HEADER REPLICATION/DNA 06-JAN-06 2FLP
TITLE BINARY COMPLEX OF THE CATALYTIC CORE OF HUMAN DNA POLYMERASE IOTA WITH
TITLE 2 DNA (TEMPLATE G)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA TEMPLATE STRAND;
COMPND 3 CHAIN: T;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA PRIMER STRAND;
COMPND 7 CHAIN: P;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: DNA POLYMERASE IOTA;
COMPND 11 CHAIN: A;
COMPND 12 SYNONYM: RAD30 HOMOLOG B, ETA2;
COMPND 13 EC: 2.7.7.7;
COMPND 14 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: POLI, RAD30B;
SOURCE 10 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 11 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 13 EXPRESSION_SYSTEM_STRAIN: BJ5464;
SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 15 EXPRESSION_SYSTEM_PLASMID: PBJ941
KEYWDS DNA POLYMERASE, LESION BYPASS, Y-FAMILY, BINARY COMPLEX, TEMPLATE G,
KEYWDS 2 REPLICATION-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.T.NAIR,R.E.JOHNSON,L.PRAKASH,S.PRAKASH,A.K.AGGARWAL
REVDAT 5 03-APR-24 2FLP 1 REMARK
REVDAT 4 14-FEB-24 2FLP 1 LINK
REVDAT 3 13-JUL-11 2FLP 1 VERSN
REVDAT 2 24-FEB-09 2FLP 1 VERSN
REVDAT 1 05-DEC-06 2FLP 0
JRNL AUTH D.T.NAIR,R.E.JOHNSON,L.PRAKASH,S.PRAKASH,A.K.AGGARWAL
JRNL TITL AN INCOMING NUCLEOTIDE IMPOSES AN ANTI TO SYN CONFORMATIONAL
JRNL TITL 2 CHANGE ON THE TEMPLATING PURINE IN THE HUMAN DNA
JRNL TITL 3 POLYMERASE-IOTA ACTIVE SITE.
JRNL REF STRUCTURE V. 14 749 2006
JRNL REFN ISSN 0969-2126
JRNL PMID 16615915
JRNL DOI 10.1016/J.STR.2006.01.010
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 20314
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) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2224
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1408
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 151
REMARK 3 BIN FREE R VALUE : 0.3440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2813
REMARK 3 NUCLEIC ACID ATOMS : 322
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 115
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) : 45.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.30000
REMARK 3 B22 (A**2) : 0.30000
REMARK 3 B33 (A**2) : -0.45000
REMARK 3 B12 (A**2) : 0.15000
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): 0.383
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.278
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.202
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.627
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.920
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.888
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3212 ; 0.060 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4406 ; 3.182 ; 2.103
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 363 ; 8.312 ; 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): 506 ; 0.213 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2265 ; 0.014 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1457 ; 0.301 ; 0.200
