HEADER REPLICATION 14-MAY-04 1T94
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF HUMAN DNA POLYMERASE KAPPA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYMERASE (DNA DIRECTED) KAPPA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DINB PROTEIN, POLYMERASE (DNA-DIRECTED) KAPPA;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DINB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 CODON +;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX
KEYWDS REPLICATION; DNA REPAIR; Y-FAMILY DNA POLYMERASE; TRANSLESION DNA
KEYWDS 2 SYNTHESIS; LESION BYPASS, REPLICATION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.N.ULJON,R.E.JOHNSON,T.A.EDWARDS,S.PRAKASH,L.PRAKASH,A.K.AGGARWAL
REVDAT 4 14-FEB-24 1T94 1 REMARK
REVDAT 3 31-JAN-18 1T94 1 REMARK
REVDAT 2 24-FEB-09 1T94 1 VERSN
REVDAT 1 31-AUG-04 1T94 0
JRNL AUTH S.N.ULJON,R.E.JOHNSON,T.A.EDWARDS,S.PRAKASH,L.PRAKASH,
JRNL AUTH 2 A.K.AGGARWAL
JRNL TITL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF HUMAN DNA
JRNL TITL 2 POLYMERASE KAPPA.
JRNL REF STRUCTURE V. 12 1395 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15296733
JRNL DOI 10.1016/J.STR.2004.05.011
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3842947.110
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.2
REMARK 3 NUMBER OF REFLECTIONS : 71651
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 SET) : 0.246
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3529
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 10070
REMARK 3 BIN R VALUE (WORKING SET) : 0.3300
REMARK 3 BIN FREE R VALUE : 0.3520
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 501
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6172
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 360
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.97000
REMARK 3 B22 (A**2) : 5.15000
REMARK 3 B33 (A**2) : 3.82000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM SIGMAA (A) : 0.40
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.43
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.700
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.130
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.310 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.240 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.910 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.890 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 38.87
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1T94 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000022466.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUN-03; 30-JUN-03
REMARK 200 TEMPERATURE (KELVIN) : 110; NULL
REMARK 200 PH : 7.75
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; APS
REMARK 200 BEAMLINE : 14-ID-B; 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.12709; 0.97934, 0.97920,
REMARK 200 0.96859
REMARK 200 MONOCHROMATOR : DIAMOND (111) DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR; SI 111 / SI 220
REMARK 200 OPTICS : DIAMOND (111) DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR; BENT CYLINDRICAL
REMARK 200 SI-MIRROR (RH COATING)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; SBC-2
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76925
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : 0.06400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.43600
REMARK 200 R SYM FOR SHELL (I) : 0.01900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 8K, 8% ETHYLENE GLYCOL, AND
