Header list of 1ug0.pdb file
Complete list - r 2 2 Bytes
HEADER RNA BINDING PROTEIN 11-JUN-03 1UG0 TITLE SOLUTION STRUCTURE OF SURP DOMAIN IN BAB30904 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPLICING FACTOR 4; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SURP 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 5730496N02; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P020924-06; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS SURP DOMAIN, STRUCTURAL GENOMICS, RIKEN STRUCTURAL KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, RNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR F.HE,Y.MUTO,R.USHIKOSHI,S.KOSHIBA,M.SHIROUZU,T.TERADA,T.KIGAWA, AUTHOR 2 M.INOUE,T.YABUKI,M.AOKI,E.SEKI,T.MATSUDA,H.HIROTA,M.YOSHIDA, AUTHOR 3 N.KOBAYASHI,A.TANAKA,T.OSANAI,Y.MATSUO,Y.HAYASHIZAKI,S.YOKOYAMA, AUTHOR 4 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1UG0 1 REMARK SEQADV REVDAT 2 24-FEB-09 1UG0 1 VERSN REVDAT 1 03-AUG-04 1UG0 0 JRNL AUTH F.HE,Y.MUTO,R.USHIKOSHI,S.KOSHIBA,M.SHIROUZU,T.TERADA, JRNL AUTH 2 T.KIGAWA,M.INOUE,T.YABUKI,M.AOKI,E.SEKI,T.MATSUDA,H.HIROTA, JRNL AUTH 3 M.YOSHIDA,N.KOBAYASHI,A.TANAKA,T.OSANAI,Y.MATSUO, JRNL AUTH 4 Y.HAYASHIZAKI,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF SURP DOMAIN IN BAB30904 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 1UG0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JUN-03. REMARK 100 THE DEPOSITION ID IS D_1000005787. 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 : 20MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.7MM SURP DOMAIN U-15N,13C; REMARK 210 20MM PHOSPHATE BUFFER NA(PH 6.0); REMARK 210 0.02% NAN3; 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 20020425, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.811, 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, 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 45 H ALA A 49 1.55 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 67.37 -113.33 REMARK 500 1 SER A 3 119.81 -163.11 REMARK 500 1 GLU A 8 -67.79 -152.30 REMARK 500 1 VAL A 38 -75.69 -92.79 REMARK 500 1 ASP A 55 73.98 -116.99 REMARK 500 1 LEU A 62 -71.45 -40.19 REMARK 500 1 HIS A 63 -72.03 -47.88 REMARK 500 1 ASP A 64 150.29 -40.35 REMARK 500 1 ASN A 66 35.79 -160.01 REMARK 500 1 SER A 87 -71.21 -169.23 REMARK 500 2 SER A 3 79.83 -167.13 REMARK 500 2 GLU A 8 62.82 -104.29 REMARK 500 2 VAL A 38 -72.01 -69.02 REMARK 500 2 ALA A 39 -31.82 -39.24 REMARK 500 2 LEU A 62 -71.88 -46.70 REMARK 500 2 SER A 67 -81.46 -100.68 REMARK 500 2 ARG A 68 -30.82 174.68 REMARK 500 2 SER A 83 -43.76 -163.03 REMARK 500 2 SER A 87 94.76 46.50 REMARK 500 3 SER A 5 170.74 179.07 REMARK 500 3 GLU A 9 -29.41 -39.10 REMARK 500 3 TYR A 11 -29.96 -38.08 REMARK 500 3 VAL A 38 -76.02 -73.25 REMARK 500 3 ASP A 55 77.12 -106.47 REMARK 500 3 HIS A 63 -70.62 -53.03 REMARK 500 3 SER A 67 -86.01 -110.11 REMARK 500 3 ARG A 68 -30.61 174.21 REMARK 500 3 SER A 83 86.47 178.14 REMARK 500 