HEADER TRANSFERASE 19-SEP-13 4C72
TITLE CRYSTAL STRUCTURE OF M. TUBERCULOSIS C171Q KASA IN COMPLEX WITH TLM5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BETA-KETOACYL ACP SYNTHASE;
COMPND 5 EC: 2.3.1.41;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS H37RV;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 EXPRESSION_SYSTEM: MYCOBACTERIUM SMEGMATIS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 1772;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: MC2155;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PFPCA1
KEYWDS TRANSFERASE, BETO-KETOACYL-ACP SYNTHASE, KAS ENZYME, CONDENSING
KEYWDS 2 ENZYME, TYPE 2 FATTY ACID BIOSYNTHESIS, MYCOLIC ACID SYNTHESIS,
KEYWDS 3 THIOLACTOMYCIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SCHIEBEL,K.KAPILASHRAMI,A.FEKETE,G.R.BOMMINENI,C.M.SCHAEFER,
AUTHOR 2 M.J.MUELLER,P.J.TONGE,C.KISKER
REVDAT 5 20-DEC-23 4C72 1 REMARK LINK
REVDAT 4 11-DEC-13 4C72 1 JRNL
REVDAT 3 23-OCT-13 4C72 1 JRNL
REVDAT 2 16-OCT-13 4C72 1 JRNL
REVDAT 1 09-OCT-13 4C72 0
JRNL AUTH J.SCHIEBEL,K.KAPILASHRAMI,A.FEKETE,G.R.BOMMINENI,
JRNL AUTH 2 C.M.SCHAEFER,M.J.MUELLER,P.J.TONGE,C.KISKER
JRNL TITL STRUCTURAL BASIS FOR THE RECOGNITION OF MYCOLIC ACID
JRNL TITL 2 PRECURSORS BY KASA, A CONDENSING ENZYME AND DRUG TARGET FROM
JRNL TITL 3 MYCOBACTERIUM TUBERCULOSIS
JRNL REF J.BIOL.CHEM. V. 288 34190 2013
JRNL REFN ISSN 0021-9258
JRNL PMID 24108128
JRNL DOI 10.1074/JBC.M113.511436
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 91.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 184715
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) : 0.137
REMARK 3 R VALUE (WORKING SET) : 0.136
REMARK 3 FREE R VALUE : 0.156
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9803
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 13541
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 738
REMARK 3 BIN FREE R VALUE : 0.2580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6036
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 200
REMARK 3 SOLVENT ATOMS : 911
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.13000
REMARK 3 B22 (A**2) : 1.05000
REMARK 3 B33 (A**2) : -0.92000
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): 0.046
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.048
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.030
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.780
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.977
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.971
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6770 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9230 ; 1.776 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 953 ; 6.268 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 279 ;32.165 ;23.728
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1077 ;12.034 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 54 ;16.685 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1019 ; 0.124 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5250 ; 0.016 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 4294 ; 1.366 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6910 ; 2.100 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2476 ; 3.863 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2255 ; 5.864 ; 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 : 18
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 4 A 63
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0835 -33.3151 10.2514
REMARK 3 T TENSOR
REMARK 3 T11: 0.0469 T22: 0.0343
REMARK 3 T33: 0.0571 T12: 0.0138
REMARK 3 T13: 0.0048 T23: 0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 0.8340 L22: 0.4479
REMARK 3 L33: 0.4939 L12: 0.0751
REMARK 3 L13: -0.0514 L23: -0.0106
REMARK 3 S TENSOR
REMARK 3 S11: -0.0381 S12: 0.0289 S13: -0.1203
REMARK 3 S21: -0.0164 S22: 0.0070 S23: -0.0431
REMARK 3 S31: 0.1023 S32: 0.0790 S33: 0.0311
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 64 A 82
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1675 -43.7695 25.6012
REMARK 3 T TENSOR
REMARK 3 T11: 0.1541 T22: 0.0685
REMARK 3 T33: 0.1114 T12: 0.0246
REMARK 3 T13: 0.0104 T23: 0.0375
REMARK 3 L TENSOR
REMARK 3 L11: 0.3188 L22: 0.4239
REMARK 3 L33: 2.3394 L12: 0.3547
REMARK 3 L13: -0.6872 L23: -0.7389
REMARK 3 S TENSOR
REMARK 3 S11: -0.0556 S12: -0.0695 S13: -0.1346
REMARK 3 S21: -0.0065 S22: -0.0801 S23: -0.1344
