Header list of 1wln.pdb file
Complete list - r 2 2 Bytes
HEADER CELL ADHESION 28-JUN-04 1WLN TITLE SOLUTION STRUCTURE OF THE FHA DOMAIN OF MOUSE AFADIN 6 COMPND MOL_ID: 1; COMPND 2 MOLECULE: AFADIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FHA DOMAIN; COMPND 5 SYNONYM: AF-6 PROTEIN, AFADIN 6; COMPND 6 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 LIBRARY 4932441D06; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P020805-25; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS BETA SANDWICH, FHA DOMAIN, AF-6, S-AFADIN, STRUCTURAL GENOMICS, KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, KEYWDS 4 CELL ADHESION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR F.HAYASHI,Y.HIRATA,P.GUENTERT,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1WLN 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WLN 1 VERSN REVDAT 1 12-JUL-05 1WLN 0 JRNL AUTH F.HAYASHI,Y.HIRATA,P.GUENTERT,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE FHA DOMAIN OF MOUSE AFADIN 6 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1C, CYANA 1.0.7 REMARK 3 AUTHORS : VARIAN (VNMR), GUENTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WLN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1000023713. 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 : 0.7MM FHA DOMAIN; U-15N,13C; REMARK 210 20MM PHOSPHATE BUFFER NA; 100MM REMARK 210 NACL; 0.02% NAN3; 1MMDTT REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.902, 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 LOWEST REMARK 210 ENERGY, TARGET 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 GLY A 41 H LEU A 52 1.56 REMARK 500 H LEU A 17 O VAL A 108 1.57 REMARK 500 O PRO A 12 H LEU A 33 1.59 REMARK 500 H MET A 67 O VAL A 70 1.60 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 -61.22 -133.34 REMARK 500 1 SER A 18 174.27 -51.85 REMARK 500 1 SER A 24 179.65 -55.88 REMARK 500 1 LEU A 35 157.91 -40.09 REMARK 500 1 SER A 36 163.57 85.59 REMARK 500 1 ASN A 48 60.84 -113.27 REMARK 500 1 HIS A 60 78.69 -107.67 REMARK 500 1 HIS A 61 -70.59 -69.64 REMARK 500 1 ASP A 68 68.63 67.55 REMARK 500 1 ALA A 80 97.99 -63.61 REMARK 500 1 ASP A 85 37.61 80.67 REMARK 500 1 GLU A 91 -174.88 -179.59 REMARK 500 1 THR A 92 107.01 -51.46 REMARK 500 1 THR A 105 56.15 37.70 REMARK 500 1 SER A 106 -43.91 -166.50 REMARK 500 1 SER A 118 88.38 51.89 REMARK 500 1 SER A 119 143.41 64.26 REMARK 500 2 SER A 3 -58.61 -134.89 REMARK 500 2 GLU A 9 45.17 -102.74 REMARK 500 2 LYS A 10 30.67 -165.02 REMARK 500 2 SER A 18 171.99 -52.79 REMARK 500 2 SER A 24 54.08 -150.07 REMARK 500 2 ARG A 25 57.30 -146.68 REMARK 500 2 ASP A 26 179.42 66.52 REMARK 500 2 LEU A 35 156.60 -40.17 REMARK 500 2 SER A 36 162.88 85.83 REMARK 500 2 PHE A 45 -67.50 -104.54 REMARK 500 2 ASN A 48 62.99 -115.26 REMARK 