HEADER TRANSCRIPTION 14-JUN-08 3DGP
TITLE CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN TFB5 AND THE C-TERMINAL
TITLE 2 DOMAIN OF TFB2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA POLYMERASE II TRANSCRIPTION FACTOR B SUBUNIT 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 SYNONYM: RNA POLYMERASE II TRANSCRIPTION FACTOR B P52 SUBUNIT, RNA
COMPND 6 POLYMERASE II TRANSCRIPTION FACTOR B 52 KDA SUBUNIT, GENERAL
COMPND 7 TRANSCRIPTION AND DNA REPAIR FACTOR IIH SUBUNIT TFB2, TFIIH SUBUNIT
COMPND 8 TFB2;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: RNA POLYMERASE II TRANSCRIPTION FACTOR B SUBUNIT 5;
COMPND 12 CHAIN: B;
COMPND 13 SYNONYM: GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH SUBUNIT
COMPND 14 TFB5, TFIIH SUBUNIT TFB5;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: TFB2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PSKB2;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 14 ORGANISM_TAXID: 4932;
SOURCE 15 GENE: TFB5;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PSKB2
KEYWDS PROTEIN-PROTEIN COMPLEX, BETA-ALPHA-BETA SPILT, HETERODIMER, DNA
KEYWDS 2 DAMAGE, DNA EXCISION, DNA REPAIR, NUCLEUS, TRANSCRIPTION,
KEYWDS 3 TRANSCRIPTION REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR D.E.KAINOV,J.CAVARELLI,J.M.EGLY,A.POTERSZMAN
REVDAT 4 21-FEB-24 3DGP 1 SEQADV
REVDAT 3 13-JUL-11 3DGP 1 VERSN
REVDAT 2 10-FEB-09 3DGP 1 VERSN JRNL
REVDAT 1 19-AUG-08 3DGP 0
JRNL AUTH D.E.KAINOV,M.VITORINO,J.CAVARELLI,A.POTERSZMAN,J.M.EGLY
JRNL TITL STRUCTURAL BASIS FOR GROUP A TRICHOTHIODYSTROPHY
JRNL REF NAT.STRUCT.MOL.BIOL. V. 15 980 2008
JRNL REFN ISSN 1545-9993
JRNL PMID 19172752
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 18822
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1006
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1275
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.76
REMARK 3 BIN R VALUE (WORKING SET) : 0.2120
REMARK 3 BIN FREE R VALUE SET COUNT : 84
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1017
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 126
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 23.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.12000
REMARK 3 B22 (A**2) : 1.12000
REMARK 3 B33 (A**2) : -1.68000
REMARK 3 B12 (A**2) : 0.56000
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): 0.103
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.107
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.071
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.311
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1031 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1383 ; 1.270 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 123 ; 5.053 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 49 ;37.302 ;25.306
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 208 ;13.803 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;20.909 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 157 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 746 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 477 ; 0.204 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 717 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 83 ; 0.153 ; 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): 43 ; 0.220 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.129 ; 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): 637 ; 0.975 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1000 ; 1.660 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 439 ; 2.454 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 383 ; 3.950 ; 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 : 2
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 450 A 508
REMARK 3 ORIGIN FOR THE GROUP (A): 19.5040 41.7965 25.9854
REMARK 3 T TENSOR
REMARK 3 T11: -0.0980 T22: 0.0384
REMARK 3 T33: -0.0807 T12: 0.0316
REMARK 3 T13: 0.0094 T23: 0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 1.5438 L22: 0.9405
REMARK 3 L33: 3.8330 L12: -0.3146
REMARK 3 L13: 0.8761 L23: -0.6952
REMARK 3 S TENSOR
REMARK 3 S11: 0.0209 S12: -0.0953 S13: -0.0998
REMARK 3 S21: -0.0242 S22: 0.0699 S23: 0.0770
REMARK 3 S31: 0.1044 S32: -0.2917 S33: -0.0908
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 : B 2 B 63
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7533 59.4856 16.1255
REMARK 3 T TENSOR
REMARK 3 T11: -0.0915 T22: -0.0020
REMARK 3 T33: -0.0601 T12: 0.0488
REMARK 3 T13: -0.0029 T23: -0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 1.6168 L22: 3.8839
REMARK 3 L33: 3.3693 L12: -0.9162
REMARK 3 L13: 0.9352 L23: -1.9754
REMARK 3 S TENSOR
REMARK 3 S11: -0.0647 S12: -0.1454 S13: 0.1761
REMARK 3 S21: 0.1300 S22: 0.0815 S23: 0.0695
REMARK 3 S31: -0.2532 S32: -0.1066 S33: -0.0168
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 3DGP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-08.
