HEADER DNA-BINDING 31-OCT-04 1WBB
TITLE CRYSTAL STRUCTURE OF E. COLI DNA MISMATCH REPAIR ENZYME MUTS, E38A
TITLE 2 MUTANT, IN COMPLEX WITH A G.T MISMATCH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA MISMATCH REPAIR PROTEIN MUTS;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 1-800;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 5'-D(*AP*GP*CP*TP*GP*CP*CP*AP*GP*GP
COMPND 9 *CP*AP*CP*CP*AP*GP*TP*G)-3';
COMPND 10 CHAIN: E;
COMPND 11 ENGINEERED: YES;
COMPND 12 OTHER_DETAILS: G\:T MISMATCH DNA;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: 5'-D(*AP*CP*TP*GP*GP*TP*GP*CP*TP*TP *GP*GP*CP*AP*GP*CP*T)-
COMPND 15 3';
COMPND 16 CHAIN: F;
COMPND 17 ENGINEERED: YES
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: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: B834 (BL21);
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET3D;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PM800;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 MOL_ID: 3;
SOURCE 13 SYNTHETIC: YES
KEYWDS DNA-BINDING, ATP-BINDING, DNA BINDING, DNA REPAIR, MISMATCH
KEYWDS 2 RECOGNITION
EXPDTA X-RAY DIFFRACTION
AUTHOR G.NATRAJAN,D.GEORGIJEVIC,J.H.G.LEBBINK,H.H.K.WINTERWERP,N.DE WIND,
AUTHOR 2 T.K.SIXMA
REVDAT 4 13-DEC-23 1WBB 1 LINK
REVDAT 3 13-JUL-11 1WBB 1 VERSN
REVDAT 2 24-FEB-09 1WBB 1 VERSN
REVDAT 1 18-JAN-06 1WBB 0
JRNL AUTH J.H.G.LEBBINK,D.GEORGIJEVIC,G.NATRAJAN,A.FISH,
JRNL AUTH 2 H.H.K.WINTERWERP,T.K.SIXMA,N.DE WIND
JRNL TITL DUAL ROLE OF MUTS GLUTAMATE 38 IN DNA MISMATCH
JRNL TITL 2 DISCRIMINATION AND IN THE AUTHORIZATION OF REPAIR.
JRNL REF EMBO J. V. 25 409 2006
JRNL REFN ISSN 0261-4189
JRNL PMID 16407973
JRNL DOI 10.1038/SJ.EMBOJ.7600936
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 73763
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : SAME AS FOR ENTRY 1E3M
REMARK 3 R VALUE (WORKING + TEST SET) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1452
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5238
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3090
REMARK 3 BIN FREE R VALUE SET COUNT : 99
REMARK 3 BIN FREE R VALUE : 0.3670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12163
REMARK 3 NUCLEIC ACID ATOMS : 714
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 285
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 53.02
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.16900
REMARK 3 B22 (A**2) : 4.91500
REMARK 3 B33 (A**2) : -2.74600
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): 0.439
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.288
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.246
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.618
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13200 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 11955 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18018 ; 1.225 ; 2.044
REMARK 3 BOND ANGLES OTHERS (DEGREES): 27736 ; 0.799 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1536 ; 6.067 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2012 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14142 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2512 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2700 ; 0.190 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 13825 ; 0.216 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 8174 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 310 ; 0.152 ; 0.200
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): 24 ; 0.220 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 112 ; 0.216 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.162 ; 0.200
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): 7676 ; 0.352 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12327 ; 0.673 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5524 ; 1.041 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5691 ; 1.763 ; 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 : 21
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 2 A 115
REMARK 3 ORIGIN FOR THE GROUP (A): 95.7440 82.3160 33.8580
REMARK 3 T TENSOR
REMARK 3 T11: 0.2392 T22: 0.1741
REMARK 3 T33: 0.1879 T12: -0.0180
REMARK 3 T13: 0.0201 T23: 0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 3.3665 L22: 3.2067
REMARK 3 L33: 3.4547 L12: -0.6675
REMARK 3 L13: 0.9725 L23: -0.0381
REMARK 3 S TENSOR
REMARK 3 S11: 0.0773 S12: -0.0629 S13: -0.0237
REMARK 3 S21: -0.0397 S22: 0.0071 S23: 0.1484
REMARK 3 S31: -0.0091 S32: -0.0304 S33: -0.0844
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 116 A 265
REMARK 3 ORIGIN FOR THE GROUP (A): 121.3500 83.4950 18.8990
REMARK 3 T TENSOR
REMARK 3 T11: 0.1475 T22: 0.0990
REMARK 3 T33: 0.1986 T12: 0.0163
REMARK 3 T13: -0.0182 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 2.9339 L22: 1.8845
REMARK 3 L33: 1.4724 L12: 0.5863
REMARK 3 L13: -0.7067 L23: 0.0304
REMARK 3 S TENSOR
REMARK 3 S11: 0.0642 S12: 0.1274 S13: -0.0618
REMARK 3 S21: -0.1072 S22: 0.0274 S23: 0.0791
REMARK 3 S31: 0.0026 S32: 0.1095 S33: -0.0916
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 266 A 387
