HEADER DNA BINDING PROTEIN/DNA 12-DEC-06 2O8F
TITLE HUMAN MUTSALPHA (MSH2/MSH6) BOUND TO DNA WITH A SINGLE BASE T INSERT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*GP*AP*CP*GP*GP*CP*CP*GP*CP*CP*GP*CP*TP*AP*GP*CP*G)-
COMPND 3 3';
COMPND 4 CHAIN: E;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: 5'-D(*CP*GP*CP*TP*AP*GP*CP*GP*TP*GP*CP*GP*GP*CP*CP*GP*TP*C)
COMPND 8 -3';
COMPND 9 CHAIN: F;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: DNA MISMATCH REPAIR PROTEIN MSH2;
COMPND 13 CHAIN: A;
COMPND 14 SYNONYM: MUTS PROTEIN HOMOLOG 2;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: DNA MISMATCH REPAIR PROTEIN MSH6;
COMPND 18 CHAIN: B;
COMPND 19 FRAGMENT: RESIDUES 341-1360;
COMPND 20 SYNONYM: MUTS-ALPHA 160 KDA SUBUNIT, G/T MISMATCH-BINDING PROTEIN,
COMPND 21 GTBP, GTMBP, P160;
COMPND 22 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 GENE: MSH2;
SOURCE 10 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 11 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 13 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 15 EXPRESSION_SYSTEM_PLASMID: PFASBACDUAL;
SOURCE 16 MOL_ID: 4;
SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 18 ORGANISM_COMMON: HUMAN;
SOURCE 19 ORGANISM_TAXID: 9606;
SOURCE 20 GENE: MSH6, GTBP;
SOURCE 21 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 22 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 24 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 25 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 26 EXPRESSION_SYSTEM_PLASMID: PFASBACDUAL
KEYWDS DNA MISMATCH REPAIR, DNA DAMAGE RESPONSE, SOMATIC HYPERMUTATION,
KEYWDS 2 PROTEIN-DNA COMPLEX, DNA MISPAIR, CANCER, ABC TRANSPORTER ATPASE,
KEYWDS 3 DNA BINDING PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.WARREN,T.J.POHLHAUS,A.CHANGELA,P.L.MODRICH,L.S.BEESE
REVDAT 4 30-AUG-23 2O8F 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 2O8F 1 VERSN
REVDAT 2 24-FEB-09 2O8F 1 VERSN
REVDAT 1 05-JUN-07 2O8F 0
JRNL AUTH J.J.WARREN,T.J.POHLHAUS,A.CHANGELA,R.R.IYER,P.L.MODRICH,
JRNL AUTH 2 L.S.BEESE
JRNL TITL STRUCTURE OF THE HUMAN MUTSALPHA DNA LESION RECOGNITION
JRNL TITL 2 COMPLEX.
JRNL REF MOL.CELL V. 26 579 2007
JRNL REFN ISSN 1097-2765
JRNL PMID 17531815
JRNL DOI 10.1016/J.MOLCEL.2007.04.018
REMARK 2
REMARK 2 RESOLUTION. 3.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 3.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 47000
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) : 0.246
REMARK 3 R VALUE (WORKING SET) : 0.243
REMARK 3 FREE R VALUE : 0.293
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2373
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) : 3.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.33
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3174
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.76
REMARK 3 BIN R VALUE (WORKING SET) : 0.3960
REMARK 3 BIN FREE R VALUE SET COUNT : 180
REMARK 3 BIN FREE R VALUE : 0.4270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13950
REMARK 3 NUCLEIC ACID ATOMS : 711
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 19
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 110.5
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.557
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.529
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 71.626
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.923
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.884
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15021 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 20413 ; 1.198 ; 2.033
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1748 ; 2.009 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 653 ;19.558 ;24.472
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2597 ; 8.794 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 88 ; 7.872 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2296 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10939 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 6537 ; 0.156 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 10158 ; 0.307 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 596 ; 0.150 ; 0.500
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): 55 ; 0.125 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.163 ; 0.500
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): 9129 ; 0.166 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14111 ; 0.298 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7003 ; 0.285 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6302 ; 0.510 ; 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 : 11
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 124
REMARK 3 ORIGIN FOR THE GROUP (A): -52.1892 29.6087 10.3735
REMARK 3 T TENSOR
REMARK 3 T11: -0.2209 T22: -0.0797
REMARK 3 T33: -0.6984 T12: -0.1462
REMARK 3 T13: 0.0460 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 8.1865 L22: 3.9018
REMARK 3 L33: 12.1220 L12: -1.6650
REMARK 3 L13: 0.6763 L23: 0.9531
REMARK 3 S TENSOR
REMARK 3 S11: -0.1939 S12: 0.6874 S13: 0.1896
REMARK 3 S21: -0.7905 S22: -0.0347 S23: -0.0135
REMARK 3 S31: 0.0522 S32: 0.0127 S33: 0.2285
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 620 A 855
REMARK 3 RESIDUE RANGE : A 935 A 935
REMARK 3 RESIDUE RANGE : A 936 A 936
REMARK 3 ORIGIN FOR THE GROUP (A): -38.7416 -9.2971 42.0426
