Header list of 2cp7.pdb file
Complete list - r 9 2 Bytes
HEADER PROTEIN BINDING 19-MAY-05 2CP7 TITLE SOLUTION STRUCTURE OF THE 1ST CAP-GLY DOMAIN IN MOUSE CLIP-170/RESTIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: RESTIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CAP-GLY DOMAIN; COMPND 5 SYNONYM: CYTOPLASMIC LINKER PROTEIN-170 ALPHA-2, CLIP-170, REED- COMPND 6 STERNBERG INTERMEDIATE FILAMENT ASSOCIATED PROTEIN; COMPND 7 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 4631429H07; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040301-92; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS MICROTUBULE BINDING, CYTOSKELETON ASSOCIATED PROTEIN, RESTIN, KEYWDS 2 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL KEYWDS 3 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS KEYWDS 4 INITIATIVE, RSGI, PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.SAITO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2CP7 1 REMARK SEQADV REVDAT 2 24-FEB-09 2CP7 1 VERSN REVDAT 1 19-NOV-05 2CP7 0 JRNL AUTH K.SAITO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE 1ST CAP-GLY DOMAIN IN MOUSE JRNL TITL 2 CLIP-170/RESTIN 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, CNS 1.1 REMARK 3 AUTHORS : BRUKER (XWINNMR), REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI, REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2CP7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000024472. 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 : 120 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM PROTEIN, 20MM D-TRIS-HCL, REMARK 210 PH7.0, 100MM NACL, 1MM D-DTT, REMARK 210 0.02% NAN3, 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, CNS REMARK 210 1.1 REMARK 210 METHOD USED : SIMULATED ANNEALING 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 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 3 109.50 60.43 REMARK 500 1 SER A 5 102.37 60.51 REMARK 500 1 ASN A 19 37.21 -176.81 REMARK 500 1 GLN A 25 -51.96 -120.03 REMARK 500 1 ILE A 46 31.98 -145.76 REMARK 500 1 LYS A 48 -48.04 -132.23 REMARK 500 1 TYR A 58 -48.54 -146.58 REMARK 500 1 LYS A 73 30.01 -95.62 REMARK 500 1 LYS A 77 -176.77 60.06 REMARK 500 1 SER A 79 -71.02 -143.39 REMARK 500 2 SER A 3 -65.73 -145.63 REMARK 500 2 SER A 5 110.82 60.56 REMARK 500 2 ASN A 19 36.42 -175.84 REMARK 500 2 LYS A 20 91.50 -161.36 REMARK 500 2 TYR A 58 -65.76 -128.43 REMARK 500 2 LYS A 73 33.66 -97.74 REMARK 500 2 LYS A 77 170.19 59.80 REMARK 500 2 PRO A 81 98.16 -54.06 REMARK 500 2 SER A 83 -51.56 -153.47 REMARK 500 3 SER A 3 84.92 60.52 REMARK 500 3 SER A 5 -58.18 -123.16 REMARK 500 3 ASN A 19 40.36 -177.39 REMARK 500 3 LYS A 20 86.65 -162.20 REMARK 500 3 PRO A 34 -168.07 -72.87 REMARK 500 3 ASN A 49 149.50 -170.85 REMARK 500 3 LYS A 73 33.73 -97.03 REMARK 500 3 LYS A 77 154.97 61.15 REMARK 500 4 SER A 2 85.02 60.21 REMARK 500 4 ASN A 19 36.95 -177.58 REMARK 500 4 LYS A 20 93.73 -161.34 REMARK 500 4 TYR A 58 -49.48 -138.80 REMARK 500 4 LYS A 73 30.19 -98.02 REMARK 500 4 LYS A 77 147.85 62.80 REMARK 500 4 SER A 79 -77.97 64.95 REMARK 500 4 SER A 82 110.72 60.29 REMARK 500 5 ASN A 19 36.66 -176.33 REMARK 500 5 LYS A 20 86.75 -164.17 REMARK 500 5 LYS A 77 -168.67 59.07 REMARK 500 6 ASN A 19 31.81 -165.49 REMARK 500 6 LYS A 20 84.16 -160.42 REMARK 500 6 LYS A 48 -46.86 -152.47 REMARK 500 6 ASP A 50 36.19 -149.74 REMARK 500 6 LYS A 77 166.58 61.23 REMARK 500 6 SER A 79 162.23 60.04 REMARK 500 7 SER A 2 -178.77 60.62 REMARK 500 7 ASN A 19 38.79 -178.75 REMARK 500 7 LYS A 20 88.04 -159.44 REMARK 500 7 LYS A 48 -46.74 -133.85 REMARK 500 7 LYS A 73 33.75 -97.23 REMARK 500 7 LYS A 77 176.74 60.63 REMARK 500 REMARK 500 THIS ENTRY HAS 153 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 2CP7 A 8 78 UNP Q922J3 Q922J3_MOUSE 58 128 SEQADV 2CP7 GLY A 1 UNP Q922J3 CLONING ARTIFACT SEQADV 2CP7 SER A 2 UNP Q922J3 CLONING ARTIFACT SEQADV 2CP7 SER A 3 UNP Q922J3 CLONING ARTIFACT SEQADV 2CP7 GLY A 4 UNP Q922J3 CLONING ARTIFACT SEQADV 2CP7 SER A 5 UNP Q922J3 CLONING ARTIFACT SEQADV 2CP7 SER A 6 UNP Q922J3 CLONING ARTIFACT SEQADV 2CP7 GLY A 7 UNP Q922J3 CLONING ARTIFACT SEQADV 2CP7 SER A 79 UNP Q922J3 CLONING ARTIFACT SEQADV 2CP7 GLY A 80 UNP Q922J3 CLONING ARTIFACT SEQADV 2CP7 PRO A 81 UNP Q922J3 CLONING ARTIFACT SEQADV 2CP7 SER A 82 UNP Q922J3 CLONING ARTIFACT SEQADV 2CP7 SER A 83 UNP Q922J3 CLONING ARTIFACT SEQADV 2CP7 GLY A 84 UNP Q922J3 CLONING ARTIFACT SEQRES 1 A 84 GLY SER SER GLY SER SER GLY PHE ARG VAL GLY GLU ARG SEQRES 2 A 84 VAL TRP VAL ASN GLY ASN LYS PRO GLY PHE ILE GLN PHE SEQRES 3 A 84 LEU GLY GLU THR GLN PHE ALA PRO GLY GLN TRP ALA GLY SEQRES 4 A 84 ILE VAL LEU ASP GLU PRO ILE GLY LYS ASN ASP GLY SER SEQRES 5 A 84 VAL ALA GLY VAL ARG TYR PHE GLN CYS GLU PRO LEU LYS SEQRES 6 A 84 GLY ILE PHE THR ARG PRO SER LYS LEU THR ARG LYS VAL SEQRES 7 A 84 SER GLY PRO SER SER GLY HELIX 1 1 ARG A 70 SER A 72 5 3 SHEET 1 A 5 ILE A 67 THR A 69 0 SHEET 2 A 5 GLN A 36 LEU A 42 -1 N ILE A 40 O ILE A 67 SHEET 3 A 5 PRO A 21 GLU A 29 -1 N PHE A 23 O VAL A 41 SHEET 4 A 5 ARG A 13 VAL A 16 -1 N VAL A 14 O GLY A 22 SHEET 5 A 5 LEU A 74 THR A 75 -1 O THR A 75 N TRP A 15 SHEET 1 B 2 SER A 52 VAL A 53 0 SHEET 2 B 2 VAL A 56 ARG A 57 -1 O VAL A 56 N VAL A 53 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