3 SER A 86 85.47 178.09 REMARK 500 3 SER A 87 90.08 39.98 REMARK 500 4 SER A 3 90.53 179.54 REMARK 500 4 SER A 5 92.30 44.96 REMARK 500 4 GLU A 8 -58.82 -120.81 REMARK 500 4 LYS A 18 -179.68 -68.15 REMARK 500 4 VAL A 38 -73.61 -73.84 REMARK 500 4 ALA A 39 -32.74 -39.20 REMARK 500 4 PHE A 59 32.29 -86.88 REMARK 500 4 LEU A 62 -70.60 -39.65 REMARK 500 4 ASP A 64 107.22 -165.13 REMARK 500 4 ASN A 66 47.41 -173.15 REMARK 500 4 SER A 67 -83.85 -111.49 REMARK 500 4 ARG A 68 -30.72 174.46 REMARK 500 4 ARG A 75 -78.87 -66.48 REMARK 500 4 SER A 83 51.12 83.75 REMARK 500 4 SER A 86 89.14 60.77 REMARK 500 4 SER A 87 97.69 55.45 REMARK 500 5 SER A 2 161.92 64.43 REMARK 500 5 SER A 5 73.63 -108.76 REMARK 500 5 VAL A 38 -74.90 -87.86 REMARK 500 5 PHE A 59 36.63 -85.54 REMARK 500 REMARK 500 THIS ENTRY HAS 246 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMK001002415.1 RELATED DB: TARGETDB DBREF 1UG0 A 8 82 UNP Q8CH02 SF04_MOUSE 165 239 SEQADV 1UG0 GLY A 1 UNP Q8CH02 CLONING ARTIFACT SEQADV 1UG0 SER A 2 UNP Q8CH02 CLONING ARTIFACT SEQADV 1UG0 SER A 3 UNP Q8CH02 CLONING ARTIFACT SEQADV 1UG0 GLY A 4 UNP Q8CH02 CLONING ARTIFACT SEQADV 1UG0 SER A 5 UNP Q8CH02 CLONING ARTIFACT SEQADV 1UG0 SER A 6 UNP Q8CH02 CLONING ARTIFACT SEQADV 1UG0 GLY A 7 UNP Q8CH02 CLONING ARTIFACT SEQADV 1UG0 SER A 83 UNP Q8CH02 CLONING ARTIFACT SEQADV 1UG0 GLY A 84 UNP Q8CH02 CLONING ARTIFACT SEQADV 1UG0 PRO A 85 UNP Q8CH02 CLONING ARTIFACT SEQADV 1UG0 SER A 86 UNP Q8CH02 CLONING ARTIFACT SEQADV 1UG0 SER A 87 UNP Q8CH02 CLONING ARTIFACT SEQADV 1UG0 GLY A 88 UNP Q8CH02 CLONING ARTIFACT SEQRES 1 A 88 GLY SER SER GLY SER SER GLY GLU GLU ASP TYR GLU GLN SEQRES 2 A 88 TRP LEU GLU ILE LYS VAL SER PRO PRO GLU GLY ALA GLU SEQRES 3 A 88 THR ARG ARG VAL ILE GLU LYS LEU ALA ARG PHE VAL ALA SEQRES 4 A 88 GLU GLY GLY PRO GLU LEU GLU LYS VAL ALA MET GLU ASP SEQRES 5 A 88 TYR LYS ASP ASN PRO ALA PHE THR PHE LEU HIS ASP LYS SEQRES 6 A 88 ASN SER ARG GLU PHE LEU TYR TYR ARG ARG LYS VAL ALA SEQRES 7 A 88 GLU ILE ARG LYS SER GLY PRO SER SER GLY HELIX 1 1 ASP A 10 LEU A 15 1 6 HELIX 2 2 ALA A 25 GLY A 41 5 17 HELIX 3 3 PRO A 43 ASP A 52 1 10 HELIX 4 4 THR A 60 HIS A 63 1 4 HELIX 5 5 ARG A 68 LYS A 82 1 15 CISPEP 1 SER A 20 PRO A 21 1 -0.04 CISPEP 2 SER A 20 PRO A 21 2 -0.02 CISPEP 3 SER A 20 PRO A 21 3 0.02 CISPEP 4 SER A 20 PRO A 21 4 0.02 CISPEP 5 SER A 20 PRO A 21 5 0.03 CISPEP 6 SER A 20 PRO A 21 6 -0.12 CISPEP 7 SER A 20 PRO A 21 7 -0.02 CISPEP 8 SER A 20 PRO A 21 8 0.07 CISPEP 9 SER A 20 PRO A 21 9 -0.02 CISPEP 10 SER A 20 PRO A 21 10 0.04 CISPEP 11 SER A 20 PRO A 21 11 0.03 CISPEP 12 SER A 20 PRO A 21 12 0.03 CISPEP 13 SER A 20 PRO A 21 13 -0.03 CISPEP 14 SER A 20 PRO A 21 14 -0.04 CISPEP 15 SER A 20 PRO A 21 15 -0.02 CISPEP 16 SER A 20 PRO A 21 16 0.08 CISPEP 17 SER A 20 PRO A 21 17 0.01 CISPEP 18 SER A 20 PRO A 21 18 -0.06 CISPEP 19 SER A 20 PRO A 21 19 0.01 CISPEP 20 SER A 20 PRO A 21 20 -0.01 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