REMARK 3 T TENSOR
REMARK 3 T11: 0.5370 T22: -0.0011
REMARK 3 T33: -0.2520 T12: 0.6243
REMARK 3 T13: -0.0091 T23: 0.0577
REMARK 3 L TENSOR
REMARK 3 L11: 8.5516 L22: 3.2171
REMARK 3 L33: 2.4086 L12: 1.0333
REMARK 3 L13: -0.8156 L23: -0.6238
REMARK 3 S TENSOR
REMARK 3 S11: -0.1022 S12: -0.2165 S13: -0.9270
REMARK 3 S21: -0.0292 S22: 0.0061 S23: -0.3731
REMARK 3 S31: 0.7909 S32: 0.4550 S33: 0.0961
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 : B 362 B 518
REMARK 3 ORIGIN FOR THE GROUP (A): -56.4202 43.8244 46.1841
REMARK 3 T TENSOR
REMARK 3 T11: -0.5851 T22: -0.3356
REMARK 3 T33: -0.7472 T12: -0.1321
REMARK 3 T13: -0.1528 T23: 0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 3.4962 L22: 5.1529
REMARK 3 L33: 5.7746 L12: 0.8800
REMARK 3 L13: 0.3592 L23: -1.9944
REMARK 3 S TENSOR
REMARK 3 S11: 0.0012 S12: -0.5707 S13: 0.3308
REMARK 3 S21: 0.6849 S22: -0.0414 S23: -0.4594
REMARK 3 S31: -0.4624 S32: 0.6331 S33: 0.0402
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 : B 1075 B 1335
REMARK 3 ORIGIN FOR THE GROUP (A): -65.5639 -14.0382 26.2619
REMARK 3 T TENSOR
REMARK 3 T11: 0.8513 T22: -0.3378
REMARK 3 T33: 0.2066 T12: 0.2265
REMARK 3 T13: 0.0264 T23: -0.1671
REMARK 3 L TENSOR
REMARK 3 L11: 7.7540 L22: 3.1194
REMARK 3 L33: 4.1079 L12: -4.5667
REMARK 3 L13: 3.6057 L23: -1.1012
REMARK 3 S TENSOR
REMARK 3 S11: 0.2771 S12: 0.5585 S13: -1.5121
REMARK 3 S21: -0.4851 S22: 0.0621 S23: 0.1077
REMARK 3 S31: 1.1083 S32: 0.8397 S33: -0.3391
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 : B 519 B 717
REMARK 3 ORIGIN FOR THE GROUP (A): -77.2726 20.7910 45.2485
REMARK 3 T TENSOR
REMARK 3 T11: -0.4378 T22: -0.6326
REMARK 3 T33: -0.8414 T12: -0.0259
REMARK 3 T13: -0.0283 T23: 0.0621
REMARK 3 L TENSOR
REMARK 3 L11: 3.9191 L22: 7.4345
REMARK 3 L33: 8.3858 L12: -0.2549
REMARK 3 L13: 0.7467 L23: -0.4750
REMARK 3 S TENSOR
REMARK 3 S11: -0.1322 S12: -0.4589 S13: -0.4072
REMARK 3 S21: 0.6686 S22: -0.0290 S23: 0.1893
REMARK 3 S31: 0.6737 S32: -0.1199 S33: 0.1613
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 728 B 933
REMARK 3 RESIDUE RANGE : B 1009 B 1074
REMARK 3 ORIGIN FOR THE GROUP (A): -82.9693 28.4535 21.8222
REMARK 3 T TENSOR
REMARK 3 T11: -0.5975 T22: -0.5336
REMARK 3 T33: -0.8688 T12: -0.0963
REMARK 3 T13: -0.0179 T23: 0.0487
REMARK 3 L TENSOR
REMARK 3 L11: 2.6411 L22: 6.7731
REMARK 3 L33: 2.7232 L12: -0.3764
REMARK 3 L13: 0.2332 L23: 1.6114
REMARK 3 S TENSOR
REMARK 3 S11: 0.1425 S12: 0.2022 S13: -0.0376
REMARK 3 S21: 0.1688 S22: -0.1026 S23: 0.0595
REMARK 3 S31: 0.4161 S32: 0.0254 S33: -0.0399
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 15
REMARK 3 RESIDUE RANGE : F 16 F 32
REMARK 3 ORIGIN FOR THE GROUP (A): -52.8564 59.6132 26.1964
REMARK 3 T TENSOR
REMARK 3 T11: -0.2124 T22: -0.0808
REMARK 3 T33: -0.2879 T12: -0.3701
REMARK 3 T13: 0.1259 T23: 0.1124
REMARK 3 L TENSOR
REMARK 3 L11: 5.0371 L22: 8.3536
REMARK 3 L33: 0.4020 L12: -0.6924
REMARK 3 L13: 0.6666 L23: -1.7014
REMARK 3 S TENSOR
REMARK 3 S11: 0.1023 S12: 1.2004 S13: 1.0425
REMARK 3 S21: -1.4660 S22: 0.3368 S23: -0.5590
REMARK 3 S31: -0.5330 S32: 0.6661 S33: -0.4391
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 : B 935 B 1008
REMARK 3 ORIGIN FOR THE GROUP (A): -68.1009 74.4050 21.7313
REMARK 3 T TENSOR
REMARK 3 T11: 0.1840 T22: -0.4236
REMARK 3 T33: 0.3012 T12: -0.2965
REMARK 3 T13: 0.1972 T23: 0.1777
REMARK 3 L TENSOR
REMARK 3 L11: 8.8198 L22: 7.5066
REMARK 3 L33: 5.8065 L12: 3.0829
REMARK 3 L13: -2.4722 L23: -2.9284
REMARK 3 S TENSOR
REMARK 3 S11: 0.2861 S12: 0.8702 S13: 1.8148
REMARK 3 S21: -0.5535 S22: -0.3425 S23: 0.3385
REMARK 3 S31: -0.9533 S32: -0.0751 S33: 0.0563
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 125 A 297
REMARK 3 ORIGIN FOR THE GROUP (A): -24.5148 13.4247 12.5146
REMARK 3 T TENSOR
REMARK 3 T11: 0.4487 T22: 0.6368
REMARK 3 T33: -0.1162 T12: 0.3019
REMARK 3 T13: 0.2824 T23: -0.1341
REMARK 3 L TENSOR
REMARK 3 L11: 8.9304 L22: 6.1895
REMARK 3 L33: 3.5919 L12: 0.6585
REMARK 3 L13: -1.1095 L23: -1.8025
REMARK 3 S TENSOR
REMARK 3 S11: -0.5223 S12: 0.8409 S13: -0.0353
REMARK 3 S21: -0.6097 S22: 0.2576 S23: -1.1546
REMARK 3 S31: 0.8582 S32: 0.4297 S33: 0.2646
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 298 A 456
REMARK 3 RESIDUE RANGE : A 554 A 619
REMARK 3 ORIGIN FOR THE GROUP (A): -20.1166 28.9397 35.7620
REMARK 3 T TENSOR
REMARK 3 T11: 0.1046 T22: 0.7000
REMARK 3 T33: 0.2985 T12: 0.0922
REMARK 3 T13: 0.0216 T23: -0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 0.8410 L22: 7.5929
REMARK 3 L33: 1.0806 L12: 2.2652
REMARK 3 L13: -0.7623 L23: -1.2906
REMARK 3 S TENSOR
REMARK 3 S11: 0.1966 S12: 0.1835 S13: 0.3249
REMARK 3 S21: 0.0611 S22: -0.0177 S23: -0.8413
REMARK 3 S31: 0.1160 S32: 0.7524 S33: -0.1789
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 : A 457 A 553
REMARK 3 ORIGIN FOR THE GROUP (A): -33.6123 71.0871 29.8334
REMARK 3 T TENSOR
REMARK 3 T11: 0.1581 T22: 0.2406
REMARK 3 T33: 0.1878 T12: -0.7296
REMARK 3 T13: 0.2783 T23: 0.1383
REMARK 3 L TENSOR
REMARK 3 L11: 9.7547 L22: 7.0186
REMARK 3 L33: 2.6367 L12: -5.3887
REMARK 3 L13: 0.5038 L23: 0.6625
REMARK 3 S TENSOR
REMARK 3 S11: -0.1562 S12: 0.1411 S13: 0.8169
REMARK 3 S21: 0.4248 S22: 0.0337 S23: -0.7607
REMARK 3 S31: -0.1397 S32: 0.4396 S33: 0.1225
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 2O8F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-06.
