Header list of 1wg6.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 27-MAY-04 1WG6 TITLE SOLUTION STRUCTURE OF PDZ DOMAIN IN PROTEIN XP_110852 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN (RIKEN CDNA 2810455B10); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PDZ 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 2010002N16; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030407-A03; SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS KEYWDS STRUCTURAL GENOMICS, PDZ DOMAIN, RIKEN STRUCTURAL GENOMICS/PROTEOMICS KEYWDS 2 INITIATIVE, RSGI, DNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR F.HE,K.HANAKI,Y.MUTO,M.INOUE,T.KIGAWA,M.SHIROUZU,T.TERADA,S.YOKOYAMA, AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1WG6 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WG6 1 VERSN REVDAT 1 27-NOV-04 1WG6 0 JRNL AUTH F.HE,K.HANAKI,Y.MUTO,M.INOUE,T.KIGAWA,M.SHIROUZU,T.TERADA, JRNL AUTH 2 S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF PDZ DOMAIN IN PROTEIN XP_110852 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 1.0.8 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT,P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WG6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1000023545. 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 : 0.8MM U-15,13C; 20MM PHOSPHATE REMARK 210 BUFFER NA; 100MM NACL; 1MM D-DTT; REMARK 210 0.02% NAN3; 90% 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 20020425, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.863, CYANA 1.0.8 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 ILE A 59 H ASN A 77 1.49 REMARK 500 H LEU A 31 O GLY A 112 1.49 REMARK 500 O SER A 34 H GLY A 38 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 2 109.87 64.42 REMARK 500 1 SER A 3 132.92 178.28 REMARK 500 1 LEU A 8 130.16 67.13 REMARK 500 1 GLU A 11 93.21 63.66 REMARK 500 1 ASP A 13 146.68 178.03 REMARK 500 1 TYR A 15 131.43 -173.56 REMARK 500 1 LEU A 17 -59.80 -123.84 REMARK 500 1 SER A 22 153.30 -47.78 REMARK 500 1 THR A 53 -164.22 -122.54 REMARK 500 1 SER A 61 139.13 178.00 REMARK 500 1 HIS A 64 -175.65 -53.10 REMARK 500 1 ARG A 73 -29.99 -37.84 REMARK 500 1 LEU A 74 -174.03 -67.45 REMARK 500 1 MET A 76 173.62 -49.13 REMARK 500 1 ALA A 82 -176.02 178.07 REMARK 500 1 VAL A 83 114.06 -171.87 REMARK 500 1 HIS A 94 -71.91 -61.92 REMARK 500 1 LEU A 100 -74.07 -45.84 REMARK 500 1 ARG A 111 -70.70 -87.18 REMARK 500 1 ARG A 121 167.05 -45.75 REMARK 500 1 SER A 125 78.05 39.70 REMARK 500 2 SER A 2 -58.40 -136.09 REMARK 500 2 SER A 3 160.14 57.78 REMARK 500 2 SER A 5 129.11 -178.43 REMARK 500 2 LEU A 8 -68.65 -167.71 REMARK 500 2 LYS A 9 146.57 68.79 REMARK 500 2 ASP A 13 -62.61 179.97 REMARK 