Header list of 1wf8.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 26-MAY-04 1WF8 TITLE SOLUTION STRUCTURE OF THE PDZ DOMAIN OF SPINOPHILIN/NEURABINII PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEURABIN-I; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PDZ DOMAIN; COMPND 5 SYNONYM: SPINOPHILIN/NEURABINII, NEURAL TISSUE-SPECIFIC F-ACTIN COMPND 6 BINDING PROTEIN I; COMPND 7 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 CNDA FH03567; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021030-40; SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS KEYWDS PDZ DOMAIN, SPINOPHILIN/NEURABINII PROTEIN, STRUCTURAL GENOMICS, KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, KEYWDS 4 PROTEIN BINDING 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 1WF8 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WF8 1 VERSN REVDAT 1 07-JUN-05 1WF8 0 JRNL AUTH X.QIN,F.HAYASHI,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE PDZ DOMAIN OF JRNL TITL 2 SPINOPHILIN/NEURABINII 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 1WF8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1000023514. 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 : 1.05MM 13C, 15N-LABELED PROTEIN; REMARK 210 20MM PINA(PH6.0); 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 LYS A 17 O GLY A 90 1.45 REMARK 500 H GLU A 9 O ARG A 98 1.50 REMARK 500 H ASP A 69 O ARG A 93 1.50 REMARK 500 O VAL A 44 H ASN A 62 1.54 REMARK 500 O MET A 29 H GLY A 41 1.55 REMARK 500 O GLN A 78 H ALA A 82 1.55 REMARK 500 O VAL A 13 H PHE A 94 1.58 REMARK 500 H ASP A 18 O GLY A 21 1.58 REMARK 500 H VAL A 68 O ILE A 71 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 5 90.50 -163.06 REMARK 500 1 GLU A 19 -29.80 -38.95 REMARK 500 1 ASP A 34 61.92 -116.93 REMARK 500 1 ALA A 35 -79.33 78.11 REMARK 500 1 GLU A 49 95.41 -66.68 REMARK 500 1 THR A 88 158.44 -38.73 REMARK 500 1 SER A 102 80.70 -164.39 REMARK 500 2 SER A 3 -59.31 -134.35 REMARK 500 2 SER A 5 147.89 178.59 REMARK 500 2 LYS A 17 158.01 -39.12 REMARK 500 2 ASP A 20 51.21 -119.57 REMARK 500 2 ASP A 34 47.64 -87.81 REMARK 500 2 ALA A 35 -77.48 76.32 REMARK 500 2 LEU A 37 59.74 -96.85 REMARK 500 2 LEU A 73 35.88 -98.63 REMARK 500 2 THR A 88 160.27 -39.83 REMARK 500 2 SER A 102 76.55 -109.46 REMARK 500 2 SER A 105 -58.77 -146.60 REMARK 500 3 SER A 3 165.35 66.45 REMARK 500 3 SER A 6 107.39 -44.86 REMARK 500 3 LYS A 17 155.74 -39.05 REMARK 500 3 ASP A 34 36.90 -97.27 REMARK 500 3 LEU A 37 61.73 -104.76 REMARK 500 3 ARG A 58 -70.03 -51.40 REMARK 500 3 THR A 88 164.25 -42.18 REMARK 500 4 LYS A 17 156.81 -40.06 REMARK 500 4 ASP