Header list of 1va9.pdb file
Complete list - r 2 2 Bytes
HEADER CELL ADHESION 13-FEB-04 1VA9 TITLE SOLUTION STRUCTURE OF THE SECOND FNIII DOMAIN OF DSCAML1 PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: DOWN SYNDROME CELL ADHESION MOLECULE LIKE-PROTEIN 1B; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FNIII DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: KAZUSA CDNA KIAA1132; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030623-12; SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS KEYWDS FNIII DOMAIN, DSCAML1 PROTEIN, STRUCTURAL GENOMICS, RIKEN STRUCTURAL KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, CELL ADHESION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR X.-R.QIN,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS AUTHOR 2 INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1VA9 1 REMARK SEQADV REVDAT 2 24-FEB-09 1VA9 1 VERSN REVDAT 1 22-FEB-05 1VA9 0 JRNL AUTH X.-R.QIN,F.HAYASHI,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE SECOND FNIII DOMAIN OF DSCAML1 JRNL TITL 2 PROTEIN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1C, CYANA 1.0.7 REMARK 3 AUTHORS : VARIAN (VNMR), GUENTERT,P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1VA9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-FEB-04. REMARK 100 THE DEPOSITION ID IS D_1000006402. 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 : 1.05MM 13C,15N-LABELED PROTEIN; REMARK 210 20MM PINA(PH6.0); 100MM NACL; REMARK 210 D10-DTT; 0.02% NAN3; 90% H2O; 10% REMARK 210 D2O 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 : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.854, CYANA 1.0.7 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 : NULL 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: 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 GLN A 25 H GLN A 33 1.49 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 SER A 2 -57.82 -129.07 REMARK 500 1 SER A 9 100.87 -177.16 REMARK 500 1 GLU A 11 126.24 -179.11 REMARK 500 1 THR A 28 -144.15 -121.20 REMARK 500 1 LYS A 40 -170.63 46.86 REMARK 500 1 GLN A 44 -31.36 -38.50 REMARK 500 1 GLU A 57 157.75 -47.40 REMARK 500 1 PHE A 88 63.58 38.30 REMARK 500 1 ALA A 112 99.13 177.85 REMARK 500 1 THR A 114 157.75 -49.41 REMARK 500 1 LEU A 115 171.35 -54.10 REMARK 500 1 SER A 121 96.91 -64.16 REMARK 500 2 SER A 2 116.67 -165.68 REMARK 500 2 SER A 3 173.20 57.25 REMARK 500 2 SER A 5 89.70 -154.17 REMARK 500 2 SER A 6 136.09 175.00 REMARK 500 2 THR A 10 -144.93 -98.66 REMARK 500 2 ALA A 14 163.49 -48.56 REMARK 500 2 GLN A 25 118.07 -164.86 REMARK 500 2 THR A 28 -154.04 -120.21 REMARK 500 2 LYS A 40 139.65 -37.94 REMARK 500 2 VAL A 47 -178.93 -53.92 REMARK 500 2 ASN A 58 37.09 -93.74 REMARK 500 2 ASN A 63 57.08 39.25 REMARK 500 2 TYR A 66 115.89 -38.96 REMARK 500 2 ASN A 