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): 181 ; 0.228 ; 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): 23 ; 0.407 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.516 ; 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): 1829 ; 2.018 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2942 ; 3.370 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1383 ; 4.239 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1464 ; 5.852 ; 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 : 5
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 26 A 37
REMARK 3 RESIDUE RANGE : A 99 A 224
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6535 16.5701 6.0722
REMARK 3 T TENSOR
REMARK 3 T11: 0.5742 T22: 0.5259
REMARK 3 T33: 0.4667 T12: 0.0123
REMARK 3 T13: -0.0242 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 0.3643 L22: 0.6072
REMARK 3 L33: 1.8352 L12: -0.0330
REMARK 3 L13: 0.1754 L23: 0.3808
REMARK 3 S TENSOR
REMARK 3 S11: 0.0177 S12: 0.0127 S13: 0.0445
REMARK 3 S21: -0.0502 S22: -0.1037 S23: 0.0518
REMARK 3 S31: 0.0518 S32: 0.1703 S33: 0.0860
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 38 A 98
REMARK 3 ORIGIN FOR THE GROUP (A): -4.5340 15.7996 23.9983
REMARK 3 T TENSOR
REMARK 3 T11: 0.5604 T22: 0.5295
REMARK 3 T33: 0.6514 T12: -0.1560
REMARK 3 T13: 0.1208 T23: -0.1765
REMARK 3 L TENSOR
REMARK 3 L11: 4.5064 L22: 6.1221
REMARK 3 L33: 4.0913 L12: -1.9551
REMARK 3 L13: -1.3465 L23: 1.8443
REMARK 3 S TENSOR
REMARK 3 S11: 0.1735 S12: 0.1731 S13: -0.2154
REMARK 3 S21: 0.6094 S22: -0.6308 S23: 1.2469
REMARK 3 S31: 0.5297 S32: -0.3779 S33: 0.4573
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 225 A 287
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7931 35.4412 -3.1754
REMARK 3 T TENSOR
REMARK 3 T11: 0.5266 T22: 0.4210
REMARK 3 T33: 0.6746 T12: 0.0238
REMARK 3 T13: -0.1939 T23: -0.0319
REMARK 3 L TENSOR
REMARK 3 L11: 3.4874 L22: 2.0662
REMARK 3 L33: 2.6934 L12: -0.9421
REMARK 3 L13: 1.6101 L23: 0.4833
REMARK 3 S TENSOR
REMARK 3 S11: -0.3962 S12: 0.0698 S13: 0.7969
REMARK 3 S21: -0.0680 S22: -0.2220 S23: -0.0193
REMARK 3 S31: -0.0599 S32: -0.1183 S33: 0.6182
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 298 A 414
REMARK 3 ORIGIN FOR THE GROUP (A): 8.3806 40.7811 33.4158
REMARK 3 T TENSOR
REMARK 3 T11: 0.9025 T22: 0.2743
REMARK 3 T33: 0.4719 T12: -0.3572
REMARK 3 T13: 0.3822 T23: -0.3543
REMARK 3 L TENSOR
REMARK 3 L11: 3.5918 L22: 11.4552
REMARK 3 L33: 3.8706 L12: 4.1711
REMARK 3 L13: -0.3387 L23: 1.0794
REMARK 3 S TENSOR
REMARK 3 S11: 1.3307 S12: 0.0671 S13: 0.6672
REMARK 3 S21: 2.0038 S22: -0.9993 S23: 0.9986
REMARK 3 S31: 0.0157 S32: 0.4902 S33: -0.3314
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 839 T 847
REMARK 3 RESIDUE RANGE : P 867 P 873
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2689 37.9597 17.2810
REMARK 3 T TENSOR
REMARK 3 T11: 0.5529 T22: 0.4595
REMARK 3 T33: 0.8100 T12: -0.1144
REMARK 3 T13: -0.0143 T23: -0.0604
REMARK 3 L TENSOR
REMARK 3 L11: 0.6278 L22: 1.3499
REMARK 3 L33: 0.6126 L12: -0.6838
REMARK 3 L13: -0.0701 L23: 0.9646
REMARK 3 S TENSOR
REMARK 3 S11: -0.0737 S12: 0.0176 S13: 0.9275
REMARK 3 S21: 0.0805 S22: -0.0423 S23: 0.6127
REMARK 3 S31: 0.0424 S32: 0.0836 S33: 0.1160
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CNS 1.1 WAS ALSO USED FOR REFINEMENT.
REMARK 4
REMARK 4 2FLP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000036028.
