Header list of 2daw.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 14-DEC-05 2DAW TITLE SOLUTION STRUCTURE OF THE RWD DOMAIN OF HUMAN RWD OMAIN CONTAINING TITLE 2 PROTEIN 2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: RWD DOMAIN CONTAINING PROTEIN 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RWD 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: RWDD2; SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050314-15; SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS RWD DOMAIN, ALPHA+BETA SANDWICH FOLD, STRUCTURAL GENOMICS, NPPSFA, KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN KEYWDS 4 FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.YONEYAMA,T.KIGAWA,M.SATO,N.TOCHIO,S.KOSHIBA,M.INOUE,S.YOKOYAMA, AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2DAW 1 REMARK SEQADV REVDAT 2 24-FEB-09 2DAW 1 VERSN REVDAT 1 14-JUN-06 2DAW 0 JRNL AUTH M.YONEYAMA,T.KIGAWA,M.SATO,N.TOCHIO,S.KOSHIBA,M.INOUE, JRNL AUTH 2 S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE RWD DOMAIN OF HUMAN RWD OMAIN JRNL TITL 2 CONTAINING PROTEIN 2 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 2.0.17 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2DAW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-DEC-05. REMARK 100 THE DEPOSITION ID IS D_1000025197. 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 : 1.17MM RWD DOMAIN U-15N,13C; REMARK 210 20MM D-TRIS-HCL(PH 7.0); 100MM REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 10% REMARK 210 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 20030801, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.9318, CYANA 2.0.17 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 LOWEST ENERGY,STRUCTURES REMARK 210 WITH THE LEAST RESTRAINT REMARK 210 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: 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 6 131.26 -175.00 REMARK 500 1 GLU A 35 -74.86 -112.20 REMARK 500 1 ASN A 46 -36.88 -38.77 REMARK 500 1 LYS A 61 170.37 -56.36 REMARK 500 1 LYS A 74 90.54 -52.57 REMARK 500 1 PRO A 84 -171.76 -69.78 REMARK 500 1 SER A 86 -62.94 -102.34 REMARK 500 1 TYR A 87 150.01 -36.64 REMARK 500 1 LEU A 92 175.98 -54.63 REMARK 500 1 LEU A 101 155.34 -39.65 REMARK 500 1 PRO A 122 94.46 -69.80 REMARK 500 1 ASN A 137 50.97 -111.26 REMARK 500 1 LEU A 143 106.41 -38.89 REMARK 500 2 PRO A 73 -175.90 -69.74 REMARK 500 2 PRO A 84 -169.84 -69.83 REMARK 500 2 TYR A 87 148.57 -35.78 REMARK 500 2 LEU A 101 179.81 -56.48 REMARK 500 2 PHE A 120 158.37 -45.22 REMARK 500 2 ILE A 131 -74.43 -60.91 REMARK 500 2 ASN A 137 50.06 -111.60 REMARK 500 2 LYS A 146 45.96 34.56 REMARK 500 2 LEU A 147 107.68 -58.96 REMARK 500 2 SER A 152 40.81 -99.76 REMARK 500 3 PHE A 30 75.61 -116.22 REMARK 500 3 ASP A 40 114.02 -167.61 REMARK 500 3 ASN A 46 -38.74 -36.43 REMARK 500 3 LYS A 48 -33.92 -37.33 REMARK 500 3 ILE A 70 104.07 -45.58 REMARK 500 3 HIS A 85 -18.63 -49.42 REMARK 500 3 TYR A 87 148.57 -36.46 REMARK 500 3 LEU A 92 -179.47 -56.35 REMARK 500 3 PHE A 120 155.39 -41.40 REMARK 500 3 ASN A 137 48.81 -93.44 REMARK 500 3 SER A 138 -54.25 -123.33 REMARK 500 3 LEU A 143 105.60 -35.47 REMARK 500 3 ARG A 145 55.21 -95.08 REMARK 500 4 VAL A 12 -36.26 -36.86 REMARK 500 4 THR A 54 -38.10 -36.05 REMARK 500 4 LYS A 61 156.61 -43.24 REMARK 500 4 LYS A 74 82.62 -64.10 REMARK 500 4 PRO A 84 -169.16 -69.69 REMARK 500 4 TYR A 87 149.92 -33.82 REMARK 500 4 LEU A 92 171.72 -50.12 REMARK 500 4 ILE A 131 -74.48 -57.73 REMARK 500 4 ASN A 137 53.87 -102.82 REMARK 500 4 SER A 138 -54.41 -133.54 REMARK 500 4 ASN A 144 38.85 71.40 REMARK 500 4 LYS A 146 121.61 -34.50 REMARK 500 4 SER