Header list of 1i4v.pdb file
Complete list - t 27 2 Bytes
HEADER HYDROLASE 23-FEB-01 1I4V
TITLE SOLUTION STRUCTURE OF THE UMUD' HOMODIMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UMUD' PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.4.21.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: UMUD;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET5A
KEYWDS SOS RESPONSE, SOS MUTAGENESIS, DNA REPAIR, DNA POLYMERASE V, DNA
KEYWDS 2 POLYMERASE ACCESSORY PROTEIN, LEXA REPRESSOR, LAMBDA CI, SIGNAL
KEYWDS 3 PEPTIDASE, SERINE-LYSINE DYAD, AUTOCATALYTIC CLEAVAGE, SERINE
KEYWDS 4 PROTEASE, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.E.FERENTZ,G.C.WALKER,G.WAGNER
REVDAT 3 27-OCT-21 1I4V 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1I4V 1 VERSN
REVDAT 1 22-AUG-01 1I4V 0
JRNL AUTH A.E.FERENTZ,G.C.WALKER,G.WAGNER
JRNL TITL CONVERTING A DNA DAMAGE CHECKPOINT EFFECTOR (UMUD2C) INTO A
JRNL TITL 2 LESION BYPASS POLYMERASE (UMUD'2C).
JRNL REF EMBO J. V. 20 4287 2001
JRNL REFN ISSN 0261-4189
JRNL PMID 11483531
JRNL DOI 10.1093/EMBOJ/20.15.4287
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 97.0, X-PLOR 3.851
REMARK 3 AUTHORS : MOLECULAR SIMULATIONS INC. (FELIX), BRUNGER (X
REMARK 3 -PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1I4V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-01.
REMARK 100 THE DEPOSITION ID IS D_1000012906.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 150 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.9 MM UMUD' U-15N; 150 MM NACL,
REMARK 210 10 MM PHOSPHATE, PH 6.0, 1MM DTT,
REMARK 210 0.1 MM EDTA; 1.3 MM UMUD' U-15N,
REMARK 210 13C; 150 MM NACL, 20 MM
REMARK 210 PHOSPHATE, PH 6.0, 1 MM DTT, 0.1
REMARK 210 MM EDTA; 1.5 MM UMUD' UNLABELED;
REMARK 210 150 MM NACL, 20 MM PHOSPHATE, PH
REMARK 210 6.0, 1 MM DTT, 0.1 MM EDTA; 1.4
REMARK 210 MM UMUD' UNLABELED; 150 MM NACL,
REMARK 210 20 MM PHOSPHATE, PH 6.0, 1 MM
REMARK 210 DTT, 0.1 MM EDTA; 0.5 MM UMUD' U-
REMARK 210 10% 13C; 150 MM NACL, 20 MM
REMARK 210 PHOSPHATE, PH 6.0, 1 MM DTT, 0.1
REMARK 210 MM EDTA; 2.7 MM UMUD' U-100% 2H,
REMARK 210 15N AND 2.7 MM UNLABELED UMUD';
REMARK 210 150 MM NACL, 20 MM PHOSPHATE, PH
REMARK 210 6.0, 1 MM DTT, 0.1 MM EDTA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNHA; 3D_15N-SEPARATED_NOESY;
REMARK 210 2D_NOESY; 3D_13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 400 MHZ; 600 MHZ; 500
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS; AMX; VXR
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.9
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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
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 1 PRO A 27 84.57 -61.86
REMARK 500 1 ALA A 30 -80.07 -154.80
REMARK 500 1 GLU A 35 88.09 -156.06
REMARK 500 1 ILE A 38 78.85 -103.74
REMARK 500 1 ILE A 45 -151.93 -116.74
REMARK 500 1 GLN A 46 33.22 -175.49
REMARK 500 1 SER A 49 73.14 -175.96
REMARK 500 1 ALA A 50 38.44 -147.80
REMARK 500 1 ASP A 59 55.08 -173.68