REMARK 280 100MM HEPES (PH 7.75), VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 20K, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 42.60450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.60250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.73000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.60250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.60450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.73000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 68
REMARK 465 GLN A 69
REMARK 465 GLN A 70
REMARK 465 GLY A 226
REMARK 465 SER A 227
REMARK 465 SER A 228
REMARK 465 GLU A 254
REMARK 465 GLU A 255
REMARK 465 SER A 256
REMARK 465 PRO A 257
REMARK 465 SER A 258
REMARK 465 ASP A 259
REMARK 465 VAL A 260
REMARK 465 GLN A 261
REMARK 465 PRO A 262
REMARK 465 PRO A 263
REMARK 465 GLY A 264
REMARK 465 ASP A 265
REMARK 465 PRO A 266
REMARK 465 PHE A 267
REMARK 465 GLN A 268
REMARK 465 VAL A 269
REMARK 465 ASN A 270
REMARK 465 PHE A 271
REMARK 465 GLU A 272
REMARK 465 GLU A 273
REMARK 465 GLN A 274
REMARK 465 ASN A 275
REMARK 465 THR A 408
REMARK 465 ARG A 409
REMARK 465 ASP A 410
REMARK 465 GLU A 412
REMARK 465 ARG A 413
REMARK 465 LYS A 448
REMARK 465 GLU A 449
REMARK 465 ARG A 450
REMARK 465 THR A 473
REMARK 465 ALA A 481
REMARK 465 GLU A 482
REMARK 465 PHE A 516
REMARK 465 PRO A 517
REMARK 465 ASN A 518
REMARK 465 GLU A 519
REMARK 465 GLU A 520
REMARK 465 ASP A 521
REMARK 465 ARG A 522
REMARK 465 LYS A 523
REMARK 465 HIS A 524
REMARK 465 GLN A 525
REMARK 465 GLN A 526
REMARK 465 MET B 68
REMARK 465 GLN B 69
REMARK 465 GLN B 70
REMARK 465 LYS B 71
REMARK 465 ALA B 72
REMARK 465 GLN B 73
REMARK 465 ILE B 74
REMARK 465 MET B 225
REMARK 465 GLY B 226
REMARK 465 SER B 227
REMARK 465 SER B 228
REMARK 465 VAL B 229
REMARK 465 GLU B 230
REMARK 465 ASN B 231
REMARK 465 ASP B 232
REMARK 465 ASN B 233
REMARK 465 PRO B 234
REMARK 465 GLY B 235
REMARK 465 LYS B 236
REMARK 465 GLU B 237
REMARK 465 VAL B 238
REMARK 465 ASN B 239
REMARK 465 LYS B 240
REMARK 465 LEU B 241
REMARK 465 SER B 242
REMARK 465 GLU B 243
REMARK 465 HIS B 244
REMARK 465 GLU B 245
REMARK 465 ARG B 246
REMARK 465 SER B 247
REMARK 465 ILE B 248
REMARK 465 SER B 249
REMARK 465 PRO B 250
REMARK 465 LEU B 251
REMARK 465 LEU B 252
REMARK 465 PHE B 253
REMARK 465 GLU B 254
REMARK 465 GLU B 255
REMARK 465 SER B 256
REMARK 465 PRO B 257
REMARK 465 SER B 258
REMARK 465 ASP B 259
REMARK 465 VAL B 260
REMARK 465 GLN B 261
REMARK 465 PRO B 262
REMARK 465 PRO B 263
REMARK 465 GLY B 264
REMARK 465 ASP B 265
REMARK 465 PRO B 266
REMARK 465 PHE B 267
REMARK 465 GLN B 268
REMARK 465 VAL B 269
REMARK 465 ASN B 270
REMARK 465 PHE B 271
REMARK 465 GLU B 272
REMARK 465 GLU B 273
REMARK 465 GLN B 274
REMARK 465 ASN B 275
REMARK 465 ASN B 276
REMARK 465 PRO B 277
REMARK 465 GLN B 278
REMARK 465 ILE B 279
REMARK 465 LEU B 280
REMARK 465 ASP B 410
REMARK 465 GLY B 411
REMARK 465 GLU B 412
REMARK 465 VAL B 474
REMARK 465 SER B 475
REMARK 465 ASN B 518
REMARK 465 GLU B 519
REMARK 465 GLU B 520
REMARK 465 ASP B 521
REMARK 465 ARG B 522
REMARK 465 LYS B 523
REMARK 465 HIS B 524
REMARK 465 GLN B 525
REMARK 465 GLN B 526
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 GLN A 77 CG CD OE1 NE2
REMARK 470 ARG A 80 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 81 CG CD CE NZ
REMARK 470 LYS A 124 CG CD CE NZ
REMARK 470 LYS A 179 CG CD CE NZ
REMARK 470 LYS A 347 CG CD CE NZ
REMARK 470 LYS A 359 CG CD CE NZ
REMARK 470 LYS A 414 CG CD CE NZ
REMARK 470 ASP A 445 CG OD1 OD2
REMARK 470 LEU A 451 CG CD1 CD2
REMARK 470 LYS A 452 CG CD CE NZ
