Header list of 1wf5.pdb file
Complete list - r 2 2 Bytes
HEADER CELL ADHESION 26-MAY-04 1WF5 TITLE SOLUTION STRUCTURE OF THE FIRST FN3 DOMAIN OF SIDEKICK-2 PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: SIDEKICK 2 PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FNIII 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: KAZUSA CDNA FH00815; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040223-40; SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS KEYWDS FNIII DOMAIN, SIDEKICK-2, STRUCTURAL GENOMICS, NPPSFA, NATIONAL KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, CELL ADHESION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR X.QIN,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS AUTHOR 2 INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1WF5 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WF5 1 VERSN REVDAT 1 07-JUN-05 1WF5 0 JRNL AUTH X.QIN,F.HAYASHI,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE FIRST FN3 DOMAIN OF SIDEKICK-2 JRNL TITL 2 PROTEIN 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 1WF5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-MAY-04. REMARK 100 THE DEPOSITION ID IS D_1000023511. 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 : 1.29MM 13C,15N-LABELED PROTEIN; REMARK 210 20MM PINA(PH7.0); 100MM NACL; REMARK 210 1MM D-DTT; 0.02%NAN3 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 0.854, 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 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 H VAL A 84 OH TYR A 89 1.53 REMARK 500 O GLY A 46 H SER A 48 1.55 REMARK 500 H LEU A 38 O VAL A 78 1.56 REMARK 500 H TYR A 89 O VAL A 111 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 -57.60 -176.80 REMARK 500 1 SER A 6 -59.89 -137.94 REMARK 500 1 ARG A 8 -57.83 -161.28 REMARK 500 1 SER A 9 136.25 62.45 REMARK 500 1 HIS A 11 122.15 -177.73 REMARK 500 1 LEU A 12 172.08 66.95 REMARK 500 1 ARG A 13 154.40 -46.96 REMARK 500 1 HIS A 23 54.13 37.88 REMARK 500 1 VAL A 31 -49.18 -178.01 REMARK 500 1 ASN A 47 -53.91 69.54 REMARK 500 1 ILE A 51 -55.33 -124.66 REMARK 500 1 GLU A 59 -167.11 -68.33 REMARK 500 1 ASN A 60 96.66 -55.09 REMARK 500 1 VAL A 66 101.20 -55.23 REMARK 500 1 ARG A 92 107.73 -167.46 REMARK 500 1 GLU A 109 127.44 -38.07 REMARK 500 1 ARG A 110 99.62 -38.92 REMARK 500 2 SER A 5 110.06 62.15 REMARK 500 2 ARG A 8 165.61 57.06 REMARK 500 2 LEU A 12 -177.67 60.08 REMARK 500 2 HIS A 23 54.52 37.87 REMARK 500 2 LEU A 28 173.62 -47.29 REMARK 500 2 VAL A 31 -54.42 -150.56 REMARK 500 2 ASN A 47 -45.55 76.08 REMARK 500 2 GLU A 59 -147.41 -62.04 REMARK 500 2 VAL A 66 101.06 -57.07 REMARK 500 2 ARG A 92 108.90 -170.33 REMARK 500 2 ARG A 110 96.78 -37.64 REMARK 500 2 SER A 119 96.94 48.93 REMARK 500 3 SER A 2 91.33 59.85 