REMARK 3 ORIGIN FOR THE GROUP (A): 135.0840 71.1630 32.8050
REMARK 3 T TENSOR
REMARK 3 T11: 0.2350 T22: 0.2211
REMARK 3 T33: 0.2827 T12: 0.0109
REMARK 3 T13: -0.0360 T23: 0.0477
REMARK 3 L TENSOR
REMARK 3 L11: 1.2821 L22: 1.2183
REMARK 3 L33: 2.3782 L12: -0.2093
REMARK 3 L13: -1.0058 L23: 0.9897
REMARK 3 S TENSOR
REMARK 3 S11: 0.0325 S12: -0.2007 S13: -0.1825
REMARK 3 S21: 0.1607 S22: 0.0853 S23: -0.1436
REMARK 3 S31: 0.1139 S32: 0.0681 S33: -0.1178
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 550 A 567
REMARK 3 ORIGIN FOR THE GROUP (A): 142.7480 64.0090 32.0870
REMARK 3 T TENSOR
REMARK 3 T11: 0.2530 T22: 0.2316
REMARK 3 T33: 0.2101 T12: 0.0346
REMARK 3 T13: -0.0605 T23: 0.0494
REMARK 3 L TENSOR
REMARK 3 L11: 4.5033 L22: 3.5696
REMARK 3 L33: 3.7476 L12: -2.9273
REMARK 3 L13: -3.4967 L23: 4.3965
REMARK 3 S TENSOR
REMARK 3 S11: -0.4245 S12: -0.2327 S13: -0.1123
REMARK 3 S21: 0.0998 S22: 0.5612 S23: -0.0357
REMARK 3 S31: 0.4281 S32: 0.4678 S33: -0.1367
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 444 A 503
REMARK 3 ORIGIN FOR THE GROUP (A): 92.4360 75.7510 77.0280
REMARK 3 T TENSOR
REMARK 3 T11: 0.2824 T22: 0.1689
REMARK 3 T33: 0.1578 T12: 0.0572
REMARK 3 T13: 0.0140 T23: -0.0424
REMARK 3 L TENSOR
REMARK 3 L11: 3.7280 L22: 4.9995
REMARK 3 L33: 10.2921 L12: 1.3102
REMARK 3 L13: 0.5419 L23: 0.8123
REMARK 3 S TENSOR
REMARK 3 S11: -0.1246 S12: 0.0480 S13: -0.1058
REMARK 3 S21: 0.0820 S22: 0.2811 S23: -0.1068
REMARK 3 S31: -0.1984 S32: 0.4562 S33: -0.1565
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 388 A 443
REMARK 3 ORIGIN FOR THE GROUP (A): 126.2770 83.3760 54.1010
REMARK 3 T TENSOR
REMARK 3 T11: 0.4150 T22: 0.4838
REMARK 3 T33: 0.2876 T12: -0.0131
REMARK 3 T13: -0.0588 T23: -0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 3.4105 L22: 1.8152
REMARK 3 L33: 3.2201 L12: -0.9384
REMARK 3 L13: -2.4731 L23: 1.2425
REMARK 3 S TENSOR
REMARK 3 S11: 0.0247 S12: -0.7152 S13: 0.3890
REMARK 3 S21: 0.4364 S22: 0.0976 S23: 0.0754
REMARK 3 S31: 0.0926 S32: 0.2331 S33: -0.1224
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 504 A 549
REMARK 3 ORIGIN FOR THE GROUP (A): 116.2760 87.7240 54.8960
REMARK 3 T TENSOR
REMARK 3 T11: 0.4025 T22: 0.4969
REMARK 3 T33: 0.3568 T12: -0.0634
REMARK 3 T13: 0.0443 T23: -0.0762
REMARK 3 L TENSOR
REMARK 3 L11: 1.4752 L22: 0.2166
REMARK 3 L33: 1.7110 L12: -0.4072
REMARK 3 L13: -2.7779 L23: 0.3605
REMARK 3 S TENSOR
REMARK 3 S11: 0.2803 S12: 0.0107 S13: 0.3838
REMARK 3 S21: 0.1807 S22: -0.0167 S23: 0.0608
REMARK 3 S31: -0.2209 S32: -0.0972 S33: -0.2635
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 568 A 741
REMARK 3 RESIDUE RANGE : A 1801 A 1801
REMARK 3 RESIDUE RANGE : A 1802 A 1802
REMARK 3 ORIGIN FOR THE GROUP (A): 140.2760 58.2480 5.3390
REMARK 3 T TENSOR
REMARK 3 T11: 0.1822 T22: 0.0742
REMARK 3 T33: 0.3034 T12: -0.0033
REMARK 3 T13: 0.0322 T23: -0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 1.1173 L22: 1.0802
REMARK 3 L33: 2.5458 L12: 0.3453
REMARK 3 L13: 0.5659 L23: 1.1075
REMARK 3 S TENSOR
REMARK 3 S11: 0.0464 S12: -0.0947 S13: 0.0042
REMARK 3 S21: -0.0191 S22: 0.0244 S23: -0.0745
REMARK 3 S31: 0.0249 S32: -0.1126 S33: -0.0708
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 742 A 765
REMARK 3 ORIGIN FOR THE GROUP (A): 143.6240 41.0890 5.8500
REMARK 3 T TENSOR
REMARK 3 T11: 0.3350 T22: 0.1279
REMARK 3 T33: 0.5147 T12: 0.0401
REMARK 3 T13: 0.0160 T23: -0.0263
REMARK 3 L TENSOR
REMARK 3 L11: 1.3922 L22: 4.0940
REMARK 3 L33: 5.4016 L12: -2.2606
REMARK 3 L13: 1.8825 L23: 0.9477
REMARK 3 S TENSOR
REMARK 3 S11: 0.2159 S12: -0.3257 S13: -0.5915
REMARK 3 S21: 0.6763 S22: -0.2107 S23: 0.2710
REMARK 3 S31: 0.7840 S32: 0.3804 S33: -0.0052
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 : A 766 A 800
REMARK 3 ORIGIN FOR THE GROUP (A): 133.5770 32.4770 -5.0130
REMARK 3 T TENSOR
REMARK 3 T11: 0.1505 T22: 0.0800
REMARK 3 T33: 0.3033 T12: 0.1046
REMARK 3 T13: -0.0357 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 7.9112 L22: 6.4187
REMARK 3 L33: 6.9707 L12: 2.2780
REMARK 3 L13: -2.8345 L23: -2.0649
REMARK 3 S TENSOR
REMARK 3 S11: -0.1669 S12: -0.1465 S13: -0.4632
REMARK 3 S21: -0.0660 S22: 0.1634 S23: -0.5399
REMARK 3 S31: 0.3053 S32: 0.2365 S33: 0.0036
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 14 B 115
REMARK 3 ORIGIN FOR THE GROUP (A): 106.1830 48.1440 43.6390
REMARK 3 T TENSOR
REMARK 3 T11: 0.5807 T22: 0.4041
REMARK 3 T33: 0.4278 T12: -0.1936
REMARK 3 T13: 0.0114 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 4.9885 L22: 3.8561
REMARK 3 L33: 4.4839 L12: 1.6637
REMARK 3 L13: -0.0049 L23: 1.4571
REMARK 3 S TENSOR
REMARK 3 S11: 0.3451 S12: -0.5228 S13: 0.2494
REMARK 3 S21: 0.6263 S22: -0.2154 S23: -0.4216
REMARK 3 S31: -0.7208 S32: 0.6432 S33: -0.1297
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 265
REMARK 3 ORIGIN FOR THE GROUP (A): 101.6180 27.4160 25.9630
REMARK 3 T TENSOR
REMARK 3 T11: 0.2538 T22: 0.1797
REMARK 3 T33: 0.2180 T12: 0.0230
REMARK 3 T13: 0.0110 T23: 0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 2.2822 L22: 2.9910
REMARK 3 L33: 2.6200 L12: 0.5958
REMARK 3 L13: -0.2087 L23: 0.8773
