Header list of 1ks6.pdb file
Complete list - b 23 2 Bytes
HEADER HORMONE/GROWTH FACTOR 10-JAN-02 1KS6 TITLE TRANSFORMING GROWTH FACTOR BETA TYPE II RECEPTOR LIGAND BINDING DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRANSFORMING GROWTH FACTOR BETA TYPE II RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN, SEQUENCE DATABASE RESIDUES 34-142; COMPND 5 SYNONYM: TGFB TYPE II RECEPTOR; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS; SOURCE 3 ORGANISM_COMMON: CHICKEN; SOURCE 4 ORGANISM_TAXID: 9031; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-32 KEYWDS THREE FINGER TOXIN FOLD, HORMONE-GROWTH FACTOR COMPLEX EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.S.MARLOW,C.B.BROWN,J.V.BARNETT,A.M.KREZEL REVDAT 3 23-FEB-22 1KS6 1 REMARK REVDAT 2 24-FEB-09 1KS6 1 VERSN REVDAT 1 25-FEB-03 1KS6 0 JRNL AUTH M.S.MARLOW,C.B.BROWN,J.V.BARNETT,A.M.KREZEL JRNL TITL SOLUTION STRUCTURE OF THE CHICK TGFB TYPE II RECEPTOR LIGAND JRNL TITL 2 BINDING DOMAIN JRNL REF J.MOL.BIOL. V. 326 989 2003 JRNL REFN ISSN 0022-2836 JRNL PMID 12589747 JRNL DOI 10.1016/S0022-2836(03)00023-8 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5 REMARK 3 AUTHORS : GUENTERT (DYANA), GUENTERT (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1KS6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-02. REMARK 100 THE DEPOSITION ID IS D_1000015286. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 1 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1-2MM TBRII NATURAL ABUNDANCE; 1 REMARK 210 -2MM TBRII U-15N,13C; 1-2MM REMARK 210 TBRII U-15N,13C REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 3D_13C- REMARK 210 SEPARATED_NOESY; HNCA-J REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER 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 : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 6 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 ASN A 46 H ASN A 49 1.41 REMARK 500 H ARG A 45 O LEU A 87 1.47 REMARK 500 H MET A 78 O ILE A 103 1.49 REMARK 500 H THR A 14 O VAL A 50 1.50 REMARK 500 O LEU A 63 H HIS A 66 1.55 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 3 -123.90 -72.29 REMARK 500 1 ASN A 25 -1.37 73.48 REMARK 500 1 ASN A 27 37.94 -142.92 REMARK 500 1 ASN A 35 -178.43 167.19 REMARK 500 1 GLU A 37 155.91 -42.85 REMARK 500 1 ASP A 47 -98.80 42.62 REMARK 500 1 PRO A 59 31.35 -72.35 REMARK 500 1 ASP A 70 24.15 170.07 REMARK 500 1 LYS A 82 103.71 -54.36 REMARK 500 1 CYS A 93 134.92 -175.56 REMARK 500 1 GLU A 97 -2.73 56.03 REMARK 500 1 ALA A 106 -71.35 -62.53 REMARK 500 2 PRO A 3 -139.96 -72.44 REMARK 500 2 ASN A 18 66.83 -66.16 REMARK 500 2 ASN A 25 -10.23 73.60 REMARK 500 2 