REMARK 500 3 SER A 6 -55.77 -177.51 REMARK 500 3 ALA A 10 -62.34 -108.51 REMARK 500 3 LEU A 12 108.78 64.68 REMARK 500 3 PRO A 18 -168.67 -75.00 REMARK 500 3 LEU A 28 173.34 -48.85 REMARK 500 3 VAL A 31 -42.03 178.68 REMARK 500 3 ASN A 47 32.65 -170.77 REMARK 500 3 GLU A 59 -153.55 -62.63 REMARK 500 3 ASN A 60 92.35 -69.29 REMARK 500 3 TRP A 64 108.83 -49.40 REMARK 500 3 VAL A 66 100.60 -55.84 REMARK 500 3 ALA A 86 46.48 74.74 REMARK 500 3 ARG A 92 114.01 -179.23 REMARK 500 3 LYS A 106 163.46 -42.86 REMARK 500 3 THR A 108 154.39 -44.52 REMARK 500 3 ARG A 110 104.87 -38.04 REMARK 500 3 GLU A 115 153.70 -37.56 REMARK 500 4 SER A 2 -58.55 -144.14 REMARK 500 4 ARG A 8 -57.58 -137.77 REMARK 500 4 HIS A 11 -75.48 -90.55 REMARK 500 REMARK 500 THIS ENTRY HAS 318 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSK002101486.4 RELATED DB: TARGETDB DBREF 1WF5 A 8 115 UNP Q58EX2 Q58EX2_HUMAN 204 311 SEQADV 1WF5 GLY A 1 UNP Q58EX2 CLONING ARTIFACT SEQADV 1WF5 SER A 2 UNP Q58EX2 CLONING ARTIFACT SEQADV 1WF5 SER A 3 UNP Q58EX2 CLONING ARTIFACT SEQADV 1WF5 GLY A 4 UNP Q58EX2 CLONING ARTIFACT SEQADV 1WF5 SER A 5 UNP Q58EX2 CLONING ARTIFACT SEQADV 1WF5 SER A 6 UNP Q58EX2 CLONING ARTIFACT SEQADV 1WF5 GLY A 7 UNP Q58EX2 CLONING ARTIFACT SEQADV 1WF5 SER A 116 UNP Q58EX2 CLONING ARTIFACT SEQADV 1WF5 GLY A 117 UNP Q58EX2 CLONING ARTIFACT SEQADV 1WF5 PRO A 118 UNP Q58EX2 CLONING ARTIFACT SEQADV 1WF5 SER A 119 UNP Q58EX2 CLONING ARTIFACT SEQADV 1WF5 SER A 120 UNP Q58EX2 CLONING ARTIFACT SEQADV 1WF5 GLY A 121 UNP Q58EX2 CLONING ARTIFACT SEQRES 1 A 121 GLY SER SER GLY SER SER GLY ARG SER ALA HIS LEU ARG SEQRES 2 A 121 VAL ARG GLN LEU PRO HIS ALA PRO GLU HIS PRO VAL ALA SEQRES 3 A 121 THR LEU SER THR VAL GLU ARG ARG ALA ILE ASN LEU THR SEQRES 4 A 121 TRP THR LYS PRO PHE ASP GLY ASN SER PRO LEU ILE ARG SEQRES 5 A 121 TYR ILE LEU GLU MET SER GLU ASN ASN ALA PRO TRP THR SEQRES 6 A 121 VAL LEU LEU ALA SER VAL ASP PRO LYS ALA THR SER VAL SEQRES 7 A 121 THR VAL LYS GLY LEU VAL PRO ALA ARG SER TYR GLN PHE SEQRES 8 A 121 ARG LEU CYS ALA VAL ASN ASP VAL GLY LYS GLY GLN PHE SEQRES 9 A 121 SER LYS ASP THR GLU ARG VAL SER LEU PRO GLU SER GLY SEQRES 10 A 121 PRO SER SER GLY SHEET 1 A 3 VAL A 25 LEU A 28 0 SHEET 2 A 3 ALA A 35 THR A 39 -1 O ASN A 37 N THR A 27 SHEET 3 A 3 SER A 77 LYS A 81 -1 O VAL A 78 N LEU A 38 SHEET 1 B 4 THR A 65 LEU A 68 0 SHEET 2 B 4 LEU A 50 SER A 58 -1 N MET A 57 O THR A 65 SHEET 3 B 4 SER A 88 ASN A 97 -1 O VAL A 96 N ILE A 51 SHEET 4 B 4 LYS A 101 PHE A 104 -1 O GLY A 102 N ALA A 95 SHEET 1 C 4 THR A 65 LEU A 68 0 SHEET 2 C 4 LEU A 50 SER A 58 -1 N MET A 57 O THR A 65 SHEET 3 C 4 SER A 88 ASN A 97 -1 O VAL A 96 N ILE A 51 SHEET 4 C 4 VAL A 111 SER A 112 -1 O VAL A 111 N TYR A 89 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