REMARK 3 S TENSOR
REMARK 3 S11: -0.0429 S12: 0.0232 S13: -0.1743
REMARK 3 S21: -0.0519 S22: 0.1178 S23: -0.3799
REMARK 3 S31: 0.2838 S32: 0.3601 S33: -0.0749
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 266 B 387
REMARK 3 ORIGIN FOR THE GROUP (A): 87.1150 40.7980 13.6710
REMARK 3 T TENSOR
REMARK 3 T11: 0.2367 T22: 0.0835
REMARK 3 T33: 0.2290 T12: 0.0035
REMARK 3 T13: -0.0021 T23: 0.0370
REMARK 3 L TENSOR
REMARK 3 L11: 1.4820 L22: 0.7276
REMARK 3 L33: 2.3719 L12: -0.0832
REMARK 3 L13: -1.3644 L23: 0.0140
REMARK 3 S TENSOR
REMARK 3 S11: 0.0543 S12: -0.0279 S13: 0.0386
REMARK 3 S21: -0.0362 S22: -0.0163 S23: -0.0033
REMARK 3 S31: -0.1037 S32: 0.0517 S33: -0.0380
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 550 B 567
REMARK 3 ORIGIN FOR THE GROUP (A): 85.4060 43.7160 3.8180
REMARK 3 T TENSOR
REMARK 3 T11: 0.1573 T22: 0.0915
REMARK 3 T33: 0.1821 T12: 0.1070
REMARK 3 T13: 0.0084 T23: 0.0217
REMARK 3 L TENSOR
REMARK 3 L11: 4.6860 L22: 1.6210
REMARK 3 L33: 11.8593 L12: 4.0139
REMARK 3 L13: -4.3870 L23: -2.7945
REMARK 3 S TENSOR
REMARK 3 S11: 0.1205 S12: 0.2076 S13: 0.1665
REMARK 3 S21: -0.0919 S22: -0.0551 S23: 0.1284
REMARK 3 S31: -0.1509 S32: -0.4930 S33: -0.0655
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 444 B 503
REMARK 3 ORIGIN FOR THE GROUP (A): 72.2800 73.9030 61.7310
REMARK 3 T TENSOR
REMARK 3 T11: 0.3348 T22: 0.4056
REMARK 3 T33: 0.2188 T12: 0.0607
REMARK 3 T13: -0.0359 T23: -0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 4.7865 L22: 8.6492
REMARK 3 L33: 3.4585 L12: 3.3224
REMARK 3 L13: -1.0751 L23: 1.2379
REMARK 3 S TENSOR
REMARK 3 S11: -0.0389 S12: -0.1340 S13: 0.0092
REMARK 3 S21: 0.0822 S22: -0.1360 S23: 0.4018
REMARK 3 S31: -0.1515 S32: -0.4250 S33: 0.1749
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 388 B 443
REMARK 3 ORIGIN FOR THE GROUP (A): 70.3610 44.2950 33.6500
REMARK 3 T TENSOR
REMARK 3 T11: 0.3073 T22: 0.1294
REMARK 3 T33: 0.2880 T12: -0.0328
REMARK 3 T13: 0.0320 T23: 0.0922
REMARK 3 L TENSOR
REMARK 3 L11: 2.3749 L22: 2.1664
REMARK 3 L33: 7.6140 L12: -1.4764
REMARK 3 L13: -1.9218 L23: 4.0878
REMARK 3 S TENSOR
REMARK 3 S11: -0.0427 S12: -0.1321 S13: -0.1076
REMARK 3 S21: 0.1077 S22: -0.2586 S23: 0.2525
REMARK 3 S31: 0.0614 S32: -0.6561 S33: 0.3013
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 504 B 549
REMARK 3 ORIGIN FOR THE GROUP (A): 73.3560 44.8220 43.8790
REMARK 3 T TENSOR
REMARK 3 T11: 0.3620 T22: 0.2595
REMARK 3 T33: 0.2686 T12: -0.0235
REMARK 3 T13: 0.0194 T23: 0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 1.1715 L22: 2.2145
REMARK 3 L33: 1.8474 L12: -0.7490
REMARK 3 L13: -0.9158 L23: 1.7078
REMARK 3 S TENSOR
REMARK 3 S11: -0.1485 S12: -0.1855 S13: 0.0663
REMARK 3 S21: 0.6004 S22: -0.0318 S23: 0.1732
REMARK 3 S31: 0.4912 S32: -0.1407 S33: 0.1803
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 568 B 741
REMARK 3 ORIGIN FOR THE GROUP (A): 110.0770 37.8310 -6.8090
REMARK 3 T TENSOR
REMARK 3 T11: 0.1981 T22: 0.0080
REMARK 3 T33: 0.2190 T12: 0.0136
REMARK 3 T13: 0.0109 T23: 0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 5.6085 L22: 0.2380
REMARK 3 L33: 0.9526 L12: -0.2629
REMARK 3 L13: -0.7604 L23: -0.2048
REMARK 3 S TENSOR
REMARK 3 S11: 0.0347 S12: 0.0153 S13: -0.1503
REMARK 3 S21: -0.0308 S22: 0.0015 S23: -0.0710
REMARK 3 S31: -0.0168 S32: 0.0182 S33: -0.0362
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 : B 742 B 765
REMARK 3 ORIGIN FOR THE GROUP (A): 111.9710 52.5420 -16.3810
REMARK 3 T TENSOR
REMARK 3 T11: 0.2563 T22: 0.2557
REMARK 3 T33: 0.2960 T12: 0.0304
REMARK 3 T13: -0.0133 T23: 0.0167
REMARK 3 L TENSOR
REMARK 3 L11: 2.0978 L22: 27.7252
REMARK 3 L33: -1.4585 L12: 0.3599
REMARK 3 L13: -0.9920 L23: 1.2382
REMARK 3 S TENSOR
REMARK 3 S11: -0.1506 S12: 0.1711 S13: 0.5990
REMARK 3 S21: 0.2699 S22: 0.2320 S23: 0.3020
REMARK 3 S31: -0.0291 S32: 0.0243 S33: -0.0814
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 : B 766 B 800
REMARK 3 ORIGIN FOR THE GROUP (A): 129.0600 57.6790 -16.3100
REMARK 3 T TENSOR
REMARK 3 T11: 0.2262 T22: 0.1101
REMARK 3 T33: 0.1778 T12: 0.0471
REMARK 3 T13: 0.0335 T23: 0.0842
REMARK 3 L TENSOR
REMARK 3 L11: 4.4128 L22: 7.4580
REMARK 3 L33: 4.7590 L12: 2.7350
REMARK 3 L13: 1.1662 L23: 4.4597
REMARK 3 S TENSOR
REMARK 3 S11: -0.1367 S12: -0.0106 S13: 0.2950
REMARK 3 S21: -0.6158 S22: 0.1867 S23: -0.1549
REMARK 3 S31: -0.2735 S32: 0.2684 S33: -0.0500
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 18
REMARK 3 RESIDUE RANGE : F 14 F 30
REMARK 3 ORIGIN FOR THE GROUP (A): 85.2960 77.9250 51.1300
REMARK 3 T TENSOR
REMARK 3 T11: 0.3759 T22: 0.3386
REMARK 3 T33: 0.2849 T12: -0.0675
REMARK 3 T13: 0.0055 T23: 0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 1.7847 L22: 2.2977
REMARK 3 L33: 5.6939 L12: 1.0517
REMARK 3 L13: -0.7246 L23: -1.8376
REMARK 3 S TENSOR
REMARK 3 S11: -0.0117 S12: 0.0817 S13: 0.1088
REMARK 3 S21: 0.2694 S22: 0.1417 S23: 0.5831
REMARK 3 S31: -0.1310 S32: -0.4068 S33: -0.1300
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL PLUS 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 1WBB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-OCT-04.