A 34 37.25 -99.08 REMARK 500 4 LEU A 37 61.86 -102.13 REMARK 500 4 ARG A 58 -67.11 -91.07 REMARK 500 4 THR A 88 168.18 -44.12 REMARK 500 4 SER A 102 77.53 -164.37 REMARK 500 4 SER A 105 147.19 178.80 REMARK 500 5 SER A 3 99.32 51.96 REMARK 500 5 ASP A 20 51.41 -118.04 REMARK 500 5 GLU A 49 95.66 -68.36 REMARK 500 5 ASN A 62 -0.60 77.34 REMARK 500 5 THR A 88 155.73 -37.18 REMARK 500 5 SER A 102 88.71 -150.86 REMARK 500 5 SER A 105 -58.15 -150.60 REMARK 500 6 SER A 5 -64.42 -159.03 REMARK 500 6 LYS A 17 156.86 -38.85 REMARK 500 6 ASP A 34 40.75 -98.34 REMARK 500 6 LEU A 37 61.70 -102.06 REMARK 500 6 ASP A 69 19.70 53.81 REMARK 500 6 THR A 88 164.19 -42.35 REMARK 500 6 SER A 102 69.31 178.88 REMARK 500 7 SER A 5 155.95 63.07 REMARK 500 7 LYS A 17 155.70 -40.39 REMARK 500 7 THR A 88 160.86 -39.77 REMARK 500 7 SER A 102 56.11 70.95 REMARK 500 REMARK 500 THIS ENTRY HAS 154 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSK002001196 RELATED DB: TARGETDB DBREF 1WF8 A 8 101 UNP Q9ULJ8 NEB1_HUMAN 144 237 SEQADV 1WF8 GLY A 1 UNP Q9ULJ8 CLONING ARTIFACT SEQADV 1WF8 SER A 2 UNP Q9ULJ8 CLONING ARTIFACT SEQADV 1WF8 SER A 3 UNP Q9ULJ8 CLONING ARTIFACT SEQADV 1WF8 GLY A 4 UNP Q9ULJ8 CLONING ARTIFACT SEQADV 1WF8 SER A 5 UNP Q9ULJ8 CLONING ARTIFACT SEQADV 1WF8 SER A 6 UNP Q9ULJ8 CLONING ARTIFACT SEQADV 1WF8 GLY A 7 UNP Q9ULJ8 CLONING ARTIFACT SEQADV 1WF8 SER A 102 UNP Q9ULJ8 CLONING ARTIFACT SEQADV 1WF8 GLY A 103 UNP Q9ULJ8 CLONING ARTIFACT SEQADV 1WF8 PRO A 104 UNP Q9ULJ8 CLONING ARTIFACT SEQADV 1WF8 SER A 105 UNP Q9ULJ8 CLONING ARTIFACT SEQADV 1WF8 SER A 106 UNP Q9ULJ8 CLONING ARTIFACT SEQADV 1WF8 GLY A 107 UNP Q9ULJ8 CLONING ARTIFACT SEQRES 1 A 107 GLY SER SER GLY SER SER GLY LEU GLU LEU PHE PRO VAL SEQRES 2 A 107 GLU LEU GLU LYS ASP GLU ASP GLY LEU GLY ILE SER ILE SEQRES 3 A 107 ILE GLY MET GLY VAL GLY ALA ASP ALA GLY LEU GLU LYS SEQRES 4 A 107 LEU GLY ILE PHE VAL LYS THR VAL THR GLU GLY GLY ALA SEQRES 5 A 107 ALA GLN ARG ASP GLY ARG ILE GLN VAL ASN ASP GLN ILE SEQRES 6 A 107 VAL GLU VAL ASP GLY ILE SER LEU VAL GLY VAL THR GLN SEQRES 7 A 107 ASN PHE ALA ALA THR VAL LEU ARG ASN THR LYS GLY ASN SEQRES 8 A 107 VAL ARG PHE VAL ILE GLY ARG GLU LYS PRO SER GLY PRO SEQRES 9 A 107 SER SER GLY HELIX 1 1 GLY A 51 GLY A 57 1 7 HELIX 2 2 THR A 77 THR A 88 1 12 SHEET 1 A 4 LEU A 8 GLU A 16 0 SHEET 2 A 4 ASN A 91 GLU A 99 -1 O ARG A 98 N GLU A 9 SHEET 3 A 4 ILE A 65 VAL A 68 -1 N GLU A 67 O VAL A 95 SHEET 4 A 4 ILE A 71 SER A 72 -1 O ILE A 71 N VAL A 68 SHEET 1 B 2 ILE A 24 VAL A 31 0 SHEET 2 B 2 LYS A 39 VAL A 47 -1 O GLY A 41 N MET A 29 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