500 2 HIS A 60 77.63 -104.82 REMARK 500 2 HIS A 61 -71.09 -67.27 REMARK 500 2 ASP A 68 61.11 67.09 REMARK 500 2 ASP A 85 31.46 74.98 REMARK 500 2 GLU A 91 -175.06 -177.36 REMARK 500 2 THR A 92 102.57 -55.39 REMARK 500 2 THR A 105 57.82 178.26 REMARK 500 2 SER A 106 -38.46 -179.10 REMARK 500 2 SER A 118 -56.07 -160.67 REMARK 500 3 LYS A 10 43.74 -152.62 REMARK 500 3 SER A 18 172.34 -57.29 REMARK 500 3 SER A 36 -134.61 172.44 REMARK 500 3 PHE A 45 -62.15 -138.71 REMARK 500 3 ASN A 48 62.02 -103.68 REMARK 500 3 ASP A 68 75.39 65.97 REMARK 500 3 THR A 92 105.59 -58.92 REMARK 500 3 THR A 105 52.07 37.74 REMARK 500 3 SER A 106 -54.50 -156.44 REMARK 500 3 SER A 119 100.08 51.86 REMARK 500 4 LYS A 10 -39.55 -172.55 REMARK 500 4 SER A 18 174.95 -57.88 REMARK 500 4 SER A 24 177.65 -59.89 REMARK 500 REMARK 500 THIS ENTRY HAS 335 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMT007011839.1 RELATED DB: TARGETDB DBREF 1WLN A 8 114 UNP Q9QZQ1 AFAD_MOUSE 381 487 SEQADV 1WLN GLY A 1 UNP Q9QZQ1 CLONING ARTIFACT SEQADV 1WLN SER A 2 UNP Q9QZQ1 CLONING ARTIFACT SEQADV 1WLN SER A 3 UNP Q9QZQ1 CLONING ARTIFACT SEQADV 1WLN GLY A 4 UNP Q9QZQ1 CLONING ARTIFACT SEQADV 1WLN SER A 5 UNP Q9QZQ1 CLONING ARTIFACT SEQADV 1WLN SER A 6 UNP Q9QZQ1 CLONING ARTIFACT SEQADV 1WLN GLY A 7 UNP Q9QZQ1 CLONING ARTIFACT SEQADV 1WLN SER A 115 UNP Q9QZQ1 CLONING ARTIFACT SEQADV 1WLN GLY A 116 UNP Q9QZQ1 CLONING ARTIFACT SEQADV 1WLN PRO A 117 UNP Q9QZQ1 CLONING ARTIFACT SEQADV 1WLN SER A 118 UNP Q9QZQ1 CLONING ARTIFACT SEQADV 1WLN SER A 119 UNP Q9QZQ1 CLONING ARTIFACT SEQADV 1WLN GLY A 120 UNP Q9QZQ1 CLONING ARTIFACT SEQRES 1 A 120 GLY SER SER GLY SER SER GLY PRO GLU LYS LEU PRO TYR SEQRES 2 A 120 LEU VAL GLU LEU SER PRO ASP GLY SER ASP SER ARG ASP SEQRES 3 A 120 LYS PRO LYS LEU TYR ARG LEU GLN LEU SER VAL THR GLU SEQRES 4 A 120 VAL GLY THR GLU LYS PHE ASP ASP ASN SER ILE GLN LEU SEQRES 5 A 120 PHE GLY PRO GLY ILE GLN PRO HIS HIS CYS ASP LEU THR SEQRES 6 A 120 ASN MET ASP GLY VAL VAL THR VAL THR PRO ARG SER MET SEQRES 7 A 120 ASP ALA GLU THR TYR VAL ASP GLY GLN ARG ILE SER GLU SEQRES 8 A 120 THR THR MET LEU GLN SER GLY MET ARG LEU GLN PHE GLY SEQRES 9 A 120 THR SER HIS VAL PHE LYS PHE VAL ASP PRO SER GLY PRO SEQRES 10 A 120 SER SER GLY HELIX 1 1 GLY A 7 LEU A 11 5 5 SHEET 1 A 5 LEU A 30 ARG A 32 0 SHEET 2 A 5 TYR A 13 LEU A 17 -1 N LEU A 14 O TYR A 31 SHEET 3 A 5 HIS A 107 VAL A 112 -1 O VAL A 108 N LEU A 17 SHEET 4 A 5 ARG A 100 PHE A 103 -1 N PHE A 103 O HIS A 107 SHEET 5 A 5 THR A 82 VAL A 84 -1 N TYR A 83 O GLN A 102 SHEET 1 B 4 SER A 36 GLU A 39 0 SHEET 2 B 4 CYS A 62 ASN A 66 -1 O LEU A 64 N THR A 38 SHEET 3 B 4 VAL A 71 PRO A 75 -1 O THR A 74 N ASP A 63 SHEET 4 B 4 THR A 93 LEU A 95 -1 O LEU A 95 N VAL A 71 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