REMARK 3 S31: 0.3018 S32: 0.2081 S33: 0.1356
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 83 A 102
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9552 -33.4151 27.0805
REMARK 3 T TENSOR
REMARK 3 T11: 0.0903 T22: 0.1066
REMARK 3 T33: 0.0863 T12: 0.0408
REMARK 3 T13: -0.0294 T23: 0.0250
REMARK 3 L TENSOR
REMARK 3 L11: 1.3323 L22: 1.5356
REMARK 3 L33: 0.7491 L12: 0.9245
REMARK 3 L13: -0.1873 L23: 0.1766
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: -0.0632 S13: -0.2239
REMARK 3 S21: 0.1341 S22: 0.0203 S23: -0.1816
REMARK 3 S31: 0.1661 S32: 0.2067 S33: -0.0244
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 103 A 160
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7532 -32.7173 31.9440
REMARK 3 T TENSOR
REMARK 3 T11: 0.0970 T22: 0.0576
REMARK 3 T33: 0.0737 T12: -0.0002
REMARK 3 T13: -0.0055 T23: 0.0159
REMARK 3 L TENSOR
REMARK 3 L11: 0.8582 L22: 0.3781
REMARK 3 L33: 0.6685 L12: 0.4360
REMARK 3 L13: -0.0272 L23: 0.1123
REMARK 3 S TENSOR
REMARK 3 S11: 0.0110 S12: -0.0613 S13: -0.0502
REMARK 3 S21: 0.1006 S22: -0.0013 S23: -0.0034
REMARK 3 S31: 0.1220 S32: 0.0214 S33: -0.0097
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 161 A 183
REMARK 3 ORIGIN FOR THE GROUP (A): 3.3702 -19.0182 23.3336
REMARK 3 T TENSOR
REMARK 3 T11: 0.0641 T22: 0.0767
REMARK 3 T33: 0.0869 T12: 0.0104
REMARK 3 T13: -0.0067 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 0.0992 L22: 0.4874
REMARK 3 L33: 0.5150 L12: -0.0284
REMARK 3 L13: -0.0041 L23: -0.1875
REMARK 3 S TENSOR
REMARK 3 S11: -0.0071 S12: -0.0444 S13: 0.0071
REMARK 3 S21: 0.0398 S22: -0.0066 S23: -0.0568
REMARK 3 S31: -0.0281 S32: -0.0230 S33: 0.0136
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 184 A 251
REMARK 3 ORIGIN FOR THE GROUP (A): -0.0391 -28.5528 9.5722
REMARK 3 T TENSOR
REMARK 3 T11: 0.0491 T22: 0.0566
REMARK 3 T33: 0.0594 T12: 0.0076
REMARK 3 T13: -0.0010 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.5593 L22: 0.3700
REMARK 3 L33: 0.4607 L12: 0.1162
REMARK 3 L13: -0.0889 L23: -0.0572
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S12: 0.0570 S13: -0.0382
REMARK 3 S21: -0.0282 S22: 0.0158 S23: -0.0141
REMARK 3 S31: 0.0565 S32: 0.0003 S33: -0.0045
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 252 A 266
REMARK 3 ORIGIN FOR THE GROUP (A): 23.5092 -19.3974 21.7718
REMARK 3 T TENSOR
REMARK 3 T11: 0.0141 T22: 0.1664
REMARK 3 T33: 0.1090 T12: -0.0148
REMARK 3 T13: -0.0209 T23: -0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 2.1104 L22: 2.2587
REMARK 3 L33: 3.4224 L12: -0.4949
REMARK 3 L13: 0.9013 L23: 0.1537
REMARK 3 S TENSOR
REMARK 3 S11: 0.1068 S12: 0.0348 S13: 0.0129
REMARK 3 S21: 0.0773 S22: -0.0190 S23: -0.2634
REMARK 3 S31: -0.0202 S32: 0.4496 S33: -0.0878
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 267 A 372
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3659 -16.8310 5.6613
REMARK 3 T TENSOR
REMARK 3 T11: 0.0555 T22: 0.0786
REMARK 3 T33: 0.0725 T12: -0.0003
REMARK 3 T13: -0.0010 T23: 0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 0.5934 L22: 0.2955
REMARK 3 L33: 0.4624 L12: -0.1011
REMARK 3 L13: -0.1699 L23: 0.0476
REMARK 3 S TENSOR
REMARK 3 S11: -0.0004 S12: 0.0613 S13: 0.0567
REMARK 3 S21: -0.0313 S22: -0.0007 S23: -0.0237
REMARK 3 S31: -0.0338 S32: 0.0263 S33: 0.0012
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 : A 373 A 416
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4506 -19.6724 1.7403
REMARK 3 T TENSOR
REMARK 3 T11: 0.0558 T22: 0.0795
REMARK 3 T33: 0.0706 T12: 0.0001
REMARK 3 T13: 0.0074 T23: 0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 0.9235 L22: 0.2883
REMARK 3 L33: 0.7103 L12: -0.0130
REMARK 3 L13: -0.3393 L23: 0.1849
REMARK 3 S TENSOR
REMARK 3 S11: -0.0064 S12: 0.0723 S13: 0.0451
REMARK 3 S21: -0.0537 S22: 0.0172 S23: -0.0222
REMARK 3 S31: -0.0214 S32: 0.0638 S33: -0.0108
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 4 B 63
REMARK 3 ORIGIN FOR THE GROUP (A): -19.4108 -14.1465 39.2546
REMARK 3 T TENSOR
REMARK 3 T11: 0.0346 T22: 0.0799
REMARK 3 T33: 0.0377 T12: 0.0043
REMARK 3 T13: 0.0239 T23: -0.0345
REMARK 3 L TENSOR
REMARK 3 L11: 0.6341 L22: 1.0117
REMARK 3 L33: 0.8259 L12: 0.1709
REMARK 3 L13: 0.1163 L23: -0.0489
REMARK 3 S TENSOR
REMARK 3 S11: -0.0141 S12: -0.0972 S13: 0.0656
REMARK 3 S21: 0.1038 S22: -0.0456 S23: 0.1146
REMARK 3 S31: -0.0627 S32: -0.2197 S33: 0.0597
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 64 B 82
