Header list of 1wj4.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 28-MAY-04 1WJ4 TITLE SOLUTION STRUCTURE OF THE UBX DOMAIN OF KIAA0794 PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: KIAA0794 PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UBX 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 HK06006; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040114-84; SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS KEYWDS UBX DOMAIN, BETA-GRASP FOLD, STRUCTURAL GENOMICS, RIKEN STRUCTURAL KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR H.ZHANG,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS AUTHOR 2 INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1WJ4 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WJ4 1 VERSN REVDAT 1 28-NOV-04 1WJ4 0 JRNL AUTH H.ZHANG,F.HAYASHI,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE UBX DOMAIN OF KIAA0794 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), GUENTENT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WJ4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1000023634. 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 : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.96MM 13C, 15N-LABELED PROTEIN; REMARK 210 20MM D-TRIS-HCL (PH 7.0), 100MM REMARK 210 NACL, 1MM D-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 : 900 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 20031121, KUJIRA 0.8995, REMARK 210 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, STRUCTURES REMARK 210 WITH THE LOWEST ENERGY 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 67 H LYS A 71 1.45 REMARK 500 O LEU A 48 H GLU A 56 1.56 REMARK 500 O ARG A 49 H VAL A 116 1.59 REMARK 500 H GLU A 84 O GLN A 117 1.60 REMARK 500 O LYS A 65 H ALA A 68 1.60 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 3 167.15 176.60 REMARK 500 1 SER A 5 167.70 178.68 REMARK 500 1 SER A 6 170.57 177.47 REMARK 500 1 ALA A 9 167.84 178.83 REMARK 500 1 HIS A 12 125.46 -178.16 REMARK 500 1 LEU A 15 136.07 -170.94 REMARK 500 1 GLU A 21 -67.00 -120.95 REMARK 500 1 MET A 25 90.06 29.58 REMARK 500 1 GLU A 28 137.16 178.82 REMARK 500 1 ALA A 30 107.62 -178.09 REMARK 500 1 ASP A 31 156.03 173.72 REMARK 500 1 VAL A 33 -153.51 -77.54 REMARK 500 1 ILE A 37 87.38 39.42 REMARK 500 1 TYR A 78 98.57 -160.54 REMARK 500 1 ARG A 82 -69.51 -97.80 REMARK 500 1 THR A 87 -166.41 -112.28 REMARK 500 1 PHE A 89 135.28 -178.88 REMARK 500 1 ARG A 91 107.40 -55.85 REMARK 500 1 LEU A 94 92.02 -54.49 REMARK 500 1 SER A 95 -68.47 -179.35 REMARK 500 1 LEU A 97 -87.34 -39.53 REMARK 500 1 ASP A 98 168.94 172.76 REMARK 500 1 ILE A 101 -163.22 -71.89 REMARK 500 1 SER A 122 87.79 57.05 REMARK 500 1 SER A 123 -61.69 70.65 REMARK 500 2 SER A 6 169.82 178.35 REMARK 500 2 SER A 20 83.37 64.07 REMARK 500 2 GLU A 24 76.88 -105.62 REMARK 500 2 ASP A 31 164.51 58.26 REMARK 500 2 VAL A 34 87.57 41.32 REMARK 500 2 ASN A 40 83.20 48.57 REMARK 500 2 GLU A 81 -30.14 -38.21 REMARK 500 2 ARG A 82 -79.30 -96.17 REMARK 500 2 THR A 87 -160.47 -112.78 REMARK 500 2 PHE A 89 134.03 -178.02 REMARK 500 2 ARG A 91 82.60 -62.25 REMARK 500 2 LEU A 94 92.10 -53.23 REMARK 500 2 SER A 95 -65.71 -177.49 REMARK 500 2 LEU A 97 -86.85 -42.27 REMARK 500 2 ASP A 98 157.91 168.05 REMARK 500 2 ILE A 101 -153.53 -78.92 REMARK 500 2 SER A 123 161.47 63.96 REMARK 500 3 SER A 2 129.77 -177.97 REMARK 500 3 SER A 5 148.53 177.16 REMARK 500 3 HIS A 12 118.08 -179.97 REMARK 