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 : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22540
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 10.30
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: AMORE
REMARK 200 STARTING MODEL: PDB CODE ALZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 134.99800
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 67.49900
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 101.24850
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 33.74950
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 168.74750
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 134.99800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 67.49900
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 33.74950
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 101.24850
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 168.74750
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: T, P, A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.500000 -0.866025 0.000000 49.18350
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 85.18832
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 33.74950
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 DT T 837
REMARK 465 DC T 838
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 LEU A 3
REMARK 465 ALA A 4
REMARK 465 ASP A 5
REMARK 465 VAL A 6
REMARK 465 GLY A 7
REMARK 465 ALA A 8
REMARK 465 ALA A 9
REMARK 465 ALA A 10
REMARK 465 SER A 11
REMARK 465 SER A 12
REMARK 465 GLN A 13
REMARK 465 GLY A 14
REMARK 465 VAL A 15
REMARK 465 HIS A 16
REMARK 465 ASP A 17
REMARK 465 GLN A 18
REMARK 465 VAL A 19
REMARK 465 LEU A 20
REMARK 465 PRO A 21
REMARK 465 THR A 22
REMARK 465 PRO A 23
REMARK 465 ASN A 24
REMARK 465 ALA A 25
REMARK 465 SER A 350
REMARK 465 SER A 351
REMARK 465 GLU A 352
REMARK 465 LYS A 353
REMARK 465 HIS A 354
REMARK 465 LYS A 371
REMARK 465 LEU A 372
REMARK 465 GLY A 373
REMARK 465 THR A 374
REMARK 465 GLY A 375
REMARK 465 ASN A 376
REMARK 465 TYR A 377
REMARK 465 ASP A 378
REMARK 465 VAL A 395
REMARK 465 ASN A 396
REMARK 465 VAL A 397
REMARK 465 LYS A 398
REMARK 465 MET A 399
REMARK 465 PRO A 400
REMARK 465 PHE A 401
REMARK 465 HIS A 402
REMARK 465 LEU A 403
REMARK 465 ALA A 415
REMARK 465 LEU A 416
REMARK 465 ASN A 417
REMARK 465 THR A 418
REMARK 465 ALA A 419
REMARK 465 LYS A 420
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 DT T 839 P OP1 OP2
REMARK 470 LYS A 51 CG CD CE NZ
REMARK 470 ASP A 52 CG OD1 OD2
REMARK 470 LYS A 53 CG CD CE NZ
REMARK 470 TYR A 61 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 72 CG CD CE NZ
REMARK 470 LYS A 77 CG CD CE NZ
REMARK 470 VAL A 81 CG1 CG2
REMARK 470 ASP A 83 CG OD1 OD2
REMARK 470 ASP A 146 CG OD1 OD2
REMARK 470 LYS A 245 CG CD CE NZ
REMARK 470 LYS A 271 CG CD CE NZ
REMARK 470 LYS A 310 CG CD CE NZ
REMARK 470 VAL A 315 CG1 CG2
REMARK 470 GLU A 316 CG CD OE1 OE2
REMARK 470 LYS A 338 CG CD CE NZ
REMARK 470 TYR A 349 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR A 355 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL A 379 CG1 CG2