REMARK 100 THE DEPOSITION ID IS D_1000040817.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : SI 220
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47220
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.250
REMARK 200 RESOLUTION RANGE LOW (A) : 82.077
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.12900
REMARK 200 R SYM (I) : 0.12900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.49200
REMARK 200 R SYM FOR SHELL (I) : 0.49200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC 5.2.005
REMARK 200 STARTING MODEL: PDB ENTRY 2O8B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 8000, 10 MM MAGNESIUM SULFATE,
REMARK 280 100 MM BIS-TRIS-PROPANE, PH 7, VAPOR DIFFUSION, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 3 2
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 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 Y+1/4,X+3/4,-Z+3/4
REMARK 290 14555 -Y+1/4,-X+1/4,-Z+1/4
REMARK 290 15555 Y+3/4,-X+3/4,Z+1/4
REMARK 290 16555 -Y+3/4,X+1/4,Z+3/4
REMARK 290 17555 X+1/4,Z+3/4,-Y+3/4
REMARK 290 18555 -X+3/4,Z+1/4,Y+3/4
REMARK 290 19555 -X+1/4,-Z+1/4,-Y+1/4
REMARK 290 20555 X+3/4,-Z+3/4,Y+1/4
REMARK 290 21555 Z+1/4,Y+3/4,-X+3/4
REMARK 290 22555 Z+3/4,-Y+3/4,X+1/4
REMARK 290 23555 -Z+3/4,Y+1/4,X+3/4
REMARK 290 24555 -Z+1/4,-Y+1/4,-X+1/4
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 129.77500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 129.77500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 129.77500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 129.77500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 129.77500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 129.77500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 129.77500
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 129.77500
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 129.77500
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 129.77500
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 129.77500
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 129.77500
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 129.77500
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 129.77500
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 129.77500
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 129.77500
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 129.77500
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 129.77500
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 64.88750
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 194.66250
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 194.66250
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 64.88750
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 64.88750
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 64.88750
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 194.66250
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 194.66250
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 64.88750
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 194.66250
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 64.88750
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 194.66250
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 64.88750
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 194.66250
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 194.66250
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 194.66250
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 64.88750
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 194.66250
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 64.88750
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 64.88750
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 64.88750
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 194.66250
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 194.66250
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 64.88750
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 64.88750
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 194.66250
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 194.66250
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 194.66250
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 194.66250
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 64.88750
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 194.66250
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 64.88750
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 194.66250
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 64.88750
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 64.88750
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 64.88750
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 300 REMARK: THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT CONTAINS ONE
REMARK 300 BIOLOGICAL ASSEMBLY, WHICH CONSISTS OF A PROTEIN HETERODIMER (MSH2/
REMARK 300 MSH6) BOUND TO DOUBLE-STRANDED DNA AND TWO ADP MOLECULES
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 APPLY THE FOLLOWING TO CHAINS: E, F, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 26 LIES ON A SPECIAL POSITION.
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 ASN A 109
REMARK 465 LYS A 110
REMARK 465 ALA A 111
REMARK 465 ASP A 140
REMARK 465 MET A 141
REMARK 465 SER A 142
REMARK 465 ALA A 143
REMARK 465 SER A 144
REMARK 465 GLY A 157
REMARK 465 LEU A 244
REMARK 465 LEU A 245
REMARK 465 SER A 316
REMARK 465 VAL A 317
REMARK 465 GLU A 318
REMARK 465 ALA A 714
REMARK 465 GLY A 715
REMARK 465 ASP A 716
REMARK 465 SER A 717
REMARK 465 GLN A 718
REMARK 465 LEU A 719
REMARK 465 LYS A 720
REMARK 465 GLY A 721
REMARK 465 VAL A 722
REMARK 465 TYR A 856
REMARK 465 ILE A 857
REMARK 465 GLY A 858
REMARK 465 GLU A 859
REMARK 465 SER A 860
REMARK 465 GLN A 861
REMARK 465 GLY A 862
REMARK 465 TYR A 863
REMARK 465 ASP A 864
REMARK 465 ILE A 865
REMARK 465 MET A 866
REMARK 465 GLU A 867
REMARK 465 PRO A 868
REMARK 465 ALA A 869
REMARK 465 ALA A 870
REMARK 465 LYS A 871
REMARK 465 LYS A 872
REMARK 465 CYS A 873
REMARK 465 TYR A 874
REMARK 465 LEU A 875
REMARK 465 GLU A 876
REMARK 465 ARG A 877
REMARK 465 GLU A 878
REMARK 465 GLN A 879
REMARK 465 GLY A 880
REMARK 465 GLU A 881
REMARK 465 LYS A 882
REMARK 465 ILE A 883
REMARK 465 ILE A 884
REMARK 465 GLN A 885
REMARK 465 GLU A 886
REMARK 465 PHE A 887
REMARK 465 LEU A 888
REMARK 465 SER A 889
REMARK 465 LYS A 890
REMARK 465 VAL A 891
REMARK 465 LYS A 892
REMARK 465 GLN A 893
REMARK 465 MET A 894
REMARK 465 PRO A 895
REMARK 465 PHE A 896
REMARK 465 THR A 897
REMARK 465 GLU A 898