REMARK 3 ORIGIN FOR THE GROUP (A): -27.5501 -19.2413 23.3281
REMARK 3 T TENSOR
REMARK 3 T11: 0.0534 T22: 0.2187
REMARK 3 T33: 0.0971 T12: 0.0137
REMARK 3 T13: -0.0097 T23: -0.0587
REMARK 3 L TENSOR
REMARK 3 L11: 0.2797 L22: 1.3214
REMARK 3 L33: 3.6801 L12: -0.4966
REMARK 3 L13: -0.8676 L23: 1.1342
REMARK 3 S TENSOR
REMARK 3 S11: 0.0156 S12: 0.1184 S13: -0.0525
REMARK 3 S21: -0.1154 S22: -0.2138 S23: 0.2009
REMARK 3 S31: 0.0021 S32: -0.6477 S33: 0.1983
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 83 B 102
REMARK 3 ORIGIN FOR THE GROUP (A): -19.4997 -5.9733 23.3719
REMARK 3 T TENSOR
REMARK 3 T11: 0.0832 T22: 0.0950
REMARK 3 T33: 0.1060 T12: 0.0490
REMARK 3 T13: -0.0008 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 1.1808 L22: 1.0547
REMARK 3 L33: 1.0540 L12: 0.9648
REMARK 3 L13: -0.1223 L23: 0.3782
REMARK 3 S TENSOR
REMARK 3 S11: -0.0144 S12: 0.0498 S13: 0.2114
REMARK 3 S21: -0.0708 S22: -0.0191 S23: 0.2449
REMARK 3 S31: -0.1798 S32: -0.1844 S33: 0.0335
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 103 B 160
REMARK 3 ORIGIN FOR THE GROUP (A): -15.7249 -22.3652 17.4167
REMARK 3 T TENSOR
REMARK 3 T11: 0.0517 T22: 0.0725
REMARK 3 T33: 0.0843 T12: 0.0010
REMARK 3 T13: 0.0014 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.2258 L22: 1.0595
REMARK 3 L33: 0.4819 L12: 0.2797
REMARK 3 L13: 0.0716 L23: 0.2925
REMARK 3 S TENSOR
REMARK 3 S11: 0.0284 S12: -0.0088 S13: 0.0275
REMARK 3 S21: 0.0285 S22: -0.0510 S23: 0.0845
REMARK 3 S31: 0.0005 S32: -0.1161 S33: 0.0226
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 161 B 183
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2448 -13.4330 28.2828
REMARK 3 T TENSOR
REMARK 3 T11: 0.0772 T22: 0.0549
REMARK 3 T33: 0.0922 T12: 0.0060
REMARK 3 T13: 0.0039 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.1272 L22: 0.9926
REMARK 3 L33: 0.8634 L12: -0.0159
REMARK 3 L13: 0.1517 L23: -0.6827
REMARK 3 S TENSOR
REMARK 3 S11: -0.0071 S12: -0.0337 S13: 0.0675
REMARK 3 S21: 0.0233 S22: -0.0329 S23: -0.0298
REMARK 3 S31: 0.0508 S32: -0.0298 S33: 0.0400
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 184 B 251
REMARK 3 ORIGIN FOR THE GROUP (A): -13.9426 -19.5066 40.3104
REMARK 3 T TENSOR
REMARK 3 T11: 0.0678 T22: 0.0744
REMARK 3 T33: 0.0393 T12: -0.0112
REMARK 3 T13: 0.0260 T23: -0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 0.4617 L22: 0.4692
REMARK 3 L33: 0.6721 L12: 0.0500
REMARK 3 L13: 0.1015 L23: -0.0142
REMARK 3 S TENSOR
REMARK 3 S11: 0.0135 S12: -0.1329 S13: 0.0254
REMARK 3 S21: 0.1064 S22: -0.0510 S23: 0.0407
REMARK 3 S31: 0.0101 S32: -0.1146 S33: 0.0375
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 252 B 266
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9871 6.1818 30.7968
REMARK 3 T TENSOR
REMARK 3 T11: 0.1894 T22: 0.0085
REMARK 3 T33: 0.1347 T12: 0.0093
REMARK 3 T13: -0.0177 T23: -0.0323
REMARK 3 L TENSOR
REMARK 3 L11: 3.4567 L22: 2.0139
REMARK 3 L33: 5.0810 L12: -0.9998
REMARK 3 L13: 1.2979 L23: -1.8350
REMARK 3 S TENSOR
REMARK 3 S11: -0.0605 S12: -0.0626 S13: 0.2885
REMARK 3 S21: 0.1459 S22: 0.0254 S23: 0.0131
REMARK 3 S31: -0.5423 S32: -0.0554 S33: 0.0352
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 : B 267 B 372
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5957 -13.4658 45.8317
REMARK 3 T TENSOR
REMARK 3 T11: 0.0949 T22: 0.0661
REMARK 3 T33: 0.0414 T12: -0.0102
REMARK 3 T13: 0.0006 T23: -0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 0.5810 L22: 0.3034
REMARK 3 L33: 0.7191 L12: -0.0640
REMARK 3 L13: 0.0591 L23: 0.0872
REMARK 3 S TENSOR
REMARK 3 S11: -0.0021 S12: -0.1147 S13: 0.0661
REMARK 3 S21: 0.1310 S22: -0.0351 S23: -0.0162
REMARK 3 S31: -0.0314 S32: -0.0195 S33: 0.0372
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 : B 373 B 416
REMARK 3 ORIGIN FOR THE GROUP (A): -7.3073 -9.8697 49.5098
REMARK 3 T TENSOR
REMARK 3 T11: 0.1107 T22: 0.0851
REMARK 3 T33: 0.0497 T12: -0.0052
REMARK 3 T13: 0.0032 T23: -0.0390
REMARK 3 L TENSOR
REMARK 3 L11: 0.5076 L22: 0.6959
REMARK 3 L33: 0.9402 L12: 0.1312
REMARK 3 L13: -0.0128 L23: 0.0397
REMARK 3 S TENSOR
REMARK 3 S11: 0.0175 S12: -0.1379 S13: 0.0905
REMARK 3 S21: 0.1650 S22: -0.0461 S23: 0.0091
REMARK 3 S31: -0.0933 S32: -0.0769 S33: 0.0286
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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.
REMARK 4
REMARK 4 4C72 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-SEP-13.
