Header list of 2cp6.pdb file
Complete list - r 9 2 Bytes
HEADER PROTEIN BINDING 19-MAY-05 2CP6
TITLE SOLUTION STRUCTURE OF THE 2ND 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: P040816-06;
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 2CP6 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CP6 1 VERSN
REVDAT 1 19-NOV-05 2CP6 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-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 2CP6 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_1000024471.
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 2 -42.27 -172.59
REMARK 500 1 SER A 3 36.71 -98.59
REMARK 500 1 SER A 5 -79.33 64.29
REMARK 500 1 ALA A 8 30.75 -98.85
REMARK 500 1 ILE A 12 146.79 62.89
REMARK 500 1 ASN A 14 -42.20 -171.33
REMARK 500 1 ALA A 19 151.70 61.82
REMARK 500 1 SER A 22 174.42 61.51
REMARK 500 1 ASN A 25 85.17 -174.85
REMARK 500 1 LEU A 26 -50.85 -170.77
REMARK 500 1 SER A 27 98.76 -170.18
REMARK 500 1 GLU A 28 87.41 -66.71
REMARK 500 1 ALA A 29 -45.52 -159.30
REMARK 500 1 SER A 31 -79.86 62.65
REMARK 500 1 LYS A 34 115.88 61.74
REMARK 500 1 THR A 50 -45.97 -155.62
REMARK 500 1 PRO A 76 78.99 -68.17
REMARK 500 1 LEU A 77 27.62 -143.63
REMARK 500 1 LYS A 79 -50.28 -152.86
REMARK 500 1 ASP A 81 33.36 -98.86
REMARK 500 1 TYR A 89 -71.80 -127.19
REMARK 500 1 TYR A 96 -46.33 -153.94
REMARK 500 1 SER A 112 -68.93 -177.45
REMARK 500 1 ALA A 116 78.61 -65.50
REMARK 500 1 LYS A 119 96.81 -162.83
REMARK 500 1 ASN A 121 -59.84 -126.13
REMARK 500 1 ALA A 122 -54.01 -173.85
REMARK 500 1 ARG A 125 105.53 61.62
REMARK 500 1 MET A 127 77.06 -168.53
REMARK 500 1 SER A 131 91.07 -63.16
REMARK 500 1 ARG A 136 -49.80 -156.63
REMARK 500 1 SER A 155 85.31 60.32
REMARK 500 1 ARG A 156 91.82 -172.08
REMARK 500 1 PRO A 157 95.20 -68.27
REMARK 500 1 SER A 170 -56.83 -131.25
REMARK 500 2 SER A 5 -46.68 -153.50
REMARK 500 2 SER A 6 -43.03 -169.16
REMARK 500 2 ALA A 8 -55.09 -122.38
REMARK 500 2 THR A 9 55.30 -145.26
REMARK 500 2 THR A 16 74.99 60.27
REMARK 500 2 LEU A 26 83.90 -151.65
REMARK 500 2 SER A 27 -46.70 -155.33
REMARK 500 2 SER A 31 -71.27 -90.04
REMARK 500 2 ARG A 37 86.77 -173.76
REMARK 500 2 GLU A 38 -63.74 -93.19
REMARK 500 2 THR A 50 -42.53 -170.57
REMARK 500 2 PRO A 76 75.99 -68.86
REMARK 500 2 LEU A 77 31.00 -140.93
REMARK 500 2 ASP A 81 30.72 -99.48
REMARK 500 2 TYR A 89 -51.99 -121.98
REMARK 500
REMARK 500 THIS ENTRY HAS 692 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSO002001267.2 RELATED DB: TARGETDB
DBREF 2CP6 A 8 166 UNP P30622 REST_HUMAN 181 339
SEQADV 2CP6 GLY A 1 UNP P30622 CLONING ARTIFACT
SEQADV 2CP6 SER A 2 UNP P30622 CLONING ARTIFACT
SEQADV 2CP6 SER A 3 UNP P30622 CLONING ARTIFACT
SEQADV 2CP6 GLY A 4 UNP P30622 CLONING ARTIFACT
SEQADV 2CP6 SER A 5 UNP P30622 CLONING ARTIFACT
SEQADV 2CP6 SER A 6 UNP P30622 CLONING ARTIFACT
SEQADV 2CP6 GLY A 7 UNP P30622 CLONING ARTIFACT
SEQADV 2CP6 SER A 167 UNP P30622 CLONING ARTIFACT
SEQADV 2CP6 GLY A 168 UNP P30622 CLONING ARTIFACT
SEQADV 2CP6 PRO A 169 UNP P30622 CLONING ARTIFACT
SEQADV 2CP6 SER A 170 UNP P30622 CLONING ARTIFACT
SEQADV 2CP6 SER A 171 UNP P30622 CLONING ARTIFACT
SEQADV 2CP6 GLY A 172 UNP P30622 CLONING ARTIFACT
SEQRES 1 A 172 GLY SER SER GLY SER SER GLY ALA THR PRO PRO ILE SER
SEQRES 2 A 172 ASN LEU THR LYS THR ALA SER GLU SER ILE SER ASN LEU
SEQRES 3 A 172 SER GLU ALA GLY SER ILE LYS LYS GLY GLU ARG GLU LEU
SEQRES 4 A 172 LYS ILE GLY ASP ARG VAL LEU VAL GLY GLY THR LYS ALA
SEQRES 5 A 172 GLY VAL VAL ARG PHE LEU GLY GLU THR ASP PHE ALA LYS
SEQRES 6 A 172 GLY GLU TRP CYS GLY VAL GLU LEU ASP GLU PRO LEU GLY
SEQRES 7 A 172 LYS ASN ASP GLY ALA VAL ALA GLY THR ARG TYR PHE GLN
SEQRES 8 A 172 CYS GLN PRO LYS TYR GLY LEU PHE ALA PRO VAL HIS LYS
SEQRES 9 A 172 VAL THR LYS ILE GLY PHE PRO SER THR THR PRO ALA LYS
SEQRES 10 A 172 ALA LYS ALA ASN ALA VAL ARG ARG VAL MET ALA THR THR
SEQRES 11 A 172 SER ALA SER LEU LYS ARG SER PRO SER ALA SER SER LEU
SEQRES 12 A 172 SER SER MET SER SER VAL ALA SER SER VAL SER SER ARG
SEQRES 13 A 172 PRO SER ARG THR GLY LEU LEU THR GLU THR SER GLY PRO
SEQRES 14 A 172 SER SER GLY
HELIX 1 1 HIS A 103 VAL A 105 5 3
SHEET 1 A 5 GLY A 97 PRO A 101 0
SHEET 2 A 5 GLU A 67 LEU A 73 -1 N CYS A 69 O ALA A 100
SHEET 3 A 5 LYS A 51 GLU A 60 -1 N PHE A 57 O GLY A 70
SHEET 4 A 5 ARG A 44 VAL A 47 -1 N VAL A 47 O LYS A 51
SHEET 5 A 5 THR A 106 LYS A 107 -1 O THR A 106 N LEU A 46
SHEET 1 B 2 ALA A 83 VAL A 84 0
SHEET 2 B 2 THR A 87 ARG A 88 -1 O THR A 87 N VAL A 84
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