Header list of 1wj1.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 28-MAY-04 1WJ1 TITLE SOLUTION STRUCTURE OF PHOSPHOTYROSINE INTERACTION DOMAIN OF MOUSE NUMB TITLE 2 PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: NUMB PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PID 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 1200002O22; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P031020-52; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS PTB, PID DOMAIN, NUMB PROTEIN, STRUCTURAL GENOMICS, RIKEN STRUCTURAL KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.SATO,T.TOMIZAWA,S.KOSHIBA,N.TOCHIO,M.INOUE,T.KIGAWA,S.YOKOYAMA, AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1WJ1 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WJ1 1 VERSN REVDAT 1 28-NOV-04 1WJ1 0 JRNL AUTH M.SATO,T.TOMIZAWA,S.KOSHIBA,N.TOCHIO,M.INOUE,T.KIGAWA, JRNL AUTH 2 S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF PHOSPHOTYROSINE INTERACTION DOMAIN OF JRNL TITL 2 MOUSE NUMB PROTEIN 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 1.0.7 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WJ1 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_1000023631. 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 : 1.3MM PID DOMAIN U-15N,13C; 20MM REMARK 210 PHOSPHATE BUFFER NA; 100MM NACL; REMARK 210 5MM D-DTT; 0.02% NAN3; 10% 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 : 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 GLU A 19 H THR A 23 1.41 REMARK 500 O VAL A 75 H ILE A 84 1.54 REMARK 500 O CYS A 109 H ILE A 118 1.55 REMARK 500 O ALA A 139 H CYS A 143 1.56 REMARK 500 O LEU A 144 H GLN A 148 1.56 REMARK 500 O PHE A 140 H LEU A 144 1.58 REMARK 500 O SER A 69 H GLY A 72 1.59 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 -56.67 -132.61 REMARK 500 1 SER A 3 -52.73 -178.32 REMARK 500 1 SER A 6 105.64 176.30 REMARK 500 1 LYS A 25 44.83 -175.02 REMARK 500 1 CYS A 26 68.51 -111.70 REMARK 500 1 ASP A 39 -47.66 -135.98 REMARK 500 1 SER A 41 3.00 84.79 REMARK 500 1 ARG A 42 119.52 -161.16 REMARK 500 1 LYS A 59 -149.96 -129.34 REMARK 500 1 LYS A 79 -71.27 -43.60 REMARK 500 1 ASP A 82 -171.20 -54.23 REMARK 500 1 GLU A 90 -70.58 -45.30 REMARK 500 1 VAL A 92 109.05 -39.52 REMARK 500 1 PRO A 97 -165.30 -75.04 REMARK 500 1 ARG A 99 60.15 -173.13 REMARK 500 1 ASN A 100 -44.47 -162.22 REMARK 500 1 ARG A 103 81.12 -172.51 REMARK 500 1 ASP A 111 155.77 -42.76 REMARK 500 1 THR A 113 -51.29 -142.87 REMARK 500 1 THR A 114 -103.38 -93.36 REMARK 500 1 ARG A 115 47.58 -178.04 REMARK 500 1 ALA A 124 157.73 -45.38 REMARK 500 1 VAL A 125 -65.28 -93.84 REMARK 500 1 GLN A 148 -172.22 -62.50 REMARK 500 2 SER A 2 85.90 59.85 REMARK 500 2 SER A 6 108.94 -165.63 REMARK 500 2 ALA A 8 110.30 -175.36 REMARK 500 2 SER A 9 135.64 62.51 REMARK 500 2 GLN A 13 -39.14 87.58 REMARK 500 2 LYS A 25 37.32 -178.85 REMARK 500 2 CYS A 26 73.59 -101.09 REMARK 500 2 VAL A 38 -169.24 -69.13 REMARK 500 2 ASP A 39 -43.19 -135.10 REMARK 500 2 SER A 41 4.34 85.66 REMARK 500 2 LYS A 59 -154.14 -122.74 REMARK 500 2 GLU A 78 -29.44 -39.40 REMARK 500 2 LYS A 79 -76.95 -44.35 REMARK 500 2 ASP A 82 -177.97 -52.66 REMARK 500 2 PRO A 97 -165.34 -75.03 REMARK 500 2 ALA A 124 156.04 -46.33 REMARK 500 2 VAL A 125 -62.54 -92.72 REMARK 500 2 SER A 151 92.97 49.65 REMARK 500 2 SER A 154 55.65 175.11 REMARK 500 2 SER A 155 -58.85 74.49 REMARK 500 3 SER A 3 -58.79 -128.74 REMARK 500 3 SER A 5 143.12 63.83 REMARK 500 3 SER A 6 128.08 75.76 REMARK 500 3 ALA A 8 128.15 68.07 REMARK 500 3 GLN A 13 -67.03 -156.82 REMARK 500 3 LYS A 25 40.61 178.80 REMARK 500 REMARK 500 THIS ENTRY HAS 434 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 700 REMARK 700 SHEET REMARK 700 AUTHOR DETERMINATION METHOD: AUTHOR DETERMINED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMT007011213.1 RELATED DB: TARGETDB DBREF 1WJ1 A 8 150 UNP Q9QZS3 NUMB_MOUSE 19 161 SEQADV 1WJ1 GLY A 1 UNP Q9QZS3 CLONING ARTIFACT SEQADV 1WJ1 SER A 2 UNP Q9QZS3 CLONING ARTIFACT SEQADV 1WJ1 SER A 3 UNP Q9QZS3 CLONING ARTIFACT SEQADV 1WJ1 GLY A 4 UNP Q9QZS3 CLONING ARTIFACT SEQADV 1WJ1 SER A 5 UNP Q9QZS3 CLONING ARTIFACT SEQADV 1WJ1 SER A 6 UNP Q9QZS3 CLONING ARTIFACT SEQADV 1WJ1 GLY A 7 UNP Q9QZS3 CLONING ARTIFACT SEQADV 1WJ1 SER A 151 UNP Q9QZS3 CLONING ARTIFACT SEQADV 1WJ1 GLY A 152 UNP Q9QZS3 CLONING ARTIFACT SEQADV 1WJ1 PRO A 153 UNP Q9QZS3 CLONING ARTIFACT SEQADV 1WJ1 SER A 154 UNP Q9QZS3 CLONING ARTIFACT SEQADV 1WJ1 SER A 155 UNP Q9QZS3 CLONING ARTIFACT SEQADV 1WJ1 GLY A 156 UNP Q9QZS3 CLONING ARTIFACT SEQRES 1 A 156 GLY SER SER GLY SER SER GLY ALA SER ARG PRO HIS GLN SEQRES 2 A 156 TRP GLN THR ASP GLU GLU GLY VAL ARG THR GLY LYS CYS SEQRES 3 A 156 SER PHE PRO VAL LYS TYR LEU GLY HIS VAL GLU VAL ASP SEQRES 4 A 156 GLU SER ARG GLY MET HIS ILE CYS GLU ASP ALA VAL LYS SEQRES 5 A 156 ARG LEU LYS ALA THR GLY LYS LYS ALA VAL LYS ALA VAL SEQRES 6 A 156 LEU TRP VAL SER ALA ASP GLY LEU ARG VAL VAL ASP GLU SEQRES 7 A 156 LYS THR LYS ASP LEU ILE VAL ASP GLN THR ILE GLU LYS SEQRES 8 A 156 VAL SER PHE CYS ALA PRO ASP ARG ASN PHE ASP ARG ALA SEQRES 9 A 156 PHE SER TYR ILE CYS ARG ASP GLY THR THR ARG ARG TRP SEQRES 10 A 156 ILE CYS HIS CYS PHE MET ALA VAL LYS ASP THR GLY GLU SEQRES 11 A 156 ARG LEU SER HIS ALA VAL GLY CYS ALA PHE ALA ALA CYS SEQRES 12 A 156 LEU GLU ARG LYS GLN LYS ARG SER GLY PRO SER SER GLY HELIX 1 1 TRP A 14 VAL A 21 1 8 HELIX 2 2 GLY A 43 GLY A 58 1 16 HELIX 3 3 THR A 128 GLN A 148 1 21 SHEET 1 A 7 ASP A 82 VAL A 85 0 SHEET 2 A 7 GLY A 72 ASP A 77 -1 N VAL A 75 O ILE A 84 SHEET 3 A 7 VAL A 62 SER A 69 -1 N SER A 69 O GLY A 72 SHEET 4 A 7 SER A 27 GLU A 37 -1 N PHE A 28 O LEU A 66 SHEET 5 A 7 TRP A 117 ALA A 124 -1 O CYS A 119 N VAL A 36 SHEET 6 A 7 ALA A 104 ARG A 110 -1 N CYS A 109 O ILE A 118 SHEET 7 A 7 PHE A 94 ALA A 96 -1 N PHE A 94 O ILE A 108 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