Header list of 1x1g.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 04-APR-05 1X1G TITLE SOLUTION STRUCTURE OF THE C-TERMINAL PH DOMAIN OF HUMAN PLECKSTRIN 2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PLECKSTRIN 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PH 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: PLEK2; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040614-11; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS PLECKSTRIN 2, PH DOMAIN, STRUCTURAL GENOMICS, RIKEN STRUCTURAL KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, NPPSFA, NATIONAL PROJECT ON KEYWDS 3 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR H.LI,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1X1G 1 REMARK SEQADV REVDAT 2 24-FEB-09 1X1G 1 VERSN REVDAT 1 04-OCT-05 1X1G 0 JRNL AUTH H.LI,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE C-TERMINAL PH DOMAIN OF HUMAN JRNL TITL 2 PLECKSTRIN 2 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 1X1G COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-APR-05. REMARK 100 THE DEPOSITION ID IS D_1000024258. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 296 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.24MM PH DOMAIN U-13C, 15N; REMARK 210 20MM D-TRIS-HCL(PH7.0); 100MM REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 90% REMARK 210 H2O, 10% D2O 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 20031121, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.913, 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 : TARGET FUNCTION, STRUCTURES WITH REMARK 210 THE LEAST RESTRAINT VIOLATIONS 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 24 H ARG A 37 1.49 REMARK 500 H VAL A 40 O HIS A 49 1.58 REMARK 500 O TYR A 50 H VAL A 61 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 3 126.54 -178.67 REMARK 500 1 SER A 8 -60.38 -129.89 REMARK 500 1 LEU A 9 171.92 -47.30 REMARK 500 1 THR A 11 161.01 -41.48 REMARK 500 1 VAL A 12 -82.42 -141.66 REMARK 500 1 SER A 15 49.30 -100.37 REMARK 500 1 HIS A 29 171.32 -54.31 REMARK 500 1 LYS A 30 154.81 60.39 REMARK 500 1 ARG A 31 175.86 64.00 REMARK 500 1 LYS A 32 161.43 -44.62 REMARK 500 1 ASN A 33 -72.80 -42.45 REMARK 500 1 ASP A 44 76.59 49.20 REMARK 500 1 ASP A 76 109.81 -43.43 REMARK 500 1 PRO A 80 -81.73 -75.03 REMARK 500 1 THR A 81 -68.09 -136.21 REMARK 500 1 GLN A 88 -159.42 -56.13 REMARK 500 1 ASN A 90 56.90 76.80 REMARK 500 1 HIS A 101 91.06 76.62 REMARK 500 1 GLU A 111 -39.72 -39.62 REMARK 500 1 ARG A 112 -72.08 -60.04 REMARK 500 1 ALA A 113 -38.02 -39.78 REMARK 500 1 ILE A 116 -77.12 -71.95 REMARK 500 1 SER A 127 -58.88 -170.44 REMARK 500 1 SER A 128 153.52 -45.43 REMARK 500 2 SER A 2 -63.10 69.73 REMARK 500 2 SER A 3 159.35 -41.52 REMARK 500 2 SER A 5 164.05 61.42 REMARK 500 2 SER A 8 138.35 63.77 REMARK 500 2 SER A 10 131.87 -177.88 REMARK 500 2 VAL A 12 -68.34 -144.12 REMARK 500 2 SER A 15 52.61 -93.13 REMARK 500 2 HIS A 29 -70.81 -165.28 REMARK 500 2 ARG A 31 146.13 65.57 REMARK 500 2 LYS A 32 114.12 60.44 REMARK 500 2 ASP A 44 78.31 48.02 REMARK 500 2 ASN A 58 59.31 -90.81 REMARK 500 2 ARG A 