REMARK 470 ARG A 454 CG CD NE CZ NH1 NH2
REMARK 470 THR A 455 OG1 CG2
REMARK 470 VAL A 474 CG1 CG2
REMARK 470 SER A 475 OG
REMARK 470 SER A 476 OG
REMARK 470 VAL A 477 CG1 CG2
REMARK 470 VAL A 478 CG1 CG2
REMARK 470 SER A 479 OG
REMARK 470 THR A 480 OG1 CG2
REMARK 470 PHE A 500 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 513 CG1 CG2 CD1
REMARK 470 SER A 514 OG
REMARK 470 SER A 515 OG
REMARK 470 GLN B 78 CG CD OE1 NE2
REMARK 470 SER B 134 OG
REMARK 470 ARG B 145 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 353 CG CD CE NZ
REMARK 470 LYS B 359 CG CD CE NZ
REMARK 470 LYS B 363 CG CD CE NZ
REMARK 470 LEU B 368 CG CD1 CD2
REMARK 470 LYS B 414 CG CD CE NZ
REMARK 470 LEU B 446 CG CD1 CD2
REMARK 470 ARG B 450 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 451 CG CD1 CD2
REMARK 470 LYS B 452 CG CD CE NZ
REMARK 470 ARG B 454 CG CD NE CZ NH1 NH2
REMARK 470 SER B 476 OG
REMARK 470 VAL B 477 CG1 CG2
REMARK 470 VAL B 478 CG1 CG2
REMARK 470 SER B 479 OG
REMARK 470 THR B 480 OG1 CG2
REMARK 470 GLU B 482 CG CD OE1 OE2
REMARK 470 GLU B 483 CG CD OE1 OE2
REMARK 470 ILE B 484 CG1 CG2 CD1
REMARK 470 SER B 514 OG
REMARK 470 SER B 515 OG
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 GLU A 389 CD GLU A 389 OE2 0.080
REMARK 500 THR A 455 N THR A 455 CA 0.127
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 ASN A 231 C - N - CA ANGL. DEV. = 16.2 DEGREES
REMARK 500 LEU A 451 N - CA - C ANGL. DEV. = 19.6 DEGREES
REMARK 500 LYS A 452 N - CA - C ANGL. DEV. = 18.0 DEGREES
REMARK 500 SER A 475 N - CA - C ANGL. DEV. = 21.6 DEGREES
REMARK 500 GLU B 449 N - CA - C ANGL. DEV. = -17.8 DEGREES
REMARK 500 PRO B 517 C - N - CD ANGL. DEV. = -30.7 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 SER A 76 50.50 -67.11
REMARK 500 GLN A 77 -64.75 -151.86
REMARK 500 PHE A 111 -75.98 -32.83
REMARK 500 ASN A 170 81.39 -155.02
REMARK 500 ASP A 189 99.80 -160.50
REMARK 500 SER A 196 -159.49 -161.15
REMARK 500 ARG A 219 31.45 -140.94
REMARK 500 ARG A 246 -77.51 -46.37
REMARK 500 THR A 306 -8.30 80.42
REMARK 500 ASN A 327 48.24 -99.88
REMARK 500 LYS A 328 -118.03 -20.28
REMARK 500 PRO A 329 110.83 -34.78
REMARK 500 PRO A 337 33.06 -57.46
REMARK 500 ILE A 371 -62.71 -122.82
REMARK 500 GLN A 379 30.10 -92.40
REMARK 500 GLU A 419 127.41 178.78
REMARK 500 GLU A 424 125.84 -36.08
REMARK 500 LEU A 442 37.52 -86.12
REMARK 500 GLN A 444 72.77 -53.89
REMARK 500 ASP A 445 -99.72 -71.52
REMARK 500 LEU A 446 4.37 58.35
REMARK 500 LYS A 452 -96.74 162.87
REMARK 500 ARG A 454 -169.63 3.81
REMARK 500 THR A 455 92.20 -10.70
REMARK 500 SER A 475 153.10 114.33
REMARK 500 VAL A 478 147.76 -20.29
REMARK 500 SER A 479 162.65 172.67
REMARK 500 ALA A 498 116.13 -178.05
REMARK 500 PHE A 500 -34.83 -30.11
REMARK 500 SER A 514 -20.96 -147.20
REMARK 500 ALA B 110 45.99 38.45
REMARK 500 PHE B 111 -63.78 -28.78
REMARK 500 ASN B 120 74.16 -114.06
REMARK 500 MET B 135 127.20 178.28
REMARK 500 ARG B 219 35.88 -145.27
REMARK 500 THR B 305 -147.88 -101.50
REMARK 500 THR B 306 11.50 -148.81
REMARK 500 PRO B 329 -115.97 -63.37
REMARK 500 ASN B 330 71.61 -44.91
REMARK 500 LEU B 336 142.94 -38.16
REMARK 500 PRO B 337 61.05 -64.27
REMARK 500 ASP B 348 56.24 -101.04
REMARK 500 GLU B 424 131.53 -21.85
REMARK 500 GLU B 441 12.23 -69.98
REMARK 500 GLN B 447 37.67 -91.92
REMARK 500 LEU B 451 72.89 27.33
REMARK 500 PHE B 465 15.31 88.93
REMARK 500 VAL B 477 100.30 95.19
REMARK 500 PRO B 503 -132.58 -50.10
REMARK 500 LEU B 504 106.44 -166.96
REMARK 500
REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS.