REMARK 100 THE DEPOSITION ID IS D_1290056309.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 194886
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 28.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 6.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.44000
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 2WGG
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M KSCN, 15% PEG 3350, PH 9.5
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 37.15500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 91.80500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.55000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 91.80500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.15500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.55000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.9 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 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 -22
REMARK 465 GLY A -21
REMARK 465 SER A -20
REMARK 465 SER A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 SER A -12
REMARK 465 SER A -11
REMARK 465 GLY A -10
REMARK 465 LEU A -9
REMARK 465 VAL A -8
REMARK 465 PRO A -7
REMARK 465 ARG A -6
REMARK 465 GLY A -5
REMARK 465 SER A -4
REMARK 465 HIS A -3
REMARK 465 MET A -2
REMARK 465 ALA A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLN A 3
REMARK 465 MET B -22
REMARK 465 GLY B -21
REMARK 465 SER B -20
REMARK 465 SER B -19
REMARK 465 HIS 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 SER B -12
REMARK 465 SER B -11
REMARK 465 GLY B -10
REMARK 465 LEU B -9
REMARK 465 VAL B -8
REMARK 465 PRO B -7
REMARK 465 ARG B -6
REMARK 465 GLY B -5
REMARK 465 SER B -4
REMARK 465 HIS B -3
REMARK 465 MET B -2
REMARK 465 ALA B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLN B 3
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASP A 28 O HOH A 2036 1.49
REMARK 500 O HOH A 2028 O HOH A 2030 1.54
REMARK 500 OE2 GLU A 224 O HOH A 2323 1.65
REMARK 500 OD1 ASP B 28 O HOH B 2032 1.65
REMARK 500 O HOH B 2087 O HOH B 2214 1.65
REMARK 500 OE1 GLU A 49 O HOH A 2091 1.71
REMARK 500 O HOH B 2184 O HOH B 2187 1.76
REMARK 500 OD1 ASP B 393 NH1 ARG B 415 1.78
REMARK 500 O HOH A 2020 O HOH A 2237 1.78
REMARK 500 O HOH B 2092 O HOH B 2216 1.78
REMARK 500 O ILE A 380 O HOH A 2449 1.83
REMARK 500 O HOH B 2207 O HOH B 2208 1.83
REMARK 500 OE1 GLU B 224 O HOH B 2253 1.84
REMARK 500 O HOH B 2295 O HOH B 2296 1.86
REMARK 500 O2 EDO A 1417 O HOH A 2107 1.86
REMARK 500 O HOH A 2203 O HOH A 2209 1.88
REMARK 500 OXT TYR B 416 O HOH B 2284 1.96
REMARK 500 O HOH B 2145 O HOH B 2296 1.96
REMARK 500 O HOH B 2047 O HOH B 2386 1.97
REMARK 500 O HOH A 2057 O HOH A 2459 1.99
REMARK 500 O HOH A 2020 O HOH A 2459 2.00
REMARK 500 O HOH B 2160 O HOH B 2161 2.01
REMARK 500 CD GLU A 224 O HOH A 2323 2.04
REMARK 500 O HOH B 2097 O HOH B 2098 2.05
REMARK 500 CE MET B 77 O HOH B 2104 2.06
REMARK 500 O HOH A 2201 O HOH A 2202 2.06
REMARK 500 O HOH A 2307 O HOH A 2309 2.06
REMARK 500 OG SER B 301 O HOH B 2320 2.07
REMARK 500 O HOH A 2265 O HOH A 2289 2.07
REMARK 500 O2 EDO B 1421 O HOH B 2404 2.09
REMARK 500 O HOH A 2425 O HOH A 2454 2.09
REMARK 500 O HOH A 2179 O HOH A 2350 2.10
REMARK 500 OXT TYR A 416 O HOH A 2355 2.10
REMARK 500 O HOH A 2104 O HOH A 2107 2.11
REMARK 500 O HOH A 2480 O HOH A 2486 2.11
REMARK 500 O2 EDO B 1422 O HOH B 2407 2.11
REMARK 500 O HOH A 2378 O HOH A 2379 2.12
REMARK 500 O HOH A 2424 O HOH A 2425 2.13
REMARK 500 O1 EDO B 1424 O HOH B 2090 2.14
REMARK 500 O HOH A 2364 O HOH A 2365 2.14
REMARK 500 O HOH A 2352 O HOH A 2353 2.14
REMARK 500 O HOH A 2077 O HOH A 2116 2.15
REMARK 500 O HOH A 2149 O HOH A 2369 2.17
REMARK 500 O HOH A 2028 O HOH A 2123 2.18
REMARK 500 O HOH A 2134 O HOH A 2136 2.18
REMARK 500 O HOH B 2203 O HOH B 2368 2.18
REMARK 500 O HOH A 2462 O HOH A 2463 2.19
REMARK 500 SD MET A 165 O HOH A 2269 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 2408 O HOH A 2440 4445 2.09
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 ARG A 214 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 415 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG B 79 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 MET B 80 CG - SD - CE ANGL. DEV. = -17.4 DEGREES
REMARK 500 MET B 165 CG - SD - CE ANGL. DEV. = -18.4 DEGREES
REMARK 500 PHE B 404 CB - CG - CD2 ANGL. DEV. = -4.6 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 LEU A 116 -50.06 -138.27
REMARK 500 SER A 169 43.82 -145.52
REMARK 500 ALA A 170 -127.87 54.57
REMARK 500 PHE A 230 -4.20 73.06
REMARK 500 ASP A 235 35.94 -147.07
REMARK 500 ALA A 274 59.19 36.18
REMARK 500 PHE A 275 -62.48 -125.67