REMARK 465 MET A 899
REMARK 465 SER A 900
REMARK 465 GLU A 901
REMARK 465 GLU A 902
REMARK 465 ASN A 903
REMARK 465 ILE A 904
REMARK 465 THR A 905
REMARK 465 ILE A 906
REMARK 465 LYS A 907
REMARK 465 LEU A 908
REMARK 465 LYS A 909
REMARK 465 GLN A 910
REMARK 465 LEU A 911
REMARK 465 LYS A 912
REMARK 465 ALA A 913
REMARK 465 GLU A 914
REMARK 465 VAL A 915
REMARK 465 ILE A 916
REMARK 465 ALA A 917
REMARK 465 LYS A 918
REMARK 465 ASN A 919
REMARK 465 ASN A 920
REMARK 465 SER A 921
REMARK 465 PHE A 922
REMARK 465 VAL A 923
REMARK 465 ASN A 924
REMARK 465 GLU A 925
REMARK 465 ILE A 926
REMARK 465 ILE A 927
REMARK 465 SER A 928
REMARK 465 ARG A 929
REMARK 465 ILE A 930
REMARK 465 LYS A 931
REMARK 465 VAL A 932
REMARK 465 THR A 933
REMARK 465 THR A 934
REMARK 465 MET B 339
REMARK 465 GLY B 340
REMARK 465 SER B 341
REMARK 465 ALA B 342
REMARK 465 PRO B 343
REMARK 465 GLN B 344
REMARK 465 ASN B 345
REMARK 465 SER B 346
REMARK 465 GLU B 347
REMARK 465 SER B 348
REMARK 465 GLN B 349
REMARK 465 ALA B 350
REMARK 465 HIS B 351
REMARK 465 VAL B 352
REMARK 465 SER B 353
REMARK 465 GLY B 354
REMARK 465 GLY B 355
REMARK 465 GLY B 356
REMARK 465 ASP B 357
REMARK 465 ASP B 358
REMARK 465 SER B 359
REMARK 465 SER B 360
REMARK 465 ARG B 361
REMARK 465 GLY B 551
REMARK 465 GLY B 652
REMARK 465 THR B 719
REMARK 465 THR B 720
REMARK 465 ARG B 721
REMARK 465 SER B 722
REMARK 465 GLY B 723
REMARK 465 ALA B 724
REMARK 465 ILE B 725
REMARK 465 PHE B 726
REMARK 465 THR B 727
REMARK 465 ASP B 934
REMARK 465 GLU B 992
REMARK 465 LYS B 1101
REMARK 465 THR B 1102
REMARK 465 PHE B 1103
REMARK 465 PHE B 1104
REMARK 465 GLY B 1105
REMARK 465 GLY B 1125
REMARK 465 ALA B 1179
REMARK 465 SER B 1180
REMARK 465 ASP B 1181
REMARK 465 ARG B 1182
REMARK 465 ILE B 1183
REMARK 465 MET B 1184
REMARK 465 SER B 1185
REMARK 465 GLY B 1186
REMARK 465 GLU B 1187
REMARK 465 VAL B 1271
REMARK 465 GLU B 1272
REMARK 465 ASN B 1273
REMARK 465 GLU B 1274
REMARK 465 CYS B 1275
REMARK 465 GLU B 1276
REMARK 465 ASP B 1277
REMARK 465 PRO B 1278
REMARK 465 SER B 1279
REMARK 465 GLN B 1280
REMARK 465 GLU B 1281
REMARK 465 THR B 1282
REMARK 465 ILE B 1283
REMARK 465 VAL B 1336
REMARK 465 CYS B 1337
REMARK 465 LEU B 1338
REMARK 465 ALA B 1339
REMARK 465 SER B 1340
REMARK 465 GLU B 1341
REMARK 465 ARG B 1342
REMARK 465 SER B 1343
REMARK 465 THR B 1344
REMARK 465 VAL B 1345
REMARK 465 ASP B 1346
REMARK 465 ALA B 1347
REMARK 465 GLU B 1348
REMARK 465 ALA B 1349
REMARK 465 VAL B 1350
REMARK 465 HIS B 1351
REMARK 465 LYS B 1352
REMARK 465 LEU B 1353
REMARK 465 LEU B 1354
REMARK 465 THR B 1355
REMARK 465 LEU B 1356
REMARK 465 ILE B 1357
REMARK 465 LYS B 1358
REMARK 465 GLU B 1359
REMARK 465 LEU B 1360
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP A 156 CG OD1 OD2
REMARK 470 PHE A 232 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 246 CG CD CE NZ
REMARK 470 GLN A 252 CG CD OE1 NE2
REMARK 470 GLU A 260 CG CD OE1 OE2
REMARK 470 GLN A 264 CG CD OE1 NE2
REMARK 470 ASP A 319 CG OD1 OD2
REMARK 470 ARG A 396 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 427 CG CD CE NZ
REMARK 470 GLU A 489 CG CD OE1 OE2
REMARK 470 ARG A 534 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 535 CG OD1 ND2
REMARK 470 ASN A 536 CG OD1 ND2
REMARK 470 PHE A 854 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 855 O CG CD OE1 NE2
REMARK 470 PHE B 933 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE B1099 CG1 CG2 CD1
REMARK 470 THR B1100 OG1 CG2
REMARK 470 LYS B1126 CG CD CE NZ
REMARK 470 ARG B1334 CG CD NE CZ NH1 NH2
REMARK 470 GLU B1335 CG CD OE1 OE2
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 DG E 1 C3' - O3' - P ANGL. DEV. = 8.5 DEGREES
REMARK 500 DA E 2 C3' - O3' - P ANGL. DEV. = 8.6 DEGREES
REMARK 500 DC E 3 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DG E 5 C3' - O3' - P ANGL. DEV. = 8.5 DEGREES
REMARK 500 DC E 6 C3' - C2' - C1' ANGL. DEV. = -5.2 DEGREES
REMARK 500 DC E 6 O4' - C1' - N1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 DT E 13 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DG E 15 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DC E 16 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DC E 16 C3' - O3' - P ANGL. DEV. = 7.4 DEGREES
REMARK 500 DC F 15 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DC F 21 O4' - C1' - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 DT F 23 O3' - P - O5' ANGL. DEV. = -22.3 DEGREES
REMARK 500 DT F 23 O3' - P - OP2 ANGL. DEV. = -16.7 DEGREES
REMARK 500 DT F 23 O3' - P - OP1 ANGL. DEV. = -17.5 DEGREES
REMARK 500 DG F 27 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DC F 28 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DG F 30 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 PRO A 618 C - N - CA ANGL. DEV. = 10.0 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 ALA A 2 119.52 67.46
REMARK 500 PRO A 27 152.11 -45.77
REMARK 500 PRO A 69 -178.69 -64.61
REMARK 500 ALA A 72 52.63 -162.16
REMARK 500 VAL A 95 -62.50 -120.62
REMARK 500 GLU A 114 -160.05 -109.39
REMARK 500 PHE A 136 99.93 -58.74
REMARK 500 ASN A 138 -52.72 -124.74
REMARK 500 ASN A 181 -162.04 -71.57
REMARK 500 ALA A 207 78.89 57.99
REMARK 500 LYS A 228 35.72 -89.40
REMARK 500 ALA A 230 59.46 -95.36
REMARK 500 ASP A 231 50.69 -106.80
REMARK 500 ASP A 236 -72.75 69.59
REMARK 500 GLN A 239 -63.98 -134.01
REMARK 500 ASP A 240 25.69 -74.02
REMARK 500 GLU A 251 63.37 -114.16
REMARK 500 ALA A 256 -43.18 -153.85
REMARK 500 PHE A 286 -107.80 -93.76
REMARK 500 GLN A 288 -133.02 -123.56
REMARK 500 PHE A 289 155.83 72.34
REMARK 500 THR A 293 -169.69 -124.71
REMARK 500 PHE A 313 -52.88 -130.69
REMARK 500 THR A 321 99.62 -61.17
REMARK 500 ALA A 370 -49.93 63.55
REMARK 500 GLN A 397 -34.50 64.75
REMARK 500 LYS A 423 -59.60 -125.65
REMARK 500 HIS A 424 -122.47 49.54
REMARK 500 GLU A 425 -37.32 -130.21
REMARK 500 LYS A 427 96.08 65.91
REMARK 500 GLN A 429 54.37 -117.78
REMARK 500 LEU A 433 41.56 -97.37
REMARK 500 HIS A 466 7.09 54.12
REMARK 500 SER A 473 -24.84 -156.42
REMARK 500 LYS A 509 -66.29 -101.19
REMARK 500 PHE A 519 -54.57 -134.08
REMARK 500 THR A 526 26.91 -62.19
REMARK 500 LYS A 528 15.20 -148.30
REMARK 500 VAL A 532 -81.28 -78.14
REMARK 500 LEU A 533 -56.07 -0.58
REMARK 500 ARG A 534 31.21 -144.96
REMARK 500 ASN A 535 -51.70 -137.65
REMARK 500 ASN A 538 -0.49 67.73
REMARK 500 SER A 540 -160.33 -100.45
REMARK 500 TYR A 588 30.22 -96.39
REMARK 500 VAL A 617 88.48 67.78
REMARK 500 PRO A 618 141.70 -36.13
REMARK 500 LYS A 627 98.14 -54.12
REMARK 500 ARG A 631 110.55 -164.49
REMARK 500 ALA A 636 61.65 62.36
REMARK 500
REMARK 500 THIS ENTRY HAS 113 RAMACHANDRAN OUTLIERS.