500 3 GLN A 13 147.20 -175.53 REMARK 500 3 ALA A 17 42.84 178.90 REMARK 500 3 GLU A 24 77.09 -114.80 REMARK 500 3 MET A 25 121.92 -171.69 REMARK 500 3 ASP A 31 141.34 178.79 REMARK 500 REMARK 500 THIS ENTRY HAS 439 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSK002000776.1 RELATED DB: TARGETDB DBREF 1WJ4 A 8 118 UNP O94888 UBXD7_HUMAN 378 488 SEQADV 1WJ4 GLY A 1 UNP O94888 CLONING ARTIFACT SEQADV 1WJ4 SER A 2 UNP O94888 CLONING ARTIFACT SEQADV 1WJ4 SER A 3 UNP O94888 CLONING ARTIFACT SEQADV 1WJ4 GLY A 4 UNP O94888 CLONING ARTIFACT SEQADV 1WJ4 SER A 5 UNP O94888 CLONING ARTIFACT SEQADV 1WJ4 SER A 6 UNP O94888 CLONING ARTIFACT SEQADV 1WJ4 GLY A 7 UNP O94888 CLONING ARTIFACT SEQADV 1WJ4 SER A 119 UNP O94888 CLONING ARTIFACT SEQADV 1WJ4 GLY A 120 UNP O94888 CLONING ARTIFACT SEQADV 1WJ4 PRO A 121 UNP O94888 CLONING ARTIFACT SEQADV 1WJ4 SER A 122 UNP O94888 CLONING ARTIFACT SEQADV 1WJ4 SER A 123 UNP O94888 CLONING ARTIFACT SEQADV 1WJ4 GLY A 124 UNP O94888 CLONING ARTIFACT SEQRES 1 A 124 GLY SER SER GLY SER SER GLY THR ALA THR ASN HIS GLN SEQRES 2 A 124 GLY LEU PRO ALA VAL ASP SER GLU ILE LEU GLU MET PRO SEQRES 3 A 124 PRO GLU LYS ALA ASP GLY VAL VAL GLU GLY ILE ASP VAL SEQRES 4 A 124 ASN GLY PRO LYS ALA GLN LEU MET LEU ARG TYR PRO ASP SEQRES 5 A 124 GLY LYS ARG GLU GLN ILE THR LEU PRO GLU GLN ALA LYS SEQRES 6 A 124 LEU LEU ALA LEU VAL LYS HIS VAL GLN SER LYS GLY TYR SEQRES 7 A 124 PRO ASN GLU ARG PHE GLU LEU LEU THR ASN PHE PRO ARG SEQRES 8 A 124 ARG LYS LEU SER HIS LEU ASP TYR ASP ILE THR LEU GLN SEQRES 9 A 124 GLU ALA GLY LEU CYS PRO GLN GLU THR VAL PHE VAL GLN SEQRES 10 A 124 GLU SER GLY PRO SER SER GLY HELIX 1 1 LYS A 65 TYR A 78 1 14 SHEET 1 A 5 LYS A 54 LEU A 60 0 SHEET 2 A 5 ALA A 44 TYR A 50 -1 N LEU A 46 O ILE A 58 SHEET 3 A 5 GLN A 111 GLU A 118 1 N VAL A 114 O MET A 47 SHEET 4 A 5 PHE A 83 THR A 87 -1 N LEU A 86 O PHE A 115 SHEET 5 A 5 ARG A 92 LEU A 94 -1 N LEU A 94 O LEU A 85 CISPEP 1 PHE A 89 PRO A 90 1 0.06 CISPEP 2 CYS A 109 PRO A 110 1 -0.02 CISPEP 3 PHE A 89 PRO A 90 2 0.03 CISPEP 4 CYS A 109 PRO A 110 2 0.03 CISPEP 5 PHE A 89 PRO A 90 3 0.02 CISPEP 6 CYS A 109 PRO A 110 3 0.01 CISPEP 7 PHE A 89 PRO A 90 4 0.02 CISPEP 8 CYS A 109 PRO A 110 4 -0.04 CISPEP 9 PHE A 89 PRO A 90 5 0.01 CISPEP 10 CYS A 109 PRO A 110 5 0.04 CISPEP 11 PHE A 89 PRO A 90 6 0.02 CISPEP 12 CYS A 109 PRO A 110 6 0.03 CISPEP 13 PHE A 89 PRO A 90 7 0.02 CISPEP 14 CYS A 109 PRO A 110 7 -0.02 CISPEP 15 PHE A 89 PRO A 90 8 0.03 CISPEP 16 CYS A 109 PRO A 110 8 -0.01 CISPEP 17 PHE A 89 PRO A 90 9 0.01 CISPEP 18 CYS A 109 PRO A 110 9 -0.04 CISPEP 19 PHE A 89 PRO A 90 10 -0.04 CISPEP 20 CYS A 109 PRO A 110 10 -0.01 CISPEP 21 PHE A 89 PRO A 90 11 0.04 CISPEP 22 CYS A 109 PRO A 110 11 -0.05 CISPEP 23 PHE A 89 PRO A 90 12 0.00 CISPEP 24 CYS A 109 PRO A 110 12 -0.01 CISPEP 25 PHE A 89 PRO A 90 13 0.00 CISPEP 26 CYS A 109 PRO A 110 13 -0.01 CISPEP 27 PHE A 89 PRO A 90 14 0.00 CISPEP 28 CYS A 109 PRO A 110 14 -0.02 CISPEP 29 PHE A 89 PRO A 90 15 -0.06 CISPEP 30 CYS A 109 PRO A 110 15 -0.02 CISPEP 31 PHE A 89 PRO A 90 16 -0.03 CISPEP 32 CYS A 109 PRO A 110 16 0.00 CISPEP 33 PHE A 89 PRO A 90 17 -0.02 CISPEP 34 CYS A 109 PRO A 110 17 -0.04 CISPEP 35 PHE A 89 PRO A 90 18 0.01 CISPEP 36 CYS A 109 PRO A 110 18 -0.04 CISPEP 37 PHE A 89 PRO A 90 19 0.04 CISPEP 38 CYS A 109 PRO A 110 19 0.00 CISPEP 39 PHE A 89 PRO A 90 20 0.02 CISPEP 40 CYS A 109 PRO A 110 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