Header list of 1wjk.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 29-MAY-04 1WJK TITLE SOLUTION STRUCTURE OF HYPOTHETICAL PROTEIN C330018D20RIK FROM MUS TITLE 2 MUSCULUS COMPND MOL_ID: 1; COMPND 2 MOLECULE: C330018D20RIK PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: GLUTAREDOXIN DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: RIKEN CDNA C330018D20; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P031125-30; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS GLUTAREDOXIN, THIOREDOXIN FOLD, STRUCTURAL GENOMICS, RIKEN STRUCTURAL KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.SATO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1WJK 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WJK 1 VERSN REVDAT 1 29-NOV-04 1WJK 0 JRNL AUTH M.SATO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF HYPOTHETICAL PROTEIN C330018D20RIK JRNL TITL 2 FROM MUS MUSCULUS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 1.0.7 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WJK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1000023644. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 120 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.6MM GLUTAREDOXIN DOMAIN U REMARK 210 -15N,13C; 20MM D-TRIS HCL; 100MM REMARK 210 NACL; 10MM D-DTT; 0.02% NAN3; 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 : 600 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 0.8996, 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 : 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: 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 LEU A 21 H VAL A 49 1.52 REMARK 500 O SER A 57 H GLU A 61 1.54 REMARK 500 O LEU A 19 H GLN A 47 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 SER A 6 95.38 -177.31 REMARK 500 1 SER A 10 -56.67 -147.86 REMARK 500 1 ALA A 11 71.50 56.69 REMARK 500 1 ALA A 15 116.81 -178.16 REMARK 500 1 CYS A 27 104.55 -162.36 REMARK 500 1 PHE A 44 177.97 178.69 REMARK 500 1 PHE A 76 102.83 -38.17 REMARK 500 1 MET A 78 149.05 -175.62 REMARK 500 1 HIS A 80 9.73 87.53 REMARK 500 1 ARG A 81 -166.69 164.34 REMARK 500 1 LEU A 94 -72.66 -140.23 REMARK 500 1 SER A 98 98.34 55.63 REMARK 500 1 SER A 99 108.39 -172.86 REMARK 500 2 SER A 2 156.48 66.31 REMARK 500 2 ALA A 11 144.55 -175.20 REMARK 500 2 ALA A 15 117.75 -172.41 REMARK 500 2 MET A 78 149.07 -174.87 REMARK 500 2 HIS A 80 9.56 87.50 REMARK 500 2 ARG A 81 -167.65 161.82 REMARK 500 2 LEU A 94 -70.41 -134.30 REMARK 500 2 SER A 95 81.57 56.00 REMARK 500 3 SER A 5 78.07 66.90 REMARK 500 3 ASN A 8 112.37 64.31 REMARK 500 3 MET A 78 149.74 -176.86 REMARK 500 3 HIS A 80 9.15 87.82 REMARK 500 3 ARG A 81 -166.34 162.17 REMARK 500 3 LEU A 94 -66.78 -160.87 REMARK 500 4 SER A 3 82.59 -178.32 REMARK 500 4 SER A 10 140.10 63.27 REMARK 500 4 ALA A 11 176.69 -56.09 REMARK 500 4 ASN A 13 97.25 -177.81 REMARK 500 4 CYS A 27 101.85 -165.39 REMARK 500 4 PHE A 44 175.15 178.35 REMARK 500 4 SER A 57 -32.04 -38.84 REMARK 500 4 PHE A 76 106.87 -37.62 REMARK 500 4 MET A 78 149.42 -174.46 REMARK 500 4 HIS A 80 9.94 87.79 REMARK 500 4 ARG A 81 -168.77 159.33 REMARK 500 4 LEU A 94 -63.25 -165.69 REMARK 500 4 SER A 95 139.05 62.64 REMARK 500 5 SER A 2 118.23 -177.24 REMARK 500 5 SER A 5 131.91 171.84 REMARK 500 5 SER A 12 169.55 178.37 REMARK 500 5 ALA A 15 117.16 -164.42 REMARK 500 