500 2 CYS A 14 104.34 64.19 REMARK 500 2 TYR A 15 -42.60 -168.57 REMARK 500 2 ALA A 16 164.34 64.61 REMARK 500 2 LEU A 17 -107.67 -69.28 REMARK 500 2 LEU A 19 -46.43 -153.23 REMARK 500 2 SER A 21 -51.75 81.66 REMARK 500 2 SER A 22 -178.49 60.18 REMARK 500 2 LEU A 39 -70.80 -39.40 REMARK 500 2 SER A 61 145.05 -175.40 REMARK 500 2 HIS A 64 -178.78 -57.91 REMARK 500 2 ARG A 73 -30.48 -37.49 REMARK 500 2 MET A 76 173.72 -46.45 REMARK 500 2 ALA A 82 166.26 163.08 REMARK 500 2 ASN A 84 18.60 57.54 REMARK 500 2 LYS A 91 -141.22 -87.75 REMARK 500 2 SER A 92 -150.16 -139.06 REMARK 500 2 LEU A 100 -71.04 -39.73 REMARK 500 2 ARG A 111 -71.63 -83.98 REMARK 500 3 SER A 5 82.10 -168.82 REMARK 500 3 SER A 6 -59.02 74.70 REMARK 500 3 LYS A 9 67.13 -171.14 REMARK 500 3 GLU A 11 144.21 -174.07 REMARK 500 3 ASP A 13 -65.11 81.52 REMARK 500 REMARK 500 THIS ENTRY HAS 343 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMT007007474.1 RELATED DB: TARGETDB DBREF 1WG6 A 8 121 GB 38049537 XP_110852 478 591 SEQADV 1WG6 GLY A 1 GB 38049537 CLONING ARTIFACT SEQADV 1WG6 SER A 2 GB 38049537 CLONING ARTIFACT SEQADV 1WG6 SER A 3 GB 38049537 CLONING ARTIFACT SEQADV 1WG6 GLY A 4 GB 38049537 CLONING ARTIFACT SEQADV 1WG6 SER A 5 GB 38049537 CLONING ARTIFACT SEQADV 1WG6 SER A 6 GB 38049537 CLONING ARTIFACT SEQADV 1WG6 GLY A 7 GB 38049537 CLONING ARTIFACT SEQADV 1WG6 SER A 122 GB 38049537 CLONING ARTIFACT SEQADV 1WG6 GLY A 123 GB 38049537 CLONING ARTIFACT SEQADV 1WG6 PRO A 124 GB 38049537 CLONING ARTIFACT SEQADV 1WG6 SER A 125 GB 38049537 CLONING ARTIFACT SEQADV 1WG6 SER A 126 GB 38049537 CLONING ARTIFACT SEQADV 1WG6 GLY A 127 GB 38049537 CLONING ARTIFACT SEQRES 1 A 127 GLY SER SER GLY SER SER GLY LEU LYS GLY GLU PRO ASP SEQRES 2 A 127 CYS TYR ALA LEU SER LEU GLU SER SER GLU GLN LEU THR SEQRES 3 A 127 LEU GLU ILE PRO LEU ASN ASP SER GLY SER ALA GLY LEU SEQRES 4 A 127 GLY VAL SER LEU LYS GLY ASN LYS SER ARG GLU THR GLY SEQRES 5 A 127 THR ASP LEU GLY ILE PHE ILE LYS SER ILE ILE HIS GLY SEQRES 6 A 127 GLY ALA ALA PHE LYS ASP GLY ARG LEU ARG MET ASN ASP SEQRES 7 A 127 GLN LEU ILE ALA VAL ASN GLY GLU THR LEU LEU GLY LYS SEQRES 8 A 127 SER ASN HIS GLU ALA MET GLU THR LEU ARG ARG SER MET SEQRES 9 A 127 SER MET GLU GLY ASN ILE ARG GLY MET ILE GLN LEU VAL SEQRES 10 A 127 ILE LEU ARG ARG SER GLY PRO SER SER GLY HELIX 1 1 ALA A 68 ARG A 73 1 6 HELIX 2 2 SER A 92 ARG A 111 1 20 SHEET 1 A 4 GLU A 23 PRO A 30 0 SHEET 2 A 4 MET A 113 ARG A 120 -1 O ILE A 114 N ILE A 29 SHEET 3 A 4 LEU A 80 VAL A 83 -1 N ILE A 81 O VAL A 117 SHEET 4 A 4 GLU A 86 THR A 87 -1 O GLU A 86 N VAL A 83 SHEET 1 B 2 SER A 42 SER A 48 0 SHEET 2 B 2 THR A 53 SER A 61 -1 O PHE A 58 N LYS A 44 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