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 A 935 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 676 OG
REMARK 620 2 ADP A 936 O1B 78.3
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 935
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 936
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2O8B RELATED DB: PDB
REMARK 900 HUMAN MUTSALPHA (MSH2/MSH6) BOUND TO ADP AND A G T MISPAIR
REMARK 900 RELATED ID: 2O8C RELATED DB: PDB
REMARK 900 HUMAN MUTSALPHA (MSH2/MSH6) BOUND TO ADP AND A G DU MISPAIR
REMARK 900 RELATED ID: 2O8E RELATED DB: PDB
REMARK 900 HUMAN MUTSALPHA (MSH2/MSH6) BOUND TO ADP AND AN O6-METHYL-GUANINE T
REMARK 900 MISPAIR
REMARK 900 RELATED ID: 2O8D RELATED DB: PDB
REMARK 900 HUMAN MUTSALPHA (MSH2/MSH6) BOUND TO ADP AND A G DU MISPAIR
DBREF 2O8F A 1 934 UNP P43246 MSH2_HUMAN 1 934
DBREF 2O8F B 341 1360 UNP P52701 MSH6_HUMAN 341 1360
DBREF 2O8F E 1 17 PDB 2O8F 2O8F 1 17
DBREF 2O8F F 15 32 PDB 2O8F 2O8F 15 32
SEQADV 2O8F MET B 339 UNP P52701 INITIATING METHIONINE
SEQADV 2O8F GLY B 340 UNP P52701 CLONING ARTIFACT
SEQRES 1 E 17 DG DA DC DG DG DC DC DG DC DC DG DC DT
SEQRES 2 E 17 DA DG DC DG
SEQRES 1 F 18 DC DG DC DT DA DG DC DG DT DG DC DG DG
SEQRES 2 F 18 DC DC DG DT DC
SEQRES 1 A 934 MET ALA VAL GLN PRO LYS GLU THR LEU GLN LEU GLU SER
SEQRES 2 A 934 ALA ALA GLU VAL GLY PHE VAL ARG PHE PHE GLN GLY MET
SEQRES 3 A 934 PRO GLU LYS PRO THR THR THR VAL ARG LEU PHE ASP ARG
SEQRES 4 A 934 GLY ASP PHE TYR THR ALA HIS GLY GLU ASP ALA LEU LEU
SEQRES 5 A 934 ALA ALA ARG GLU VAL PHE LYS THR GLN GLY VAL ILE LYS
SEQRES 6 A 934 TYR MET GLY PRO ALA GLY ALA LYS ASN LEU GLN SER VAL
SEQRES 7 A 934 VAL LEU SER LYS MET ASN PHE GLU SER PHE VAL LYS ASP
SEQRES 8 A 934 LEU LEU LEU VAL ARG GLN TYR ARG VAL GLU VAL TYR LYS
SEQRES 9 A 934 ASN ARG ALA GLY ASN LYS ALA SER LYS GLU ASN ASP TRP
SEQRES 10 A 934 TYR LEU ALA TYR LYS ALA SER PRO GLY ASN LEU SER GLN
SEQRES 11 A 934 PHE GLU ASP ILE LEU PHE GLY ASN ASN ASP MET SER ALA
SEQRES 12 A 934 SER ILE GLY VAL VAL GLY VAL LYS MET SER ALA VAL ASP
SEQRES 13 A 934 GLY GLN ARG GLN VAL GLY VAL GLY TYR VAL ASP SER ILE
SEQRES 14 A 934 GLN ARG LYS LEU GLY LEU CYS GLU PHE PRO ASP ASN ASP
SEQRES 15 A 934 GLN PHE SER ASN LEU GLU ALA LEU LEU ILE GLN ILE GLY
SEQRES 16 A 934 PRO LYS GLU CYS VAL LEU PRO GLY GLY GLU THR ALA GLY
SEQRES 17 A 934 ASP MET GLY LYS LEU ARG GLN ILE ILE GLN ARG GLY GLY
SEQRES 18 A 934 ILE LEU ILE THR GLU ARG LYS LYS ALA ASP PHE SER THR
SEQRES 19 A 934 LYS ASP ILE TYR GLN ASP LEU ASN ARG LEU LEU LYS GLY
SEQRES 20 A 934 LYS LYS GLY GLU GLN MET ASN SER ALA VAL LEU PRO GLU
SEQRES 21 A 934 MET GLU ASN GLN VAL ALA VAL SER SER LEU SER ALA VAL
SEQRES 22 A 934 ILE LYS PHE LEU GLU LEU LEU SER ASP ASP SER ASN PHE
SEQRES 23 A 934 GLY GLN PHE GLU LEU THR THR PHE ASP PHE SER GLN TYR
SEQRES 24 A 934 MET LYS LEU ASP ILE ALA ALA VAL ARG ALA LEU ASN LEU
SEQRES 25 A 934 PHE GLN GLY SER VAL GLU ASP THR THR GLY SER GLN SER
SEQRES 26 A 934 LEU ALA ALA LEU LEU ASN LYS CYS LYS THR PRO GLN GLY
SEQRES 27 A 934 GLN ARG LEU VAL ASN GLN TRP ILE LYS GLN PRO LEU MET
SEQRES 28 A 934 ASP LYS ASN ARG ILE GLU GLU ARG LEU ASN LEU VAL GLU
SEQRES 29 A 934 ALA PHE VAL GLU ASP ALA GLU LEU ARG GLN THR LEU GLN
SEQRES 30 A 934 GLU ASP LEU LEU ARG ARG PHE PRO ASP LEU ASN ARG LEU
SEQRES 31 A 934 ALA LYS LYS PHE GLN ARG GLN ALA ALA ASN LEU GLN ASP
SEQRES 32 A 934 CYS TYR ARG LEU TYR GLN GLY ILE ASN GLN LEU PRO ASN
SEQRES 33 A 934 VAL ILE GLN ALA LEU GLU LYS HIS GLU GLY LYS HIS GLN
SEQRES 34 A 934 LYS LEU LEU LEU ALA VAL PHE VAL THR PRO LEU THR ASP
SEQRES 35 A 934 LEU ARG SER ASP PHE SER LYS PHE GLN GLU MET ILE GLU
SEQRES 36 A 934 THR THR LEU ASP MET ASP GLN VAL GLU ASN HIS GLU PHE
SEQRES 37 A 934 LEU VAL LYS PRO SER PHE ASP PRO ASN LEU SER GLU LEU
SEQRES 38 A 934 ARG GLU ILE MET ASN ASP LEU GLU LYS LYS MET GLN SER
SEQRES 39 A 934 THR LEU ILE SER ALA ALA ARG ASP LEU GLY LEU ASP PRO
SEQRES 40 A 934 GLY LYS GLN ILE LYS LEU ASP SER SER ALA GLN PHE GLY
SEQRES 41 A 934 TYR TYR PHE ARG VAL THR CYS LYS GLU GLU LYS VAL LEU
SEQRES 42 A 934 ARG ASN ASN LYS ASN PHE SER THR VAL ASP ILE GLN LYS
SEQRES 43 A 934 ASN GLY VAL LYS PHE THR ASN SER LYS LEU THR SER LEU
SEQRES 44 A 934 ASN GLU GLU TYR THR LYS ASN LYS THR GLU TYR GLU GLU
SEQRES 45 A 934 ALA GLN ASP ALA ILE VAL LYS GLU ILE VAL ASN ILE SER
SEQRES 46 A 934 SER GLY TYR VAL GLU PRO MET GLN THR LEU ASN ASP VAL
SEQRES 47 A 934 LEU ALA GLN LEU ASP ALA VAL VAL SER PHE ALA HIS VAL
