Header list of 1wk1.pdb file
Complete list - r 2 2 Bytes
HEADER SUGAR BINDING PROTEIN 29-MAY-04 1WK1 TITLE SOLUTION STRUCTURE OF LECTIN C-TYPE DOMAIN DERIVED FROM A HYPOTHETICAL TITLE 2 PROTEIN FROM C. ELEGANS COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN YK1067A12; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: LECTIN C-TYPE HOMOLOGUE DOMAIN; COMPND 5 SYNONYM: WNT INHIBITORY FAMILY MEMBER; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS; SOURCE 3 ORGANISM_TAXID: 6239; SOURCE 4 GENE: NIG KOHARA SUGANO CLONE YK1067A12; SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 6 EXPRESSION_SYSTEM_PLASMID: P030929-39; SOURCE 7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS LECTIN C-TYPE DOMAIN, STRUCTURAL GENOMICS, RIKEN STRUCTURAL KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, SUGAR BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR N.KOBAYASHI,S.KOSHIBA,M.INOUE,N.TOCHIO,T.KIGAWA,S.YOKOYAMA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1WK1 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WK1 1 VERSN REVDAT 1 29-NOV-04 1WK1 0 JRNL AUTH N.KOBAYASHI,S.KOSHIBA,M.INOUE,N.TOCHIO,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF LECTIN C-TYPE DOMAIN DERIVED FROM A JRNL TITL 2 HYPOTHETICAL PROTEIN FROM C. ELEGANS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 2.0.17 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WK1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-MAY-04. REMARK 100 THE DEPOSITION ID IS D_1000023661. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.89MM LECTIN C-TYPE DOMAIN U REMARK 210 -13C,15N; 20MM PHOSPHATE BUFFER REMARK 210 NA (PH6.0); 100MM NACL; 1MM D- REMARK 210 DTT; 0.02% NAN3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.901, CYANA 2.0.17 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 : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, TARGET REMARK 210 FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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: 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 SER A 5 -57.79 -125.08 REMARK 500 1 ASP A 16 101.91 -34.47 REMARK 500 1 ASP A 37 70.13 -118.74 REMARK 500 1 ASP A 40 -70.37 -41.70 REMARK 500 1 ASP A 41 -26.82 -38.77 REMARK 500 1 SER A 47 -39.20 -39.97 REMARK 500 1 ALA A 51 94.68 -49.48 REMARK 500 1 LEU A 80 94.79 -63.30 REMARK 500 1 ASN A 89 101.42 -59.47 REMARK 500 1 SER A 107 102.15 -46.91 REMARK 500 1 HIS A 130 152.16 -48.99 REMARK 500 1 ARG A 131 36.61 -89.11 REMARK 500 1 ASP A 135 -59.33 -131.06 REMARK 500 1 ALA A 144 118.55 -35.14 REMARK 500 2 ASP A 16 106.64 -36.34 REMARK 500 2 SER A 48 -73.06 -57.98 REMARK 500 2 ALA A 51 97.11 -49.84 REMARK 500 2 ALA A 88 176.72 -56.91 REMARK 500 2 ASN A 94 47.63 -86.76 REMARK 500 2 SER A 107 102.84 -42.45 REMARK 500 2 ASP A 133 53.22 36.47 REMARK 500 2 PRO A 138 -176.77 -69.78 REMARK 500 2 THR A 140 40.39 36.59 REMARK 500 3 ASP A 16 102.26 -35.16 REMARK 500 3 SER A 48 -72.22 -54.92 REMARK 500 3 ALA A 51 103.57 -47.09 REMARK 500 3 LEU A 79 158.12 -41.22 REMARK 500 3 ALA A 88 176.28 -56.99 REMARK 500 3 ASN A 89 105.68 -57.26 REMARK 500 3 ASN A 94 40.74 -86.38 REMARK 500 3 SER A 107 108.61 -44.44 REMARK 500 3 ASP A 135 79.08 -102.80 REMARK 500 3 ASN A 139 30.22 70.54 REMARK 500 3 ILE A 141 116.35 -36.99 REMARK 500 3 ALA A 144 42.20 -98.14 REMARK 500 3 SER A 145 103.88 -55.77 REMARK 500 4 SER A 2 43.08 34.70 