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 VAL A 474 SER A 475 149.10
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1T94 A 68 526 UNP Q9UBT6 POLK_HUMAN 68 526
DBREF 1T94 B 68 526 UNP Q9UBT6 POLK_HUMAN 68 526
SEQRES 1 A 459 MET GLN GLN LYS ALA GLN ILE THR SER GLN GLN LEU ARG
SEQRES 2 A 459 LYS ALA GLN LEU GLN VAL ASP ARG PHE ALA MET GLU LEU
SEQRES 3 A 459 GLU GLN SER ARG ASN LEU SER ASN THR ILE VAL HIS ILE
SEQRES 4 A 459 ASP MET ASP ALA PHE TYR ALA ALA VAL GLU MET ARG ASP
SEQRES 5 A 459 ASN PRO GLU LEU LYS ASP LYS PRO ILE ALA VAL GLY SER
SEQRES 6 A 459 MET SER MET LEU SER THR SER ASN TYR HIS ALA ARG ARG
SEQRES 7 A 459 PHE GLY VAL ARG ALA ALA MET PRO GLY PHE ILE ALA LYS
SEQRES 8 A 459 ARG LEU CYS PRO GLN LEU ILE ILE VAL PRO PRO ASN PHE
SEQRES 9 A 459 ASP LYS TYR ARG ALA VAL SER LYS GLU VAL LYS GLU ILE
SEQRES 10 A 459 LEU ALA ASP TYR ASP PRO ASN PHE MET ALA MET SER LEU
SEQRES 11 A 459 ASP GLU ALA TYR LEU ASN ILE THR LYS HIS LEU GLU GLU
SEQRES 12 A 459 ARG GLN ASN TRP PRO GLU ASP LYS ARG ARG TYR PHE ILE
SEQRES 13 A 459 LYS MET GLY SER SER VAL GLU ASN ASP ASN PRO GLY LYS
SEQRES 14 A 459 GLU VAL ASN LYS LEU SER GLU HIS GLU ARG SER ILE SER
SEQRES 15 A 459 PRO LEU LEU PHE GLU GLU SER PRO SER ASP VAL GLN PRO
SEQRES 16 A 459 PRO GLY ASP PRO PHE GLN VAL ASN PHE GLU GLU GLN ASN
SEQRES 17 A 459 ASN PRO GLN ILE LEU GLN ASN SER VAL VAL PHE GLY THR
SEQRES 18 A 459 SER ALA GLN GLU VAL VAL LYS GLU ILE ARG PHE ARG ILE
SEQRES 19 A 459 GLU GLN LYS THR THR LEU THR ALA SER ALA GLY ILE ALA
SEQRES 20 A 459 PRO ASN THR MET LEU ALA LYS VAL CYS SER ASP LYS ASN
SEQRES 21 A 459 LYS PRO ASN GLY GLN TYR GLN ILE LEU PRO ASN ARG GLN
SEQRES 22 A 459 ALA VAL MET ASP PHE ILE LYS ASP LEU PRO ILE ARG LYS
SEQRES 23 A 459 VAL SER GLY ILE GLY LYS VAL THR GLU LYS MET LEU LYS
SEQRES 24 A 459 ALA LEU GLY ILE ILE THR CYS THR GLU LEU TYR GLN GLN
SEQRES 25 A 459 ARG ALA LEU LEU SER LEU LEU PHE SER GLU THR SER TRP
SEQRES 26 A 459 HIS TYR PHE LEU HIS ILE SER LEU GLY LEU GLY SER THR
SEQRES 27 A 459 HIS LEU THR ARG ASP GLY GLU ARG LYS SER MET SER VAL
SEQRES 28 A 459 GLU ARG THR PHE SER GLU ILE ASN LYS ALA GLU GLU GLN
