Header list of 2cp3.pdb file
Complete list - r 9 2 Bytes
HEADER PROTEIN BINDING 19-MAY-05 2CP3
TITLE SOLUTION STRUCTURE OF THE 2ND CAP-GLY DOMAIN IN HUMAN CLIP-115/CYLN2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CLIP-115;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CAP-GLY DOMAIN;
COMPND 5 SYNONYM: KIAA0291; SIMILAR RODENT CYTOPLASMIC LINKER PROTEIN CLIP-115
COMPND 6 AND RESTIN;
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 CDNA FH25236;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040301-94;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS MICROTUBULE BINDING, CYTOSKELETON ASSOCIATED PROTEIN, CYLN2,
KEYWDS 2 KIAA0291, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 3 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS 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 2CP3 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CP3 1 VERSN
REVDAT 1 19-NOV-05 2CP3 0
JRNL AUTH K.SAITO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE 2ND CAP-GLY DOMAIN IN HUMAN
JRNL TITL 2 CLIP-115/CYLN2
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), BRUNGER, A.T. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CP3 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_1000024469.
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 LEU A 8 126.87 63.59
REMARK 500 1 THR A 19 -43.47 -173.42
REMARK 500 1 PHE A 32 -46.86 -139.75
REMARK 500 1 PRO A 45 63.37 -69.87
REMARK 500 1 LYS A 64 70.58 61.37
REMARK 500 1 PHE A 65 -45.23 -159.84
REMARK 500 1 SER A 83 -51.84 -138.55
REMARK 500 2 SER A 2 -176.93 60.57
REMARK 500 2 SER A 3 -175.22 60.69
REMARK 500 2 SER A 6 164.62 60.76
REMARK 500 2 THR A 19 -71.49 -156.71
REMARK 500 2 PRO A 45 64.60 -68.50
REMARK 500 2 LYS A 64 63.23 60.99
REMARK 500 2 PHE A 65 -45.12 -159.91
REMARK 500 2 SER A 79 84.72 -155.73
REMARK 500 2 SER A 83 84.07 60.53
REMARK 500 3 SER A 3 38.73 -171.62
REMARK 500 3 SER A 6 172.56 61.63
REMARK 500 3 THR A 19 -49.74 -162.72
REMARK 500 3 LYS A 48 30.76 -147.45
REMARK 500 3 PHE A 65 -45.89 -130.29
REMARK 500 3 ILE A 77 30.82 -142.36
REMARK 500 4 THR A 19 -43.20 -168.55
REMARK 500 4 PHE A 32 -44.41 -133.31
REMARK 500 4 PRO A 45 87.37 -54.71
REMARK 500 4 LYS A 64 67.20 62.57
REMARK 500 4 PHE A 65 -45.05 -157.68
REMARK 500 4 SER A 79 79.82 -158.79
REMARK 500 5 LYS A 20 99.98 -62.21
REMARK 500 5 PRO A 45 88.55 -53.91
REMARK 500 5 LEU A 46 31.36 -142.41
REMARK 500 5 PRO A 62 170.95 -57.69
REMARK 500 5 PHE A 65 -52.37 -121.20
REMARK 500 5 SER A 82 35.13 -99.25
REMARK 500 6 SER A 5 -67.65 -142.06
REMARK 500 6 SER A 6 -79.74 62.94
REMARK 500 6 THR A 19 -45.05 -162.52
REMARK 500 6 PRO A 45 92.56 -54.20
REMARK 500 6 LEU A 46 31.21 -151.79
REMARK 500 6 PHE A 65 -46.47 -147.60
REMARK 500 6 SER A 82 -59.90 -153.68
REMARK 500 7 SER A 6 31.32 -159.19
REMARK 500 7 THR A 19 -58.48 -176.93
REMARK 500 7 LYS A 20 108.72 -59.76
REMARK 500 7 PHE A 32 -46.85 -140.76
REMARK 500 7 PRO A 45 87.34 -54.64
REMARK 500 7 LEU A 46 30.74 -145.02
REMARK 500 7 PHE A 65 -49.23 -143.06
REMARK 500 8 THR A 19 -44.79 -161.10
REMARK 500 8 PHE A 32 -44.78 -136.22
REMARK 500
REMARK 500 THIS ENTRY HAS 140 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002100283.1 RELATED DB: TARGETDB
DBREF 2CP3 A 8 78 UNP Q9UDT6 CYLN2_HUMAN 219 289
SEQADV 2CP3 GLY A 1 UNP Q9UDT6 CLONING ARTIFACT
SEQADV 2CP3 SER A 2 UNP Q9UDT6 CLONING ARTIFACT
SEQADV 2CP3 SER A 3 UNP Q9UDT6 CLONING ARTIFACT
SEQADV 2CP3 GLY A 4 UNP Q9UDT6 CLONING ARTIFACT
SEQADV 2CP3 SER A 5 UNP Q9UDT6 CLONING ARTIFACT
SEQADV 2CP3 SER A 6 UNP Q9UDT6 CLONING ARTIFACT
SEQADV 2CP3 GLY A 7 UNP Q9UDT6 CLONING ARTIFACT
SEQADV 2CP3 SER A 79 UNP Q9UDT6 CLONING ARTIFACT
SEQADV 2CP3 GLY A 80 UNP Q9UDT6 CLONING ARTIFACT
SEQADV 2CP3 PRO A 81 UNP Q9UDT6 CLONING ARTIFACT
SEQADV 2CP3 SER A 82 UNP Q9UDT6 CLONING ARTIFACT
SEQADV 2CP3 SER A 83 UNP Q9UDT6 CLONING ARTIFACT
SEQADV 2CP3 GLY A 84 UNP Q9UDT6 CLONING ARTIFACT
SEQRES 1 A 84 GLY SER SER GLY SER SER GLY LEU ARG LEU GLY ASP ARG
SEQRES 2 A 84 VAL LEU VAL GLY GLY THR LYS THR GLY VAL VAL ARG TYR
SEQRES 3 A 84 VAL GLY GLU THR ASP PHE ALA LYS GLY GLU TRP CYS GLY
SEQRES 4 A 84 VAL GLU LEU ASP GLU PRO LEU GLY LYS ASN ASP GLY ALA
SEQRES 5 A 84 VAL ALA GLY THR ARG TYR PHE GLN CYS PRO PRO LYS PHE
SEQRES 6 A 84 GLY LEU PHE ALA PRO ILE HIS LYS VAL ILE ARG ILE GLY
SEQRES 7 A 84 SER GLY PRO SER SER GLY
SHEET 1 A 5 GLY A 66 PRO A 70 0
SHEET 2 A 5 GLU A 36 LEU A 42 -1 N CYS A 38 O ALA A 69
SHEET 3 A 5 LYS A 20 GLU A 29 -1 N ARG A 25 O GLY A 39
SHEET 4 A 5 ARG A 13 VAL A 16 -1 N VAL A 14 O GLY A 22
SHEET 5 A 5 VAL A 74 ARG A 76 -1 O ILE A 75 N LEU A 15
SHEET 1 B 2 ALA A 52 VAL A 53 0
SHEET 2 B 2 THR A 56 ARG A 57 -1 O THR 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