REMARK 470 ASP A 385 CG OD1 OD2
REMARK 470 ILE A 386 CG1 CG2 CD1
REMARK 470 LYS A 389 CG CD CE NZ
REMARK 470 LEU A 405 CG CD1 CD2
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 MET A 388 NH1 ARG A 392 1.72
REMARK 500 O TYR A 158 O HOH A 999 1.87
REMARK 500 O PRO A 292 O HOH A 929 2.00
REMARK 500 ND2 ASN A 290 O HOH A 905 2.14
REMARK 500 OE1 GLN A 361 O HOH A 946 2.18
REMARK 500 O HOH A 914 O HOH A 965 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O3' DT T 847 O5' DA P 867 10665 1.55
REMARK 500 O3' DT T 847 C5' DA P 867 10665 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 DT T 839 C5' DT T 839 C4' 0.071
REMARK 500 DT T 839 C1' DT T 839 N1 0.103
REMARK 500 DT T 839 N1 DT T 839 C2 0.066
REMARK 500 DG T 840 C2 DG T 840 N3 0.053
REMARK 500 DG T 841 C2 DG T 841 N3 0.063
REMARK 500 DG T 842 P DG T 842 O5' 0.071
REMARK 500 DG T 842 O3' DG T 842 C3' -0.039
REMARK 500 DG T 842 N3 DG T 842 C4 -0.060
REMARK 500 DG T 842 C5 DG T 842 N7 0.046
REMARK 500 DG T 843 C2 DG T 843 N3 0.072
REMARK 500 DT T 844 P DT T 844 O5' 0.085
REMARK 500 DT T 844 O3' DT T 844 C3' -0.052
REMARK 500 DT T 844 C5 DT T 844 C7 0.065
REMARK 500 DC T 845 N1 DC T 845 C6 0.045
REMARK 500 DC T 845 C4 DC T 845 C5 0.069
REMARK 500 DC T 845 C5 DC T 845 C6 0.054
REMARK 500 DT T 847 C5' DT T 847 C4' 0.053
REMARK 500 DT T 847 C4' DT T 847 C3' 0.061
REMARK 500 DT T 847 C3' DT T 847 C2' 0.080
REMARK 500 DT T 847 C2' DT T 847 C1' 0.081
REMARK 500 DT T 847 O3' DT T 847 C3' 0.227
REMARK 500 DT T 847 C1' DT T 847 N1 0.139
REMARK 500 DT T 847 C5 DT T 847 C7 0.073
REMARK 500 DG P 869 P DG P 869 O5' 0.064
REMARK 500 DG P 869 C4 DG P 869 C5 0.053
REMARK 500 DG P 869 C5 DG P 869 N7 0.037
REMARK 500 DA P 870 C2 DA P 870 N3 0.091
REMARK 500 DC P 871 C2' DC P 871 C1' 0.086
REMARK 500 DC P 871 O3' DC P 871 C3' -0.122
REMARK 500 DC P 872 P DC P 872 O5' 0.065
REMARK 500 DC P 872 O3' DOC P 873 P -0.084
REMARK 500 VAL A 31 CB VAL A 31 CG2 0.165
REMARK 500 TYR A 39 CG TYR A 39 CD1 -0.089
REMARK 500 TYR A 68 CG TYR A 68 CD1 0.098
REMARK 500 TYR A 102 CG TYR A 102 CD2 0.085
REMARK 500 ARG A 103 CZ ARG A 103 NH2 0.097
REMARK 500 GLU A 104 CD GLU A 104 OE2 0.077
REMARK 500 LYS A 108 CD LYS A 108 CE 0.160
REMARK 500 GLU A 111 CD GLU A 111 OE2 0.069
REMARK 500 SER A 117 CB SER A 117 OG 0.081
REMARK 500 GLU A 121 CG GLU A 121 CD 0.104
REMARK 500 ARG A 122 CD ARG A 122 NE -0.112
REMARK 500 GLU A 134 CG GLU A 134 CD 0.092
REMARK 500 GLU A 134 CD GLU A 134 OE1 0.069
REMARK 500 SER A 177 CB SER A 177 OG 0.082
REMARK 500 ARG A 184 CD ARG A 184 NE -0.112
REMARK 500 GLU A 185 CD GLU A 185 OE1 0.080
REMARK 500 GLU A 185 CD GLU A 185 OE2 0.131
REMARK 500 TYR A 188 CG TYR A 188 CD2 0.083
REMARK 500 LYS A 214 CA LYS A 214 C -0.173
REMARK 500
REMARK 500 THIS ENTRY HAS 108 BOND DEVIATIONS.
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 DT T 839 N1 - C1' - C2' ANGL. DEV. = 8.7 DEGREES
REMARK 500 DT T 839 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DT T 839 N1 - C2 - O2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 DT T 839 N3 - C2 - O2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 DT T 839 N3 - C4 - O4 ANGL. DEV. = 7.2 DEGREES
