Header list of 1dd2.pdb file
Complete list - b 16 2 Bytes
HEADER TRANSFERASE 06-NOV-99 1DD2
TITLE BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCARBOXYLASE 1.3S SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.1.3.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PROPIONIBACTERIUM FREUDENREICHII SUBSP.
SOURCE 3 SHERMANII;
SOURCE 4 ORGANISM_TAXID: 1752;
SOURCE 5 STRAIN: SUBSP. SHERMANII;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HB101;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET20B
KEYWDS ANTIPARALLEL BETA SHEET, HAMMERHEAD, BIOCYTIN, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 32
MDLTYP MINIMIZED AVERAGE
AUTHOR D.V.REDDY,B.C.SHENOY,P.R.CAREY,F.D.SONNICHSEN
REVDAT 4 16-FEB-22 1DD2 1 REMARK
REVDAT 3 24-FEB-09 1DD2 1 VERSN
REVDAT 2 01-APR-03 1DD2 1 JRNL
REVDAT 1 24-MAR-00 1DD2 0
JRNL AUTH D.V.REDDY,B.C.SHENOY,P.R.CAREY,F.D.SONNICHSEN
JRNL TITL HIGH RESOLUTION SOLUTION STRUCTURE OF THE 1.3S SUBUNIT OF
JRNL TITL 2 TRANSCARBOXYLASE FROM PROPIONIBACTERIUM SHERMANII.
JRNL REF BIOCHEMISTRY V. 39 2509 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10704200
JRNL DOI 10.1021/BI9925367
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.V.REDDY,S.ROTHEMUND,B.C.SHENOY,P.R.CAREY,F.D.SONNICHSEN
REMARK 1 TITL STRUCTURAL CHARACTERIZATION OF THE ENTIRE 1.3S SUBUNIT OF
REMARK 1 TITL 2 TRANSCARBOXYLASE FROM PROPIONIBACTERIUM SHERMANII
REMARK 1 REF PROTEIN SCI. V. 7 2156 1998
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.V.REDDY,B.C.SHENOY,P.R.CAREY,F.D.SONNICHSEN
REMARK 1 TITL ABSENCE OF OBSERVABLE BIOTIN-PROTEIN INTERACTIONS IN THE
REMARK 1 TITL 2 1.3S SUBUNIT OF TRANSCARBOXYLASE: AN NMR STUDY
REMARK 1 REF BIOCHEMISTRY V. 36 14676 1997
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI971674Y
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE SGI6X.M4, X-PLOR 3.81
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), BRUENGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DG_SUB_EMBED, DGSA, REFINE WITH DIRECT
REMARK 3 J-REFINEMENT
REMARK 4
REMARK 4 1DD2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1000009983.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 20
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2 MM PROTEIN, N15/C13 LABELED TC
REMARK 210 1.3S 1-123, BIOTIN (UNLABELED)
REMARK 210 COVALENTLY ATTACHED TO LYS 89; 2
REMARK 210 MM PROTEIN, N15/C13 LABELED TC
REMARK 210 1.3S 1-123, BIOTIN (UNLABELED)
REMARK 210 COVALENTLY ATTACHED TO LYS 89;
REMARK 210 2MM PROTEIN, N15 LABELED, TC
REMARK 210 1.3S 1-123, BIOTIN (UNLABELED)
REMARK 210 COVALENTLY ATTACHED TO LYS 89
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; 4D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PIPP 3.7.3, X-PLOR 3.81
REMARK 210 METHOD USED : DISTANCE GEOMETRY/SIMULATED
REMARK 210 ANNEALING HYBRID METHOD
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 32
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1DCZ
REMARK 210
REMARK 210 REMARK: BIOTIN ATTACHED TO LYS 89 WAS OMITTED FROM COORDINATES.
REMARK 210 RESIDUES 1-46 APPEARED UNSTRUCTURED, OMITTED FROM CALCULATIONS
REMARK 210 AND COORDINATES.
