HEADER TRANSFERASE/DNA 02-APR-10 3MFH
TITLE DNA POLYMERASE ETA IN COMPLEX WITH UNDAMAGED DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA POLYMERASE ETA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-513;
COMPND 5 SYNONYM: RADIATION-SENSITIVE PROTEIN 30;
COMPND 6 EC: 2.7.7.7;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: 5'-D(*GP*TP*CP*CP*TP*CP*CP*CP*CP*TP*(DOC))-3';
COMPND 11 CHAIN: P;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: 5'-D(*TP*AP*AP*TP*TP*GP*AP*GP*GP*GP*GP*AP*GP*GP*AP*C)-3';
COMPND 15 CHAIN: T;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: RAD30, DBH1, YDR419W;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ER2566;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PSL414;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES
KEYWDS DNA POLYMERASE ETA, DNA-DIRECTED DNA POLYMERASE, DNA REPLICATION, DNA
KEYWDS 2 SYNTHESIS, DNA DAMAGE, DNA BINDING, PROTEIN-DNA COMPLEX, MAGNESIUM,
KEYWDS 3 METAL BINDING, NUCLEOTIDYLTRANSFERASE, THYMIDINE DIMER, CPD, UV-
KEYWDS 4 DAMAGE, DNA REPAIR, NUCLEUS, MUTATOR PROTEIN, TRANSFERASE-DNA
KEYWDS 5 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.D.SILVERSTEIN,R.E.JOHNSON,R.JAIN,L.PRAKASH,S.PRAKASH,A.K.AGGARWAL
REVDAT 5 06-SEP-23 3MFH 1 REMARK
REVDAT 4 06-OCT-21 3MFH 1 REMARK SEQADV LINK
REVDAT 3 08-NOV-17 3MFH 1 REMARK
REVDAT 2 07-JUL-10 3MFH 1 JRNL
REVDAT 1 23-JUN-10 3MFH 0
JRNL AUTH T.D.SILVERSTEIN,R.E.JOHNSON,R.JAIN,L.PRAKASH,S.PRAKASH,
JRNL AUTH 2 A.K.AGGARWAL
JRNL TITL STRUCTURAL BASIS FOR THE SUPPRESSION OF SKIN CANCERS BY DNA
JRNL TITL 2 POLYMERASE ETA.
JRNL REF NATURE V. 465 1039 2010
JRNL REFN ISSN 0028-0836
JRNL PMID 20577207
JRNL DOI 10.1038/NATURE09104
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 58583
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2972
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.06
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3913
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.4220
REMARK 3 BIN FREE R VALUE SET COUNT : 188
REMARK 3 BIN FREE R VALUE : 0.4770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4019
REMARK 3 NUCLEIC ACID ATOMS : 484
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 627
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.40000
REMARK 3 B22 (A**2) : -0.23000
REMARK 3 B33 (A**2) : -0.17000
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): 0.154
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.142
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.096
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.721
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4756 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3073 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6548 ; 1.460 ; 2.104
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7564 ; 0.929 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 529 ; 5.866 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 184 ;37.602 ;25.054