REMARK 500 DT T 839 C5 - C4 - O4 ANGL. DEV. = -6.1 DEGREES
REMARK 500 DT T 839 C6 - N1 - C1' ANGL. DEV. = -10.6 DEGREES
REMARK 500 DT T 839 C2 - N1 - C1' ANGL. DEV. = 13.3 DEGREES
REMARK 500 DT T 839 C3' - O3' - P ANGL. DEV. = 9.3 DEGREES
REMARK 500 DG T 840 C5' - C4' - C3' ANGL. DEV. = -18.0 DEGREES
REMARK 500 DG T 840 C5' - C4' - O4' ANGL. DEV. = 10.0 DEGREES
REMARK 500 DG T 840 C6 - N1 - C2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 DG T 840 C2 - N3 - C4 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DG T 840 C5 - C6 - N1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DG T 841 C3' - C2' - C1' ANGL. DEV. = -4.8 DEGREES
REMARK 500 DG T 841 C6 - N1 - C2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 DG T 842 C1' - O4' - C4' ANGL. DEV. = 4.6 DEGREES
REMARK 500 DG T 843 O4' - C4' - C3' ANGL. DEV. = 6.3 DEGREES
REMARK 500 DG T 843 C4' - C3' - C2' ANGL. DEV. = -5.3 DEGREES
REMARK 500 DG T 843 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DG T 843 C5 - C6 - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DG T 843 N1 - C6 - O6 ANGL. DEV. = -3.7 DEGREES
REMARK 500 DT T 844 O4' - C4' - C3' ANGL. DEV. = 3.7 DEGREES
REMARK 500 DT T 844 C1' - O4' - C4' ANGL. DEV. = -6.5 DEGREES
REMARK 500 DT T 844 C4 - C5 - C6 ANGL. DEV. = -5.5 DEGREES
REMARK 500 DT T 844 N3 - C4 - O4 ANGL. DEV. = -5.4 DEGREES
REMARK 500 DT T 844 C4 - C5 - C7 ANGL. DEV. = 10.9 DEGREES
REMARK 500 DT T 844 C6 - C5 - C7 ANGL. DEV. = -5.3 DEGREES
REMARK 500 DT T 844 C3' - O3' - P ANGL. DEV. = -8.1 DEGREES
REMARK 500 DC T 845 C4 - C5 - C6 ANGL. DEV. = -3.1 DEGREES
REMARK 500 DC T 845 N3 - C4 - N4 ANGL. DEV. = -4.9 DEGREES
REMARK 500 DC T 846 O3' - P - OP2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 DC T 846 O3' - P - OP1 ANGL. DEV. = -15.8 DEGREES
REMARK 500 DC T 846 C6 - N1 - C2 ANGL. DEV. = -2.8 DEGREES
REMARK 500 DT T 847 O4' - C4' - C3' ANGL. DEV. = 6.1 DEGREES
REMARK 500 DT T 847 C4' - C3' - O3' ANGL. DEV. = 15.8 DEGREES
REMARK 500 DT T 847 O4' - C1' - C2' ANGL. DEV. = 5.1 DEGREES
REMARK 500 DT T 847 N3 - C4 - C5 ANGL. DEV. = 6.7 DEGREES
REMARK 500 DT T 847 C4 - C5 - C6 ANGL. DEV. = -7.5 DEGREES
REMARK 500 DT T 847 N3 - C4 - O4 ANGL. DEV. = -4.2 DEGREES
REMARK 500 DT T 847 C6 - C5 - C7 ANGL. DEV. = 4.2 DEGREES
REMARK 500 DA P 867 O4' - C4' - C3' ANGL. DEV. = -4.2 DEGREES
REMARK 500 DA P 867 C1' - O4' - C4' ANGL. DEV. = 7.3 DEGREES
REMARK 500 DA P 867 O4' - C1' - N9 ANGL. DEV. = 10.4 DEGREES
REMARK 500 DA P 867 C6 - N1 - C2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 DA P 867 C5 - C6 - N1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 DA P 867 N7 - C8 - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DA P 867 C8 - N9 - C4 ANGL. DEV. = -3.6 DEGREES
REMARK 500 DA P 867 N1 - C6 - N6 ANGL. DEV. = -3.8 DEGREES
REMARK 500 DG P 868 C5' - C4' - O4' ANGL. DEV. = 6.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 85 ANGLE DEVIATIONS.
