Header list of 1lq7.pdb file
Complete list - b 23 2 Bytes
HEADER DE NOVO PROTEIN 09-MAY-02 1LQ7
TITLE DE NOVO DESIGNED PROTEIN MODEL OF RADICAL ENZYMES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA3W;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: PROTEIN MODEL FOR TRYPTOPHANYL RADICAL
SOURCE MOL_ID: 1;
SOURCE 2 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 3 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET32;
SOURCE 7 OTHER_DETAILS: DE NOVO DESIGN/SYNTHETIC GENE: GENE GENERATED USING
SOURCE 8 OVERLAPPING PCR METHOD FROM SYNTHETIC OLIGOS
KEYWDS THREE HELIX BUNDLE, DE NOVO PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR Q.-H.DAI,C.TOMMOS,E.J.FUENTES,M.BLOMBERG,P.L.DUTTON,A.J.WAND
REVDAT 4 23-FEB-22 1LQ7 1 REMARK
REVDAT 3 24-FEB-09 1LQ7 1 VERSN
REVDAT 2 18-DEC-02 1LQ7 1 JRNL
REVDAT 1 05-JUN-02 1LQ7 0
JRNL AUTH Q.-H.DAI,C.TOMMOS,E.J.FUENTES,M.BLOMBERG,P.L.DUTTON,A.J.WAND
JRNL TITL STRUCTURE OF A DE NOVO DESIGNED PROTEIN MODEL OF RADICAL
JRNL TITL 2 ENZYMES
JRNL REF J.AM.CHEM.SOC. V. 124 10952 2002
JRNL REFN ISSN 0002-7863
JRNL PMID 12224922
JRNL DOI 10.1021/JA0264201
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.TOMMOS,J.J.SKALICKY,D.L.PILLOUD,A.J.WAND,P.L.DUTTON
REMARK 1 TITL DE NOVO PROTEINS AS MODELS OF RADICAL ENZYMES
REMARK 1 REF BIOCHEMISTRY V. 38 9495 1999
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI990609G
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : GNTERT, C. MUMENTHALER, K. WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1130 NOES, 43 PHI RESTRAINTS
REMARK 4
REMARK 4 1LQ7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-02.
REMARK 100 THE DEPOSITION ID IS D_1000016177.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 301; 301
REMARK 210 PH : 5.5; 5.5
REMARK 210 IONIC STRENGTH : 70 MM; 70 MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.85 MM U-15N,13C-A3W, 20 MM
REMARK 210 ACETATE, 50 MM KCL; 0.85 MM U-
REMARK 210 15N,13C-A3W, 20 MM ACETATE, 50
REMARK 210 MM KCL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 4D_13C
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST REFINEMENT FUNCTION
REMARK 210 PENALTY, BEST CHEMICAL SHIFT
REMARK 210 AGREEMENT
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 16
REMARK 210
REMARK 210 REMARK: NULL
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: 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 O ILE A 27 H LYS A 31 1.44
REMARK 500 O LEU A 60 H ILE A 64 1.54
REMARK 500 O GLU A 61 H LYS A 65 1.56
REMARK 500 O VAL A 4 H GLU A 8 1.58
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 ARG A 3 -59.28 69.36
REMARK 500 1 GLU A 8 -32.96 -36.59
REMARK 500 1 ARG A 26 -34.82 177.46
REMARK 500 1 GLU A 29 -73.68 -47.21
REMARK 500 1 LEU A 44 99.99 -43.48
REMARK 500 1 LYS A 51 -31.79 -37.58
REMARK 500 1 LEU A 60 -70.12 -74.74
REMARK 500 2 ARG A 3 -57.54 -127.90
REMARK 500 2 GLU A 8 -32.38 -37.43
REMARK 500 2 ARG A 26 -84.82 -62.10
REMARK 500 2 LEU A 44 102.96 -41.65
REMARK 500 2 GLU A 49 34.54 -90.38
REMARK 500 2 LYS A 51 -31.71 -37.44
REMARK 500 2 LEU A 60 -71.69 -73.52
REMARK 500 3 SER A 2 78.66 -100.61
REMARK 500 3 ARG A 3 -66.38 -148.08
REMARK 500 3 GLU A 8 -33.15 -35.73
REMARK 500 3 ARG A 26 -81.71 -63.35
REMARK 500 3 LEU A 44 99.58 -41.28
REMARK 500 3 GLU A 49 33.29 -91.95
REMARK 500 3 LYS A 51 -31.57 -37.88
REMARK 500 3 LEU A 60 -72.42 -68.85
REMARK 500 4 SER A 2 -53.67 179.48
REMARK 500 4 GLU A 8 -33.23 -36.49
REMARK 500 4 ARG A 26 -77.51 -102.76
REMARK 500 4 GLU A 29 -73.95 -44.43
REMARK 500 4 LEU A 44 105.72 -41.70
REMARK 500 4 GLU A 49 34.12 -92.89
REMARK 500 4 LYS A 51 -32.33 -37.29
REMARK 500 4 LEU A 60 -74.11 -72.07
REMARK 500 5 SER A 2 68.71 -178.62
REMARK 500 5 ARG A 3 -58.64 -146.90
REMARK 500 5 GLU A 8 -33.85 -36.81
REMARK 500 5 ARG A 26 -69.76 -143.68
REMARK 500 5 GLU A 29 -74.53 -46.35
REMARK 500 5 LEU A 44 101.55 -41.28
REMARK 500 5 GLU A 49 34.12 -90.58
REMARK 500 5 LYS A 51 -31.19 -37.95
REMARK 500 5 VAL A 53 -71.67 -41.39
REMARK 500 5 GLU A 54 -70.29 -38.13
REMARK 500 5 LEU A 60 -72.57 -73.20
REMARK 500 6 SER A 2 -61.08 71.31
REMARK 500 6 ARG A 3 -61.52 -98.04
REMARK 500 6 GLU A 8 -31.73 -37.81
REMARK 500 6 ARG A 26 -84.36 -166.28
REMARK 500 6 LEU A 44 99.25 -43.30
REMARK 500 6 GLU A 49 36.37 -94.38
REMARK 500 6 LYS A 51 -31.13 -37.84
REMARK 500 6 VAL A 53 -70.60 -41.92
REMARK 500 6 LEU A 60 -72.27 -78.76
REMARK 500
REMARK 500 THIS ENTRY HAS 140 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AN APPROPRIATE SEQUENCE DATABASE REFERENCE
REMARK 999 WAS NOT AVAILABLE AT THE TIME OF PROCESSING.
DBREF 1LQ7 A 1 67 PDB 1LQ7 1LQ7 1 67
SEQRES 1 A 67 GLY SER ARG VAL LYS ALA LEU GLU GLU LYS VAL LYS ALA
SEQRES 2 A 67 LEU GLU GLU LYS VAL LYS ALA LEU GLY GLY GLY GLY ARG
SEQRES 3 A 67 ILE GLU GLU LEU LYS LYS LYS TRP GLU GLU LEU LYS LYS
SEQRES 4 A 67 LYS ILE GLU GLU LEU GLY GLY GLY GLY GLU VAL LYS LYS
SEQRES 5 A 67 VAL GLU GLU GLU VAL LYS LYS LEU GLU GLU GLU ILE LYS
SEQRES 6 A 67 LYS LEU
HELIX 1 1 ARG A 3 LEU A 21 1 19
HELIX 2 2 ARG A 26 LEU A 44 1 19
HELIX 3 3 GLU A 49 LEU A 67 1 19
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 23 2 Bytes