REMARK 500 1 SER A 67 66.05 -119.35
REMARK 500 1 ASP A 70 -174.15 -174.40
REMARK 500 1 ALA A 77 -49.29 -175.25
REMARK 500 1 ALA A 80 -153.97 -61.15
REMARK 500 1 LYS A 97 153.72 176.26
REMARK 500 1 SER A 112 -35.73 -176.19
REMARK 500 1 PRO A 116 108.09 -59.76
REMARK 500 1 ILE A 119 -82.18 -97.98
REMARK 500 1 SER A 120 -159.19 -134.49
REMARK 500 1 ASP A 123 -77.68 -79.20
REMARK 500 1 VAL A 130 16.59 -150.04
REMARK 500 1 ILE A 132 82.46 -152.44
REMARK 500 1 SER B 28 73.55 -174.71
REMARK 500 1 GLN B 36 -153.55 -88.34
REMARK 500 1 ILE B 45 -152.04 -116.93
REMARK 500 1 GLN B 46 33.14 -175.34
REMARK 500 1 SER B 49 72.92 -175.93
REMARK 500 1 ALA B 50 38.35 -147.54
REMARK 500 1 ASP B 59 54.82 -174.10
REMARK 500 1 SER B 67 66.14 -119.32
REMARK 500 1 ASP B 70 -174.09 -174.18
REMARK 500 1 ALA B 77 -49.23 -175.19
REMARK 500 1 ALA B 80 -153.99 -60.89
REMARK 500 1 LYS B 97 141.96 -175.48
REMARK 500 1 SER B 112 -33.39 -176.25
REMARK 500 1 SER B 115 96.60 -171.44
REMARK 500 1 ILE B 119 -74.52 -100.82
REMARK 500 1 ASP B 123 -77.23 -78.94
REMARK 500 1 VAL B 130 16.68 -149.91
REMARK 500 1 ILE B 132 82.57 -152.44
REMARK 500 2 SER A 28 67.19 -157.29
REMARK 500 2 ALA A 30 59.89 -144.51
REMARK 500 2 GLU A 35 -155.14 -173.94
REMARK 500 2 GLN A 36 -159.19 -165.69
REMARK 500 2 ARG A 37 51.89 -164.75
REMARK 500 2 LEU A 40 -86.44 30.20
REMARK 500 2 GLN A 46 -44.87 -130.86
REMARK 500 2 SER A 49 47.75 -148.62
REMARK 500 2 ASP A 59 34.44 -176.68
REMARK 500 2 ASP A 68 96.16 40.39
REMARK 500 2 ALA A 77 -48.39 -174.68
REMARK 500
REMARK 500 THIS ENTRY HAS 829 RAMACHANDRAN OUTLIERS.
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 1 ARG A 37 0.20 SIDE CHAIN
REMARK 500 1 ARG A 102 0.24 SIDE CHAIN
REMARK 500 1 ARG A 139 0.29 SIDE CHAIN
REMARK 500 1 ARG B 37 0.32 SIDE CHAIN
REMARK 500 1 ARG B 102 0.18 SIDE CHAIN
REMARK 500 1 ARG B 139 0.29 SIDE CHAIN
REMARK 500 2 ARG A 37 0.26 SIDE CHAIN
REMARK 500 2 ARG A 102 0.29 SIDE CHAIN
REMARK 500 2 ARG A 139 0.28 SIDE CHAIN
REMARK 500 2 ARG B 37 0.21 SIDE CHAIN
REMARK 500 2 ARG B 102 0.32 SIDE CHAIN
REMARK 500 2 ARG B 139 0.28 SIDE CHAIN
REMARK 500 3 ARG A 37 0.23 SIDE CHAIN
REMARK 500 3 ARG A 102 0.26 SIDE CHAIN
REMARK 500 3 ARG A 139 0.20 SIDE CHAIN
REMARK 500 3 ARG B 37 0.31 SIDE CHAIN
REMARK 500 3 ARG B 102 0.32 SIDE CHAIN
REMARK 500 3 ARG B 139 0.20 SIDE CHAIN
REMARK 500 4 ARG A 37 0.22 SIDE CHAIN
REMARK 500 4 ARG A 102 0.16 SIDE CHAIN
REMARK 500 4 ARG A 139 0.23 SIDE CHAIN
REMARK 500 4 ARG B 37 0.32 SIDE CHAIN
REMARK 500 4 ARG B 102 0.31 SIDE CHAIN
REMARK 500 4 ARG B 139 0.23 SIDE CHAIN
REMARK 500 5 ARG A 37 0.23 SIDE CHAIN
REMARK 500 5 ARG A 102 0.24 SIDE CHAIN
REMARK 500 5 ARG A 139 0.31 SIDE CHAIN
REMARK 500 5 ARG B 37 0.31 SIDE CHAIN
REMARK 500 5 ARG B 102 0.30 SIDE CHAIN
REMARK 500 5 ARG B 139 0.31 SIDE CHAIN
REMARK 500 6 ARG A 37 0.32 SIDE CHAIN
REMARK 500 6 ARG A 102 0.31 SIDE CHAIN
REMARK 500 6 ARG A 139 0.21 SIDE CHAIN
REMARK 500 6 ARG B 37 0.29 SIDE CHAIN
REMARK 500 6 ARG B 102 0.24 SIDE CHAIN