REMARK 100 THE DEPOSITION ID IS D_1290021474.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93
REMARK 200 MONOCHROMATOR : DIAMOND (111), GE (220)
REMARK 200 OPTICS : SAGITAL FOCUSSING GE (220) AND
REMARK 200 MULTILAYER.
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75289
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.120
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.06
REMARK 200 R MERGE FOR SHELL (I) : 0.72000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.480
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1E3M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25 MM HEPES(7.5), 300 MM NACL, 10 MM
REMARK 280 MGCL2, 14 % PEG 6000., PH 7.50
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 44.77650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 130.63200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.24700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 130.63200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.77650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.24700
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: 11410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 70460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUES CHAINS A AND B, GLU 38 ALA
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 ALA A 659
REMARK 465 ALA A 660
REMARK 465 ASP A 661
REMARK 465 ASP A 662
REMARK 465 LEU A 663
REMARK 465 ALA A 664
REMARK 465 SER A 665
REMARK 465 GLY A 666
REMARK 465 ARG A 667
REMARK 465 SER A 668
REMARK 465 THR A 669
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ALA B 3
REMARK 465 ILE B 4
REMARK 465 GLU B 5
REMARK 465 ASN B 6
REMARK 465 PHE B 7
REMARK 465 ASP B 8
REMARK 465 ALA B 9
REMARK 465 HIS B 10
REMARK 465 THR B 11
REMARK 465 PRO B 12
REMARK 465 MET B 13
REMARK 465 LYS B 57
REMARK 465 ARG B 58
REMARK 465 GLY B 59
REMARK 465 ALA B 60
REMARK 465 SER B 61
REMARK 465 ALA B 62
REMARK 465 GLY B 63
REMARK 465 GLU B 64
REMARK 465 PRO B 65
REMARK 465 ILE B 66
REMARK 465 GLN B 95
REMARK 465 ILE B 96
REMARK 465 GLY B 97
REMARK 465 ASP B 98
REMARK 465 PRO B 99
REMARK 465 ALA B 100
REMARK 465 THR B 101
REMARK 465 SER B 102
REMARK 465 LYS B 103
REMARK 465 GLY B 104
REMARK 465 PRO B 105
REMARK 465 VAL B 106
REMARK 465 GLU B 107
REMARK 465 ALA B 659
REMARK 465 ALA B 660
REMARK 465 ASP B 661
REMARK 465 ASP B 662
REMARK 465 LEU B 663
REMARK 465 ALA B 664
REMARK 465 SER B 665
REMARK 465 GLY B 666
REMARK 465 ARG B 667
REMARK 465 SER B 668
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 A 42 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 121 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 364 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 413 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 693 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP B 121 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP B 270 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP B 296 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP B 364 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 DG E 9 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DC E 14 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DG E 16 O4' - C1' - N9 ANGL. DEV. = 5.0 DEGREES
REMARK 500 DT E 17 O4' - C1' - N1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 DA F 14 O4' - C1' - N9 ANGL. DEV. = 5.4 DEGREES
REMARK 500 DC F 15 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DT F 16 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DG F 17 O4' - C1' - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 DG F 18 O4' - C4' - C3' ANGL. DEV. = -3.8 DEGREES
REMARK 500 DG F 18 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DT F 19 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DG F 20 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DC F 21 O4' - C4' - C3' ANGL. DEV. = -2.7 DEGREES
REMARK 500 DT F 22 N3 - C2 - O2 ANGL. DEV. = -4.4 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 GLU A 5 50.83 -93.38
REMARK 500 HIS A 24 63.44 -150.32
REMARK 500 TYR A 41 -140.13 53.66
REMARK 500 ARG A 112 150.00 -171.52
REMARK 500 SER A 152 -17.30 -153.71
REMARK 500 ILE A 190 -41.92 -141.28
REMARK 500 ASN A 229 -19.34 -48.46
REMARK 500 ILE A 255 78.11 -100.31
REMARK 500 ASP A 317 109.88 -56.55
REMARK 500 SER A 387 115.01 -168.19
REMARK 500 GLU A 399 -54.67 -153.05