84 65.84 62.59 REMARK 500 2 ALA A 112 77.53 -179.03 REMARK 500 2 SER A 117 93.01 61.82 REMARK 500 2 SER A 120 -61.40 -141.89 REMARK 500 3 SER A 6 -59.82 -139.13 REMARK 500 3 SER A 9 111.93 -173.84 REMARK 500 3 THR A 10 -141.97 -84.71 REMARK 500 3 GLU A 11 30.16 -94.99 REMARK 500 3 GLU A 12 168.22 54.31 REMARK 500 3 ALA A 14 151.80 -47.00 REMARK 500 3 ASP A 16 46.91 -93.64 REMARK 500 3 THR A 28 -164.32 -117.58 REMARK 500 3 LYS A 40 -169.61 45.66 REMARK 500 3 GLU A 42 33.29 -91.46 REMARK 500 3 LEU A 43 -44.96 -130.33 REMARK 500 3 GLN A 44 -38.51 -36.75 REMARK 500 3 ASN A 58 46.67 -87.20 REMARK 500 3 PHE A 88 66.61 39.99 REMARK 500 3 ALA A 112 96.05 -171.99 REMARK 500 3 THR A 114 155.74 -46.94 REMARK 500 3 LEU A 115 175.99 -48.71 REMARK 500 3 SER A 117 123.23 63.51 REMARK 500 3 SER A 120 90.72 40.35 REMARK 500 4 ILE A 8 113.47 64.93 REMARK 500 4 SER A 9 90.54 -167.29 REMARK 500 REMARK 500 THIS ENTRY HAS 326 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSK002101106 RELATED DB: TARGETDB DBREF 1VA9 A 8 116 UNP Q8TD84 DSCL1_HUMAN 768 876 SEQADV 1VA9 GLY A 1 UNP Q8TD84 CLONING ARTIFACT SEQADV 1VA9 SER A 2 UNP Q8TD84 CLONING ARTIFACT SEQADV 1VA9 SER A 3 UNP Q8TD84 CLONING ARTIFACT SEQADV 1VA9 GLY A 4 UNP Q8TD84 CLONING ARTIFACT SEQADV 1VA9 SER A 5 UNP Q8TD84 CLONING ARTIFACT SEQADV 1VA9 SER A 6 UNP Q8TD84 CLONING ARTIFACT SEQADV 1VA9 GLY A 7 UNP Q8TD84 CLONING ARTIFACT SEQADV 1VA9 SER A 117 UNP Q8TD84 CLONING ARTIFACT SEQADV 1VA9 GLY A 118 UNP Q8TD84 CLONING ARTIFACT SEQADV 1VA9 PRO A 119 UNP Q8TD84 CLONING ARTIFACT SEQADV 1VA9 SER A 120 UNP Q8TD84 CLONING ARTIFACT SEQADV 1VA9 SER A 121 UNP Q8TD84 CLONING ARTIFACT SEQADV 1VA9 GLY A 122 UNP Q8TD84 CLONING ARTIFACT SEQRES 1 A 122 GLY SER SER GLY SER SER GLY ILE SER THR GLU GLU ALA SEQRES 2 A 122 ALA PRO ASP GLY PRO PRO MET ASP VAL THR LEU GLN PRO SEQRES 3 A 122 VAL THR SER GLN SER ILE GLN VAL THR TRP LYS ALA PRO SEQRES 4 A 122 LYS LYS GLU LEU GLN ASN GLY VAL ILE ARG GLY TYR GLN SEQRES 5 A 122 ILE GLY TYR ARG GLU ASN SER PRO GLY SER ASN GLY GLN SEQRES 6 A 122 TYR SER ILE VAL GLU MET LYS ALA THR GLY ASP SER GLU SEQRES 7 A 122 VAL TYR THR LEU ASP ASN LEU LYS LYS PHE ALA GLN TYR SEQRES 8 A 122 GLY VAL VAL VAL GLN ALA PHE ASN ARG ALA GLY THR GLY SEQRES 9 A 122 PRO SER SER SER GLU ILE ASN ALA THR THR LEU GLU SER SEQRES 10 A 122 GLY PRO SER SER GLY SHEET 1 A 3 MET A 20 PRO A 26 0 SHEET 2 A 3 SER A 31 LYS A 37 -1 O GLN A 33 N GLN A 25 SHEET 3 A 3 SER A 77 ASP A 83 -1 O LEU A 82 N ILE A 32 SHEET 1 B 3 GLY A 50 GLU A 57 0 SHEET 2 B 3 TYR A 91 ASN A 99 -1 O GLN A 96 N GLN A 52 SHEET 3 B 3 GLY A 102 THR A 103 -1 O GLY A 102 N ASN A 99 SHEET 1 C 3 GLY A 50 GLU A 57 0 SHEET 2 C 3 TYR A 91 ASN A 99 -1 O GLN A 96 N GLN A 52 SHEET 3 C 3 ILE A 110 ASN A 111 -1 O ILE A 110 N VAL A 93 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