REMARK 500 4 ASP A 16 103.48 -39.64 REMARK 500 4 LEU A 34 142.31 -38.98 REMARK 500 4 ALA A 51 104.52 -55.66 REMARK 500 4 LEU A 80 93.56 -64.30 REMARK 500 4 ALA A 88 174.80 -49.97 REMARK 500 4 ASN A 89 109.02 -55.12 REMARK 500 4 ASN A 94 34.15 -86.36 REMARK 500 4 ARG A 131 47.09 34.94 REMARK 500 4 SER A 134 118.76 -172.17 REMARK 500 4 PRO A 138 -179.16 -69.80 REMARK 500 5 SER A 3 42.66 -96.13 REMARK 500 5 SER A 6 132.13 -173.76 REMARK 500 5 ASP A 16 102.32 -37.02 REMARK 500 REMARK 500 THIS ENTRY HAS 214 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: CEI001000012.1 RELATED DB: TARGETDB DBREF 1WK1 A 8 144 UNP Q19853 Q19853_CAEEL 1193 1329 SEQADV 1WK1 GLY A 1 UNP Q19853 CLONING ARTIFACT SEQADV 1WK1 SER A 2 UNP Q19853 CLONING ARTIFACT SEQADV 1WK1 SER A 3 UNP Q19853 CLONING ARTIFACT SEQADV 1WK1 GLY A 4 UNP Q19853 CLONING ARTIFACT SEQADV 1WK1 SER A 5 UNP Q19853 CLONING ARTIFACT SEQADV 1WK1 SER A 6 UNP Q19853 CLONING ARTIFACT SEQADV 1WK1 GLY A 7 UNP Q19853 CLONING ARTIFACT SEQADV 1WK1 SER A 145 UNP Q19853 CLONING ARTIFACT SEQADV 1WK1 GLY A 146 UNP Q19853 CLONING ARTIFACT SEQADV 1WK1 PRO A 147 UNP Q19853 CLONING ARTIFACT SEQADV 1WK1 SER A 148 UNP Q19853 CLONING ARTIFACT SEQADV 1WK1 SER A 149 UNP Q19853 CLONING ARTIFACT SEQADV 1WK1 GLY A 150 UNP Q19853 CLONING ARTIFACT SEQRES 1 A 150 GLY SER SER GLY SER SER GLY VAL LYS PHE LEU THR VAL SEQRES 2 A 150 ASN ASP ASP ILE LEU SER MET PRO GLN ALA ARG ASN PHE SEQRES 3 A 150 CYS ALA SER ALA GLY GLY TYR LEU ALA ASP ASP LEU GLY SEQRES 4 A 150 ASP ASP LYS ASN ASN PHE TYR SER SER ILE ALA ALA ASN SEQRES 5 A 150 THR GLN PHE TRP ILE GLY LEU PHE LYS ASN SER ASP GLY SEQRES 6 A 150 GLN PHE TYR TRP ASP ARG GLY GLN GLY ILE ASN PRO ASP SEQRES 7 A 150 LEU LEU ASN GLN PRO ILE THR TYR TRP ALA ASN GLY GLU SEQRES 8 A 150 PRO SER ASN ASP PRO THR ARG GLN CYS VAL TYR PHE ASP SEQRES 9 A 150 GLY ARG SER GLY ASP LYS SER LYS VAL TRP THR THR ASP SEQRES 10 A 150 THR CYS ALA THR PRO ARG PRO PHE ILE CYS GLN LYS HIS SEQRES 11 A 150 ARG TYR ASP SER ASP HIS LYS PRO ASN THR ILE GLY ASP SEQRES 12 A 150 ALA SER GLY PRO SER SER GLY HELIX 1 1 SER A 19 GLY A 31 1 13 HELIX 2 2 GLY A 39 ALA A 50 1 12 HELIX 3 3 ASP A 109 LYS A 112 5 4 SHEET 1 A 2 TYR A 33 LEU A 34 0 SHEET 2 A 2 CYS A 127 GLN A 128 -1 O GLN A 128 N TYR A 33 SHEET 1 B 5 ASP A 78 LEU A 79 0 SHEET 2 B 5 PHE A 67 TRP A 69 -1 N TRP A 69 O ASP A 78 SHEET 3 B 5 GLN A 54 LYS A 61 -1 N PHE A 60 O TYR A 68 SHEET 4 B 5 CYS A 100 ASP A 104 -1 O PHE A 103 N PHE A 55 SHEET 5 B 5 TRP A 114 ASP A 117 -1 O ASP A 117 N CYS A 100 SSBOND 1 CYS A 27 CYS A 127 1555 1555 2.00 SSBOND 2 CYS A 100 CYS A 119 1555 1555 2.03 CISPEP 1 GLU A 91 PRO A 92 1 -0.03 CISPEP 2 GLU A 91 PRO A 92 2 0.02 CISPEP 3 GLU A 91 PRO A 92 3 0.02 CISPEP 4 GLU A 91 PRO A 92 4 -0.09 CISPEP 5 GLU A 91 PRO A 92 5 -0.03 CISPEP 6 GLU A 91 PRO A 92 6 0.01 CISPEP 7 GLU A 91 PRO A 92 7 0.00 CISPEP 8 GLU A 91 PRO A 92 8 0.03 CISPEP 9 GLU A 91 PRO A 92 9 0.05 CISPEP 10 GLU A 91 PRO A 92 10 -0.03 CISPEP 11 GLU A 91 PRO A 92 11 0.01 CISPEP 12 GLU A 91 PRO A 92 12 -0.05 CISPEP 13 GLU A 91 PRO A 92 13 0.01 CISPEP 14 GLU A 91 PRO A 92 14 0.03 CISPEP 15 GLU A 91 PRO A 92 15 0.04 CISPEP 16 GLU A 91 PRO A 92 16 0.01 CISPEP 17 GLU A 91 PRO A 92 17 -0.05 CISPEP 18 GLU A 91 PRO A 92 18 0.06 CISPEP 19 GLU A 91 PRO A 92 19 -0.06 CISPEP 20 GLU A 91 PRO A 92 20 -0.07 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 - r 2 2 Bytes