REMARK 500 ALA A 314 11.97 81.45
REMARK 500 ILE A 347 -115.98 57.72
REMARK 500 ASP A 381 69.06 -110.56
REMARK 500 LEU B 116 -49.77 -137.93
REMARK 500 SER B 169 42.57 -147.87
REMARK 500 ALA B 170 -128.93 52.33
REMARK 500 PHE B 230 -1.55 65.27
REMARK 500 ASP B 235 32.34 -145.52
REMARK 500 PHE B 275 -66.66 -123.51
REMARK 500 ILE B 347 -117.03 53.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLY B 387 10.75
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 A2185 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH B2080 DISTANCE = 6.57 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1418 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 309 O
REMARK 620 2 ASN A 309 OD1 73.3
REMARK 620 3 ALA A 310 O 79.5 77.1
REMARK 620 4 GLU A 354 OE1 162.7 95.6 85.2
REMARK 620 5 ASN A 399 OD1 79.8 79.5 152.4 111.7
REMARK 620 6 ASN A 400 O 89.0 160.7 107.8 103.3 89.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B1417 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 309 OD1
REMARK 620 2 ASN B 309 O 72.5
REMARK 620 3 ALA B 310 O 78.0 78.9
REMARK 620 4 GLU B 354 OE1 96.8 163.2 86.3
REMARK 620 5 ASN B 399 OD1 78.9 79.3 152.0 112.0
REMARK 620 6 ASN B 400 O 160.3 89.2 106.2 102.7 90.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1418
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 1417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1419
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1420
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1418
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1421
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1422
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1423
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1419
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1424
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1425
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1426
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1420
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1427
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1421
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1428
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1422
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1423
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1424
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TLG A 1429
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TLG B 1425
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE M7U A 1430
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE M7U B 1426
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4C6U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF M. TUBERCULOSIS KASA IN COMPLEX WITH TLM5
REMARK 900 RELATED ID: 4C6V RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF M. TUBERCULOSIS KASA IN COMPLEX WITH TLM5
REMARK 900 (SOAK FOR 5 MIN)
REMARK 900 RELATED ID: 4C6W RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF M. TUBERCULOSIS C171Q KASA
REMARK 900 RELATED ID: 4C6X RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF M. TUBERCULOSIS C171Q KASA IN COMPLEX WITH
REMARK 900 THIOLACTOMYCIN (TLM)
REMARK 900 RELATED ID: 4C6Z RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF M. TUBERCULOSIS C171Q KASA IN COMPLEX WITH TLM3
REMARK 900 RELATED ID: 4C70 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF M. TUBERCULOSIS C171Q KASA IN COMPLEX WITH TLM4
REMARK 900 RELATED ID: 4C71 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF M. TUBERCULOSIS C171Q KASA IN COMPLEX WITH
REMARK 900 TLM18
REMARK 900 RELATED ID: 4C73 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF M. TUBERCULOSIS C171Q KASA IN COMPLEX WITH TLM6
DBREF 4C72 A 1 416 UNP I6Y8T4 I6Y8T4_MYCTU 1 416
DBREF 4C72 B 1 416 UNP I6Y8T4 I6Y8T4_MYCTU 1 416
SEQADV 4C72 MET A -22 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 GLY A -21 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 SER A -20 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 SER A -19 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 HIS A -18 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 HIS A -17 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 HIS A -16 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 HIS A -15 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 HIS A -14 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 HIS A -13 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 SER A -12 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 SER A -11 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 GLY A -10 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 LEU A -9 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 VAL A -8 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 PRO A -7 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 ARG A -6 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 GLY A -5 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 SER A -4 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 HIS A -3 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 MET A -2 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 ALA A -1 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 SER A 0 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 GLN A 171 UNP I6Y8T4 CYS 171 ENGINEERED MUTATION