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 762 ;13.471 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;21.315 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 731 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4902 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 871 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2585 ; 0.769 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1045 ; 0.174 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4191 ; 1.414 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2171 ; 1.986 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2351 ; 3.026 ; 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 : 7
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 104
REMARK 3 ORIGIN FOR THE GROUP (A): -19.4754 36.6074 0.7359
REMARK 3 T TENSOR
REMARK 3 T11: 0.1183 T22: 0.1182
REMARK 3 T33: 0.1340 T12: 0.0086
REMARK 3 T13: 0.0315 T23: 0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 0.2442 L22: 0.9435
REMARK 3 L33: 0.6816 L12: -0.2229
REMARK 3 L13: -0.2945 L23: 0.6097
REMARK 3 S TENSOR
REMARK 3 S11: 0.0081 S12: -0.0039 S13: -0.0615
REMARK 3 S21: -0.0532 S22: -0.0500 S23: -0.0811
REMARK 3 S31: 0.0006 S32: -0.0501 S33: 0.0419
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 105 A 149
REMARK 3 ORIGIN FOR THE GROUP (A): -16.9128 26.1888 3.3153
REMARK 3 T TENSOR
REMARK 3 T11: 0.1150 T22: 0.0885
REMARK 3 T33: 0.1821 T12: 0.0139
REMARK 3 T13: 0.0386 T23: 0.0588
REMARK 3 L TENSOR
REMARK 3 L11: 0.4035 L22: 4.7252
REMARK 3 L33: 3.3857 L12: -0.9222
REMARK 3 L13: -0.5617 L23: 3.3275
REMARK 3 S TENSOR
REMARK 3 S11: -0.0419 S12: -0.1229 S13: -0.0955
REMARK 3 S21: 0.0473 S22: 0.0406 S23: -0.2040
REMARK 3 S31: 0.1654 S32: 0.0847 S33: 0.0013
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 150 A 306
REMARK 3 ORIGIN FOR THE GROUP (A): -24.1161 55.1745 13.1398
REMARK 3 T TENSOR
REMARK 3 T11: 0.0997 T22: 0.1277
REMARK 3 T33: 0.1051 T12: -0.0254
REMARK 3 T13: -0.0013 T23: 0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 0.4996 L22: 0.4063
REMARK 3 L33: 0.8255 L12: -0.1211
REMARK 3 L13: -0.1314 L23: 0.3235
REMARK 3 S TENSOR
REMARK 3 S11: 0.0045 S12: 0.0227 S13: 0.0231
REMARK 3 S21: -0.0032 S22: -0.0026 S23: -0.0441
REMARK 3 S31: -0.0731 S32: 0.0312 S33: -0.0019
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 307 A 388
REMARK 3 ORIGIN FOR THE GROUP (A): -48.2756 48.2649 0.2377
REMARK 3 T TENSOR
REMARK 3 T11: 0.0651 T22: 0.1382
REMARK 3 T33: 0.1341 T12: 0.0254
REMARK 3 T13: -0.0231 T23: -0.0301
REMARK 3 L TENSOR
REMARK 3 L11: 2.1115 L22: 1.3173
REMARK 3 L33: 0.9085 L12: -0.6448
REMARK 3 L13: 0.6631 L23: -0.3514
REMARK 3 S TENSOR
REMARK 3 S11: 0.1282 S12: 0.1006 S13: -0.2183
REMARK 3 S21: 0.0253 S22: -0.0965 S23: 0.2985
REMARK 3 S31: -0.0630 S32: 0.0000 S33: -0.0317
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 389 A 512
REMARK 3 ORIGIN FOR THE GROUP (A): -31.8739 13.2287 4.0950
REMARK 3 T TENSOR
REMARK 3 T11: 0.1323 T22: 0.0076
REMARK 3 T33: 0.1431 T12: 0.0244
REMARK 3 T13: 0.0366 T23: 0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 1.1198 L22: 1.2170
REMARK 3 L33: 2.9294 L12: 0.8013
REMARK 3 L13: 0.9525 L23: 0.6529
REMARK 3 S TENSOR
REMARK 3 S11: 0.0179 S12: -0.0176 S13: -0.0803
REMARK 3 S21: 0.0426 S22: -0.0203 S23: 0.1070
REMARK 3 S31: 0.0134 S32: -0.0872 S33: 0.0024
