Header list of 1x5d.pdb file
Complete list - r 2 2 Bytes
HEADER ISOMERASE 15-MAY-05 1X5D TITLE THE SOLUTION STRUCTURE OF THE SECOND THIOREDOXIN-LIKE DOMAIN OF HUMAN TITLE 2 PROTEIN DISULFIDE-ISOMERASE A6 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN DISULFIDE-ISOMERASE A6; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: THIOREDOXIN LIKE DOMAIN; COMPND 5 SYNONYM: PROTEIN DISULFIDE ISOMERASE P5, THIOREDOXIN DOMAIN COMPND 6 CONTAINING PROTEIN 7; COMPND 7 EC: 5.3.4.1; COMPND 8 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: PDIA6; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040628-10; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS PDIA6, ERP5, P5, TXNDC7, THIOREDOXIN LIKE DOMAIN, REDOX, STRUCTURAL KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS KEYWDS 4 INITIATIVE, RSGI, ISOMERASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1X5D 1 REMARK SEQADV REVDAT 2 24-FEB-09 1X5D 1 VERSN REVDAT 1 15-NOV-05 1X5D 0 JRNL AUTH N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA JRNL TITL THE SOLUTION STRUCTURE OF THE SECOND THIOREDOXIN-LIKE DOMAIN JRNL TITL 2 OF HUMAN PROTEIN DISULFIDE-ISOMERASE A6 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), GUNTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1X5D COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000024399. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 296 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.1MM THIOREDOXIN LIKE DOMAIN U REMARK 210 -15N,13C; 20MM D-TRIS HCL; 100MM REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 10% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C 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 20031121, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.9049, 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 : TARGET FUNCTION,STRUCTURES WITH REMARK 210 THE LEAST RESTRAINT VIOLATIONS 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 6 149.74 -174.74 REMARK 500 1 GLU A 25 34.43 -92.51 REMARK 500 1 ARG A 105 -37.51 -34.47 REMARK 500 1 ALA A 112 -38.13 -39.65 REMARK 500 1 ASN A 119 -72.49 -83.83 REMARK 500 1 PRO A 123 85.90 -69.77 REMARK 500 1 GLU A 124 117.51 -171.11 REMARK 500 1 LEU A 125 142.20 -34.12 REMARK 500 1 GLU A 127 151.46 -47.46 REMARK 500 1 SER A 132 43.70 39.26 REMARK 500 2 SER A 6 35.74 -91.81 REMARK 500 2 ASP A 8 -29.67 -39.23 REMARK 500 2 VAL A 21 -63.43 -97.34 REMARK 500 2 ARG A 105 -33.01 -35.87 REMARK 500 2 ALA A 112 -35.46 -39.61 REMARK 500 2 ASN A 119 -74.77 -87.91 REMARK 500 2 GLU A 124 92.29 -68.55 REMARK 500 3 SER A 5 -52.40 -120.96 REMARK 500 3 VAL A 21 -63.62 -103.04 REMARK 500 3 ARG A 105 -33.12 -35.40 REMARK 500 3 ALA A 112 -39.40 -34.12 REMARK 500 3 ASN A 119 -73.06 -34.70 REMARK 500 3 GLU A 124 93.17 -47.51 REMARK 500 3 SER A 131 38.97 72.61 REMARK 500 4 SER A 6 116.13 -174.84 REMARK 500 4 ARG A 105 -33.66 -34.63 REMARK 500 4 ASN A 119 -75.08 -96.00 REMARK 500 5 SER A 3 91.45 -59.00 REMARK 500 5 ARG A 103 32.91 -84.52 REMARK 500 5 ARG A 105 -35.19 -38.60 REMARK 500 5 ASN A 119 -74.92 -48.23 REMARK 500 5 PRO A 123 -173.43 -69.79 REMARK 500 6 VAL A 21 -60.08 -104.54 REMARK 500 6 LYS A 61 -74.71 -61.21 REMARK 500 6 ARG A 103 48.56 -78.26 REMARK 500 6 ARG A 105 -37.34 -37.09 REMARK 500 6 ASN A 119 -74.97 -106.82 REMARK 500 7 SER A 5 42.91 -92.58 REMARK 500 7 GLU A 25 30.31 -94.23 REMARK 500 7 ARG A 103 25.94 38.83 REMARK 500 7 ARG A 105 -33.37 -37.81 REMARK 500 7 ASN A 119 -74.94 -74.82 REMARK 500 7 PRO A 123 -179.46 -69.81 REMARK 500 7 GLU A 124 52.56 37.44 REMARK 500 8 SER A 6 55.22 -92.26 REMARK 500 8 VAL A 21 -63.94 -104.48 REMARK 500 8 GLU A 25 34.30 -83.46 REMARK 500 8 LYS A 59 29.41 47.71 REMARK 500 8 ARG A 103 50.10 -101.90 REMARK 500 8 ARG A 105 -37.42 -36.41 REMARK 500 REMARK 500 THIS ENTRY HAS 147 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSS001002512.1 RELATED DB: TARGETDB DBREF 1X5D A 8 127 UNP Q15084 PDIA6_HUMAN 161 280 SEQADV 1X5D GLY A 1 UNP Q15084 CLONING ARTIFACT SEQADV 1X5D SER A 2 UNP Q15084 CLONING ARTIFACT SEQADV 1X5D SER A 3 UNP Q15084 CLONING ARTIFACT SEQADV 1X5D GLY A 4 UNP Q15084 CLONING ARTIFACT SEQADV 1X5D SER A 5 UNP Q15084 CLONING ARTIFACT SEQADV 1X5D SER A 6 UNP Q15084 CLONING ARTIFACT SEQADV 1X5D GLY A 7 UNP Q15084 CLONING ARTIFACT SEQADV 1X5D SER A 128 UNP Q15084 CLONING ARTIFACT SEQADV 1X5D GLY A 129 UNP Q15084 CLONING ARTIFACT SEQADV 1X5D PRO A 130 UNP Q15084 CLONING ARTIFACT SEQADV 1X5D SER A 131 UNP Q15084 CLONING ARTIFACT SEQADV 1X5D SER A 132 UNP Q15084 CLONING ARTIFACT SEQADV 1X5D GLY A 133 UNP Q15084 CLONING ARTIFACT SEQRES 1 A 133 GLY SER SER GLY SER SER GLY ASP VAL ILE GLU LEU THR SEQRES 2 A 133 ASP ASP SER PHE ASP LYS ASN VAL LEU ASP SER GLU ASP SEQRES 3 A 133 VAL TRP MET VAL GLU PHE TYR ALA PRO TRP CYS GLY HIS SEQRES 4 A 133 CYS LYS ASN LEU GLU PRO GLU TRP ALA ALA ALA ALA SER SEQRES 5 A 133 GLU VAL LYS GLU GLN THR LYS GLY LYS VAL LYS LEU ALA SEQRES 6 A 133 ALA VAL ASP ALA THR VAL ASN GLN VAL LEU ALA SER ARG SEQRES 7 A 133 TYR GLY ILE ARG GLY PHE PRO THR ILE LYS ILE PHE GLN SEQRES 8 A 133 LYS GLY GLU SER PRO VAL ASP TYR ASP GLY GLY ARG THR SEQRES 9 A 133 ARG SER ASP ILE VAL SER ARG ALA LEU ASP LEU PHE SER SEQRES 10 A 133 ASP ASN ALA PRO PRO PRO GLU LEU LEU GLU SER GLY PRO SEQRES 11 A 133 SER SER GLY HELIX 1 1 ASP A 15 VAL A 21 1 7 HELIX 2 2 CYS A 37 ASN A 42 1 6 HELIX 3 3 ASN A 42 THR A 58 1 17 HELIX 4 4 GLN A 73 GLY A 80 1 8 HELIX 5 5 THR A 104 ALA A 120 1 17 HELIX 6 6 GLY A 129 GLY A 133 5 5 SHEET 1 A 5 ILE A 10 GLU A 11 0 SHEET 2 A 5 VAL A 62 ASP A 68 1 O ALA A 66 N ILE A 10 SHEET 3 A 5 VAL A 27 TYR A 33 1 N MET A 29 O ALA A 65 SHEET 4 A 5 THR A 86 GLN A 91 -1 O LYS A 88 N VAL A 30 SHEET 5 A 5 GLU A 94 TYR A 99 -1 O VAL A 97 N ILE A 89 CISPEP 1 PHE A 84 PRO A 85 1 0.08 CISPEP 2 PHE A 84 PRO A 85 2 -0.06 CISPEP 3 PHE A 84 PRO A 85 3 0.02 CISPEP 4 PHE A 84 PRO A 85 4 -0.03 CISPEP 5 PHE A 84 PRO A 85 5 0.08 CISPEP 6 PHE A 84 PRO A 85 6 0.05 CISPEP 7 PHE A 84 PRO A 85 7 0.00 CISPEP 8 PHE A 84 PRO A 85 8 0.00 CISPEP 9 PHE A 84 PRO A 85 9 0.00 CISPEP 10 PHE A 84 PRO A 85 10 0.04 CISPEP 11 PHE A 84 PRO A 85 11 0.01 CISPEP 12 PHE A 84 PRO A 85 12 0.04 CISPEP 13 PHE A 84 PRO A 85 13 0.09 CISPEP 14 PHE A 84 PRO A 85 14 -0.08 CISPEP 15 PHE A 84 PRO A 85 15 0.05 CISPEP 16 PHE A 84 PRO A 85 16 0.01 CISPEP 17 PHE A 84 PRO A 85 17 -0.03 CISPEP 18 PHE A 84 PRO A 85 18 -0.05 CISPEP 19 PHE A 84 PRO A 85 19 0.00 CISPEP 20 PHE A 84 PRO A 85 20 0.03 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