REMARK 500 VAL A 424 -53.19 -120.41
REMARK 500 ALA A 440 32.58 -83.99
REMARK 500 THR A 444 -88.69 -65.99
REMARK 500 ARG A 492 -50.87 -131.80
REMARK 500 ASN A 566 62.32 64.62
REMARK 500 LEU A 592 116.95 165.94
REMARK 500 ASN A 593 40.74 -102.61
REMARK 500 ASP A 703 -64.66 -25.11
REMARK 500 HIS A 752 67.58 -164.47
REMARK 500 ASP A 754 42.27 -74.01
REMARK 500 MET B 33 85.14 -152.00
REMARK 500 TYR B 41 -132.76 59.58
REMARK 500 LYS B 141 -72.89 -90.57
REMARK 500 ASN B 229 44.59 -106.38
REMARK 500 LEU B 252 73.58 -119.56
REMARK 500 CYS B 297 40.52 -108.71
REMARK 500 GLU B 399 -55.29 -135.28
REMARK 500 ASN B 616 -89.44 -88.33
REMARK 500 PRO B 641 82.76 -69.00
REMARK 500 LYS B 718 -61.03 -123.62
REMARK 500
REMARK 500 REMARK: NULL
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 MG A1802 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 621 OG
REMARK 620 2 ADP A1801 O2B 92.5
REMARK 620 3 HOH A2105 O 94.7 167.6
REMARK 620 4 HOH A2114 O 92.3 98.5 91.3
REMARK 620 5 HOH A2137 O 86.9 80.2 90.1 178.5
REMARK 620 6 HOH A2138 O 173.7 81.2 91.6 87.9 92.7
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 MG A1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A1801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E3M RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A G:T
REMARK 900 MISMATCH
REMARK 900 RELATED ID: 1NG9 RELATED DB: PDB
REMARK 900 E.COLI MUTS R697A: AN ATPASE-ASYMMETRY MUTANT
REMARK 900 RELATED ID: 1OH5 RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A C:A
REMARK 900 MISMATCH
REMARK 900 RELATED ID: 1OH6 RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH AN A:A
REMARK 900 MISMATCH
REMARK 900 RELATED ID: 1OH7 RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A G:G
REMARK 900 MISMATCH
REMARK 900 RELATED ID: 1OH8 RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH AN
REMARK 900 UNPAIRED THYMIDINE
REMARK 900 RELATED ID: 1W7A RELATED DB: PDB
REMARK 900 ATP BOUND MUTS
REMARK 900 RELATED ID: 1WB9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E. COLI DNA MISMATCH REPAIR ENZYME MUTS, E38T
REMARK 900 MUTANT, IN COMPLEX WITH A G.T MISMATCH
REMARK 900 RELATED ID: 1WBD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E. COLI DNA MISMATCH REPAIR ENZYME MUTS, E38Q
REMARK 900 MUTANT, IN COMPLEX WITH A G.T MISMATCH
DBREF 1WBB A 1 800 UNP P23909 MUTS_ECOLI 1 800
DBREF 1WBB B 1 800 UNP P23909 MUTS_ECOLI 1 800
DBREF 1WBB E 1 18 PDB 1WBB 1WBB 1 18
DBREF 1WBB F 14 30 PDB 1WBB 1WBB 14 30
SEQADV 1WBB ALA A 38 UNP P23909 GLU 38 ENGINEERED MUTATION
SEQADV 1WBB ALA B 38 UNP P23909 GLU 38 ENGINEERED MUTATION
SEQRES 1 A 800 MET SER ALA ILE GLU ASN PHE ASP ALA HIS THR PRO MET
SEQRES 2 A 800 MET GLN GLN TYR LEU ARG LEU LYS ALA GLN HIS PRO GLU
SEQRES 3 A 800 ILE LEU LEU PHE TYR ARG MET GLY ASP PHE TYR ALA LEU
SEQRES 4 A 800 PHE TYR ASP ASP ALA LYS ARG ALA SER GLN LEU LEU ASP
SEQRES 5 A 800 ILE SER LEU THR LYS ARG GLY ALA SER ALA GLY GLU PRO
SEQRES 6 A 800 ILE PRO MET ALA GLY ILE PRO TYR HIS ALA VAL GLU ASN
SEQRES 7 A 800 TYR LEU ALA LYS LEU VAL ASN GLN GLY GLU SER VAL ALA
SEQRES 8 A 800 ILE CYS GLU GLN ILE GLY ASP PRO ALA THR SER LYS GLY
SEQRES 9 A 800 PRO VAL GLU ARG LYS VAL VAL ARG ILE VAL THR PRO GLY
SEQRES 10 A 800 THR ILE SER ASP GLU ALA LEU LEU GLN GLU ARG GLN ASP
SEQRES 11 A 800 ASN LEU LEU ALA ALA ILE TRP GLN ASP SER LYS GLY PHE
SEQRES 12 A 800 GLY TYR ALA THR LEU ASP ILE SER SER GLY ARG PHE ARG
SEQRES 13 A 800 LEU SER GLU PRO ALA ASP ARG GLU THR MET ALA ALA GLU
SEQRES 14 A 800 LEU GLN ARG THR ASN PRO ALA GLU LEU LEU TYR ALA GLU
SEQRES 15 A 800 ASP PHE ALA GLU MET SER LEU ILE GLU GLY ARG ARG GLY
SEQRES 16 A 800 LEU ARG ARG ARG PRO LEU TRP GLU PHE GLU ILE ASP THR
SEQRES 17 A 800 ALA ARG GLN GLN LEU ASN LEU GLN PHE GLY THR ARG ASP
SEQRES 18 A 800 LEU VAL GLY PHE GLY VAL GLU ASN ALA PRO ARG GLY LEU
SEQRES 19 A 800 CYS ALA ALA GLY CYS LEU LEU GLN TYR ALA LYS ASP THR
SEQRES 20 A 800 GLN ARG THR THR LEU PRO HIS ILE ARG SER ILE THR MET
SEQRES 21 A 800 GLU ARG GLU GLN ASP SER ILE ILE MET ASP ALA ALA THR
SEQRES 22 A 800 ARG ARG ASN LEU GLU ILE THR GLN ASN LEU ALA GLY GLY
SEQRES 23 A 800 ALA GLU ASN THR LEU ALA SER VAL LEU ASP CYS THR VAL
SEQRES 24 A 800 THR PRO MET GLY SER ARG MET LEU LYS ARG TRP LEU HIS
SEQRES 25 A 800 MET PRO VAL ARG ASP THR ARG VAL LEU LEU GLU ARG GLN
SEQRES 26 A 800 GLN THR ILE GLY ALA LEU GLN ASP PHE THR ALA GLY LEU
