Header list of 2cp5.pdb file
Complete list - r 9 2 Bytes
HEADER PROTEIN BINDING 19-MAY-05 2CP5
TITLE SOLUTION STRUCTURE OF THE 1ST CAP-GLY DOMAIN IN HUMAN 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: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FB2383_D01;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040816-08;
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 2CP5 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CP5 1 VERSN
REVDAT 1 19-NOV-05 2CP5 0
JRNL AUTH K.SAITO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE 1ST CAP-GLY DOMAIN IN HUMAN
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 2CP5 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_1000024470.
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 94.67 -60.41
REMARK 500 1 MET A 8 97.03 -173.62
REMARK 500 1 SER A 9 175.70 60.44
REMARK 500 1 PRO A 13 -173.02 -53.51
REMARK 500 1 ALA A 18 -53.18 -178.37
REMARK 500 1 LYS A 24 77.55 -150.26
REMARK 500 1 LEU A 30 107.43 60.94
REMARK 500 1 LYS A 31 -60.53 -109.79
REMARK 500 1 SER A 45 42.62 -95.63
REMARK 500 1 SER A 46 -178.66 59.50
REMARK 500 1 GLU A 47 125.95 63.35
REMARK 500 1 ALA A 49 -169.07 60.28
REMARK 500 1 SER A 50 -70.10 -130.42
REMARK 500 1 SER A 51 115.45 61.27
REMARK 500 1 THR A 52 -63.34 -171.52
REMARK 500 1 PRO A 53 92.78 -59.16
REMARK 500 1 THR A 57 89.77 60.19
REMARK 500 1 GLU A 60 -178.56 60.21
REMARK 500 1 VAL A 62 99.39 -69.06
REMARK 500 1 ASP A 63 32.58 -142.89
REMARK 500 1 ASN A 76 49.13 -179.22
REMARK 500 1 LYS A 77 82.68 -167.65
REMARK 500 1 LYS A 105 -54.51 -143.24
REMARK 500 1 LYS A 122 -47.43 -150.07
REMARK 500 1 LYS A 134 164.17 60.21
REMARK 500 1 PRO A 138 -176.72 -52.25
REMARK 500 2 SER A 14 -62.14 -146.75
REMARK 500 2 LEU A 16 159.92 60.66
REMARK 500 2 LYS A 17 96.87 60.56
REMARK 500 2 PRO A 19 -169.86 -70.13
REMARK 500 2 ILE A 22 -39.07 -178.21
REMARK 500 2 LEU A 23 79.53 63.85
REMARK 500 2 LYS A 24 84.97 59.68
REMARK 500 2 SER A 27 165.21 61.25
REMARK 500 2 THR A 28 31.18 -162.75
REMARK 500 2 LEU A 30 -62.78 -170.80
REMARK 500 2 LYS A 31 165.39 60.51
REMARK 500 2 THR A 34 -53.62 -167.20
REMARK 500 2 LYS A 48 116.38 62.43
REMARK 500 2 ALA A 49 -56.31 -120.28
REMARK 500 2 SER A 50 -62.71 -173.12
REMARK 500 2 SER A 51 -45.07 -158.45
REMARK 500 2 THR A 52 63.44 63.71
REMARK 500 2 SER A 54 -179.06 -170.80
REMARK 500 2 GLU A 59 28.98 -158.83
REMARK 500 2 PHE A 61 97.36 59.95
REMARK 500 2 VAL A 62 39.40 -98.28
REMARK 500 2 ASP A 63 179.87 61.56
REMARK 500 2 ASN A 76 52.76 -177.89
REMARK 500 2 LYS A 77 82.04 -177.72
REMARK 500
REMARK 500 THIS ENTRY HAS 494 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSO002001267.1 RELATED DB: TARGETDB
DBREF 2CP5 A 8 135 UNP P30622 REST_HUMAN 1 128
SEQADV 2CP5 GLY A 1 UNP P30622 CLONING ARTIFACT
SEQADV 2CP5 SER A 2 UNP P30622 CLONING ARTIFACT
SEQADV 2CP5 SER A 3 UNP P30622 CLONING ARTIFACT
SEQADV 2CP5 GLY A 4 UNP P30622 CLONING ARTIFACT
SEQADV 2CP5 SER A 5 UNP P30622 CLONING ARTIFACT
SEQADV 2CP5 SER A 6 UNP P30622 CLONING ARTIFACT
SEQADV 2CP5 GLY A 7 UNP P30622 CLONING ARTIFACT
SEQADV 2CP5 SER A 136 UNP P30622 CLONING ARTIFACT
SEQADV 2CP5 GLY A 137 UNP P30622 CLONING ARTIFACT
SEQADV 2CP5 PRO A 138 UNP P30622 CLONING ARTIFACT
SEQADV 2CP5 SER A 139 UNP P30622 CLONING ARTIFACT
SEQADV 2CP5 SER A 140 UNP P30622 CLONING ARTIFACT
SEQADV 2CP5 GLY A 141 UNP P30622 CLONING ARTIFACT
SEQRES 1 A 141 GLY SER SER GLY SER SER GLY MET SER MET LEU LYS PRO
SEQRES 2 A 141 SER GLY LEU LYS ALA PRO THR LYS ILE LEU LYS PRO GLY
SEQRES 3 A 141 SER THR ALA LEU LYS THR PRO THR ALA VAL VAL ALA PRO
SEQRES 4 A 141 VAL GLU LYS THR ILE SER SER GLU LYS ALA SER SER THR
SEQRES 5 A 141 PRO SER SER GLU THR GLN GLU GLU PHE VAL ASP ASP PHE
SEQRES 6 A 141 ARG VAL GLY GLU ARG VAL TRP VAL ASN GLY ASN LYS PRO
SEQRES 7 A 141 GLY PHE ILE GLN PHE LEU GLY GLU THR GLN PHE ALA PRO
SEQRES 8 A 141 GLY GLN TRP ALA GLY ILE VAL LEU ASP GLU PRO ILE GLY
SEQRES 9 A 141 LYS ASN ASP GLY SER VAL ALA GLY VAL ARG TYR PHE GLN
SEQRES 10 A 141 CYS GLU PRO LEU LYS GLY ILE PHE THR ARG PRO SER LYS
SEQRES 11 A 141 LEU THR ARG LYS VAL SER GLY PRO SER SER GLY
HELIX 1 1 ARG A 127 SER A 129 5 3
SHEET 1 A 5 GLY A 123 THR A 126 0
SHEET 2 A 5 GLN A 93 LEU A 99 -1 N ILE A 97 O ILE A 124
SHEET 3 A 5 PRO A 78 GLU A 86 -1 N GLY A 85 O TRP A 94
SHEET 4 A 5 ARG A 70 VAL A 73 -1 N VAL A 71 O GLY A 79
SHEET 5 A 5 LEU A 131 THR A 132 -1 O THR A 132 N TRP A 72
SHEET 1 B 2 SER A 109 VAL A 110 0
SHEET 2 B 2 VAL A 113 ARG A 114 -1 O VAL A 113 N VAL A 110
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