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 : P 1 P 11
REMARK 3 ORIGIN FOR THE GROUP (A): -43.7952 24.5375 4.4845
REMARK 3 T TENSOR
REMARK 3 T11: 0.1555 T22: 0.1577
REMARK 3 T33: 0.1338 T12: -0.0364
REMARK 3 T13: 0.0005 T23: -0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 0.6676 L22: 2.1602
REMARK 3 L33: 0.2711 L12: -0.5418
REMARK 3 L13: -0.2267 L23: -0.3900
REMARK 3 S TENSOR
REMARK 3 S11: -0.0628 S12: -0.2263 S13: 0.0036
REMARK 3 S21: -0.1706 S22: 0.0449 S23: 0.0531
REMARK 3 S31: 0.1138 S32: 0.1244 S33: 0.0179
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 : D 4 D 16
REMARK 3 ORIGIN FOR THE GROUP (A): -40.9752 24.8425 2.7428
REMARK 3 T TENSOR
REMARK 3 T11: 0.1565 T22: 0.1377
REMARK 3 T33: 0.1397 T12: -0.0461
REMARK 3 T13: 0.0179 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 2.1041 L22: 0.3651
REMARK 3 L33: 0.2387 L12: 0.7955
REMARK 3 L13: -0.6894 L23: -0.2765
REMARK 3 S TENSOR
REMARK 3 S11: -0.0402 S12: 0.0253 S13: 0.2700
REMARK 3 S21: -0.0974 S22: 0.0888 S23: 0.1296
REMARK 3 S31: 0.0603 S32: -0.0259 S33: -0.0486
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 3MFH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058479.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI (111) CHANNEL
REMARK 200 OPTICS : SI (111) MONOCHROMATOR, TOROIDAL
REMARK 200 FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58752
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.11200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.86000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1JIH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG 4000, 0.1 M TRIS, 0.2 M
REMARK 280 LITHIUM SULFATE, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.98350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.98350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 44.37250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 113.96750
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 44.37250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 113.96750
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 42.98350
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 44.37250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 113.96750
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 42.98350
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 44.37250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 113.96750
REMARK 290 SMTRY3 8 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P, T
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -6
REMARK 465 PRO A -5
REMARK 465 GLY A -4
REMARK 465 GLY A -3
REMARK 465 ASP A -2
REMARK 465 PRO A -1
REMARK 465 HIS A 0
REMARK 465 GLN A 113
REMARK 465 ASP A 114
REMARK 465 LYS A 513
REMARK 465 DT T 1
REMARK 465 DA T 2
REMARK 465 DA T 3
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 LYS A 17 CE NZ
REMARK 470 LYS A 47 CG CD CE NZ
REMARK 470 LYS A 117 CG CD CE NZ
REMARK 470 LYS A 211 CE NZ
REMARK 470 LYS A 351 CG CD CE NZ
REMARK 470 ARG A 357 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 402 CZ NH1 NH2
REMARK 470 LYS A 404 CD CE NZ
REMARK 470 LYS A 464 CD CE NZ