SEQRES 27 A 800 GLN PRO VAL LEU ARG GLN VAL GLY ASP LEU GLU ARG ILE
SEQRES 28 A 800 LEU ALA ARG LEU ALA LEU ARG THR ALA ARG PRO ARG ASP
SEQRES 29 A 800 LEU ALA ARG MET ARG HIS ALA PHE GLN GLN LEU PRO GLU
SEQRES 30 A 800 LEU ARG ALA GLN LEU GLU THR VAL ASP SER ALA PRO VAL
SEQRES 31 A 800 GLN ALA LEU ARG GLU LYS MET GLY GLU PHE ALA GLU LEU
SEQRES 32 A 800 ARG ASP LEU LEU GLU ARG ALA ILE ILE ASP THR PRO PRO
SEQRES 33 A 800 VAL LEU VAL ARG ASP GLY GLY VAL ILE ALA SER GLY TYR
SEQRES 34 A 800 ASN GLU GLU LEU ASP GLU TRP ARG ALA LEU ALA ASP GLY
SEQRES 35 A 800 ALA THR ASP TYR LEU GLU ARG LEU GLU VAL ARG GLU ARG
SEQRES 36 A 800 GLU ARG THR GLY LEU ASP THR LEU LYS VAL GLY PHE ASN
SEQRES 37 A 800 ALA VAL HIS GLY TYR TYR ILE GLN ILE SER ARG GLY GLN
SEQRES 38 A 800 SER HIS LEU ALA PRO ILE ASN TYR MET ARG ARG GLN THR
SEQRES 39 A 800 LEU LYS ASN ALA GLU ARG TYR ILE ILE PRO GLU LEU LYS
SEQRES 40 A 800 GLU TYR GLU ASP LYS VAL LEU THR SER LYS GLY LYS ALA
SEQRES 41 A 800 LEU ALA LEU GLU LYS GLN LEU TYR GLU GLU LEU PHE ASP
SEQRES 42 A 800 LEU LEU LEU PRO HIS LEU GLU ALA LEU GLN GLN SER ALA
SEQRES 43 A 800 SER ALA LEU ALA GLU LEU ASP VAL LEU VAL ASN LEU ALA
SEQRES 44 A 800 GLU ARG ALA TYR THR LEU ASN TYR THR CYS PRO THR PHE
SEQRES 45 A 800 ILE ASP LYS PRO GLY ILE ARG ILE THR GLU GLY ARG HIS
SEQRES 46 A 800 PRO VAL VAL GLU GLN VAL LEU ASN GLU PRO PHE ILE ALA
SEQRES 47 A 800 ASN PRO LEU ASN LEU SER PRO GLN ARG ARG MET LEU ILE
SEQRES 48 A 800 ILE THR GLY PRO ASN MET GLY GLY LYS SER THR TYR MET
SEQRES 49 A 800 ARG GLN THR ALA LEU ILE ALA LEU MET ALA TYR ILE GLY
SEQRES 50 A 800 SER TYR VAL PRO ALA GLN LYS VAL GLU ILE GLY PRO ILE
SEQRES 51 A 800 ASP ARG ILE PHE THR ARG VAL GLY ALA ALA ASP ASP LEU
SEQRES 52 A 800 ALA SER GLY ARG SER THR PHE MET VAL GLU MET THR GLU
SEQRES 53 A 800 THR ALA ASN ILE LEU HIS ASN ALA THR GLU TYR SER LEU
SEQRES 54 A 800 VAL LEU MET ASP GLU ILE GLY ARG GLY THR SER THR TYR
SEQRES 55 A 800 ASP GLY LEU SER LEU ALA TRP ALA CYS ALA GLU ASN LEU
SEQRES 56 A 800 ALA ASN LYS ILE LYS ALA LEU THR LEU PHE ALA THR HIS
SEQRES 57 A 800 TYR PHE GLU LEU THR GLN LEU PRO GLU LYS MET GLU GLY
SEQRES 58 A 800 VAL ALA ASN VAL HIS LEU ASP ALA LEU GLU HIS GLY ASP
SEQRES 59 A 800 THR ILE ALA PHE MET HIS SER VAL GLN ASP GLY ALA ALA
SEQRES 60 A 800 SER LYS SER TYR GLY LEU ALA VAL ALA ALA LEU ALA GLY
SEQRES 61 A 800 VAL PRO LYS GLU VAL ILE LYS ARG ALA ARG GLN LYS LEU
SEQRES 62 A 800 ARG GLU LEU GLU SER ILE SER
SEQRES 1 B 800 MET SER ALA ILE GLU ASN PHE ASP ALA HIS THR PRO MET
SEQRES 2 B 800 MET GLN GLN TYR LEU ARG LEU LYS ALA GLN HIS PRO GLU
SEQRES 3 B 800 ILE LEU LEU PHE TYR ARG MET GLY ASP PHE TYR ALA LEU
SEQRES 4 B 800 PHE TYR ASP ASP ALA LYS ARG ALA SER GLN LEU LEU ASP
SEQRES 5 B 800 ILE SER LEU THR LYS ARG GLY ALA SER ALA GLY GLU PRO
SEQRES 6 B 800 ILE PRO MET ALA GLY ILE PRO TYR HIS ALA VAL GLU ASN
SEQRES 7 B 800 TYR LEU ALA LYS LEU VAL ASN GLN GLY GLU SER VAL ALA
SEQRES 8 B 800 ILE CYS GLU GLN ILE GLY ASP PRO ALA THR SER LYS GLY
SEQRES 9 B 800 PRO VAL GLU ARG LYS VAL VAL ARG ILE VAL THR PRO GLY
SEQRES 10 B 800 THR ILE SER ASP GLU ALA LEU LEU GLN GLU ARG GLN ASP
SEQRES 11 B 800 ASN LEU LEU ALA ALA ILE TRP GLN ASP SER LYS GLY PHE
SEQRES 12 B 800 GLY TYR ALA THR LEU ASP ILE SER SER GLY ARG PHE ARG
SEQRES 13 B 800 LEU SER GLU PRO ALA ASP ARG GLU THR MET ALA ALA GLU
SEQRES 14 B 800 LEU GLN ARG THR ASN PRO ALA GLU LEU LEU TYR ALA GLU
SEQRES 15 B 800 ASP PHE ALA GLU MET SER LEU ILE GLU GLY ARG ARG GLY
SEQRES 16 B 800 LEU ARG ARG ARG PRO LEU TRP GLU PHE GLU ILE ASP THR
SEQRES 17 B 800 ALA ARG GLN GLN LEU ASN LEU GLN PHE GLY THR ARG ASP
SEQRES 18 B 800 LEU VAL GLY PHE GLY VAL GLU ASN ALA PRO ARG GLY LEU
SEQRES 19 B 800 CYS ALA ALA GLY CYS LEU LEU GLN TYR ALA LYS ASP THR
SEQRES 20 B 800 GLN ARG THR THR LEU PRO HIS ILE ARG SER ILE THR MET
SEQRES 21 B 800 GLU ARG GLU GLN ASP SER ILE ILE MET ASP ALA ALA THR
SEQRES 22 B 800 ARG ARG ASN LEU GLU ILE THR GLN ASN LEU ALA GLY GLY
SEQRES 23 B 800 ALA GLU ASN THR LEU ALA SER VAL LEU ASP CYS THR VAL
SEQRES 24 B 800 THR PRO MET GLY SER ARG MET LEU LYS ARG TRP LEU HIS
SEQRES 25 B 800 MET PRO VAL ARG ASP THR ARG VAL LEU LEU GLU ARG GLN
SEQRES 26 B 800 GLN THR ILE GLY ALA LEU GLN ASP PHE THR ALA GLY LEU
SEQRES 27 B 800 GLN PRO VAL LEU ARG GLN VAL GLY ASP LEU GLU ARG ILE
SEQRES 28 B 800 LEU ALA ARG LEU ALA LEU ARG THR ALA ARG PRO ARG ASP