REMARK 500 6 ARG B 139 0.21 SIDE CHAIN
REMARK 500 7 ARG A 37 0.32 SIDE CHAIN
REMARK 500 7 ARG A 102 0.24 SIDE CHAIN
REMARK 500 7 ARG A 139 0.31 SIDE CHAIN
REMARK 500 7 ARG B 37 0.27 SIDE CHAIN
REMARK 500 7 ARG B 102 0.19 SIDE CHAIN
REMARK 500 7 ARG B 139 0.31 SIDE CHAIN
REMARK 500 8 ARG A 37 0.20 SIDE CHAIN
REMARK 500 8 ARG A 102 0.32 SIDE CHAIN
REMARK 500 8 ARG A 139 0.31 SIDE CHAIN
REMARK 500 8 ARG B 37 0.30 SIDE CHAIN
REMARK 500 8 ARG B 102 0.28 SIDE CHAIN
REMARK 500 8 ARG B 139 0.31 SIDE CHAIN
REMARK 500 9 ARG A 37 0.29 SIDE CHAIN
REMARK 500 9 ARG A 102 0.23 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 120 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1I4V A 25 139 UNP P04153 UMUD_ECOLI 25 139
DBREF 1I4V B 25 139 UNP P04153 UMUD_ECOLI 25 139
SEQADV 1I4V ALA A 25 UNP P04153 GLY 25 ENGINEERED MUTATION
SEQADV 1I4V ALA B 25 UNP P04153 GLY 25 ENGINEERED MUTATION
SEQRES 1 A 115 ALA PHE PRO SER PRO ALA ALA ASP TYR VAL GLU GLN ARG
SEQRES 2 A 115 ILE ASP LEU ASN GLN LEU LEU ILE GLN HIS PRO SER ALA
SEQRES 3 A 115 THR TYR PHE VAL LYS ALA SER GLY ASP SER MET ILE ASP
SEQRES 4 A 115 GLY GLY ILE SER ASP GLY ASP LEU LEU ILE VAL ASP SER
SEQRES 5 A 115 ALA ILE THR ALA SER HIS GLY ASP ILE VAL ILE ALA ALA
SEQRES 6 A 115 VAL ASP GLY GLU PHE THR VAL LYS LYS LEU GLN LEU ARG
SEQRES 7 A 115 PRO THR VAL GLN LEU ILE PRO MET ASN SER ALA TYR SER
SEQRES 8 A 115 PRO ILE THR ILE SER SER GLU ASP THR LEU ASP VAL PHE
SEQRES 9 A 115 GLY VAL VAL ILE HIS VAL VAL LYS ALA MET ARG
SEQRES 1 B 115 ALA PHE PRO SER PRO ALA ALA ASP TYR VAL GLU GLN ARG
SEQRES 2 B 115 ILE ASP LEU ASN GLN LEU LEU ILE GLN HIS PRO SER ALA
SEQRES 3 B 115 THR TYR PHE VAL LYS ALA SER GLY ASP SER MET ILE ASP
SEQRES 4 B 115 GLY GLY ILE SER ASP GLY ASP LEU LEU ILE VAL ASP SER
SEQRES 5 B 115 ALA ILE THR ALA SER HIS GLY ASP ILE VAL ILE ALA ALA
SEQRES 6 B 115 VAL ASP GLY GLU PHE THR VAL LYS LYS LEU GLN LEU ARG
SEQRES 7 B 115 PRO THR VAL GLN LEU ILE PRO MET ASN SER ALA TYR SER
SEQRES 8 B 115 PRO ILE THR ILE SER SER GLU ASP THR LEU ASP VAL PHE
SEQRES 9 B 115 GLY VAL VAL ILE HIS VAL VAL LYS ALA MET ARG
HELIX 1 1 ASP A 39 ILE A 45 1 7
HELIX 2 2 ASP B 39 ILE B 45 1 7
SHEET 1 A 6 TYR A 52 ALA A 56 0
SHEET 2 A 6 ASP A 70 SER A 76 -1 O ASP A 70 N ALA A 56
SHEET 3 A 6 GLY A 129 LYS A 136 -1 N VAL A 130 O ASP A 75
SHEET 4 A 6 GLY B 129 LYS B 136 -1 O VAL B 134 N LYS A 136
SHEET 5 A 6 ASP B 70 SER B 76 -1 O LEU B 71 N VAL B 135
SHEET 6 A 6 TYR B 52 ALA B 56 -1 N TYR B 52 O VAL B 74
SHEET 1 B 3 THR A 95 LYS A 97 0
SHEET 2 B 3 VAL A 86 ALA A 89 -1 O VAL A 86 N LYS A 97
SHEET 3 B 3 ASP A 126 VAL A 127 -1 O ASP A 126 N ALA A 89
SHEET 1 C 2 GLN A 106 LEU A 107 0
SHEET 2 C 2 ILE A 117 THR A 118 -1 O ILE A 117 N LEU A 107
SHEET 1 D 3 THR B 95 LYS B 97 0
SHEET 2 D 3 VAL B 86 ALA B 89 -1 O VAL B 86 N LYS B 97
SHEET 3 D 3 ASP B 126 VAL B 127 -1 O ASP B 126 N ALA B 89
SHEET 1 E 2 GLN B 106 LEU B 107 0
SHEET 2 E 2 ILE B 117 THR B 118 -1 O ILE B 117 N LEU B 107
CRYST1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - t 27 2 Bytes