REMARK 470 LYS A 487 CD CE NZ
REMARK 470 LYS A 489 CD CE NZ
REMARK 470 DT T 4 P OP1 OP2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 719 O HOH A 840 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 332 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 332 NE - CZ - NH2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 DT P 2 C4 - C5 - C7 ANGL. DEV. = 4.5 DEGREES
REMARK 500 DC P 3 O4' - C1' - N1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 DC P 4 O4' - C1' - N1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 DC P 6 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DC P 7 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC P 8 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DC P 9 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 DT P 10 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DT T 5 O4' - C1' - N1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 DG T 6 O4' - C1' - N9 ANGL. DEV. = 4.1 DEGREES
REMARK 500 DG T 8 C1' - O4' - C4' ANGL. DEV. = -8.9 DEGREES
REMARK 500 DG T 8 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DG T 9 O4' - C4' - C3' ANGL. DEV. = 3.9 DEGREES
REMARK 500 DG T 9 O4' - C1' - N9 ANGL. DEV. = 6.9 DEGREES
REMARK 500 DG T 10 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DG T 11 O4' - C1' - N9 ANGL. DEV. = 2.0 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 TRP A 56 -113.62 62.99
REMARK 500 SER A 63 155.08 -49.54
REMARK 500 HIS A 105 70.76 -108.08
REMARK 500 TRP A 111 -144.86 -74.34
REMARK 500 LYS A 117 56.00 -155.31
REMARK 500 ILE A 119 74.96 48.93
REMARK 500 SER A 153 -177.78 -170.37
REMARK 500 ASN A 223 61.68 -160.56
REMARK 500 THR A 307 -18.76 92.47
REMARK 500 TYR A 355 -70.83 -52.65
REMARK 500 ASP A 356 71.46 100.02
REMARK 500 TYR A 493 -86.22 -137.87
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 517 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 30 OD1
REMARK 620 2 MET A 31 O 84.0
REMARK 620 3 ASP A 155 OD1 95.7 78.9
REMARK 620 4 DTP A 514 O1B 168.2 86.4 89.0
REMARK 620 5 DTP A 514 O1G 87.6 98.9 175.8 87.3
REMARK 620 6 DTP A 514 O1A 102.2 170.3 92.9 88.3 89.0
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 DTP A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 518
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JIH RELATED DB: PDB
REMARK 900 DNA POLYMERASE ETA APOENZYME
REMARK 900 RELATED ID: 3MFI RELATED DB: PDB
DBREF 3MFH A 1 513 UNP Q04049 POLH_YEAST 1 513
DBREF 3MFH P 1 11 PDB 3MFH 3MFH 1 11
DBREF 3MFH T 1 16 PDB 3MFH 3MFH 1 16
SEQADV 3MFH GLY A -6 UNP Q04049 EXPRESSION TAG
SEQADV 3MFH PRO A -5 UNP Q04049 EXPRESSION TAG
SEQADV 3MFH GLY A -4 UNP Q04049 EXPRESSION TAG
SEQADV 3MFH GLY A -3 UNP Q04049 EXPRESSION TAG
SEQADV 3MFH ASP A -2 UNP Q04049 EXPRESSION TAG
SEQADV 3MFH PRO A -1 UNP Q04049 EXPRESSION TAG
SEQADV 3MFH HIS A 0 UNP Q04049 EXPRESSION TAG
SEQADV 3MFH ALA A 140 UNP Q04049 LYS 140 ENGINEERED MUTATION
SEQADV 3MFH TRP A 144 UNP Q04049 SER 144 ENGINEERED MUTATION
SEQRES 1 A 520 GLY PRO GLY GLY ASP PRO HIS MET SER LYS PHE THR TRP
SEQRES 2 A 520 LYS GLU LEU ILE GLN LEU GLY SER PRO SER LYS ALA TYR
SEQRES 3 A 520 GLU SER SER LEU ALA CYS ILE ALA HIS ILE ASP MET ASN