REMARK 100 THE DEPOSITION ID IS D_1000048016.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUL-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9198
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19737
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 (%) : 98.5
REMARK 200 DATA REDUNDANCY : 10.30
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 0.9
REMARK 200 DATA REDUNDANCY IN SHELL : 8.10
REMARK 200 R MERGE FOR SHELL (I) : 0.24900
REMARK 200 R SYM FOR SHELL (I) : 0.24900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
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 (%): 59.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS 20 MM, NACL 50 MM, PH 8.9,
REMARK 280 EVAPORATION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 12.42067
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 24.84133
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 18.63100
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 31.05167
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 6.21033
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 434
REMARK 465 PRO A 435
REMARK 465 THR A 436
REMARK 465 VAL A 437
REMARK 465 VAL A 438
REMARK 465 ASP A 439
REMARK 465 GLN A 440
REMARK 465 ILE A 441
REMARK 465 ARG A 442
REMARK 465 LEU A 443
REMARK 465 TRP A 444
REMARK 465 GLN A 445
REMARK 465 LEU A 446
REMARK 465 LEU A 509
REMARK 465 LYS A 510
REMARK 465 LYS A 511
REMARK 465 LYS A 512
REMARK 465 GLN A 513
REMARK 465 PRO B 65
REMARK 465 MET B 66
REMARK 465 ASP B 67
REMARK 465 GLU B 68
REMARK 465 GLU B 69
REMARK 465 GLU B 70
REMARK 465 ASN B 71
REMARK 465 GLN B 72
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 B 28 167.41 60.24
REMARK 500 ILE B 30 -61.48 -103.19
REMARK 500 ASP B 36 -167.29 -160.79
REMARK 500 TYR B 63 68.52 -106.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YDL RELATED DB: PDB
REMARK 900 RELATED ID: 2JNJ RELATED DB: PDB
DBREF 3DGP A 435 513 UNP Q02939 TFB2_YEAST 435 513
DBREF 3DGP B 2 72 UNP Q3E7C1 TFB5_YEAST 2 72
SEQADV 3DGP GLY A 434 UNP Q02939 EXPRESSION TAG
SEQRES 1 A 80 GLY PRO THR VAL VAL ASP GLN ILE ARG LEU TRP GLN LEU
SEQRES 2 A 80 GLU LEU ASP ARG VAL ILE THR TYR GLU GLY SER LEU TYR
SEQRES 3 A 80 SER ASP PHE GLU THR SER GLN GLU TYR ASN LEU LEU SER
SEQRES 4 A 80 LYS TYR ALA GLN ASP ILE GLY VAL LEU LEU TRP LYS ASP
SEQRES 5 A 80 ASP LYS LYS LYS LYS PHE PHE ILE SER LYS GLU GLY ASN
SEQRES 6 A 80 SER GLN VAL LEU ASP PHE ALA LYS ARG LYS LEU LYS LYS
SEQRES 7 A 80 LYS GLN
SEQRES 1 B 71 ALA ARG ALA ARG LYS GLY ALA LEU VAL GLN CYS ASP PRO
SEQRES 2 B 71 SER ILE LYS ALA LEU ILE LEU GLN ILE ASP ALA LYS MET
SEQRES 3 B 71 SER ASP ILE VAL LEU GLU GLU LEU ASP ASP THR HIS LEU
SEQRES 4 B 71 LEU VAL ASN PRO SER LYS VAL GLU PHE VAL LYS HIS GLU
SEQRES 5 B 71 LEU ASN ARG LEU LEU SER LYS ASN ILE TYR ASN PRO MET
SEQRES 6 B 71 ASP GLU GLU GLU ASN GLN
FORMUL 3 HOH *126(H2 O)
HELIX 1 1 GLU A 447 VAL A 451 5 5
HELIX 2 2 THR A 464 ILE A 478 1 15
HELIX 3 3 GLY A 497 LYS A 506 1 10
HELIX 4 4 ASP B 13 SER B 28 1 16
HELIX 5 5 LYS B 46 LYS B 60 1 15
SHEET 1 A 6 LEU A 481 ASP A 485 0
SHEET 2 A 6 LYS A 490 SER A 494 -1 O PHE A 492 N LEU A 482
SHEET 3 A 6 ILE A 452 SER A 460 -1 N TYR A 459 O PHE A 491
SHEET 4 A 6 ARG B 3 GLN B 11 -1 O ARG B 5 N LEU A 458
SHEET 5 A 6 HIS B 39 VAL B 42 -1 O VAL B 42 N ALA B 8
SHEET 6 A 6 VAL B 31 ASP B 36 -1 N LEU B 32 O LEU B 41
CRYST1 99.992 99.992 37.262 90.00 90.00 120.00 P 61 6
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 0.010001 0.005774 0.000000 0.00000
SCALE2 0.000000 0.011548 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026837 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