SEQRES 29 A 459 TYR SER LEU CYS GLN GLU LEU CYS SER GLU LEU ALA GLN
SEQRES 30 A 459 ASP LEU GLN LYS GLU ARG LEU LYS GLY ARG THR VAL THR
SEQRES 31 A 459 ILE LYS LEU LYS ASN VAL ASN PHE GLU VAL LYS THR ARG
SEQRES 32 A 459 ALA SER THR VAL SER SER VAL VAL SER THR ALA GLU GLU
SEQRES 33 A 459 ILE PHE ALA ILE ALA LYS GLU LEU LEU LYS THR GLU ILE
SEQRES 34 A 459 ASP ALA ASP PHE PRO HIS PRO LEU ARG LEU ARG LEU MET
SEQRES 35 A 459 GLY VAL ARG ILE SER SER PHE PRO ASN GLU GLU ASP ARG
SEQRES 36 A 459 LYS HIS GLN GLN
SEQRES 1 B 459 MET GLN GLN LYS ALA GLN ILE THR SER GLN GLN LEU ARG
SEQRES 2 B 459 LYS ALA GLN LEU GLN VAL ASP ARG PHE ALA MET GLU LEU
SEQRES 3 B 459 GLU GLN SER ARG ASN LEU SER ASN THR ILE VAL HIS ILE
SEQRES 4 B 459 ASP MET ASP ALA PHE TYR ALA ALA VAL GLU MET ARG ASP
SEQRES 5 B 459 ASN PRO GLU LEU LYS ASP LYS PRO ILE ALA VAL GLY SER
SEQRES 6 B 459 MET SER MET LEU SER THR SER ASN TYR HIS ALA ARG ARG
SEQRES 7 B 459 PHE GLY VAL ARG ALA ALA MET PRO GLY PHE ILE ALA LYS
SEQRES 8 B 459 ARG LEU CYS PRO GLN LEU ILE ILE VAL PRO PRO ASN PHE
SEQRES 9 B 459 ASP LYS TYR ARG ALA VAL SER LYS GLU VAL LYS GLU ILE
SEQRES 10 B 459 LEU ALA ASP TYR ASP PRO ASN PHE MET ALA MET SER LEU
SEQRES 11 B 459 ASP GLU ALA TYR LEU ASN ILE THR LYS HIS LEU GLU GLU
SEQRES 12 B 459 ARG GLN ASN TRP PRO GLU ASP LYS ARG ARG TYR PHE ILE
SEQRES 13 B 459 LYS MET GLY SER SER VAL GLU ASN ASP ASN PRO GLY LYS
SEQRES 14 B 459 GLU VAL ASN LYS LEU SER GLU HIS GLU ARG SER ILE SER
SEQRES 15 B 459 PRO LEU LEU PHE GLU GLU SER PRO SER ASP VAL GLN PRO
SEQRES 16 B 459 PRO GLY ASP PRO PHE GLN VAL ASN PHE GLU GLU GLN ASN
SEQRES 17 B 459 ASN PRO GLN ILE LEU GLN ASN SER VAL VAL PHE GLY THR
SEQRES 18 B 459 SER ALA GLN GLU VAL VAL LYS GLU ILE ARG PHE ARG ILE
SEQRES 19 B 459 GLU GLN LYS THR THR LEU THR ALA SER ALA GLY ILE ALA
SEQRES 20 B 459 PRO ASN THR MET LEU ALA LYS VAL CYS SER ASP LYS ASN
SEQRES 21 B 459 LYS PRO ASN GLY GLN TYR GLN ILE LEU PRO ASN ARG GLN
SEQRES 22 B 459 ALA VAL MET ASP PHE ILE LYS ASP LEU PRO ILE ARG LYS
SEQRES 23 B 459 VAL SER GLY ILE GLY LYS VAL THR GLU LYS MET LEU LYS