SEQRES 4 A 520 ALA PHE PHE ALA GLN VAL GLU GLN MET ARG CYS GLY LEU
SEQRES 5 A 520 SER LYS GLU ASP PRO VAL VAL CYS VAL GLN TRP ASN SER
SEQRES 6 A 520 ILE ILE ALA VAL SER TYR ALA ALA ARG LYS TYR GLY ILE
SEQRES 7 A 520 SER ARG MET ASP THR ILE GLN GLU ALA LEU LYS LYS CYS
SEQRES 8 A 520 SER ASN LEU ILE PRO ILE HIS THR ALA VAL PHE LYS LYS
SEQRES 9 A 520 GLY GLU ASP PHE TRP GLN TYR HIS ASP GLY CYS GLY SER
SEQRES 10 A 520 TRP VAL GLN ASP PRO ALA LYS GLN ILE SER VAL GLU ASP
SEQRES 11 A 520 HIS LYS VAL SER LEU GLU PRO TYR ARG ARG GLU SER ARG
SEQRES 12 A 520 LYS ALA LEU ALA ILE PHE LYS TRP ALA CYS ASP LEU VAL
SEQRES 13 A 520 GLU ARG ALA SER ILE ASP GLU VAL PHE LEU ASP LEU GLY
SEQRES 14 A 520 ARG ILE CYS PHE ASN MET LEU MET PHE ASP ASN GLU TYR
SEQRES 15 A 520 GLU LEU THR GLY ASP LEU LYS LEU LYS ASP ALA LEU SER
SEQRES 16 A 520 ASN ILE ARG GLU ALA PHE ILE GLY GLY ASN TYR ASP ILE
SEQRES 17 A 520 ASN SER HIS LEU PRO LEU ILE PRO GLU LYS ILE LYS SER
SEQRES 18 A 520 LEU LYS PHE GLU GLY ASP VAL PHE ASN PRO GLU GLY ARG
SEQRES 19 A 520 ASP LEU ILE THR ASP TRP ASP ASP VAL ILE LEU ALA LEU
SEQRES 20 A 520 GLY SER GLN VAL CYS LYS GLY ILE ARG ASP SER ILE LYS
SEQRES 21 A 520 ASP ILE LEU GLY TYR THR THR SER CYS GLY LEU SER SER
SEQRES 22 A 520 THR LYS ASN VAL CYS LYS LEU ALA SER ASN TYR LYS LYS
SEQRES 23 A 520 PRO ASP ALA GLN THR ILE VAL LYS ASN ASP CYS LEU LEU
SEQRES 24 A 520 ASP PHE LEU ASP CYS GLY LYS PHE GLU ILE THR SER PHE
SEQRES 25 A 520 TRP THR LEU GLY GLY VAL LEU GLY LYS GLU LEU ILE ASP
SEQRES 26 A 520 VAL LEU ASP LEU PRO HIS GLU ASN SER ILE LYS HIS ILE
SEQRES 27 A 520 ARG GLU THR TRP PRO ASP ASN ALA GLY GLN LEU LYS GLU
SEQRES 28 A 520 PHE LEU ASP ALA LYS VAL LYS GLN SER ASP TYR ASP ARG
SEQRES 29 A 520 SER THR SER ASN ILE ASP PRO LEU LYS THR ALA ASP LEU
SEQRES 30 A 520 ALA GLU LYS LEU PHE LYS LEU SER ARG GLY ARG TYR GLY
SEQRES 31 A 520 LEU PRO LEU SER SER ARG PRO VAL VAL LYS SER MET MET
SEQRES 32 A 520 SER ASN LYS ASN LEU ARG GLY LYS SER CYS ASN SER ILE
SEQRES 33 A 520 VAL ASP CYS ILE SER TRP LEU GLU VAL PHE CYS ALA GLU
SEQRES 34 A 520 LEU THR SER ARG ILE GLN ASP LEU GLU GLN GLU TYR ASN
SEQRES 35 A 520 LYS ILE VAL ILE PRO ARG THR VAL SER ILE SER LEU LYS
SEQRES 36 A 520 THR LYS SER TYR GLU VAL TYR ARG LYS SER GLY PRO VAL
SEQRES 37 A 520 ALA TYR LYS GLY ILE ASN PHE GLN SER HIS GLU LEU LEU
SEQRES 38 A 520 LYS VAL GLY ILE LYS PHE VAL THR ASP LEU ASP ILE LYS
SEQRES 39 A 520 GLY LYS ASN LYS SER TYR TYR PRO LEU THR LYS LEU SER
SEQRES 40 A 520 MET THR ILE THR ASN PHE ASP ILE ILE ASP LEU GLN LYS
SEQRES 1 P 11 DG DT DC DC DT DC DC DC DC DT DOC
SEQRES 1 T 16 DT DA DA DT DT DG DA DG DG DG DG DA DG
SEQRES 2 T 16 DG DA DC
MODRES 3MFH DOC P 11 DC 2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE
HET DOC P 11 18
HET DTP A 514 30
HET SO4 A 515 5
HET SO4 A 516 5
HET MG A 517 1
HET MG A 518 1
HETNAM DOC 2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE
HETNAM DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE
HETNAM SO4 SULFATE ION
HETNAM MG MAGNESIUM ION
FORMUL 2 DOC C9 H14 N3 O6 P
FORMUL 4 DTP C10 H16 N5 O12 P3
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 MG 2(MG 2+)