SEQADV 4C72 MET B -22 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 GLY B -21 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 SER B -20 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 SER B -19 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 HIS B -18 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 HIS B -17 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 HIS B -16 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 HIS B -15 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 HIS B -14 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 HIS B -13 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 SER B -12 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 SER B -11 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 GLY B -10 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 LEU B -9 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 VAL B -8 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 PRO B -7 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 ARG B -6 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 GLY B -5 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 SER B -4 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 HIS B -3 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 MET B -2 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 ALA B -1 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 SER B 0 UNP I6Y8T4 EXPRESSION TAG
SEQADV 4C72 GLN B 171 UNP I6Y8T4 CYS 171 ENGINEERED MUTATION
SEQRES 1 A 439 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 439 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET SER GLN
SEQRES 3 A 439 PRO SER THR ALA ASN GLY GLY PHE PRO SER VAL VAL VAL
SEQRES 4 A 439 THR ALA VAL THR ALA THR THR SER ILE SER PRO ASP ILE
SEQRES 5 A 439 GLU SER THR TRP LYS GLY LEU LEU ALA GLY GLU SER GLY
SEQRES 6 A 439 ILE HIS ALA LEU GLU ASP GLU PHE VAL THR LYS TRP ASP
SEQRES 7 A 439 LEU ALA VAL LYS ILE GLY GLY HIS LEU LYS ASP PRO VAL
SEQRES 8 A 439 ASP SER HIS MET GLY ARG LEU ASP MET ARG ARG MET SER
SEQRES 9 A 439 TYR VAL GLN ARG MET GLY LYS LEU LEU GLY GLY GLN LEU
SEQRES 10 A 439 TRP GLU SER ALA GLY SER PRO GLU VAL ASP PRO ASP ARG
SEQRES 11 A 439 PHE ALA VAL VAL VAL GLY THR GLY LEU GLY GLY ALA GLU
SEQRES 12 A 439 ARG ILE VAL GLU SER TYR ASP LEU MET ASN ALA GLY GLY
SEQRES 13 A 439 PRO ARG LYS VAL SER PRO LEU ALA VAL GLN MET ILE MET
SEQRES 14 A 439 PRO ASN GLY ALA ALA ALA VAL ILE GLY LEU GLN LEU GLY
SEQRES 15 A 439 ALA ARG ALA GLY VAL MET THR PRO VAL SER ALA GLN SER
SEQRES 16 A 439 SER GLY SER GLU ALA ILE ALA HIS ALA TRP ARG GLN ILE
SEQRES 17 A 439 VAL MET GLY ASP ALA ASP VAL ALA VAL CYS GLY GLY VAL
SEQRES 18 A 439 GLU GLY PRO ILE GLU ALA LEU PRO ILE ALA ALA PHE SER
SEQRES 19 A 439 MET MET ARG ALA MET SER THR ARG ASN ASP GLU PRO GLU
SEQRES 20 A 439 ARG ALA SER ARG PRO PHE ASP LYS ASP ARG ASP GLY PHE
SEQRES 21 A 439 VAL PHE GLY GLU ALA GLY ALA LEU MET LEU ILE GLU THR
SEQRES 22 A 439 GLU GLU HIS ALA LYS ALA ARG GLY ALA LYS PRO LEU ALA
SEQRES 23 A 439 ARG LEU LEU GLY ALA GLY ILE THR SER ASP ALA PHE HIS
SEQRES 24 A 439 MET VAL ALA PRO ALA ALA ASP GLY VAL ARG ALA GLY ARG
SEQRES 25 A 439 ALA MET THR ARG SER LEU GLU LEU ALA GLY LEU SER PRO
SEQRES 26 A 439 ALA ASP ILE ASP HIS VAL ASN ALA HIS GLY THR ALA THR
SEQRES 27 A 439 PRO ILE GLY ASP ALA ALA GLU ALA ASN ALA ILE ARG VAL
SEQRES 28 A 439 ALA GLY CYS ASP GLN ALA ALA VAL TYR ALA PRO LYS SER
SEQRES 29 A 439 ALA LEU GLY HIS SER ILE GLY ALA VAL GLY ALA LEU GLU
SEQRES 30 A 439 SER VAL LEU THR VAL LEU THR LEU ARG ASP GLY VAL ILE
SEQRES 31 A 439 PRO PRO THR LEU ASN TYR GLU THR PRO ASP PRO GLU ILE
SEQRES 32 A 439 ASP LEU ASP VAL VAL ALA GLY GLU PRO ARG TYR GLY ASP
SEQRES 33 A 439 TYR ARG TYR ALA VAL ASN ASN SER PHE GLY PHE GLY GLY
SEQRES 34 A 439 HIS ASN VAL ALA LEU ALA PHE GLY ARG TYR
SEQRES 1 B 439 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 439 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET SER GLN