SEQRES 24 B 459 ALA LEU GLY ILE ILE THR CYS THR GLU LEU TYR GLN GLN
SEQRES 25 B 459 ARG ALA LEU LEU SER LEU LEU PHE SER GLU THR SER TRP
SEQRES 26 B 459 HIS TYR PHE LEU HIS ILE SER LEU GLY LEU GLY SER THR
SEQRES 27 B 459 HIS LEU THR ARG ASP GLY GLU ARG LYS SER MET SER VAL
SEQRES 28 B 459 GLU ARG THR PHE SER GLU ILE ASN LYS ALA GLU GLU GLN
SEQRES 29 B 459 TYR SER LEU CYS GLN GLU LEU CYS SER GLU LEU ALA GLN
SEQRES 30 B 459 ASP LEU GLN LYS GLU ARG LEU LYS GLY ARG THR VAL THR
SEQRES 31 B 459 ILE LYS LEU LYS ASN VAL ASN PHE GLU VAL LYS THR ARG
SEQRES 32 B 459 ALA SER THR VAL SER SER VAL VAL SER THR ALA GLU GLU
SEQRES 33 B 459 ILE PHE ALA ILE ALA LYS GLU LEU LEU LYS THR GLU ILE
SEQRES 34 B 459 ASP ALA ASP PHE PRO HIS PRO LEU ARG LEU ARG LEU MET
SEQRES 35 B 459 GLY VAL ARG ILE SER SER PHE PRO ASN GLU GLU ASP ARG
SEQRES 36 B 459 LYS HIS GLN GLN
FORMUL 3 HOH *360(H2 O)
HELIX 1 1 GLN A 77 GLN A 95 1 19
HELIX 2 2 ALA A 110 ASN A 120 1 11
HELIX 3 3 PRO A 121 LYS A 124 5 4
HELIX 4 4 ASN A 140 PHE A 146 1 7
HELIX 5 5 PRO A 153 CYS A 161 1 9
HELIX 6 6 ASN A 170 ASP A 189 1 20
HELIX 7 7 ILE A 204 GLN A 212 1 9
HELIX 8 8 ASN A 213 TRP A 214 5 2
HELIX 9 9 PRO A 215 LYS A 218 5 4
HELIX 10 10 GLY A 235 SER A 242 5 8
HELIX 11 11 ILE A 248 LEU A 252 5 5
HELIX 12 12 SER A 289 THR A 306 1 18
HELIX 13 13 ASN A 316 ASN A 327 1 12
HELIX 14 14 ASN A 338 LYS A 347 1 10
HELIX 15 15 PRO A 350 VAL A 354 5 5
HELIX 16 16 GLY A 358 LEU A 368 1 11
HELIX 17 17 THR A 372 GLN A 379 1 8
HELIX 18 18 GLN A 379 PHE A 387 1 9
HELIX 19 19 SER A 388 LEU A 400 1 13
HELIX 20 20 LYS A 427 SER A 440 1 14
HELIX 21 21 GLU A 483 ASP A 497 1 15
HELIX 22 22 THR B 75 SER B 96 1 22
HELIX 23 23 ALA B 110 ASN B 120 1 11
HELIX 24 24 PRO B 121 LYS B 124 5 4
HELIX 25 25 ASN B 140 ARG B 145 1 6
HELIX 26 26 PRO B 153 CYS B 161 1 9
HELIX 27 27 ASN B 170 ALA B 186 1 17
HELIX 28 28 ILE B 204 GLN B 212 1 9
HELIX 29 29 ASN B 213 TRP B 214 5 2
HELIX 30 30 PRO B 215 LYS B 218 5 4
HELIX 31 31 SER B 289 THR B 305 1 17
HELIX 32 32 ASN B 316 SER B 324 1 9
HELIX 33 33 ASN B 338 ASP B 348 1 11
HELIX 34 34 LEU B 349 LEU B 349 5 1
