Header list of 1x6d.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 17-MAY-05 1X6D TITLE SOLUTION STRUCTURES OF THE PDZ DOMAIN OF HUMAN INTERLEUKIN-16 COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTERLEUKIN-16; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PDZ DOMAIN; COMPND 5 SYNONYM: IL-16, LYMPHOCYTE CHEMOATTRACTANT FACTOR, LCF; COMPND 6 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: IL16; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040614-09; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS PDZ DOMAIN, LYMPHOCYTE CHEMOATTRACTANT FACTOR (LCF), STRUCTURAL KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS KEYWDS 4 INITIATIVE, RSGI, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.SATO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1X6D 1 REMARK SEQADV REVDAT 2 24-FEB-09 1X6D 1 VERSN REVDAT 1 17-NOV-05 1X6D 0 JRNL AUTH M.SATO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURES OF THE PDZ DOMAIN OF HUMAN JRNL TITL 2 INTERLEUKIN-16 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 1.0.7 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1X6D COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000024435. 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 : 1MM PDZ DOMAIN U-15N, 13C; 20MM REMARK 210 D-TRIS HCL; 100MM NACL; 1MM D- REMARK 210 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 : 700 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 0.9295, 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 H ASN A 71 O VAL A 97 1.53 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 5 -59.26 -160.34 REMARK 500 1 LYS A 11 -69.16 -138.74 REMARK 500 1 ASP A 14 167.85 63.64 REMARK 500 1 PHE A 50 154.18 -37.34 REMARK 500 1 LYS A 63 132.81 -37.38 REMARK 500 1 ASN A 71 11.68 81.16 REMARK 500 1 THR A 79 -166.41 -69.74 REMARK 500 1 ASP A 82 -30.55 -38.83 REMARK 500 1 ALA A 107 79.68 47.63 REMARK 500 1 ASN A 112 157.93 171.18 REMARK 500 1 SER A 114 106.25 -42.37 REMARK 500 2 SER A 3 -58.57 -131.08 REMARK 500 2 SER A 6 -58.79 -176.12 REMARK 500 2 GLU A 25 103.11 -57.14 REMARK 500 2 PHE A 50 153.65 -36.84 REMARK 500 2 GLU A 106 61.45 -151.87 REMARK 500 2 LEU A 111 174.23 -55.13 REMARK 500 2 SER A 118 163.76 -49.13 REMARK 500 3 SER A 2 92.69 -175.37 REMARK 500 3 SER A 6 131.23 -172.74 REMARK 500 3 LEU A 10 94.27 56.22 REMARK 500 3 GLN A 12 166.44 172.66 REMARK 500 3 GLU A 25 105.45 -53.01 REMARK 500 3 PHE A 50 154.19 -38.67 REMARK 500 3 PRO A 93 -162.81 -75.03 REMARK 500 3 THR A 104 153.40 -37.57 REMARK 500 3 ALA A 107 111.99 61.68 REMARK 500 3 ASN A 112 162.89 62.82 REMARK 500 3 SER A 113 -53.42 -146.46 REMARK 500 3 SER A 114 121.97 61.79 REMARK 500 4 SER A 2 165.53 66.73 REMARK 500 4 GLU A 25 102.53 -58.50 REMARK 500 4 LEU A 39 -148.08 -104.89 REMARK 500 4 PHE A 50 154.44 -37.67 REMARK 500 4 LYS A 63 133.38 -38.30 REMARK 500 4 ASN A 71 1.11 81.98 REMARK 500 4 THR A 104 159.29 -44.70 REMARK 500 4 GLU A 106 -63.74 -108.79 REMARK 500 4 LEU A 111 -178.25 -59.67 REMARK 500 4 SER A 114 -61.64 -136.45 REMARK 500 4 SER A 117 147.05 -176.12 REMARK 500 4 SER A 118 162.31 65.08 REMARK 500 5 SER A 2 170.43 178.62 REMARK 500 5 SER A 3 160.82 176.32 REMARK 500 5 SER A 5 130.79 175.47 REMARK 500 5 THR A 9 81.36 -161.06 REMARK 500 5 LEU A 13 173.20 176.25 REMARK 500 5 ASP A 14 -70.43 75.24 REMARK 500 5 GLU A 25 103.05 -56.90 REMARK 500 5 PHE A 50 154.51 -39.82 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: HSS001000149.1 RELATED DB: TARGETDB DBREF 1X6D A 8 113 UNP Q14005 IL16_HUMAN 402 507 SEQADV 1X6D GLY A 1 UNP Q14005 CLONING ARTIFACT SEQADV 1X6D SER A 2 UNP Q14005 CLONING ARTIFACT SEQADV 1X6D SER A 3 UNP Q14005 CLONING ARTIFACT SEQADV 1X6D GLY A 4 UNP Q14005 CLONING ARTIFACT SEQADV 1X6D SER A 5 UNP Q14005 CLONING ARTIFACT SEQADV 1X6D SER A 6 UNP Q14005 CLONING ARTIFACT SEQADV 1X6D GLY A 7 UNP Q14005 CLONING ARTIFACT SEQADV 1X6D SER A 114 UNP Q14005 CLONING ARTIFACT SEQADV 1X6D GLY A 115 UNP Q14005 CLONING ARTIFACT SEQADV 1X6D PRO A 116 UNP Q14005 CLONING ARTIFACT SEQADV 1X6D SER A 117 UNP Q14005 CLONING ARTIFACT SEQADV 1X6D SER A 118 UNP Q14005 CLONING ARTIFACT SEQADV 1X6D GLY A 119 UNP Q14005 CLONING ARTIFACT SEQRES 1 A 119 GLY SER SER GLY SER SER GLY ALA THR LEU LYS GLN LEU SEQRES 2 A 119 ASP GLY ILE HIS VAL THR ILE LEU HIS LYS GLU GLU GLY SEQRES 3 A 119 ALA GLY LEU GLY PHE SER LEU ALA GLY GLY ALA ASP LEU SEQRES 4 A 119 GLU ASN LYS VAL ILE THR VAL HIS ARG VAL PHE PRO ASN SEQRES 5 A 119 GLY LEU ALA SER GLN GLU GLY THR ILE GLN LYS GLY ASN SEQRES 6 A 119 GLU VAL LEU SER ILE ASN GLY LYS SER LEU LYS GLY THR SEQRES 7 A 119 THR HIS HIS ASP ALA LEU ALA ILE LEU ARG GLN ALA ARG SEQRES 8 A 119 GLU PRO ARG GLN ALA VAL ILE VAL THR ARG LYS LEU THR SEQRES 9 A 119 PRO GLU ALA MET PRO ASP LEU ASN SER SER GLY PRO SER SEQRES 10 A 119 SER GLY HELIX 1 1 GLY A 53 GLY A 59 1 7 HELIX 2 2 THR A 79 ALA A 90 1 12 SHEET 1 A 4 ILE A 16 HIS A 22 0 SHEET 2 A 4 GLN A 95 ARG A 101 -1 O ALA A 96 N LEU A 21 SHEET 3 A 4 SER A 69 ILE A 70 -1 N SER A 69 O VAL A 99 SHEET 4 A 4 LYS A 73 SER A 74 -1 O LYS A 73 N ILE A 70 SHEET 1 B 2 PHE A 31 ALA A 34 0 SHEET 2 B 2 THR A 45 VAL A 49 -1 O THR A 45 N ALA A 34 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