SEQRES 3 B 439 PRO SER THR ALA ASN GLY GLY PHE PRO SER VAL VAL VAL
SEQRES 4 B 439 THR ALA VAL THR ALA THR THR SER ILE SER PRO ASP ILE
SEQRES 5 B 439 GLU SER THR TRP LYS GLY LEU LEU ALA GLY GLU SER GLY
SEQRES 6 B 439 ILE HIS ALA LEU GLU ASP GLU PHE VAL THR LYS TRP ASP
SEQRES 7 B 439 LEU ALA VAL LYS ILE GLY GLY HIS LEU LYS ASP PRO VAL
SEQRES 8 B 439 ASP SER HIS MET GLY ARG LEU ASP MET ARG ARG MET SER
SEQRES 9 B 439 TYR VAL GLN ARG MET GLY LYS LEU LEU GLY GLY GLN LEU
SEQRES 10 B 439 TRP GLU SER ALA GLY SER PRO GLU VAL ASP PRO ASP ARG
SEQRES 11 B 439 PHE ALA VAL VAL VAL GLY THR GLY LEU GLY GLY ALA GLU
SEQRES 12 B 439 ARG ILE VAL GLU SER TYR ASP LEU MET ASN ALA GLY GLY
SEQRES 13 B 439 PRO ARG LYS VAL SER PRO LEU ALA VAL GLN MET ILE MET
SEQRES 14 B 439 PRO ASN GLY ALA ALA ALA VAL ILE GLY LEU GLN LEU GLY
SEQRES 15 B 439 ALA ARG ALA GLY VAL MET THR PRO VAL SER ALA GLN SER
SEQRES 16 B 439 SER GLY SER GLU ALA ILE ALA HIS ALA TRP ARG GLN ILE
SEQRES 17 B 439 VAL MET GLY ASP ALA ASP VAL ALA VAL CYS GLY GLY VAL
SEQRES 18 B 439 GLU GLY PRO ILE GLU ALA LEU PRO ILE ALA ALA PHE SER
SEQRES 19 B 439 MET MET ARG ALA MET SER THR ARG ASN ASP GLU PRO GLU
SEQRES 20 B 439 ARG ALA SER ARG PRO PHE ASP LYS ASP ARG ASP GLY PHE
SEQRES 21 B 439 VAL PHE GLY GLU ALA GLY ALA LEU MET LEU ILE GLU THR
SEQRES 22 B 439 GLU GLU HIS ALA LYS ALA ARG GLY ALA LYS PRO LEU ALA
SEQRES 23 B 439 ARG LEU LEU GLY ALA GLY ILE THR SER ASP ALA PHE HIS
SEQRES 24 B 439 MET VAL ALA PRO ALA ALA ASP GLY VAL ARG ALA GLY ARG
SEQRES 25 B 439 ALA MET THR ARG SER LEU GLU LEU ALA GLY LEU SER PRO
SEQRES 26 B 439 ALA ASP ILE ASP HIS VAL ASN ALA HIS GLY THR ALA THR
SEQRES 27 B 439 PRO ILE GLY ASP ALA ALA GLU ALA ASN ALA ILE ARG VAL
SEQRES 28 B 439 ALA GLY CYS ASP GLN ALA ALA VAL TYR ALA PRO LYS SER
SEQRES 29 B 439 ALA LEU GLY HIS SER ILE GLY ALA VAL GLY ALA LEU GLU
SEQRES 30 B 439 SER VAL LEU THR VAL LEU THR LEU ARG ASP GLY VAL ILE
SEQRES 31 B 439 PRO PRO THR LEU ASN TYR GLU THR PRO ASP PRO GLU ILE
SEQRES 32 B 439 ASP LEU ASP VAL VAL ALA GLY GLU PRO ARG TYR GLY ASP
SEQRES 33 B 439 TYR ARG TYR ALA VAL ASN ASN SER PHE GLY PHE GLY GLY
SEQRES 34 B 439 HIS ASN VAL ALA LEU ALA PHE GLY ARG TYR
HET EDO A1417 4
HET K A1418 1
HET EDO A1419 4
HET EDO A1420 4
HET EDO A1421 4
HET EDO A1422 4
HET EDO A1423 4
HET EDO A1424 4
HET EDO A1425 8
HET EDO A1426 4
HET EDO A1427 4
HET EDO A1428 4
HET TLG A1429 16
HET M7U A1430 47
HET K B1417 1
HET EDO B1418 4
HET EDO B1419 4
HET EDO B1420 4
HET EDO B1421 8
HET EDO B1422 4
HET EDO B1423 4
HET EDO B1424 4
HET TLG B1425 16
HET M7U B1426 47
HETNAM EDO 1,2-ETHANEDIOL
HETNAM K POTASSIUM ION
HETNAM TLG (5R)-3-ACETYL-4-HYDROXY-5-METHYL-5-[(1Z)-2-METHYLBUTA-
HETNAM 2 TLG 1,3-DIEN-1-YL]THIOPHEN-2(5H)-ONE
HETNAM M7U (2R)-2-(HEXADECANOYLOXY)-3-{[(10R)-10-
HETNAM 2 M7U METHYLOCTADECANOYL]OXY}PROPYL PHOSPHATE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 18(C2 H6 O2)
FORMUL 4 K 2(K 1+)
FORMUL 15 TLG 2(C12 H14 O3 S)
FORMUL 16 M7U 2(C38 H75 O8 P)
FORMUL 27 HOH *911(H2 O)
HELIX 1 1 ASP A 28 ALA A 38 1 11
HELIX 2 2 ASP A 48 ASP A 55 1 8
HELIX 3 3 PRO A 67 MET A 72 5 6
HELIX 4 4 GLY A 73 MET A 80 1 8
HELIX 5 5 SER A 81 ALA A 98 1 18
HELIX 6 6 ASP A 104 ASP A 106 5 3
HELIX 7 7 GLY A 118 GLY A 133 1 16
HELIX 8 8 PRO A 134 VAL A 137 5 4
HELIX 9 9 LEU A 140 MET A 146 1 7
HELIX 10 10 ASN A 148 GLY A 159 1 12
HELIX 11 11 SER A 169 GLN A 171 5 3
HELIX 12 12 SER A 172 MET A 187 1 16
HELIX 13 13 GLU A 203 MET A 212 1 10
HELIX 14 14 GLU A 222 ALA A 226 5 5
HELIX 15 15 GLU A 251 GLY A 258 1 8
HELIX 16 16 GLY A 284 GLY A 299 1 16
HELIX 17 17 SER A 301 ILE A 305 5 5
HELIX 18 18 THR A 315 ALA A 329 1 15
HELIX 19 19 PRO A 339 GLY A 344 1 6
HELIX 20 20 SER A 346 GLY A 348 5 3
HELIX 21 21 ALA A 349 GLY A 365 1 17
HELIX 22 22 ASP B 28 ALA B 38 1 11
HELIX 23 23 ASP B 48 ASP B 55 1 8
HELIX 24 24 PRO B 67 MET B 72 5 6
HELIX 25 25 GLY B 73 MET B 80 1 8
HELIX 26 26 SER B 81 ALA B 98 1 18
HELIX 27 27 ASP B 104 ASP B 106 5 3
HELIX 28 28 GLY B 118 GLY B 133 1 16
HELIX 29 29 PRO B 134 VAL B 137 5 4
HELIX 30 30 LEU B 140 MET B 146 1 7
HELIX 31 31 ASN B 148 GLY B 159 1 12
HELIX 32 32 SER B 169 GLN B 171 5 3
HELIX 33 33 SER B 172 MET B 187 1 16
HELIX 34 34 GLU B 203 MET B 213 1 11
HELIX 35 35 GLU B 222 ALA B 226 5 5
HELIX 36 36 GLU B 251 GLY B 258 1 8
HELIX 37 37 GLY B 284 GLY B 299 1 16
HELIX 38 38 SER B 301 ILE B 305 5 5
HELIX 39 39 THR B 315 ALA B 329 1 15
HELIX 40 40 PRO B 339 GLY B 344 1 6
HELIX 41 41 SER B 346 GLY B 348 5 3
HELIX 42 42 ALA B 349 GLY B 365 1 17
SHEET 1 AA11 VAL A 164 MET A 165 0
SHEET 2 AA11 PHE A 108 GLY A 113 1 O VAL A 110 N MET A 165
SHEET 3 AA11 VAL A 192 GLY A 197 1 O VAL A 192 N ALA A 109