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 CYS A 37 59.73 22.71
REMARK 500 LYS A 60 -122.78 42.06
REMARK 500 LEU A 73 37.68 -88.82
REMARK 500 LYS A 77 -99.01 21.45
REMARK 500 VAL A 81 5.33 -64.65
REMARK 500 ARG A 82 -57.85 -133.36
REMARK 500 CYS A 88 98.25 -169.95
REMARK 500 GLN A 90 31.99 -74.14
REMARK 500 SER A 145 86.31 -49.22
REMARK 500 ASP A 146 -77.03 168.43
REMARK 500 LEU A 165 -8.63 -55.58
REMARK 500 PRO A 215 -76.50 -70.34
REMARK 500 GLU A 272 -22.42 -143.53
REMARK 500 ASP A 289 106.51 -168.23
REMARK 500 PHE A 308 110.67 175.40
REMARK 500 LYS A 310 -35.34 81.97
REMARK 500 GLU A 314 -141.60 177.43
REMARK 500 VAL A 315 -44.29 -27.76
REMARK 500 ALA A 317 44.48 -89.57
REMARK 500 CYS A 333 -85.70 -45.25
REMARK 500 GLN A 334 -55.74 -10.95
REMARK 500 ARG A 337 142.29 -31.92
REMARK 500 PRO A 365 95.66 -55.52
REMARK 500 SER A 366 -73.51 13.00
REMARK 500 THR A 381 -87.17 -15.02
REMARK 500 ASN A 393 -15.44 -39.23
REMARK 500 LEU A 405 149.20 154.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE A 213 LYS A 214 -134.64
REMARK 500 GLU A 305 ASP A 306 149.50
REMARK 500 MET A 388 LYS A 389 142.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 DG T 843 0.05 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1T3N RELATED DB: PDB
REMARK 900 TERNARY COMPLEX OF CATALYTIC CORE OF HUMAN DNA POLYMERASE IOTA WITH
REMARK 900 DNA AND DTTP
REMARK 900 RELATED ID: 2ALZ RELATED DB: PDB
REMARK 900 TERNARY COMPLEX OF CATALYTIC CORE OF HUMAN DNA POLYMERASE IOTA WITH
REMARK 900 DNA AND DCTP
REMARK 900 RELATED ID: 2FLN RELATED DB: PDB
REMARK 900 BINARY COMPLEX OF CATALYTIC CORE OF HUMAN DNA POLYMERASE IOTA WITH
REMARK 900 DNA (TEMPLATE A)
REMARK 900 RELATED ID: 2FLL RELATED DB: PDB
REMARK 900 TERNARY COMPLEX OF CATALYTIC CORE OF HUMAN DNA POLYMERASE IOTA WITH
REMARK 900 DNA AND DTTP (P6522)
DBREF 2FLP A 1 420 UNP Q9UNA4 POLI_HUMAN 1 420
DBREF 2FLP T 837 847 PDB 2FLP 2FLP 837 847
DBREF 2FLP P 867 873 PDB 2FLP 2FLP 867 873
SEQRES 1 T 11 DT DC DT DG DG DG DG DT DC DC DT
SEQRES 1 P 7 DA DG DG DA DC DC DOC
SEQRES 1 A 420 MET GLU LEU ALA ASP VAL GLY ALA ALA ALA SER SER GLN
SEQRES 2 A 420 GLY VAL HIS ASP GLN VAL LEU PRO THR PRO ASN ALA SER
SEQRES 3 A 420 SER ARG VAL ILE VAL HIS VAL ASP LEU ASP CYS PHE TYR
SEQRES 4 A 420 ALA GLN VAL GLU MET ILE SER ASN PRO GLU LEU LYS ASP
SEQRES 5 A 420 LYS PRO LEU GLY VAL GLN GLN LYS TYR LEU VAL VAL THR
SEQRES 6 A 420 CYS ASN TYR GLU ALA ARG LYS LEU GLY VAL LYS LYS LEU
SEQRES 7 A 420 MET ASN VAL ARG ASP ALA LYS GLU LYS CYS PRO GLN LEU
SEQRES 8 A 420 VAL LEU VAL ASN GLY GLU ASP LEU THR ARG TYR ARG GLU
SEQRES 9 A 420 MET SER TYR LYS VAL THR GLU LEU LEU GLU GLU PHE SER
SEQRES 10 A 420 PRO VAL VAL GLU ARG LEU GLY PHE ASP GLU ASN PHE VAL
SEQRES 11 A 420 ASP LEU THR GLU MET VAL GLU LYS ARG LEU GLN GLN LEU
SEQRES 12 A 420 GLN SER ASP GLU LEU SER ALA VAL THR VAL SER GLY HIS
SEQRES 13 A 420 VAL TYR ASN ASN GLN SER ILE ASN LEU LEU ASP VAL LEU
SEQRES 14 A 420 HIS ILE ARG LEU LEU VAL GLY SER GLN ILE ALA ALA GLU
SEQRES 15 A 420 MET ARG GLU ALA MET TYR ASN GLN LEU GLY LEU THR GLY
SEQRES 16 A 420 CYS ALA GLY VAL ALA SER ASN LYS LEU LEU ALA LYS LEU