A 149 -62.60 -102.93 REMARK 500 5 VAL A 12 -39.31 -38.24 REMARK 500 REMARK 500 THIS ENTRY HAS 242 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSI002012869.1 RELATED DB: TARGETDB DBREF 2DAW A 8 148 UNP Q9UIY3 RWDD2_HUMAN 1 141 SEQADV 2DAW GLY A 1 UNP Q9UIY3 CLONING ARTIFACT SEQADV 2DAW SER A 2 UNP Q9UIY3 CLONING ARTIFACT SEQADV 2DAW SER A 3 UNP Q9UIY3 CLONING ARTIFACT SEQADV 2DAW GLY A 4 UNP Q9UIY3 CLONING ARTIFACT SEQADV 2DAW SER A 5 UNP Q9UIY3 CLONING ARTIFACT SEQADV 2DAW SER A 6 UNP Q9UIY3 CLONING ARTIFACT SEQADV 2DAW GLY A 7 UNP Q9UIY3 CLONING ARTIFACT SEQADV 2DAW LEU A 90 UNP Q9UIY3 VAL 83 SEE REMARK 999 SEQADV 2DAW SER A 149 UNP Q9UIY3 CLONING ARTIFACT SEQADV 2DAW GLY A 150 UNP Q9UIY3 CLONING ARTIFACT SEQADV 2DAW PRO A 151 UNP Q9UIY3 CLONING ARTIFACT SEQADV 2DAW SER A 152 UNP Q9UIY3 CLONING ARTIFACT SEQADV 2DAW SER A 153 UNP Q9UIY3 CLONING ARTIFACT SEQADV 2DAW GLY A 154 UNP Q9UIY3 CLONING ARTIFACT SEQRES 1 A 154 GLY SER SER GLY SER SER GLY MET SER ALA SER VAL LYS SEQRES 2 A 154 GLU SER LEU GLN LEU GLN LEU LEU GLU MET GLU MET LEU SEQRES 3 A 154 PHE SER MET PHE PRO ASN GLN GLY GLU VAL LYS LEU GLU SEQRES 4 A 154 ASP VAL ASN ALA LEU THR ASN ILE LYS ARG TYR LEU GLU SEQRES 5 A 154 GLY THR ARG GLU ALA LEU PRO PRO LYS ILE GLU PHE VAL SEQRES 6 A 154 ILE THR LEU GLN ILE GLU GLU PRO LYS VAL LYS ILE ASP SEQRES 7 A 154 LEU GLN VAL THR MET PRO HIS SER TYR PRO TYR LEU ALA SEQRES 8 A 154 LEU GLN LEU PHE GLY ARG SER SER GLU LEU ASP ARG HIS SEQRES 9 A 154 GLN GLN LEU LEU LEU ASN LYS GLY LEU THR SER TYR ILE SEQRES 10 A 154 GLY THR PHE ASP PRO GLY GLU LEU CYS VAL CYS ALA ALA SEQRES 11 A 154 ILE GLN TRP LEU GLN ASP ASN SER ALA SER TYR PHE LEU SEQRES 12 A 154 ASN ARG LYS LEU VAL SER GLY PRO SER SER GLY HELIX 1 1 SER A 11 PHE A 30 1 20 HELIX 2 2 ASP A 40 ALA A 43 5 4 HELIX 3 3 LEU A 44 GLY A 53 1 10 HELIX 4 4 ASP A 102 GLY A 118 1 17 HELIX 5 5 CYS A 126 ASN A 137 1 12 HELIX 6 6 SER A 138 LEU A 143 1 6 SHEET 1 A 4 VAL A 36 LEU A 38 0 SHEET 2 A 4 ILE A 62 ILE A 70 -1 O VAL A 65 N LYS A 37 SHEET 3 A 4 VAL A 75 MET A 83 -1 O LEU A 79 N ILE A 66 SHEET 4 A 4 GLN A 93 ARG A 97 -1 O PHE A 95 N GLN A 80 CISPEP 1 GLU A 72 PRO A 73 1 0.10 CISPEP 2 TYR A 87 PRO A 88 1 -0.04 CISPEP 3 GLU A 72 PRO A 73 2 -0.03 CISPEP 4 TYR A 87 PRO A 88 2 -0.03 CISPEP 5 GLU A 72 PRO A 73 3 -0.03 CISPEP 6 TYR A 87 PRO A 88 3 -0.09 CISPEP 7 GLU A 72 PRO A 73 4 0.02 CISPEP 8 TYR A 87 PRO A 88 4 -0.06 CISPEP 9 GLU A 72 PRO A 73 5 0.03 CISPEP 10 TYR A 87 PRO A 88 5 -0.04 CISPEP 11 GLU A 72 PRO A 73 6 0.06 CISPEP 12 TYR A 87 PRO A 88 6 -0.13 CISPEP 13 GLU A 72 PRO A 73 7 0.00 CISPEP 14 TYR A 87 PRO A 88 7 -0.09 CISPEP 15 GLU A 72 PRO A 73 8 0.06 CISPEP 16 TYR A 87 PRO A 88 8 -0.05 CISPEP 17 GLU A 72 PRO A 73 9 0.05 CISPEP 18 TYR A 87 PRO A 88 9 0.01 CISPEP 19 GLU A 72 PRO A 73 10 -0.02 CISPEP 20 TYR A 87 PRO A 88 10 -0.09 CISPEP 21 GLU A 72 PRO A 73 11 -0.03 CISPEP 22 TYR A 87 PRO A 88 11 -0.09 CISPEP 23 GLU A 72 PRO A 73 12 -0.06 CISPEP 24 TYR A 87 PRO A 88 12 -0.04 CISPEP 25 GLU A 72 PRO A 73 13 -0.04 CISPEP 26 TYR A 87 PRO A 88 13 -0.04 CISPEP 27 GLU A 72 PRO A 73 14 -0.03 CISPEP 28 TYR A 87 PRO A 88 14 -0.05 CISPEP 29 GLU A 72 PRO A 73 15 -0.06 CISPEP 30 TYR A 87 PRO A 88 15 -0.05 CISPEP 31 GLU A 72 PRO A 73 16 -0.01 CISPEP 32 TYR A 87 PRO A 88 16 -0.02 CISPEP 33 GLU A 72 PRO A 73 17 -0.02 CISPEP 34 TYR A 87 PRO A 88 17 -0.05 CISPEP 35 GLU A 72 PRO A 73 18 -0.03 CISPEP 36 TYR A 87 PRO A 88 18 -0.11 CISPEP 37 GLU A 72 PRO A 73 19 0.03 CISPEP 38 TYR A 87 PRO A 88 19 -0.07 CISPEP 39 GLU A 72 PRO A 73 20 0.02 CISPEP 40 TYR A 87 PRO A 88 20 -0.11 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 9 2 Bytes