SHEET 4 AA11 ALA A 242 THR A 250 -1 O ALA A 244 N GLY A 197
SHEET 5 AA11 VAL A 14 THR A 23 -1 O VAL A 15 N GLU A 249
SHEET 6 AA11 ALA A 263 SER A 272 -1 O ALA A 263 N VAL A 16
SHEET 7 AA11 HIS A 407 GLY A 414 -1 O ASN A 408 N THR A 271
SHEET 8 AA11 TYR A 396 GLY A 403 -1 O ALA A 397 N PHE A 413
SHEET 9 AA11 HIS A 307 ASN A 309 1 O HIS A 307 N VAL A 398
SHEET 10 AA11 ALA A 335 TYR A 337 1 O ALA A 335 N VAL A 308
SHEET 11 AA11 ASP A 383 VAL A 384 1 O ASP A 383 N VAL A 336
SHEET 1 AB 2 HIS A 44 ALA A 45 0
SHEET 2 AB 2 ILE A 60 GLY A 61 -1 O GLY A 61 N HIS A 44
SHEET 1 AC 2 VAL A 366 ILE A 367 0
SHEET 2 AC 2 ARG A 390 TYR A 391 -1 O ARG A 390 N ILE A 367
SHEET 1 BA11 VAL B 164 MET B 165 0
SHEET 2 BA11 PHE B 108 GLY B 113 1 O VAL B 110 N MET B 165
SHEET 3 BA11 VAL B 192 GLY B 197 1 O VAL B 192 N ALA B 109
SHEET 4 BA11 ALA B 242 THR B 250 -1 O ALA B 244 N GLY B 197
SHEET 5 BA11 VAL B 14 THR B 23 -1 O VAL B 15 N GLU B 249
SHEET 6 BA11 ALA B 263 SER B 272 -1 O ALA B 263 N VAL B 16
SHEET 7 BA11 HIS B 407 GLY B 414 -1 O ASN B 408 N THR B 271
SHEET 8 BA11 TYR B 396 GLY B 403 -1 O ALA B 397 N PHE B 413
SHEET 9 BA11 HIS B 307 ASN B 309 1 O HIS B 307 N VAL B 398
SHEET 10 BA11 ALA B 335 TYR B 337 1 O ALA B 335 N VAL B 308
SHEET 11 BA11 ASP B 383 VAL B 384 1 O ASP B 383 N VAL B 336
SHEET 1 BB 2 HIS B 44 ALA B 45 0
SHEET 2 BB 2 ILE B 60 GLY B 61 -1 O GLY B 61 N HIS B 44
SHEET 1 BC 2 VAL B 366 ILE B 367 0
SHEET 2 BC 2 ARG B 390 TYR B 391 -1 O ARG B 390 N ILE B 367
LINK O ASN A 309 K K A1418 1555 1555 2.77
LINK OD1 ASN A 309 K K A1418 1555 1555 2.66
LINK O ALA A 310 K K A1418 1555 1555 3.03
LINK OE1 GLU A 354 K K A1418 1555 1555 2.59
LINK OD1 ASN A 399 K K A1418 1555 1555 2.63
LINK O ASN A 400 K K A1418 1555 1555 2.70
LINK OD1 ASN B 309 K K B1417 1555 1555 2.65
LINK O ASN B 309 K K B1417 1555 1555 2.77
LINK O ALA B 310 K K B1417 1555 1555 2.97
LINK OE1 GLU B 354 K K B1417 1555 1555 2.57
LINK OD1 ASN B 399 K K B1417 1555 1555 2.61
LINK O ASN B 400 K K B1417 1555 1555 2.72
SITE 1 AC1 7 ALA A 57 SER A 211 HOH A2107 HOH A2109
SITE 2 AC1 7 HOH A2489 PRO B 134 ARG B 135
SITE 1 AC2 6 ASN A 309 ALA A 310 HIS A 311 GLU A 354
SITE 2 AC2 6 ASN A 399 ASN A 400
SITE 1 AC3 6 ASN B 309 ALA B 310 HIS B 311 GLU B 354
SITE 2 AC3 6 ASN B 399 ASN B 400
SITE 1 AC4 5 ALA A 18 VAL A 19 GLU A 30 HOH A2012
SITE 2 AC4 5 HOH A2491
SITE 1 AC5 5 ARG A 121 GLU A 124 SER A 125 LEU A 128
SITE 2 AC5 5 SER A 138
SITE 1 AC6 6 VAL B 384 VAL B 385 ALA B 386 ARG B 390
SITE 2 AC6 6 HOH B2384 HOH B2403
SITE 1 AC7 7 PHE A 275 PRO A 280 ALA A 282 ILE A 317
SITE 2 AC7 7 TYR A 391 HOH A2409 HOH A2492
SITE 1 AC8 4 ALA A 282 ASP A 283 HOH A2493 HOH A2494
SITE 1 AC9 5 ASP A 283 VAL A 285 HOH A2377 HOH A2495
SITE 2 AC9 5 ARG B 161
SITE 1 BC1 5 SER B 211 ARG B 214 ALA B 215 MET B 216
SITE 2 BC1 5 THR B 218
SITE 1 BC2 8 SER A 211 ARG A 214 ALA A 215 MET A 216
SITE 2 BC2 8 THR A 218 ARG A 395 HOH A2299 HOH A2496
SITE 1 BC3 4 ARG A 79 GLN A 84 GLN A 143 HOH A2497
SITE 1 BC4 5 ASP A 69 TYR A 82 M7U A1430 HOH A2118
SITE 2 BC4 5 HOH A2127
SITE 1 BC5 3 ARG A 74 ARG A 78 GLN B 333
SITE 1 BC6 7 THR A 292 GLU A 296 LEU A 300 PRO A 302
SITE 2 BC6 7 HOH A2391 HOH A2395 HOH A2500
SITE 1 BC7 4 PRO B 201 M7U B1426 HOH B2125 HOH B2404
SITE 1 BC8 5 TYR A 126 ASN A 130 HOH A2501 HOH A2502
SITE 2 BC8 5 TRP B 54
SITE 1 BC9 5 THR B 292 GLU B 296 LEU B 300 HOH B2319
SITE 2 BC9 5 HOH B2407
SITE 1 CC1 5 TRP A 54 HOH A2295 TYR B 126 ASN B 130
SITE 2 CC1 5 HOH B2408
SITE 1 CC2 6 PRO A 134 ARG A 135 LEU B 56 ALA B 57
SITE 2 CC2 6 MET B 212 HOH B2090
SITE 1 CC3 13 GLN A 171 VAL A 278 ALA A 279 PRO A 280
SITE 2 CC3 13 HIS A 311 THR A 313 HIS A 345 PHE A 402
SITE 3 CC3 13 GLY A 403 PHE A 404 GLY A 406 HOH A2274
SITE 4 CC3 13 HOH A2406
SITE 1 CC4 14 GLN B 171 PHE B 237 VAL B 278 ALA B 279
SITE 2 CC4 14 PRO B 280 HIS B 311 THR B 313 HIS B 345
SITE 3 CC4 14 PHE B 402 GLY B 403 PHE B 404 GLY B 406
SITE 4 CC4 14 HOH B2224 HOH B2336
SITE 1 CC5 13 GLY A 115 GLU A 120 ALA A 170 GLU A 199
SITE 2 CC5 13 GLY A 200 PRO A 201 GLU A 203 ALA A 209
SITE 3 CC5 13 PHE A 239 HIS A 345 EDO A1426 HOH A2221
SITE 4 CC5 13 ILE B 145
SITE 1 CC6 17 VAL A 142 ILE A 145 GLY B 115 GLU B 120
SITE 2 CC6 17 ALA B 170 GLU B 199 GLY B 200 PRO B 201
SITE 3 CC6 17 GLU B 203 LEU B 205 ALA B 209 PHE B 239
SITE 4 CC6 17 HIS B 345 ILE B 347 EDO B1421 HOH B2125
SITE 5 CC6 17 HOH B2404
CRYST1 74.310 89.100 183.610 90.00 90.00 90.00 P 21 21 21 8
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 0.013457 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011223 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005446 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