5 CYS A 27 102.90 -161.48 REMARK 500 5 SER A 57 -33.65 -37.52 REMARK 500 5 PHE A 76 106.03 -40.81 REMARK 500 5 MET A 78 149.21 -176.48 REMARK 500 5 HIS A 80 10.01 87.52 REMARK 500 5 ARG A 81 -167.91 162.15 REMARK 500 REMARK 500 THIS ENTRY HAS 235 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMT007016800.1 RELATED DB: TARGETDB DBREF 1WJK A 8 94 UNP Q9CWB7 Q9CWB7_MOUSE 21 107 SEQADV 1WJK GLY A 1 UNP Q9CWB7 CLONING ARTIFACT SEQADV 1WJK SER A 2 UNP Q9CWB7 CLONING ARTIFACT SEQADV 1WJK SER A 3 UNP Q9CWB7 CLONING ARTIFACT SEQADV 1WJK GLY A 4 UNP Q9CWB7 CLONING ARTIFACT SEQADV 1WJK SER A 5 UNP Q9CWB7 CLONING ARTIFACT SEQADV 1WJK SER A 6 UNP Q9CWB7 CLONING ARTIFACT SEQADV 1WJK GLY A 7 UNP Q9CWB7 CLONING ARTIFACT SEQADV 1WJK SER A 95 UNP Q9CWB7 CLONING ARTIFACT SEQADV 1WJK GLY A 96 UNP Q9CWB7 CLONING ARTIFACT SEQADV 1WJK PRO A 97 UNP Q9CWB7 CLONING ARTIFACT SEQADV 1WJK SER A 98 UNP Q9CWB7 CLONING ARTIFACT SEQADV 1WJK SER A 99 UNP Q9CWB7 CLONING ARTIFACT SEQADV 1WJK GLY A 100 UNP Q9CWB7 CLONING ARTIFACT SEQRES 1 A 100 GLY SER SER GLY SER SER GLY ASN LEU SER ALA SER ASN SEQRES 2 A 100 ARG ALA LEU PRO VAL LEU THR LEU PHE THR LYS ALA PRO SEQRES 3 A 100 CYS PRO LEU CYS ASP GLU ALA LYS GLU VAL LEU GLN PRO SEQRES 4 A 100 TYR LYS ASP ARG PHE ILE LEU GLN GLU VAL ASP ILE THR SEQRES 5 A 100 LEU PRO GLU ASN SER THR TRP TYR GLU ARG TYR LYS PHE SEQRES 6 A 100 ASP ILE PRO VAL PHE HIS LEU ASN GLY GLN PHE LEU MET SEQRES 7 A 100 MET HIS ARG VAL ASN THR SER LYS LEU GLU LYS GLN LEU SEQRES 8 A 100 ARG LYS LEU SER GLY PRO SER SER GLY HELIX 1 1 CYS A 27 LEU A 37 1 11 HELIX 2 2 ASN A 56 TYR A 63 1 8 HELIX 3 3 ASN A 83 LYS A 93 1 11 SHEET 1 A 4 ILE A 45 ASP A 50 0 SHEET 2 A 4 VAL A 18 THR A 23 1 N LEU A 21 O VAL A 49 SHEET 3 A 4 VAL A 69 LEU A 72 -1 O HIS A 71 N THR A 20 SHEET 4 A 4 PHE A 76 MET A 79 -1 O LEU A 77 N PHE A 70 CISPEP 1 ALA A 25 PRO A 26 1 -0.04 CISPEP 2 ILE A 67 PRO A 68 1 -0.03 CISPEP 3 ALA A 25 PRO A 26 2 0.05 CISPEP 4 ILE A 67 PRO A 68 2 0.06 CISPEP 5 ALA A 25 PRO A 26 3 -0.02 CISPEP 6 ILE A 67 PRO A 68 3 0.00 CISPEP 7 ALA A 25 PRO A 26 4 -0.05 CISPEP 8 ILE A 67 PRO A 68 4 -0.04 CISPEP 9 ALA A 25 PRO A 26 5 0.04 CISPEP 10 ILE A 67 PRO A 68 5 -0.02 CISPEP 11 ALA A 25 PRO A 26 6 0.01 CISPEP 12 ILE A 67 PRO A 68 6 -0.04 CISPEP 13 ALA A 25 PRO A 26 7 0.09 CISPEP 14 ILE A 67 PRO A 68 7 0.03 CISPEP 15 ALA A 25 PRO A 26 8 0.01 CISPEP 16 ILE A 67 PRO A 68 8 -0.04 CISPEP 17 ALA A 25 PRO A 26 9 0.00 CISPEP 18 ILE A 67 PRO A 68 9 -0.02 CISPEP 19 ALA A 25 PRO A 26 10 0.02 CISPEP 20 ILE A 67 PRO A 68 10 0.09 CISPEP 21 ALA A 25 PRO A 26 11 -0.03 CISPEP 22 ILE A 67 PRO A 68 11 -0.08 CISPEP 23 ALA A 25 PRO A 26 12 -0.02 CISPEP 24 ILE A 67 PRO A 68 12 -0.03 CISPEP 25 ALA A 25 PRO A 26 13 0.01 CISPEP 26 ILE A 67 PRO A 68 13 -0.10 CISPEP 27 ALA A 25 PRO A 26 14 -0.05 CISPEP 28 ILE A 67 PRO A 68 14 0.03 CISPEP 29 ALA A 25 PRO A 26 15 0.03 CISPEP 30 ILE A 67 PRO A 68 15 -0.08 CISPEP 31 ALA A 25 PRO A 26 16 -0.07 CISPEP 32 ILE A 67 PRO A 68 16 0.02 CISPEP 33 ALA A 25 PRO A 26 17 -0.02 CISPEP 34 ILE A 67 PRO A 68 17 0.04 CISPEP 35 ALA A 25 PRO A 26 18 0.06 CISPEP 36 ILE A 67 PRO A 68 18 0.01 CISPEP 37 ALA A 25 PRO A 26 19 -0.01 CISPEP 38 ILE A 67 PRO A 68 19 -0.10 CISPEP 39 ALA A 25 PRO A 26 20 -0.09 CISPEP 40 ILE A 67 PRO A 68 20 -0.04 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