SEQRES 48 A 934 SER ASN GLY ALA PRO VAL PRO TYR VAL ARG PRO ALA ILE
SEQRES 49 A 934 LEU GLU LYS GLY GLN GLY ARG ILE ILE LEU LYS ALA SER
SEQRES 50 A 934 ARG HIS ALA CYS VAL GLU VAL GLN ASP GLU ILE ALA PHE
SEQRES 51 A 934 ILE PRO ASN ASP VAL TYR PHE GLU LYS ASP LYS GLN MET
SEQRES 52 A 934 PHE HIS ILE ILE THR GLY PRO ASN MET GLY GLY LYS SER
SEQRES 53 A 934 THR TYR ILE ARG GLN THR GLY VAL ILE VAL LEU MET ALA
SEQRES 54 A 934 GLN ILE GLY CYS PHE VAL PRO CYS GLU SER ALA GLU VAL
SEQRES 55 A 934 SER ILE VAL ASP CYS ILE LEU ALA ARG VAL GLY ALA GLY
SEQRES 56 A 934 ASP SER GLN LEU LYS GLY VAL SER THR PHE MET ALA GLU
SEQRES 57 A 934 MET LEU GLU THR ALA SER ILE LEU ARG SER ALA THR LYS
SEQRES 58 A 934 ASP SER LEU ILE ILE ILE ASP GLU LEU GLY ARG GLY THR
SEQRES 59 A 934 SER THR TYR ASP GLY PHE GLY LEU ALA TRP ALA ILE SER
SEQRES 60 A 934 GLU TYR ILE ALA THR LYS ILE GLY ALA PHE CYS MET PHE
SEQRES 61 A 934 ALA THR HIS PHE HIS GLU LEU THR ALA LEU ALA ASN GLN
SEQRES 62 A 934 ILE PRO THR VAL ASN ASN LEU HIS VAL THR ALA LEU THR
SEQRES 63 A 934 THR GLU GLU THR LEU THR MET LEU TYR GLN VAL LYS LYS
SEQRES 64 A 934 GLY VAL CYS ASP GLN SER PHE GLY ILE HIS VAL ALA GLU
SEQRES 65 A 934 LEU ALA ASN PHE PRO LYS HIS VAL ILE GLU CYS ALA LYS
SEQRES 66 A 934 GLN LYS ALA LEU GLU LEU GLU GLU PHE GLN TYR ILE GLY
SEQRES 67 A 934 GLU SER GLN GLY TYR ASP ILE MET GLU PRO ALA ALA LYS
SEQRES 68 A 934 LYS CYS TYR LEU GLU ARG GLU GLN GLY GLU LYS ILE ILE
SEQRES 69 A 934 GLN GLU PHE LEU SER LYS VAL LYS GLN MET PRO PHE THR
SEQRES 70 A 934 GLU MET SER GLU GLU ASN ILE THR ILE LYS LEU LYS GLN
SEQRES 71 A 934 LEU LYS ALA GLU VAL ILE ALA LYS ASN ASN SER PHE VAL
SEQRES 72 A 934 ASN GLU ILE ILE SER ARG ILE LYS VAL THR THR
SEQRES 1 B 1022 MET GLY SER ALA PRO GLN ASN SER GLU SER GLN ALA HIS
SEQRES 2 B 1022 VAL SER GLY GLY GLY ASP ASP SER SER ARG PRO THR VAL
SEQRES 3 B 1022 TRP TYR HIS GLU THR LEU GLU TRP LEU LYS GLU GLU LYS
SEQRES 4 B 1022 ARG ARG ASP GLU HIS ARG ARG ARG PRO ASP HIS PRO ASP
SEQRES 5 B 1022 PHE ASP ALA SER THR LEU TYR VAL PRO GLU ASP PHE LEU
SEQRES 6 B 1022 ASN SER CYS THR PRO GLY MET ARG LYS TRP TRP GLN ILE
SEQRES 7 B 1022 LYS SER GLN ASN PHE ASP LEU VAL ILE CYS TYR LYS VAL
SEQRES 8 B 1022 GLY LYS PHE TYR GLU LEU TYR HIS MET ASP ALA LEU ILE
SEQRES 9 B 1022 GLY VAL SER GLU LEU GLY LEU VAL PHE MET LYS GLY ASN
SEQRES 10 B 1022 TRP ALA HIS SER GLY PHE PRO GLU ILE ALA PHE GLY ARG
SEQRES 11 B 1022 TYR SER ASP SER LEU VAL GLN LYS GLY TYR LYS VAL ALA
SEQRES 12 B 1022 ARG VAL GLU GLN THR GLU THR PRO GLU MET MET GLU ALA
SEQRES 13 B 1022 ARG CYS ARG LYS MET ALA HIS ILE SER LYS TYR ASP ARG
SEQRES 14 B 1022 VAL VAL ARG ARG GLU ILE CYS ARG ILE ILE THR LYS GLY
SEQRES 15 B 1022 THR GLN THR TYR SER VAL LEU GLU GLY ASP PRO SER GLU
SEQRES 16 B 1022 ASN TYR SER LYS TYR LEU LEU SER LEU LYS GLU LYS GLU
SEQRES 17 B 1022 GLU ASP SER SER GLY HIS THR ARG ALA TYR GLY VAL CYS
SEQRES 18 B 1022 PHE VAL ASP THR SER LEU GLY LYS PHE PHE ILE GLY GLN
SEQRES 19 B 1022 PHE SER ASP ASP ARG HIS CYS SER ARG PHE ARG THR LEU
SEQRES 20 B 1022 VAL ALA HIS TYR PRO PRO VAL GLN VAL LEU PHE GLU LYS
SEQRES 21 B 1022 GLY ASN LEU SER LYS GLU THR LYS THR ILE LEU LYS SER
SEQRES 22 B 1022 SER LEU SER CYS SER LEU GLN GLU GLY LEU ILE PRO GLY
SEQRES 23 B 1022 SER GLN PHE TRP ASP ALA SER LYS THR LEU ARG THR LEU
SEQRES 24 B 1022 LEU GLU GLU GLU TYR PHE ARG GLU LYS LEU SER ASP GLY
SEQRES 25 B 1022 ILE GLY VAL MET LEU PRO GLN VAL LEU LYS GLY MET THR
SEQRES 26 B 1022 SER GLU SER ASP SER ILE GLY LEU THR PRO GLY GLU LYS
SEQRES 27 B 1022 SER GLU LEU ALA LEU SER ALA LEU GLY GLY CYS VAL PHE
SEQRES 28 B 1022 TYR LEU LYS LYS CYS LEU ILE ASP GLN GLU LEU LEU SER
SEQRES 29 B 1022 MET ALA ASN PHE GLU GLU TYR ILE PRO LEU ASP SER ASP
SEQRES 30 B 1022 THR VAL SER THR THR ARG SER GLY ALA ILE PHE THR LYS
SEQRES 31 B 1022 ALA TYR GLN ARG MET VAL LEU ASP ALA VAL THR LEU ASN
SEQRES 32 B 1022 ASN LEU GLU ILE PHE LEU ASN GLY THR ASN GLY SER THR
SEQRES 33 B 1022 GLU GLY THR LEU LEU GLU ARG VAL ASP THR CYS HIS THR
SEQRES 34 B 1022 PRO PHE GLY LYS ARG LEU LEU LYS GLN TRP LEU CYS ALA
SEQRES 35 B 1022 PRO LEU CYS ASN HIS TYR ALA ILE ASN ASP ARG LEU ASP
SEQRES 36 B 1022 ALA ILE GLU ASP LEU MET VAL VAL PRO ASP LYS ILE SER
SEQRES 37 B 1022 GLU VAL VAL GLU LEU LEU LYS LYS LEU PRO ASP LEU GLU
SEQRES 38 B 1022 ARG LEU LEU SER LYS ILE HIS ASN VAL GLY SER PRO LEU
SEQRES 39 B 1022 LYS SER GLN ASN HIS PRO ASP SER ARG ALA ILE MET TYR