ASN A 35 176.10 177.43 REMARK 500 2 GLU A 37 163.33 -46.83 REMARK 500 2 ASP A 47 -99.29 42.13 REMARK 500 2 ASP A 70 46.70 78.97 REMARK 500 2 LYS A 82 102.87 -53.03 REMARK 500 2 CYS A 93 136.58 -179.48 REMARK 500 2 GLU A 97 22.58 42.26 REMARK 500 2 ALA A 106 28.05 -74.63 REMARK 500 3 ASN A 18 65.40 -66.51 REMARK 500 3 CYS A 32 60.51 -111.87 REMARK 500 3 ASN A 35 -35.72 66.61 REMARK 500 3 ASP A 47 -98.94 41.55 REMARK 500 3 PRO A 59 20.44 -72.44 REMARK 500 3 ASP A 70 28.11 166.81 REMARK 500 3 LYS A 82 102.03 -54.49 REMARK 500 3 CYS A 93 136.27 171.03 REMARK 500 3 GLU A 97 -5.99 57.03 REMARK 500 3 ALA A 106 -71.12 -84.88 REMARK 500 4 CYS A 32 25.49 -150.54 REMARK 500 4 ASN A 35 22.98 41.95 REMARK 500 4 GLU A 37 -171.34 174.35 REMARK 500 4 ASP A 47 -98.99 41.86 REMARK 500 4 PRO A 59 28.39 -72.42 REMARK 500 4 ASP A 70 58.88 179.14 REMARK 500 4 LYS A 82 103.69 -54.03 REMARK 500 4 CYS A 93 138.74 176.24 REMARK 500 4 GLU A 97 -0.09 54.83 REMARK 500 4 ALA A 106 44.07 -97.07 REMARK 500 5 LEU A 2 165.52 61.99 REMARK 500 5 PRO A 3 -112.43 -72.38 REMARK 500 5 PHE A 8 76.68 -109.95 REMARK 500 5 ALA A 13 108.63 -51.72 REMARK 500 5 ASN A 18 67.08 -65.44 REMARK 500 5 ASN A 25 -4.18 72.99 REMARK 500 5 ASN A 27 30.87 -145.90 REMARK 500 REMARK 500 THIS ENTRY HAS 241 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1KS6 A 1 107 UNP Q90999 Q90999_CHICK 36 142 SEQADV 1KS6 THR A 23 UNP Q90999 LYS 58 SEE REMARK 999 SEQRES 1 A 107 GLN LEU PRO ARG LEU CYS LYS PHE CYS ASP VAL LYS ALA SEQRES 2 A 107 THR THR CYS SER ASN GLN ASP GLN CYS THR SER ASN CYS SEQRES 3 A 107 ASN ILE THR SER ILE CYS GLU LYS ASN ASN GLU VAL CYS SEQRES 4 A 107 ALA ALA VAL TRP ARG ARG ASN ASP GLU ASN VAL THR LEU SEQRES 5 A 107 GLU THR ILE CYS HIS ASP PRO GLN LYS ARG LEU TYR GLY SEQRES 6 A 107 HIS MET LEU ASP ASP SER SER SER GLU GLN CYS VAL MET SEQRES 7 A 107 LYS GLU LYS LYS ASP ASP GLY GLY LEU MET PHE MET CYS SEQRES 8 A 107 SER CYS THR GLY GLU GLU CYS ASN ASP VAL LEU ILE PHE SEQRES 9 A 107 SER ALA ILE HELIX 1 1 ARG A 62 HIS A 66 5 5 SHEET 1 A 2 LEU A 5 CYS A 6 0 SHEET 2 A 2 SER A 30 ILE A 31 -1 O SER A 30 N CYS A 6 SHEET 1 B 5 CYS A 9 ALA A 13 0 SHEET 2 B 5 ASN A 49 ILE A 55 -1 O THR A 54 N CYS A 9 SHEET 3 B 5 CYS A 39 ASN A 46 -1 N ASN A 46 O ASN A 49 SHEET 4 B 5 LEU A 87 CYS A 93 -1 O LEU A 87 N ARG A 45 SHEET 5 B 5 LYS A 79 LYS A 81 -1 N LYS A 81 O MET A 88 SSBOND 1 CYS A 6 CYS A 39 1555 1555 1.89 SSBOND 2 CYS A 9 CYS A 26 1555 1555 1.91 SSBOND 3 CYS A 16 CYS A 22 1555 1555 2.15 SSBOND 4 CYS A 32 CYS A 56 1555 1555 1.86 SSBOND 5 CYS A 76 CYS A 91 1555 1555 2.10 SSBOND 6 CYS A 93 CYS A 98 1555 1555 2.14 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