 161
REMARK 465 MET B 1
REMARK 465 ASP B 161
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 GLN A 2 CG CD OE1 NE2
REMARK 470 LYS B 42 CG CD CE NZ
REMARK 470 LYS B 43 CG CD CE NZ
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 SER A 130 N CA C O CB OG
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 ASP A 12 76.43 -115.83
REMARK 500 ARG A 91 -66.32 -97.24
REMARK 500 MET A 110 84.43 -151.03
REMARK 500 ASP B 12 74.96 -117.78
REMARK 500 SER B 39 74.66 -119.97
REMARK 500 GLN B 139 38.58 70.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EXG A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EXG B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 203
DBREF 6CCL A 2 159 UNP P0A6I6 COAD_ECOLI 2 159
DBREF 6CCL B 2 159 UNP P0A6I6 COAD_ECOLI 2 159
SEQADV 6CCL MET A 1 UNP P0A6I6 INITIATING METHIONINE
SEQADV 6CCL VAL A 160 UNP P0A6I6 EXPRESSION TAG
SEQADV 6CCL ASP A 161 UNP P0A6I6 EXPRESSION TAG
SEQADV 6CCL MET B 1 UNP P0A6I6 INITIATING METHIONINE
SEQADV 6CCL VAL B 160 UNP P0A6I6 EXPRESSION TAG
SEQADV 6CCL ASP B 161 UNP P0A6I6 EXPRESSION TAG
SEQRES 1 A 161 MET GLN LYS ARG ALA ILE TYR PRO GLY THR PHE ASP PRO
SEQRES 2 A 161 ILE THR ASN GLY HIS ILE ASP ILE VAL THR ARG ALA THR
SEQRES 3 A 161 GLN MET PHE ASP HIS VAL ILE LEU ALA ILE ALA ALA SER
SEQRES 4 A 161 PRO SER LYS LYS PRO MET PHE THR LEU GLU GLU ARG VAL
SEQRES 5 A 161 ALA LEU ALA GLN GLN ALA THR ALA HIS LEU GLY ASN VAL
SEQRES 6 A 161 GLU VAL VAL GLY PHE SER ASP LEU MET ALA ASN PHE ALA
SEQRES 7 A 161 ARG ASN GLN HIS ALA THR VAL LEU ILE ARG GLY LEU ARG
SEQRES 8 A 161 ALA VAL ALA ASP PHE GLU TYR GLU MET GLN LEU ALA HIS
SEQRES 9 A 161 MET ASN ARG HIS LEU MET PRO GLU LEU GLU SER VAL PHE
SEQRES 10 A 161 LEU MET PRO SER LYS GLU TRP SER PHE ILE SER SER SER
SEQRES 11 A 161 LEU VAL LYS GLU VAL ALA ARG HIS GLN GLY ASP VAL THR
SEQRES 12 A 161 HIS PHE LEU PRO GLU ASN VAL HIS GLN ALA LEU MET ALA
SEQRES 13 A 161 LYS LEU ALA VAL ASP
SEQRES 1 B 161 MET GLN LYS ARG ALA ILE TYR PRO GLY THR PHE ASP PRO
SEQRES 2 B 161 ILE THR ASN GLY HIS ILE ASP ILE VAL THR ARG ALA THR
SEQRES 3 B 161 GLN MET PHE ASP HIS VAL ILE LEU ALA ILE ALA ALA SER
SEQRES 4 B 161 PRO SER LYS LYS PRO MET PHE THR LEU GLU GLU ARG VAL
SEQRES 5 B 161 ALA LEU ALA GLN GLN ALA THR ALA HIS LEU GLY ASN VAL
SEQRES 6 B 161 GLU VAL VAL GLY PHE SER ASP LEU MET ALA ASN PHE ALA
SEQRES 7 B 161 ARG ASN GLN HIS ALA THR VAL LEU ILE ARG GLY LEU ARG
SEQRES 8 B 161 ALA VAL ALA ASP PHE GLU TYR GLU MET GLN LEU ALA HIS
SEQRES 9 B 161 MET ASN ARG HIS LEU MET PRO GLU LEU GLU SER VAL PHE
SEQRES 10 B 161 LEU MET PRO SER LYS GLU TRP SER PHE ILE SER SER SER
SEQRES 11 B 161 LEU VAL LYS GLU VAL ALA ARG HIS GLN GLY ASP VAL THR
SEQRES 12 B 161 HIS PHE LEU PRO GLU ASN VAL HIS GLN ALA LEU MET ALA
SEQRES 13 B 161 LYS LEU ALA VAL ASP