SEQRES 40 B 1022 GLU GLU THR THR TYR SER LYS LYS LYS ILE ILE ASP PHE
SEQRES 41 B 1022 LEU SER ALA LEU GLU GLY PHE LYS VAL MET CYS LYS ILE
SEQRES 42 B 1022 ILE GLY ILE MET GLU GLU VAL ALA ASP GLY PHE LYS SER
SEQRES 43 B 1022 LYS ILE LEU LYS GLN VAL ILE SER LEU GLN THR LYS ASN
SEQRES 44 B 1022 PRO GLU GLY ARG PHE PRO ASP LEU THR VAL GLU LEU ASN
SEQRES 45 B 1022 ARG TRP ASP THR ALA PHE ASP HIS GLU LYS ALA ARG LYS
SEQRES 46 B 1022 THR GLY LEU ILE THR PRO LYS ALA GLY PHE ASP SER ASP
SEQRES 47 B 1022 TYR ASP GLN ALA LEU ALA ASP ILE ARG GLU ASN GLU GLN
SEQRES 48 B 1022 SER LEU LEU GLU TYR LEU GLU LYS GLN ARG ASN ARG ILE
SEQRES 49 B 1022 GLY CYS ARG THR ILE VAL TYR TRP GLY ILE GLY ARG ASN
SEQRES 50 B 1022 ARG TYR GLN LEU GLU ILE PRO GLU ASN PHE THR THR ARG
SEQRES 51 B 1022 ASN LEU PRO GLU GLU TYR GLU LEU LYS SER THR LYS LYS
SEQRES 52 B 1022 GLY CYS LYS ARG TYR TRP THR LYS THR ILE GLU LYS LYS
SEQRES 53 B 1022 LEU ALA ASN LEU ILE ASN ALA GLU GLU ARG ARG ASP VAL
SEQRES 54 B 1022 SER LEU LYS ASP CYS MET ARG ARG LEU PHE TYR ASN PHE
SEQRES 55 B 1022 ASP LYS ASN TYR LYS ASP TRP GLN SER ALA VAL GLU CYS
SEQRES 56 B 1022 ILE ALA VAL LEU ASP VAL LEU LEU CYS LEU ALA ASN TYR
SEQRES 57 B 1022 SER ARG GLY GLY ASP GLY PRO MET CYS ARG PRO VAL ILE
SEQRES 58 B 1022 LEU LEU PRO GLU ASP THR PRO PRO PHE LEU GLU LEU LYS
SEQRES 59 B 1022 GLY SER ARG HIS PRO CYS ILE THR LYS THR PHE PHE GLY
SEQRES 60 B 1022 ASP ASP PHE ILE PRO ASN ASP ILE LEU ILE GLY CYS GLU
SEQRES 61 B 1022 GLU GLU GLU GLN GLU ASN GLY LYS ALA TYR CYS VAL LEU
SEQRES 62 B 1022 VAL THR GLY PRO ASN MET GLY GLY LYS SER THR LEU MET
SEQRES 63 B 1022 ARG GLN ALA GLY LEU LEU ALA VAL MET ALA GLN MET GLY
SEQRES 64 B 1022 CYS TYR VAL PRO ALA GLU VAL CYS ARG LEU THR PRO ILE
SEQRES 65 B 1022 ASP ARG VAL PHE THR ARG LEU GLY ALA SER ASP ARG ILE
SEQRES 66 B 1022 MET SER GLY GLU SER THR PHE PHE VAL GLU LEU SER GLU
SEQRES 67 B 1022 THR ALA SER ILE LEU MET HIS ALA THR ALA HIS SER LEU
SEQRES 68 B 1022 VAL LEU VAL ASP GLU LEU GLY ARG GLY THR ALA THR PHE
SEQRES 69 B 1022 ASP GLY THR ALA ILE ALA ASN ALA VAL VAL LYS GLU LEU
SEQRES 70 B 1022 ALA GLU THR ILE LYS CYS ARG THR LEU PHE SER THR HIS
SEQRES 71 B 1022 TYR HIS SER LEU VAL GLU ASP TYR SER GLN ASN VAL ALA
SEQRES 72 B 1022 VAL ARG LEU GLY HIS MET ALA CYS MET VAL GLU ASN GLU
SEQRES 73 B 1022 CYS GLU ASP PRO SER GLN GLU THR ILE THR PHE LEU TYR
SEQRES 74 B 1022 LYS PHE ILE LYS GLY ALA CYS PRO LYS SER TYR GLY PHE
SEQRES 75 B 1022 ASN ALA ALA ARG LEU ALA ASN LEU PRO GLU GLU VAL ILE
SEQRES 76 B 1022 GLN LYS GLY HIS ARG LYS ALA ARG GLU PHE GLU LYS MET
SEQRES 77 B 1022 ASN GLN SER LEU ARG LEU PHE ARG GLU VAL CYS LEU ALA
SEQRES 78 B 1022 SER GLU ARG SER THR VAL ASP ALA GLU ALA VAL HIS LYS
SEQRES 79 B 1022 LEU LEU THR LEU ILE LYS GLU LEU
HET MG A 935 1
HET ADP A 936 27
HETNAM MG MAGNESIUM ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 5 MG MG 2+
FORMUL 6 ADP C10 H15 N5 O10 P2
FORMUL 7 HOH *19(H2 O)
HELIX 1 1 GLU A 12 GLY A 25 1 14
HELIX 2 2 GLY A 47 VAL A 57 1 11
HELIX 3 3 LYS A 82 VAL A 95 1 14
HELIX 4 4 PHE A 184 GLY A 195 1 12
HELIX 5 5 ASP A 209 ARG A 219 1 11
HELIX 6 6 ASN A 263 LEU A 277 1 15
HELIX 7 7 GLU A 278 ASP A 282 5 5
HELIX 8 8 ASP A 295 TYR A 299 5 5
HELIX 9 9 ASP A 303 ASN A 311 1 9
HELIX 10 10 SER A 325 ASN A 331 1 7
HELIX 11 11 THR A 335 GLN A 348 1 14
HELIX 12 12 ASP A 352 GLU A 368 1 17
HELIX 13 13 ALA A 370 GLN A 377 1 8
HELIX 14 14 LEU A 380 PHE A 384 5 5
HELIX 15 15 ASP A 386 ARG A 396 1 11
HELIX 16 16 LEU A 401 GLN A 413 1 13
HELIX 17 17 GLN A 413 LEU A 421 1 9
HELIX 18 18 PHE A 436 LEU A 458 1 23
HELIX 19 19 MET A 460 HIS A 466 5 7
HELIX 20 20 ASP A 475 GLY A 504 1 30
HELIX 21 21 ASN A 553 SER A 586 1 34
HELIX 22 22 VAL A 589 ALA A 615 1 27
HELIX 23 23 GLY A 674 GLY A 692 1 19
HELIX 24 24 PHE A 725 ALA A 739 1 15
HELIX 25 25 SER A 755 LYS A 773 1 19
HELIX 26 26 PHE A 784 GLN A 793 5 10
HELIX 27 27 PHE A 826 ALA A 834 1 9
HELIX 28 28 PRO A 837 LYS A 847 1 11
HELIX 29 29 TYR B 366 LYS B 374 5 9
HELIX 30 30 PRO B 399 ASN B 404 1 6
HELIX 31 31 THR B 407 ASN B 420 1 14
HELIX 32 32 HIS B 437 LEU B 447 1 11
HELIX 33 33 ALA B 465 LYS B 476 1 12
HELIX 34 34 THR B 488 LYS B 498 1 11
HELIX 35 35 SER B 503 ARG B 507 5 5
HELIX 36 36 THR B 518 GLN B 522 5 5
HELIX 37 37 CYS B 579 TYR B 589 1 11
HELIX 38 38 GLU B 604 LEU B 613 1 10
HELIX 39 39 ASP B 629 GLU B 640 1 12
HELIX 40 40 PRO B 656 GLY B 661 1 6
HELIX 41 41 SER B 677 CYS B 694 1 18