67 110.88 -37.55 REMARK 500 2 ASP A 76 -72.24 -40.53 REMARK 500 2 ASN A 77 -163.36 42.80 REMARK 500 2 VAL A 79 137.79 64.52 REMARK 500 2 THR A 81 -95.28 -160.04 REMARK 500 2 VAL A 83 -72.48 -122.31 REMARK 500 2 LYS A 84 -170.14 -174.04 REMARK 500 2 ASN A 86 116.48 167.47 REMARK 500 2 VAL A 87 -172.56 -54.60 REMARK 500 2 GLN A 88 -88.18 -65.73 REMARK 500 2 ASN A 90 -65.19 81.55 REMARK 500 2 LEU A 91 -158.58 38.85 REMARK 500 2 HIS A 101 93.16 81.61 REMARK 500 2 ARG A 112 -74.27 -56.83 REMARK 500 REMARK 500 THIS ENTRY HAS 446 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: HSS001002623.1 RELATED DB: TARGETDB DBREF 1X1G A 8 123 UNP Q9NYT0 PLEK2_HUMAN 238 353 SEQADV 1X1G GLY A 1 UNP Q9NYT0 CLONING ARTIFACT SEQADV 1X1G SER A 2 UNP Q9NYT0 CLONING ARTIFACT SEQADV 1X1G SER A 3 UNP Q9NYT0 CLONING ARTIFACT SEQADV 1X1G GLY A 4 UNP Q9NYT0 CLONING ARTIFACT SEQADV 1X1G SER A 5 UNP Q9NYT0 CLONING ARTIFACT SEQADV 1X1G SER A 6 UNP Q9NYT0 CLONING ARTIFACT SEQADV 1X1G GLY A 7 UNP Q9NYT0 CLONING ARTIFACT SEQADV 1X1G SER A 124 UNP Q9NYT0 CLONING ARTIFACT SEQADV 1X1G GLY A 125 UNP Q9NYT0 CLONING ARTIFACT SEQADV 1X1G PRO A 126 UNP Q9NYT0 CLONING ARTIFACT SEQADV 1X1G SER A 127 UNP Q9NYT0 CLONING ARTIFACT SEQADV 1X1G SER A 128 UNP Q9NYT0 CLONING ARTIFACT SEQADV 1X1G GLY A 129 UNP Q9NYT0 CLONING ARTIFACT SEQRES 1 A 129 GLY SER SER GLY SER SER GLY SER LEU SER THR VAL GLU SEQRES 2 A 129 LEU SER GLY THR VAL VAL LYS GLN GLY TYR LEU ALA LYS SEQRES 3 A 129 GLN GLY HIS LYS ARG LYS ASN TRP LYS VAL ARG ARG PHE SEQRES 4 A 129 VAL LEU ARG LYS ASP PRO ALA PHE LEU HIS TYR TYR ASP SEQRES 5 A 129 PRO SER LYS GLU GLU ASN ARG PRO VAL GLY GLY PHE SER SEQRES 6 A 129 LEU ARG GLY SER LEU VAL SER ALA LEU GLU ASP ASN GLY SEQRES 7 A 129 VAL PRO THR GLY VAL LYS GLY ASN VAL GLN GLY ASN LEU SEQRES 8 A 129 PHE LYS VAL ILE THR LYS ASP ASP THR HIS TYR TYR ILE SEQRES 9 A 129 GLN ALA SER SER LYS ALA GLU ARG ALA GLU TRP ILE GLU SEQRES 10 A 129 ALA ILE LYS LYS LEU THR SER GLY PRO SER SER GLY HELIX 1 1 LYS A 109 LEU A 122 1 14 SHEET 1 A 4 THR A 17 GLN A 27 0 SHEET 2 A 4 TRP A 34 LYS A 43 -1 O ARG A 37 N LEU A 24 SHEET 3 A 4 PHE A 47 TYR A 51 -1 O HIS A 49 N VAL A 40 SHEET 4 A 4 PHE A 64 SER A 65 -1 O PHE A 64 N LEU A 48 SHEET 1 B 3 LEU A 70 ALA A 73 0 SHEET 2 B 3 PHE A 92 ILE A 95 -1 O LYS A 93 N SER A 72 SHEET 3 B 3 TYR A 102 GLN A 105 -1 O TYR A 102 N VAL A 94 CISPEP 1 ASP A 44 PRO A 45 1 0.01 CISPEP 2 ASP A 44 PRO A 45 2 -0.01 CISPEP 3 ASP A 44 PRO A 45 3 -0.03 CISPEP 4 ASP A 44 PRO A 45 4 0.00 CISPEP 5 ASP A 44 PRO A 45 5 0.06 CISPEP 6 ASP A 44 PRO A 45 6 -0.05 CISPEP 7 ASP A 44 PRO A 45 7 -0.01 CISPEP 8 ASP A 44 PRO A 45 8 0.13 CISPEP 9 ASP A 44 PRO A 45 9 -0.03 CISPEP 10 ASP A 44 PRO A 45 10 0.04 CISPEP 11 ASP A 44 PRO A 45 11 0.01 CISPEP 12 ASP A 44 PRO A 45 12 -0.04 CISPEP 13 ASP A 44 PRO A 45 13 -0.03 CISPEP 14 ASP A 44 PRO A 45 14 0.00 CISPEP 15 ASP A 44 PRO A 45 15 -0.03 CISPEP 16 ASP A 44 PRO A 45 16 0.04 CISPEP 17 ASP A 44 PRO A 45 17 0.02 CISPEP 18 ASP A 44 PRO A 45 18 -0.01 CISPEP 19 ASP A 44 PRO A 45 19 -0.03 CISPEP 20 ASP A 44 PRO A 45 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