HET EXG A 201 16
HET SO4 A 202 5
HET SO4 A 203 5
HET SO4 A 204 5
HET SO4 A 205 5
HET DMS A 206 4
HET EXG B 201 16
HET SO4 B 202 5
HET SO4 B 203 5
HETNAM EXG 1-BENZYL-1H-IMIDAZO[4,5-B]PYRIDINE
HETNAM SO4 SULFATE ION
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 3 EXG 2(C13 H11 N3)
FORMUL 4 SO4 6(O4 S 2-)
FORMUL 8 DMS C2 H6 O S
FORMUL 12 HOH *321(H2 O)
HELIX 1 AA1 THR A 15 PHE A 29 1 15
HELIX 2 AA2 SER A 39 LYS A 43 5 5
HELIX 3 AA3 THR A 47 ALA A 60 1 14
HELIX 4 AA4 LEU A 73 GLN A 81 1 9
HELIX 5 AA5 ALA A 92 MET A 110 1 19
HELIX 6 AA6 SER A 121 SER A 125 5 5
HELIX 7 AA7 SER A 128 HIS A 138 1 11
HELIX 8 AA8 VAL A 142 LEU A 146 5 5
HELIX 9 AA9 PRO A 147 ALA A 159 1 13
HELIX 10 AB1 THR B 15 PHE B 29 1 15
HELIX 11 AB2 THR B 47 ALA B 60 1 14
HELIX 12 AB3 LEU B 73 GLN B 81 1 9
HELIX 13 AB4 ALA B 92 MET B 110 1 19
HELIX 14 AB5 SER B 121 SER B 125 5 5
HELIX 15 AB6 SER B 128 HIS B 138 1 11
HELIX 16 AB7 VAL B 142 LEU B 146 5 5
HELIX 17 AB8 PRO B 147 VAL B 160 1 14
SHEET 1 AA110 VAL A 65 PHE A 70 0
SHEET 2 AA110 HIS A 31 ALA A 37 1 N LEU A 34 O GLU A 66
SHEET 3 AA110 ARG A 4 GLY A 9 1 N TYR A 7 O ILE A 33
SHEET 4 AA110 VAL A 85 GLY A 89 1 O ILE A 87 N ILE A 6
SHEET 5 AA110 GLU A 114 LEU A 118 1 O VAL A 116 N LEU A 86
SHEET 6 AA110 GLU B 114 LEU B 118 -1 O PHE B 117 N PHE A 117
SHEET 7 AA110 VAL B 85 GLY B 89 1 N LEU B 86 O VAL B 116
SHEET 8 AA110 ARG B 4 GLY B 9 1 N ILE B 6 O ILE B 87
SHEET 9 AA110 HIS B 31 ALA B 37 1 O ILE B 33 N TYR B 7
SHEET 10 AA110 VAL B 65 PHE B 70 1 O VAL B 68 N ILE B 36
CISPEP 1 ASP A 12 PRO A 13 0 -3.82
CISPEP 2 ASP B 12 PRO B 13 0 -2.97
SITE 1 AC1 7 ALA A 37 LEU A 73 MET A 74 LEU A 102
SITE 2 AC1 7 GLU A 134 SO4 A 203 HOH A 345
SITE 1 AC2 7 SER A 121 LYS A 122 HOH A 312 HOH A 313
SITE 2 AC2 7 HOH A 335 HIS B 104 ARG B 107
SITE 1 AC3 8 GLY A 9 THR A 10 LYS A 42 ARG A 88
SITE 2 AC3 8 EXG A 201 HOH A 308 HOH A 374 HOH A 395
SITE 1 AC4 9 HIS A 18 ARG A 91 SER A 128 SER A 129
SITE 2 AC4 9 DMS A 206 HOH A 301 HOH A 308 HOH A 319
SITE 3 AC4 9 HOH A 374
SITE 1 AC5 8 SER A 39 PRO A 40 SER A 41 GLU A 134
SITE 2 AC5 8 ARG A 137 HIS A 138 HOH A 380 HOH A 411
SITE 1 AC6 6 TYR A 7 PRO A 8 ARG A 88 GLY A 89
SITE 2 AC6 6 SO4 A 204 HOH A 306
SITE 1 AC7 8 GLY B 9 THR B 10 ALA B 37 LEU B 73
SITE 2 AC7 8 MET B 74 LEU B 102 GLU B 134 HOH B 332
SITE 1 AC8 8 HIS A 104 ARG A 107 SER B 121 LYS B 122
SITE 2 AC8 8 HOH B 301 HOH B 303 HOH B 306 HOH B 322
SITE 1 AC9 6 HIS B 18 ARG B 91 SER B 128 SER B 129
SITE 2 AC9 6 HOH B 312 HOH B 329
CRYST1 135.050 135.050 135.050 90.00 90.00 90.00 I 2 3 48
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 0.007405 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007405 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007405 0.00000
(ATOM LINES ARE NOT SHOWN.)
END