HELIX 42 42 ILE B 696 LEU B 701 1 6
HELIX 43 43 SER B 702 ALA B 704 5 3
HELIX 44 44 ASP B 713 VAL B 717 5 5
HELIX 45 45 ASP B 736 LEU B 743 1 8
HELIX 46 46 THR B 757 ASP B 763 1 7
HELIX 47 47 THR B 767 ALA B 780 1 14
HELIX 48 48 ASN B 784 VAL B 800 1 17
HELIX 49 49 VAL B 801 LYS B 813 1 13
HELIX 50 50 ASP B 817 SER B 830 1 14
HELIX 51 51 HIS B 837 ARG B 841 5 5
HELIX 52 52 GLU B 846 GLU B 876 1 31
HELIX 53 53 GLU B 877 PHE B 882 5 6
HELIX 54 54 SER B 884 SER B 892 1 9
HELIX 55 55 LEU B 905 THR B 914 1 10
HELIX 56 56 ASP B 917 ARG B 922 1 6
HELIX 57 57 SER B 935 ARG B 961 1 27
HELIX 58 58 ILE B 972 ARG B 976 5 5
HELIX 59 59 PRO B 982 THR B 986 5 5
HELIX 60 60 THR B 1010 LYS B 1042 1 33
HELIX 61 61 ASN B 1043 GLY B 1069 1 27
HELIX 62 62 LYS B 1140 GLN B 1155 1 16
HELIX 63 63 SER B 1188 ALA B 1204 1 17
HELIX 64 64 ALA B 1220 GLU B 1237 1 18
HELIX 65 65 TYR B 1249 TYR B 1256 1 8
HELIX 66 66 GLY B 1299 ARG B 1304 1 6
HELIX 67 67 PRO B 1309 PHE B 1323 1 15
HELIX 68 68 GLU B 1324 LYS B 1325 5 2
HELIX 69 69 MET B 1326 LEU B 1332 5 7
SHEET 1 A 6 LYS A 65 MET A 67 0
SHEET 2 A 6 LEU A 75 SER A 81 -1 O SER A 77 N LYS A 65
SHEET 3 A 6 PHE A 42 HIS A 46 -1 N TYR A 43 O LEU A 80
SHEET 4 A 6 THR A 33 ASP A 38 -1 N PHE A 37 O THR A 44
SHEET 5 A 6 ARG A 99 ASN A 105 1 O TYR A 103 N LEU A 36
SHEET 6 A 6 TRP A 117 ALA A 123 -1 O ALA A 123 N VAL A 100
SHEET 1 B 5 LYS A 172 PRO A 179 0
SHEET 2 B 5 GLN A 160 ASP A 167 -1 N ASP A 167 O LYS A 172
SHEET 3 B 5 VAL A 147 LYS A 151 -1 N LYS A 151 O GLY A 162
SHEET 4 B 5 GLU A 198 LEU A 201 1 O VAL A 200 N VAL A 148
SHEET 5 B 5 LEU A 223 GLU A 226 1 O THR A 225 N CYS A 199
SHEET 1 C 7 LYS A 301 LEU A 302 0
SHEET 2 C 7 CYS A 707 VAL A 712 1 O ILE A 708 N LYS A 301
SHEET 3 C 7 LEU A 744 ASP A 748 1 O ASP A 748 N ARG A 711
SHEET 4 C 7 PHE A 777 ALA A 781 1 O PHE A 777 N ILE A 745
SHEET 5 C 7 PHE A 664 ILE A 667 1 N HIS A 665 O PHE A 780
SHEET 6 C 7 VAL A 797 THR A 806 1 O LEU A 800 N ILE A 666
SHEET 7 C 7 LEU A 811 LYS A 819 -1 O THR A 812 N LEU A 805
SHEET 1 D 4 ILE A 511 SER A 515 0
SHEET 2 D 4 TYR A 521 VAL A 525 -1 O ARG A 524 N LYS A 512
SHEET 3 D 4 VAL A 549 PHE A 551 -1 O PHE A 551 N PHE A 523
SHEET 4 D 4 ASP A 543 ILE A 544 -1 N ASP A 543 O LYS A 550
SHEET 1 E 4 ALA A 623 LEU A 625 0
SHEET 2 E 4 SER A 699 SER A 703 1 O ALA A 700 N ALA A 623
SHEET 3 E 4 ARG A 631 SER A 637 -1 N LYS A 635 O SER A 699
SHEET 4 E 4 ASN A 653 GLU A 658 -1 O ASN A 653 N SER A 637
SHEET 1 F 5 HIS B 458 PRO B 462 0
SHEET 2 F 5 PHE B 432 TYR B 436 -1 N LEU B 435 O SER B 459
SHEET 3 F 5 VAL B 424 VAL B 429 -1 N TYR B 427 O GLU B 434
SHEET 4 F 5 VAL B 480 GLN B 485 1 O ALA B 481 N VAL B 424
SHEET 5 F 5 ARG B 511 ILE B 517 -1 O ARG B 515 N ARG B 482
SHEET 1 G 6 LEU B 617 LEU B 621 0
SHEET 2 G 6 PRO B 591 GLU B 597 1 N VAL B 594 O LEU B 617
SHEET 3 G 6 TYR B 538 GLU B 544 1 N LEU B 540 O LEU B 595
SHEET 4 G 6 ALA B 555 VAL B 561 -1 O VAL B 561 N LEU B 539
SHEET 5 G 6 PHE B 568 SER B 574 -1 O PHE B 569 N PHE B 560
SHEET 6 G 6 PHE B 706 GLU B 707 1 O GLU B 707 N ILE B 570
SHEET 1 H 4 VAL B 968 TRP B 970 0
SHEET 2 H 4 GLN B 978 ILE B 981 -1 O GLN B 978 N TRP B 970
SHEET 3 H 4 GLY B1002 ARG B1005 -1 O ARG B1005 N LEU B 979
SHEET 4 H 4 SER B 998 THR B 999 -1 N THR B 999 O GLY B1002
SHEET 1 I 4 VAL B1078 ILE B1079 0
SHEET 2 I 4 VAL B1164 LEU B1167 1 O CYS B1165 N VAL B1078
SHEET 3 I 4 LEU B1089 SER B1094 -1 N GLU B1090 O ARG B1166
SHEET 4 I 4 ASN B1111 ILE B1115 -1 O ILE B1115 N LEU B1089
SHEET 1 J 4 PHE B1245 SER B1246 0
SHEET 2 J 4 CYS B1129 THR B1133 1 N VAL B1132 O PHE B1245
SHEET 3 J 4 VAL B1262 MET B1267 1 O ARG B1263 N LEU B1131
SHEET 4 J 4 PHE B1289 LYS B1291 -1 O ILE B1290 N HIS B1266
SHEET 1 K 3 VAL B1173 ARG B1176 0
SHEET 2 K 3 LEU B1209 VAL B1212 1 O LEU B1211 N ARG B1176
SHEET 3 K 3 ARG B1242 THR B1243 1 O ARG B1242 N VAL B1210
LINK OG SER A 676 MG MG A 935 1555 1555 2.20
LINK MG MG A 935 O1B ADP A 936 1555 1555 2.37
SITE 1 AC1 2 SER A 676 ADP A 936
SITE 1 AC2 13 ILE A 648 PHE A 650 ILE A 651 PRO A 670
SITE 2 AC2 13 ASN A 671 MET A 672 GLY A 673 GLY A 674
SITE 3 AC2 13 LYS A 675 SER A 676 THR A 677 TYR A 815
SITE 4 AC2 13 MG A 935
CRYST1 259.550 259.550 259.550 90.00 90.00 90.00 P 43 3 2 24
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 0.003853 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003853 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003853 0.00000
(ATOM LINES ARE NOT SHOWN.)
END