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: 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 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 GLU A 54 52.27 -90.32
REMARK 500 1 GLU A 72 98.60 -61.22
REMARK 500 1 ALA A 78 92.90 -59.11
REMARK 500 1 LEU A 106 30.37 -90.29
REMARK 500 2 LYS A 51 40.73 -99.24
REMARK 500 2 GLU A 54 33.39 -165.53
REMARK 500 3 ALA A 49 37.31 -149.75
REMARK 500 3 GLU A 72 102.29 -57.05
REMARK 500 3 ALA A 78 90.48 -62.34
REMARK 500 4 ALA A 49 -70.10 -117.45
REMARK 500 4 LYS A 51 40.37 -163.71
REMARK 500 4 GLU A 72 95.53 -58.21
REMARK 500 4 ALA A 78 88.62 -62.39
REMARK 500 5 GLU A 54 52.01 -92.23
REMARK 500 5 ALA A 62 81.91 -67.77
REMARK 500 5 GLU A 72 104.95 -56.96
REMARK 500 5 ALA A 78 92.02 -60.52
REMARK 500 6 ALA A 49 -59.03 -121.20
REMARK 500 6 GLU A 54 -82.37 -61.92
REMARK 500 6 GLU A 72 101.74 -58.42
REMARK 500 6 ALA A 78 97.97 -60.94
REMARK 500 7 GLU A 72 97.00 -62.36
REMARK 500 7 ALA A 78 96.51 -58.84
REMARK 500 8 LYS A 51 40.05 -143.61
REMARK 500 8 LEU A 106 30.24 -90.27
REMARK 500 9 ALA A 49 110.17 60.91
REMARK 500 9 GLU A 72 101.52 -59.33
REMARK 500 10 GLU A 54 33.82 -167.52
REMARK 500 10 SER A 66 -61.63 -97.82
REMARK 500 10 GLU A 72 95.05 -60.34
REMARK 500 10 ALA A 78 102.04 -58.50
REMARK 500 11 ALA A 49 161.99 60.62
REMARK 500 11 GLU A 54 -149.85 -63.72
REMARK 500 11 GLU A 72 90.29 -60.78
REMARK 500 11 ALA A 78 100.25 -56.11
REMARK 500 12 ALA A 49 89.25 -162.21
REMARK 500 12 SER A 66 -62.00 -98.67
REMARK 500 12 GLU A 72 108.64 -54.61
REMARK 500 13 ALA A 49 116.86 -176.75
REMARK 500 13 LYS A 51 40.74 -160.88
REMARK 500 13 GLU A 72 96.60 -60.94
REMARK 500 13 ALA A 78 93.46 -59.84
REMARK 500 14 GLU A 54 101.60 59.20
REMARK 500 14 GLU A 72 102.59 -59.64
REMARK 500 14 ALA A 78 93.14 -59.16
REMARK 500 15 ALA A 49 95.68 60.69
REMARK 500 15 VAL A 65 117.75 63.15
REMARK 500 15 GLU A 72 99.66 -60.07
REMARK 500 16 LYS A 51 41.96 -141.93
REMARK 500 16 GLU A 72 99.08 -61.87
REMARK 500
REMARK 500 THIS ENTRY HAS 111 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 110 0.31 SIDE CHAIN
REMARK 500 2 ARG A 110 0.30 SIDE CHAIN
REMARK 500 3 ARG A 110 0.31 SIDE CHAIN
REMARK 500 4 ARG A 110 0.31 SIDE CHAIN
REMARK 500 5 ARG A 110 0.25 SIDE CHAIN
REMARK 500 6 ARG A 110 0.30 SIDE CHAIN
REMARK 500 7 ARG A 110 0.22 SIDE CHAIN
REMARK 500 8 ARG A 110 0.23 SIDE CHAIN
REMARK 500 9 ARG A 110 0.31 SIDE CHAIN
REMARK 500 10 ARG A 110 0.24 SIDE CHAIN
REMARK 500 11 ARG A 110 0.31 SIDE CHAIN
REMARK 500 12 ARG A 110 0.22 SIDE CHAIN
REMARK 500 13 ARG A 110 0.22 SIDE CHAIN
REMARK 500 14 ARG A 110 0.30 SIDE CHAIN
REMARK 500 15 ARG A 110 0.30 SIDE CHAIN
REMARK 500 16 ARG A 110 0.25 SIDE CHAIN
REMARK 500 17 ARG A 110 0.23 SIDE CHAIN
REMARK 500 18 ARG A 110 0.24 SIDE CHAIN
REMARK 500 19 ARG A 110 0.27 SIDE CHAIN
REMARK 500 20 ARG A 110 0.28 SIDE CHAIN
REMARK 500 21 ARG A 110 0.26 SIDE CHAIN
REMARK 500 22 ARG A 110 0.23 SIDE CHAIN
REMARK 500 23 ARG A 110 0.30 SIDE CHAIN
REMARK 500 24 ARG A 110 0.31 SIDE CHAIN
REMARK 500 25 ARG A 110 0.21 SIDE CHAIN
REMARK 500 26 ARG A 110 0.21 SIDE CHAIN
REMARK 500 27 ARG A 110 0.22 SIDE CHAIN
REMARK 500 28 ARG A 110 0.28 SIDE CHAIN
REMARK 500 29 ARG A 110 0.30 SIDE CHAIN
REMARK 500 30 ARG A 110 0.23 SIDE CHAIN
REMARK 500 31 ARG A 110 0.30 SIDE CHAIN
REMARK 500 32 ARG A 110 0.25 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DCZ RELATED DB: PDB
REMARK 900 MINIMIZED AVERAGE STRUCTURE
DBREF 1DD2 A 47 123 UNP P02904 BCCP_PROFR 47 123
SEQRES 1 A 77 ALA GLY ALA GLY LYS ALA GLY GLU GLY GLU ILE PRO ALA
SEQRES 2 A 77 PRO LEU ALA GLY THR VAL SER LYS ILE LEU VAL LYS GLU
SEQRES 3 A 77 GLY ASP THR VAL LYS ALA GLY GLN THR VAL LEU VAL LEU
SEQRES 4 A 77 GLU ALA MET LYS MET GLU THR GLU ILE ASN ALA PRO THR
SEQRES 5 A 77 ASP GLY LYS VAL GLU LYS VAL LEU VAL LYS GLU ARG ASP
SEQRES 6 A 77 ALA VAL GLN GLY GLY GLN GLY LEU ILE LYS ILE GLY
SHEET 1 A 4 GLU A 56 PRO A 58 0
SHEET 2 A 4 GLY A 118 ILE A 122 -1 N LEU A 119 O ILE A 57
SHEET 3 A 4 GLY A 100 VAL A 105 -1 N GLU A 103 O LYS A 121
SHEET 4 A 4 THR A 75 VAL A 76 -1 N VAL A 76 O GLY A 100
SHEET 1 B 3 THR A 64 ILE A 68 0
SHEET 2 B 3 THR A 81 GLU A 86 -1 N VAL A 84 O LYS A 67
SHEET 3 B 3 GLU A 91 ASN A 95 -1 N THR A 92 O LEU A 85
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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 - b 16 2 Bytes