SEQRES 29 B 800 LEU ALA ARG MET ARG HIS ALA PHE GLN GLN LEU PRO GLU
SEQRES 30 B 800 LEU ARG ALA GLN LEU GLU THR VAL ASP SER ALA PRO VAL
SEQRES 31 B 800 GLN ALA LEU ARG GLU LYS MET GLY GLU PHE ALA GLU LEU
SEQRES 32 B 800 ARG ASP LEU LEU GLU ARG ALA ILE ILE ASP THR PRO PRO
SEQRES 33 B 800 VAL LEU VAL ARG ASP GLY GLY VAL ILE ALA SER GLY TYR
SEQRES 34 B 800 ASN GLU GLU LEU ASP GLU TRP ARG ALA LEU ALA ASP GLY
SEQRES 35 B 800 ALA THR ASP TYR LEU GLU ARG LEU GLU VAL ARG GLU ARG
SEQRES 36 B 800 GLU ARG THR GLY LEU ASP THR LEU LYS VAL GLY PHE ASN
SEQRES 37 B 800 ALA VAL HIS GLY TYR TYR ILE GLN ILE SER ARG GLY GLN
SEQRES 38 B 800 SER HIS LEU ALA PRO ILE ASN TYR MET ARG ARG GLN THR
SEQRES 39 B 800 LEU LYS ASN ALA GLU ARG TYR ILE ILE PRO GLU LEU LYS
SEQRES 40 B 800 GLU TYR GLU ASP LYS VAL LEU THR SER LYS GLY LYS ALA
SEQRES 41 B 800 LEU ALA LEU GLU LYS GLN LEU TYR GLU GLU LEU PHE ASP
SEQRES 42 B 800 LEU LEU LEU PRO HIS LEU GLU ALA LEU GLN GLN SER ALA
SEQRES 43 B 800 SER ALA LEU ALA GLU LEU ASP VAL LEU VAL ASN LEU ALA
SEQRES 44 B 800 GLU ARG ALA TYR THR LEU ASN TYR THR CYS PRO THR PHE
SEQRES 45 B 800 ILE ASP LYS PRO GLY ILE ARG ILE THR GLU GLY ARG HIS
SEQRES 46 B 800 PRO VAL VAL GLU GLN VAL LEU ASN GLU PRO PHE ILE ALA
SEQRES 47 B 800 ASN PRO LEU ASN LEU SER PRO GLN ARG ARG MET LEU ILE
SEQRES 48 B 800 ILE THR GLY PRO ASN MET GLY GLY LYS SER THR TYR MET
SEQRES 49 B 800 ARG GLN THR ALA LEU ILE ALA LEU MET ALA TYR ILE GLY
SEQRES 50 B 800 SER TYR VAL PRO ALA GLN LYS VAL GLU ILE GLY PRO ILE
SEQRES 51 B 800 ASP ARG ILE PHE THR ARG VAL GLY ALA ALA ASP ASP LEU
SEQRES 52 B 800 ALA SER GLY ARG SER THR PHE MET VAL GLU MET THR GLU
SEQRES 53 B 800 THR ALA ASN ILE LEU HIS ASN ALA THR GLU TYR SER LEU
SEQRES 54 B 800 VAL LEU MET ASP GLU ILE GLY ARG GLY THR SER THR TYR
SEQRES 55 B 800 ASP GLY LEU SER LEU ALA TRP ALA CYS ALA GLU ASN LEU
SEQRES 56 B 800 ALA ASN LYS ILE LYS ALA LEU THR LEU PHE ALA THR HIS
SEQRES 57 B 800 TYR PHE GLU LEU THR GLN LEU PRO GLU LYS MET GLU GLY
SEQRES 58 B 800 VAL ALA ASN VAL HIS LEU ASP ALA LEU GLU HIS GLY ASP
SEQRES 59 B 800 THR ILE ALA PHE MET HIS SER VAL GLN ASP GLY ALA ALA
SEQRES 60 B 800 SER LYS SER TYR GLY LEU ALA VAL ALA ALA LEU ALA GLY
SEQRES 61 B 800 VAL PRO LYS GLU VAL ILE LYS ARG ALA ARG GLN LYS LEU
SEQRES 62 B 800 ARG GLU LEU GLU SER ILE SER
SEQRES 1 E 18 DA DG DC DT DG DC DC DA DG DG DC DA DC
SEQRES 2 E 18 DC DA DG DT DG
SEQRES 1 F 17 DA DC DT DG DG DT DG DC DT DT DG DG DC
SEQRES 2 F 17 DA DG DC DT
HET ADP A1801 27
HET MG A1802 1
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 5 ADP C10 H15 N5 O10 P2
FORMUL 6 MG MG 2+
FORMUL 7 HOH *285(H2 O)
HELIX 1 1 ASN A 6 HIS A 10 5 5
HELIX 2 2 THR A 11 GLN A 23 1 13
HELIX 3 3 TYR A 41 ASP A 52 1 12
HELIX 4 4 ALA A 75 GLN A 86 1 12
HELIX 5 5 ASP A 98 SER A 102 5 5
HELIX 6 6 ASP A 162 ASN A 174 1 13
HELIX 7 7 GLU A 186 ILE A 190 5 5
HELIX 8 8 PRO A 200 PHE A 204 5 5
HELIX 9 9 GLU A 205 GLY A 218 1 14
HELIX 10 10 ALA A 230 ARG A 249 1 20
HELIX 11 11 ARG A 262 ASP A 265 5 4
HELIX 12 12 ASP A 270 GLU A 278 1 9
HELIX 13 13 THR A 290 ASP A 296 1 7
HELIX 14 14 THR A 300 MET A 313 1 14
HELIX 15 15 ASP A 317 LEU A 331 1 15
HELIX 16 16 PHE A 334 GLY A 346 1 13
HELIX 17 17 ASP A 347 ARG A 358 1 12
HELIX 18 18 ARG A 361 GLN A 373 1 13
HELIX 19 19 GLN A 374 THR A 384 1 11
HELIX 20 20 SER A 387 MET A 397 1 11
HELIX 21 21 PHE A 400 ILE A 411 1 12
HELIX 22 22 ASN A 430 ALA A 440 1 11
HELIX 23 23 THR A 444 GLY A 459 1 16
HELIX 24 24 GLN A 481 ALA A 485 5 5
HELIX 25 25 ILE A 503 LEU A 536 1 34
HELIX 26 26 HIS A 538 ASN A 566 1 29
HELIX 27 27 GLY A 619 TYR A 635 1 17
HELIX 28 28 PHE A 670 ALA A 684 1 15
HELIX 29 29 TYR A 702 LYS A 718 1 17
HELIX 30 30 TYR A 729 THR A 733 5 5
HELIX 31 31 GLN A 734 MET A 739 1 6
HELIX 32 32 TYR A 771 ALA A 779 1 9
HELIX 33 33 PRO A 782 SER A 798 1 17
HELIX 34 34 MET B 14 HIS B 24 1 11
HELIX 35 35 TYR B 41 ASP B 52 1 12
HELIX 36 36 ALA B 75 GLN B 86 1 12
HELIX 37 37 ASP B 162 ASN B 174 1 13
HELIX 38 38 GLU B 186 ILE B 190 5 5
HELIX 39 39 PRO B 200 PHE B 204 5 5
HELIX 40 40 GLU B 205 GLY B 218 1 14
HELIX 41 41 LEU B 222 GLY B 226 5 5
HELIX 42 42 ALA B 230 ARG B 249 1 20
HELIX 43 43 ARG B 262 ASP B 265 5 4
HELIX 44 44 ASP B 270 LEU B 277 1 8
HELIX 45 45 THR B 290 ASP B 296 1 7
HELIX 46 46 THR B 300 MET B 313 1 14
HELIX 47 47 ASP B 317 LEU B 331 1 15
HELIX 48 48 PHE B 334 GLY B 346 1 13