SEQRES 17 A 420 VAL SER GLY VAL PHE LYS PRO ASN GLN GLN THR VAL LEU
SEQRES 18 A 420 LEU PRO GLU SER CYS GLN HIS LEU ILE HIS SER LEU ASN
SEQRES 19 A 420 HIS ILE LYS GLU ILE PRO GLY ILE GLY TYR LYS THR ALA
SEQRES 20 A 420 LYS CYS LEU GLU ALA LEU GLY ILE ASN SER VAL ARG ASP
SEQRES 21 A 420 LEU GLN THR PHE SER PRO LYS ILE LEU GLU LYS GLU LEU
SEQRES 22 A 420 GLY ILE SER VAL ALA GLN ARG ILE GLN LYS LEU SER PHE
SEQRES 23 A 420 GLY GLU ASP ASN SER PRO VAL ILE LEU SER GLY PRO PRO
SEQRES 24 A 420 GLN SER PHE SER GLU GLU ASP SER PHE LYS LYS CYS SER
SEQRES 25 A 420 SER GLU VAL GLU ALA LYS ASN LYS ILE GLU GLU LEU LEU
SEQRES 26 A 420 ALA SER LEU LEU ASN ARG VAL CYS GLN ASP GLY ARG LYS
SEQRES 27 A 420 PRO HIS THR VAL ARG LEU ILE ILE ARG ARG TYR SER SER
SEQRES 28 A 420 GLU LYS HIS TYR GLY ARG GLU SER ARG GLN CYS PRO ILE
SEQRES 29 A 420 PRO SER HIS VAL ILE GLN LYS LEU GLY THR GLY ASN TYR
SEQRES 30 A 420 ASP VAL MET THR PRO MET VAL ASP ILE LEU MET LYS LEU
SEQRES 31 A 420 PHE ARG ASN MET VAL ASN VAL LYS MET PRO PHE HIS LEU
SEQRES 32 A 420 THR LEU LEU SER VAL CYS PHE CYS ASN LEU LYS ALA LEU
SEQRES 33 A 420 ASN THR ALA LYS
MODRES 2FLP DOC P 873 DC 2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE
HET DOC P 873 18
HETNAM DOC 2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE
FORMUL 2 DOC C9 H14 N3 O6 P
FORMUL 4 HOH *115(H2 O)
HELIX 1 1 CYS A 37 ASN A 47 1 11
HELIX 2 2 PRO A 48 LYS A 51 5 4
HELIX 3 3 ASN A 67 LEU A 73 1 7
HELIX 4 4 LEU A 99 SER A 117 1 19
HELIX 5 5 LEU A 132 GLN A 141 1 10
HELIX 6 6 ASP A 146 VAL A 151 5 6
HELIX 7 7 ASP A 167 GLY A 192 1 26
HELIX 8 8 ASN A 202 GLY A 211 1 10
HELIX 9 9 LEU A 222 GLU A 224 5 3
HELIX 10 10 SER A 225 LEU A 233 1 9
HELIX 11 11 HIS A 235 ILE A 239 5 5
HELIX 12 12 GLY A 243 LEU A 253 1 11
HELIX 13 13 SER A 257 PHE A 264 1 8
HELIX 14 14 SER A 265 PHE A 286 1 22
HELIX 15 15 GLU A 314 ALA A 317 5 4
HELIX 16 16 LYS A 318 GLY A 336 1 19
HELIX 17 17 PRO A 365 GLN A 370 1 6
HELIX 18 18 MET A 380 ASN A 393 1 14
SHEET 1 A 6 VAL A 120 LEU A 123 0
SHEET 2 A 6 GLU A 127 ASP A 131 -1 O PHE A 129 N GLU A 121
SHEET 3 A 6 ILE A 30 LEU A 35 -1 N VAL A 33 O ASN A 128
SHEET 4 A 6 GLY A 195 ALA A 200 -1 O CYS A 196 N ASP A 34
SHEET 5 A 6 GLN A 218 VAL A 220 1 O THR A 219 N VAL A 199
SHEET 6 A 6 HIS A 156 VAL A 157 1 N HIS A 156 O GLN A 218
SHEET 1 B 4 MET A 79 ASN A 80 0
SHEET 2 B 4 LEU A 62 CYS A 66 -1 N VAL A 63 O MET A 79
SHEET 3 B 4 LEU A 55 GLN A 59 -1 N GLN A 59 O LEU A 62
SHEET 4 B 4 VAL A 92 ASN A 95 1 O VAL A 94 N GLN A 58
SHEET 1 C 4 SER A 301 SER A 307 0
SHEET 2 C 4 LEU A 405 LYS A 414 -1 O LEU A 406 N ASP A 306
SHEET 3 C 4 LYS A 338 ILE A 346 -1 N ILE A 345 O SER A 407
SHEET 4 C 4 GLU A 358 PRO A 363 -1 O CYS A 362 N VAL A 342
LINK O3' DC P 872 P DOC P 873 1555 1555 1.52
CRYST1 98.367 98.367 202.497 90.00 90.00 120.00 P 65 2 2 12
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 0.010166 0.005869 0.000000 0.00000
SCALE2 0.000000 0.011739 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004938 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
