Header list of 1j0f.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 12-NOV-02 1J0F TITLE SOLUTION STRUCTURE OF THE SH3 DOMAIN BINDING GLUTAMIC ACID-RICH TITLE 2 PROTEIN LIKE 3 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SH3 DOMAIN-BINDING GLUTAMIC ACID-RICH-LIKE PROTEIN 3; COMPND 3 CHAIN: A; COMPND 4 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 1110004L05; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P020401-39; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS THIOREDOXIN FOLD, SH3BGR, STRUCTURAL GENOMICS, RIKEN STRUCTURAL KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.MIYAMOTO,T.KIGAWA,S.KOSHIBA,N.KOBAYASHI,N.TOCHIO,M.INOUE, AUTHOR 2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 23-FEB-22 1J0F 1 REMARK SEQADV REVDAT 2 24-FEB-09 1J0F 1 VERSN REVDAT 1 02-DEC-03 1J0F 0 JRNL AUTH K.MIYAMOTO,T.KIGAWA,S.KOSHIBA,N.KOBAYASHI,N.TOCHIO,M.INOUE, JRNL AUTH 2 S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE SH3 DOMAIN BINDING GLUTAMIC JRNL TITL 2 ACID-RICH PROTEIN LIKE 3 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 1.0.6 REMARK 3 AUTHORS : BRUKER (XWINNMR), P.GUENTERT (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1J0F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-NOV-02. REMARK 100 THE DEPOSITION ID IS D_1000005473. 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 : 1.2MM SH3BGR U-15N,13C; 20MM REMARK 210 PHOSPHATE BUFFER NA; 100MM NACL; REMARK 210 1MM D-DTT; 0.02% NAN3; 90% H2O, REMARK 210 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 2D_TROSY_HNCO 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 0.613 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,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 OD1 ASP A 80 H LEU A 83 1.52 REMARK 500 O ASN A 73 H HIS A 76 1.57 REMARK 500 O GLU A 82 H GLU A 86 1.58 REMARK 500 O LYS A 25 H SER A 29 1.59 REMARK 500 O THR A 32 H ASP A 36 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 2 118.62 -162.23 REMARK 500 1 ARG A 22 -68.93 78.78 REMARK 500 1 ASN A 63 132.69 -170.00 REMARK 500 1 LYS A 65 39.98 -94.23 REMARK 500 1 CYS A 78 -70.02 -57.35 REMARK 500 1 LEU A 97 -156.79 -67.56 REMARK 500 2 MET A 8 164.75 -46.66 REMARK 500 2 ARG A 22 -57.81 82.78 REMARK 500 2 LYS A 65 48.48 -98.58 REMARK 500 2 CYS A 78 -70.64 -65.30 REMARK 500 2 ASP A 80 -163.50 -117.56 REMARK 500 2 ASP A 91 23.74 80.50 REMARK 500 3 ALA A 5 161.08 64.51 REMARK 500 3 THR A 19 145.87 -171.34 REMARK 500 3 LYS A 65 47.55 -101.11 REMARK 500 3 LEU A 97 -169.57 -78.28 REMARK 500 3 LYS A 98 48.88 -105.93 REMARK 500 4 ALA A 5 134.04 -175.77 REMARK 500 4 THR A 7 -68.08 -133.64 REMARK 500 4 MET A 8 97.76 -67.03 REMARK 500 4 ARG A 22 -46.39 85.02 REMARK 500 4 LYS A 65 50.12 -101.40 REMARK 500 4 ASN A 75 -46.17 84.77 REMARK 500 4 LEU A 97 -156.48 -61.00 REMARK 500 5 SER A 2 108.75 -172.57 REMARK 500 5 ALA A 5 133.58 -171.19 REMARK 500 5 ALA A 6 81.08 179.86 REMARK 500 5 SER A 9 144.67 -173.63 REMARK 500 5 THR A 19 110.06 -173.04 REMARK 500 5 LYS A 65 44.28 -94.19 REMARK 500 5 CYS A 78 -72.10 -63.76 REMARK 500 5 LYS A 98 49.12 -88.93 REMARK 500 6 SER A 2 155.48 59.85 REMARK 500 6 THR A 19 108.48 -178.38 REMARK 500 6 LYS A 65 30.73 -93.28 REMARK 500 6 LYS A 98 46.77 -94.54 REMARK 500 7 ALA A 5 112.04 -160.28 REMARK 500 7 SER A 9 -53.56 -142.10 REMARK 500 7 ASN A 63 128.85 -176.03 REMARK 500 7 LYS A 65 40.49 -90.63 REMARK 500 7 LEU A 97 -168.10 -75.98 REMARK 500 7 LYS A 98 50.17 -106.96 REMARK 500 8 GLU A 3 -59.19 74.53 REMARK 500 8 THR A 19 119.50 -161.33 REMARK 500 8 LYS A 65 32.95 -92.42 REMARK 500 8 CYS A 78 -72.89 -65.11 REMARK 500 8 GLU A 82 -70.72 -55.33 REMARK 500 8 LEU A 97 -154.99 -62.77 REMARK 500 9 ALA A 5 -61.05 -168.00 REMARK 500 9 ARG A 22 -49.09 83.86 REMARK 500 REMARK 500 THIS ENTRY HAS 133 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMT007010558.1 RELATED DB: TARGETDB DBREF 1J0F A 8 100 UNP Q91VW3 SH3L3_MOUSE 1 93 SEQADV 1J0F GLY A 1 UNP Q91VW3 CLONING ARTIFACT SEQADV 1J0F SER A 2 UNP Q91VW3 CLONING ARTIFACT SEQADV 1J0F GLU A 3 UNP Q91VW3 CLONING ARTIFACT SEQADV 1J0F GLY A 4 UNP Q91VW3 CLONING ARTIFACT SEQADV 1J0F ALA A 5 UNP Q91VW3 CLONING ARTIFACT SEQADV 1J0F ALA A 6 UNP Q91VW3 CLONING ARTIFACT SEQADV 1J0F THR A 7 UNP Q91VW3 CLONING ARTIFACT SEQRES 1 A 100 GLY SER GLU GLY ALA ALA THR MET SER GLY LEU ARG VAL SEQRES 2 A 100 TYR SER THR SER VAL THR GLY SER ARG GLU ILE LYS SER SEQRES 3 A 100 GLN GLN SER GLU VAL THR ARG ILE LEU ASP GLY LYS ARG SEQRES 4 A 100 ILE GLN TYR GLN LEU VAL ASP ILE SER GLN ASP ASN ALA SEQRES 5 A 100 LEU ARG ASP GLU MET ARG THR LEU ALA GLY ASN PRO LYS SEQRES 6 A 100 ALA THR PRO PRO GLN ILE VAL ASN GLY ASN HIS TYR CYS SEQRES 7 A 100 GLY ASP TYR GLU LEU PHE VAL GLU ALA VAL GLU GLN ASP SEQRES 8 A 100 THR LEU GLN GLU PHE LEU LYS LEU ALA HELIX 1 1 GLU A 23 LYS A 38 1 16 HELIX 2 2 ALA A 52 ALA A 61 1 10 HELIX 3 3 TYR A 81 GLN A 90 1 10 HELIX 4 4 LEU A 93 PHE A 96 1 4 SHEET 1 A 4 TYR A 42 ASP A 46 0 SHEET 2 A 4 LEU A 11 SER A 15 1 N VAL A 13 O GLN A 43 SHEET 3 A 4 GLN A 70 ASN A 73 -1 O VAL A 72 N ARG A 12 SHEET 4 A 4 HIS A 76 GLY A 79 -1 O HIS A 76 N ASN A 73 CISPEP 1 PRO A 68 PRO A 69 1 -0.03 CISPEP 2 PRO A 68 PRO A 69 2 -0.03 CISPEP 3 PRO A 68 PRO A 69 3 0.00 CISPEP 4 PRO A 68 PRO A 69 4 0.03 CISPEP 5 PRO A 68 PRO A 69 5 -0.04 CISPEP 6 PRO A 68 PRO A 69 6 -0.02 CISPEP 7 PRO A 68 PRO A 69 7 0.02 CISPEP 8 PRO A 68 PRO A 69 8 0.02 CISPEP 9 PRO A 68 PRO A 69 9 0.05 CISPEP 10 PRO A 68 PRO A 69 10 0.00 CISPEP 11 PRO A 68 PRO A 69 11 -0.01 CISPEP 12 PRO A 68 PRO A 69 12 -0.04 CISPEP 13 PRO A 68 PRO A 69 13 -0.02 CISPEP 14 PRO A 68 PRO A 69 14 -0.05 CISPEP 15 PRO A 68 PRO A 69 15 -0.03 CISPEP 16 PRO A 68 PRO A 69 16 -0.04 CISPEP 17 PRO A 68 PRO A 69 17 -0.06 CISPEP 18 PRO A 68 PRO A 69 18 0.00 CISPEP 19 PRO A 68 PRO A 69 19 -0.03 CISPEP 20 PRO A 68 PRO A 69 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 - b 23 2 Bytes