FORMUL 9 HOH *627(H2 O)
HELIX 1 1 THR A 5 GLN A 11 1 7
HELIX 2 2 LEU A 12 SER A 14 5 3
HELIX 3 3 LYS A 17 SER A 21 5 5
HELIX 4 4 ALA A 33 CYS A 43 1 11
HELIX 5 5 SER A 63 LYS A 68 1 6
HELIX 6 6 THR A 76 CYS A 84 1 9
HELIX 7 7 LEU A 128 CYS A 146 1 19
HELIX 8 8 LEU A 161 ASP A 172 1 12
HELIX 9 9 LEU A 183 LEU A 187 1 5
HELIX 10 10 LEU A 187 GLY A 197 1 11
HELIX 11 11 PRO A 209 LEU A 215 5 7
HELIX 12 12 ASP A 232 GLY A 257 1 26
HELIX 13 13 THR A 267 ASN A 276 1 10
HELIX 14 14 LYS A 287 ASP A 289 5 3
HELIX 15 15 CYS A 290 ASP A 296 1 7
HELIX 16 16 GLU A 301 PHE A 305 5 5
HELIX 17 17 GLY A 310 LEU A 320 1 11
HELIX 18 18 ASN A 326 TRP A 335 1 10
HELIX 19 19 ASN A 338 GLN A 352 1 15
HELIX 20 20 ASP A 363 LEU A 365 5 3
HELIX 21 21 LYS A 366 SER A 378 1 13
HELIX 22 22 SER A 408 ASN A 435 1 28
HELIX 23 23 GLY A 465 ASN A 467 5 3
HELIX 24 24 PHE A 468 GLY A 488 1 21
SHEET 1 A 6 VAL A 149 SER A 153 0
SHEET 2 A 6 GLU A 156 ASP A 160 -1 O PHE A 158 N GLU A 150
SHEET 3 A 6 ILE A 26 MET A 31 -1 N ILE A 29 O VAL A 157
SHEET 4 A 6 THR A 260 SER A 265 -1 O SER A 261 N ASP A 30
SHEET 5 A 6 ALA A 282 ILE A 285 1 O THR A 284 N CYS A 262
SHEET 6 A 6 ASP A 220 VAL A 221 1 N ASP A 220 O GLN A 283
SHEET 1 B 3 SER A 58 VAL A 62 0
SHEET 2 B 3 VAL A 51 GLN A 55 -1 N GLN A 55 O SER A 58
SHEET 3 B 3 ILE A 88 HIS A 91 1 O ILE A 90 N VAL A 54
SHEET 1 C 3 TRP A 102 GLN A 103 0
SHEET 2 C 3 ALA A 93 LYS A 96 -1 N VAL A 94 O GLN A 103
SHEET 3 C 3 HIS A 124 SER A 127 -1 O LYS A 125 N PHE A 95
SHEET 1 D 2 GLU A 176 THR A 178 0
SHEET 2 D 2 LEU A 181 LYS A 182 -1 O LEU A 181 N LEU A 177
SHEET 1 E 4 MET A 395 ASN A 400 0
SHEET 2 E 4 LYS A 498 ASP A 510 -1 O LEU A 499 N LYS A 399
SHEET 3 E 4 LYS A 436 LYS A 448 -1 N ARG A 441 O ASN A 505
SHEET 4 E 4 VAL A 454 PRO A 460 -1 O LYS A 457 N ILE A 445
LINK O3' DT P 10 P DOC P 11 1555 1555 1.59
LINK OD1 ASP A 30 MG MG A 517 1555 1555 2.01
LINK O MET A 31 MG MG A 517 1555 1555 2.20
LINK OD1 ASP A 155 MG MG A 517 1555 1555 2.20
LINK OE1 GLU A 156 MG MG A 518 1555 1555 2.81
LINK O1B DTP A 514 MG MG A 517 1555 1555 2.06
LINK O1G DTP A 514 MG MG A 517 1555 1555 2.12
LINK O1A DTP A 514 MG MG A 517 1555 1555 2.12
CISPEP 1 LYS A 279 PRO A 280 0 -3.50
CISPEP 2 TYR A 494 PRO A 495 0 -1.92
SITE 1 AC1 27 ASP A 30 MET A 31 ASN A 32 ALA A 33
SITE 2 AC1 27 PHE A 34 PHE A 35 ILE A 60 ALA A 61
SITE 3 AC1 27 TYR A 64 ARG A 67 ARG A 73 ASP A 155
SITE 4 AC1 27 LYS A 279 MG A 517 MG A 518 HOH A 542
SITE 5 AC1 27 HOH A 658 HOH A 680 HOH A 694 HOH A 736
SITE 6 AC1 27 HOH A 811 HOH A 921 DOC P 11 HOH P 463
SITE 7 AC1 27 DT T 4 DT T 5 DG T 6
SITE 1 AC2 4 SER A 446 ARG A 456 HOH A 825 DC P 7
SITE 1 AC3 6 PRO A 209 GLU A 210 LYS A 211 HOH A 589
SITE 2 AC3 6 HOH A 823 HOH A 942
SITE 1 AC4 4 ASP A 30 MET A 31 ASP A 155 DTP A 514
SITE 1 AC5 6 ASP A 30 ASP A 155 GLU A 156 DTP A 514
SITE 2 AC5 6 HOH A 921 DOC P 11
CRYST1 88.745 227.935 85.967 90.00 90.00 90.00 C 2 2 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 0.011268 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004387 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011632 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