HELIX 35 35 PRO B 350 VAL B 354 5 5
HELIX 36 36 GLY B 358 LYS B 366 1 9
HELIX 37 37 ALA B 367 GLY B 369 5 3
HELIX 38 38 THR B 372 GLN B 379 1 8
HELIX 39 39 GLN B 379 PHE B 387 1 9
HELIX 40 40 SER B 388 LEU B 400 1 13
HELIX 41 41 LYS B 427 GLN B 447 1 21
HELIX 42 42 ILE B 487 ASP B 499 1 13
SHEET 1 A 5 MET A 193 ALA A 194 0
SHEET 2 A 5 GLU A 199 ASN A 203 -1 O TYR A 201 N MET A 193
SHEET 3 A 5 ILE A 103 MET A 108 -1 N ILE A 106 O ALA A 200
SHEET 4 A 5 ALA A 309 ALA A 314 -1 O SER A 310 N ASP A 107
SHEET 5 A 5 GLN A 332 GLN A 334 1 O TYR A 333 N ILE A 313
SHEET 1 B 3 LEU A 136 SER A 139 0
SHEET 2 B 3 ILE A 128 GLY A 131 -1 N VAL A 130 O SER A 137
SHEET 3 B 3 ILE A 165 VAL A 167 1 O VAL A 167 N ALA A 129
SHEET 1 C 2 ARG A 220 PHE A 222 0
SHEET 2 C 2 SER A 283 VAL A 285 -1 O VAL A 284 N TYR A 221
SHEET 1 D 4 MET A 416 ILE A 425 0
SHEET 2 D 4 LEU A 506 ILE A 513 -1 O ARG A 507 N PHE A 422
SHEET 3 D 4 VAL A 456 ASN A 462 -1 N LYS A 459 O GLY A 510
SHEET 4 D 4 VAL A 467 ARG A 470 -1 O ARG A 470 N ILE A 458
SHEET 1 E 5 MET B 193 ALA B 194 0
SHEET 2 E 5 GLU B 199 ASN B 203 -1 O TYR B 201 N MET B 193
SHEET 3 E 5 ILE B 103 MET B 108 -1 N ILE B 106 O ALA B 200
SHEET 4 E 5 ALA B 309 ALA B 314 -1 O GLY B 312 N HIS B 105
SHEET 5 E 5 GLN B 332 GLN B 334 1 O TYR B 333 N ALA B 311
SHEET 1 F 3 MET B 135 SER B 139 0
SHEET 2 F 3 ILE B 128 SER B 132 -1 N VAL B 130 O SER B 137
SHEET 3 F 3 ILE B 165 VAL B 167 1 O VAL B 167 N GLY B 131
SHEET 1 G 2 ARG B 220 PHE B 222 0
SHEET 2 G 2 SER B 283 VAL B 285 -1 O VAL B 284 N TYR B 221
SHEET 1 H 4 SER B 415 ILE B 425 0
SHEET 2 H 4 LEU B 506 SER B 514 -1 O ILE B 513 N MET B 416
SHEET 3 H 4 THR B 455 ASN B 462 -1 N LYS B 461 O ARG B 507
SHEET 4 H 4 VAL B 467 SER B 472 -1 O ARG B 470 N ILE B 458
CISPEP 1 LYS B 328 PRO B 329 0 -2.84
CISPEP 2 PHE B 500 PRO B 501 0 2.97
CRYST1 85.209 109.460 111.205 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011736 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009136 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008992 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