HELIX 49 49 ASP B 347 LEU B 357 1 11
HELIX 50 50 ARG B 361 GLN B 373 1 13
HELIX 51 51 GLN B 373 THR B 384 1 12
HELIX 52 52 SER B 387 MET B 397 1 11
HELIX 53 53 PHE B 400 ILE B 411 1 12
HELIX 54 54 ASN B 430 GLY B 459 1 30
HELIX 55 55 GLN B 481 ALA B 485 5 5
HELIX 56 56 ILE B 503 LEU B 536 1 34
HELIX 57 57 HIS B 538 LEU B 565 1 28
HELIX 58 58 VAL B 587 LEU B 592 1 6
HELIX 59 59 GLY B 618 TYR B 635 1 18
HELIX 60 60 THR B 669 ALA B 684 1 16
HELIX 61 61 SER B 700 LYS B 718 1 19
HELIX 62 62 TYR B 729 THR B 733 5 5
HELIX 63 63 GLN B 734 MET B 739 1 6
HELIX 64 64 TYR B 771 ALA B 779 1 9
HELIX 65 65 PRO B 782 SER B 800 1 19
SHEET 1 AA 6 THR A 56 ARG A 58 0
SHEET 2 AA 6 ILE A 66 PRO A 72 -1 O ILE A 66 N ARG A 58
SHEET 3 AA 6 PHE A 36 PHE A 40 -1 O TYR A 37 N ILE A 71
SHEET 4 AA 6 LEU A 28 MET A 33 -1 O TYR A 31 N ALA A 38
SHEET 5 AA 6 VAL A 90 GLN A 95 1 O ALA A 91 N PHE A 30
SHEET 6 AA 6 ARG A 108 VAL A 114 -1 O LYS A 109 N GLU A 94
SHEET 1 AB 6 LEU A 196 ARG A 199 0
SHEET 2 AB 6 GLU A 177 ALA A 181 1 O LEU A 178 N ARG A 197
SHEET 3 AB 6 LEU A 133 GLN A 138 1 O ALA A 134 N LEU A 179
SHEET 4 AB 6 PHE A 143 LEU A 148 -1 O GLY A 144 N TRP A 137
SHEET 5 AB 6 PHE A 155 SER A 158 -1 O ARG A 156 N THR A 147
SHEET 6 AB 6 THR A 259 MET A 260 1 O THR A 259 N LEU A 157
SHEET 1 AC 7 ILE A 268 MET A 269 0
SHEET 2 AC 7 ARG A 652 VAL A 657 1 N ILE A 653 O ILE A 268
SHEET 3 AC 7 LEU A 689 ASP A 693 1 O LEU A 689 N PHE A 654
SHEET 4 AC 7 LEU A 722 ALA A 726 1 O LEU A 722 N VAL A 690
SHEET 5 AC 7 MET A 609 THR A 613 1 O LEU A 610 N PHE A 725
SHEET 6 AC 7 VAL A 742 GLU A 751 1 O ALA A 743 N ILE A 611
SHEET 7 AC 7 ILE A 756 ASP A 764 -1 O ALA A 757 N LEU A 750
SHEET 1 AD 4 LYS A 464 ASN A 468 0
SHEET 2 AD 4 GLY A 472 SER A 478 -1 O GLY A 472 N ASN A 468
SHEET 3 AD 4 ALA A 498 ILE A 502 -1 O GLU A 499 N ILE A 477
SHEET 4 AD 4 MET A 490 THR A 494 -1 O MET A 490 N ILE A 502
SHEET 1 AE 4 THR A 571 PHE A 572 0
SHEET 2 AE 4 LYS A 644 ILE A 647 1 O VAL A 645 N THR A 571
SHEET 3 AE 4 ILE A 578 GLY A 583 -1 O ARG A 579 N GLU A 646
SHEET 4 AE 4 ASN A 599 LEU A 603 -1 O ASN A 599 N GLY A 583
SHEET 1 BA 5 MET B 68 PRO B 72 0
SHEET 2 BA 5 PHE B 36 PHE B 40 -1 O TYR B 37 N ILE B 71
SHEET 3 BA 5 LEU B 28 MET B 33 -1 O TYR B 31 N ALA B 38
SHEET 4 BA 5 VAL B 90 CYS B 93 1 O ALA B 91 N PHE B 30
SHEET 5 BA 5 VAL B 110 VAL B 114 -1 N VAL B 111 O ILE B 92
SHEET 1 BB 6 LEU B 196 ARG B 199 0
SHEET 2 BB 6 GLU B 177 ALA B 181 1 O LEU B 178 N ARG B 197
SHEET 3 BB 6 LEU B 133 GLN B 138 1 O ALA B 134 N LEU B 179
SHEET 4 BB 6 PHE B 143 ASP B 149 -1 O GLY B 144 N TRP B 137
SHEET 5 BB 6 ARG B 154 SER B 158 -1 O ARG B 154 N ASP B 149
SHEET 6 BB 6 THR B 259 MET B 260 1 O THR B 259 N LEU B 157
SHEET 1 BC 4 LYS B 464 ASN B 468 0
SHEET 2 BC 4 GLY B 472 SER B 478 -1 O GLY B 472 N ASN B 468
SHEET 3 BC 4 ALA B 498 ILE B 502 -1 O GLU B 499 N ILE B 477
SHEET 4 BC 4 MET B 490 THR B 494 -1 O MET B 490 N ILE B 502
SHEET 1 BD 4 THR B 571 PHE B 572 0
SHEET 2 BD 4 LYS B 644 ILE B 647 1 O VAL B 645 N THR B 571
SHEET 3 BD 4 ILE B 578 GLY B 583 -1 O ARG B 579 N GLU B 646
SHEET 4 BD 4 ASN B 599 LEU B 603 -1 O ASN B 599 N GLY B 583
SHEET 1 BE 6 ILE B 653 ARG B 656 0
SHEET 2 BE 6 LEU B 689 ASP B 693 1 O LEU B 689 N PHE B 654
SHEET 3 BE 6 LEU B 722 ALA B 726 1 O LEU B 722 N VAL B 690
SHEET 4 BE 6 MET B 609 THR B 613 1 O LEU B 610 N PHE B 725
SHEET 5 BE 6 VAL B 742 HIS B 746 1 O ALA B 743 N ILE B 611
SHEET 6 BE 6 GLN B 763 ASP B 764 -1 O GLN B 763 N HIS B 746
SHEET 1 BF 2 ALA B 749 HIS B 752 0
SHEET 2 BF 2 THR B 755 PHE B 758 -1 O THR B 755 N HIS B 752
LINK OG SER A 621 MG MG A1802 1555 1555 1.87
LINK O2B ADP A1801 MG MG A1802 1555 1555 2.00
LINK MG MG A1802 O HOH A2105 1555 1555 2.18
LINK MG MG A1802 O HOH A2114 1555 1555 2.16
LINK MG MG A1802 O HOH A2137 1555 1555 2.16
LINK MG MG A1802 O HOH A2138 1555 1555 2.17
SITE 1 AC1 7 SER A 621 ASP A 693 ADP A1801 HOH A2105
SITE 2 AC1 7 HOH A2114 HOH A2137 HOH A2138
SITE 1 AC2 13 LEU A 592 PHE A 596 ILE A 597 MET A 617
SITE 2 AC2 13 GLY A 618 GLY A 619 LYS A 620 SER A 621
SITE 3 AC2 13 THR A 622 HIS A 760 MG A1802 HOH A2137
SITE 4 AC2 13 HOH A2138
CRYST1 89.553 92.494 261.264 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 0.011167 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010812 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003828 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
