Header list of 2cub.pdb file
Complete list - r 9 2 Bytes
HEADER SIGNALING PROTEIN 26-MAY-05 2CUB
TITLE SOLUTION STRUCTURE OF THE SH3 DOMAIN OF THE HUMAN CYTOPLASMIC PROTEIN
TITLE 2 NCK1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOPLASMIC PROTEIN NCK1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN;
COMPND 5 SYNONYM: NCK ADAPTOR PROTEIN 1, SH2/SH3 ADAPTOR PROTEIN NCK-ALPHA;
COMPND 6 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: NCK1;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040621-03;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS SH3 DOMAIN, NCK1 ADAPTOR, TYROSINE KINASE, SIGNAL TRANSDUCTION,
KEYWDS 2 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL
KEYWDS 3 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.OHNISHI,T.KIGAWA,M.SATO,T.TOMIZAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA,
AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CUB 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CUB 1 VERSN
REVDAT 1 26-NOV-05 2CUB 0
JRNL AUTH S.OHNISHI,T.KIGAWA,M.SATO,T.TOMIZAWA,S.KOSHIBA,M.INOUE,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SH3 DOMAIN OF THE HUMAN
JRNL TITL 2 CYTOPLASMIC PROTEIN NCK1
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, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CUB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000024626.
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 : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.18MM PROTEIN U-15N,13C; 20MM D
REMARK 210 -TRIS-HCL(PH7.0); 100MM NACL;
REMARK 210 1MM D-DTT; 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 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9295, CYANA 2.0.17
REMARK 210 METHOD USED : TORTION ANGLE DYNAMICS,
REMARK 210 RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LEAST RESTRAINT VIOLATIONS
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 GLU A 71 94.65 -62.81
REMARK 500 2 SER A 5 133.56 -171.96
REMARK 500 2 ASP A 15 41.75 37.19
REMARK 500 2 SER A 49 -39.22 -34.37
REMARK 500 2 GLU A 71 89.86 -63.82
REMARK 500 2 ASP A 74 177.89 -48.99
REMARK 500 2 SER A 87 42.49 39.14
REMARK 500 3 ASP A 8 151.77 -49.45
REMARK 500 3 ASP A 50 -38.34 -34.97
REMARK 500 3 GLU A 71 100.19 -59.50
REMARK 500 4 SER A 6 105.29 -59.93
REMARK 500 4 ASN A 17 35.66 71.19
REMARK 500 4 SER A 83 119.03 -38.55
REMARK 500 4 PRO A 85 95.48 -69.73
REMARK 500 4 SER A 86 158.71 -44.95
REMARK 500 5 SER A 5 98.81 -54.96
REMARK 500 5 ASN A 17 36.16 70.03
REMARK 500 5 VAL A 22 97.64 -63.26
REMARK 500 5 LYS A 38 109.60 -56.42
REMARK 500 5 GLU A 71 96.57 -58.22
REMARK 500 6 PRO A 9 93.12 -69.75
REMARK 500 6 ASN A 17 34.60 71.16
REMARK 500 6 TYR A 57 114.02 -162.45
REMARK 500 6 GLU A 71 98.45 -65.68
REMARK 500 6 SER A 83 38.23 -87.57
REMARK 500 6 SER A 86 45.75 36.31
REMARK 500 7 SER A 5 46.02 37.75
REMARK 500 7 ARG A 12 52.63 39.11
REMARK 500 7 LEU A 13 111.64 -37.72
REMARK 500 7 ASN A 17 31.57 70.66
REMARK 500 7 ASP A 79 150.16 -43.49
REMARK 500 8 ASP A 15 37.07 39.84
REMARK 500 8 SER A 49 -34.53 -39.19
REMARK 500 8 ASP A 74 151.35 -47.37
REMARK 500 9 ASP A 15 39.58 39.44
REMARK 500 9 ASN A 17 32.62 73.75
REMARK 500 10 ASP A 15 39.78 35.01
REMARK 500 10 VAL A 22 98.89 -66.09
REMARK 500 10 GLU A 71 93.25 -57.61
REMARK 500 10 ASP A 79 52.11 -91.07
REMARK 500 10 PRO A 85 98.69 -69.74
REMARK 500 10 SER A 87 157.73 -47.59
REMARK 500 11 SER A 3 126.37 -172.72
REMARK 500 11 ASN A 17 32.80 71.73
REMARK 500 11 LYS A 38 109.48 -57.83
REMARK 500 11 TYR A 57 115.05 -160.52
REMARK 500 12 SER A 5 -55.27 -122.57
REMARK 500 12 SER A 6 103.31 -47.68
REMARK 500 12 ASP A 8 139.81 -36.12
REMARK 500 12 ASP A 15 41.74 37.41
REMARK 500
REMARK 500 THIS ENTRY HAS 85 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001002947.1 RELATED DB: TARGETDB
DBREF 2CUB A 8 82 UNP P16333 NCK1_HUMAN 99 173
SEQADV 2CUB GLY A 1 UNP P16333 CLONING ARTIFACT
SEQADV 2CUB SER A 2 UNP P16333 CLONING ARTIFACT
SEQADV 2CUB SER A 3 UNP P16333 CLONING ARTIFACT
SEQADV 2CUB GLY A 4 UNP P16333 CLONING ARTIFACT
SEQADV 2CUB SER A 5 UNP P16333 CLONING ARTIFACT
SEQADV 2CUB SER A 6 UNP P16333 CLONING ARTIFACT
SEQADV 2CUB GLY A 7 UNP P16333 CLONING ARTIFACT
SEQADV 2CUB SER A 83 UNP P16333 CLONING ARTIFACT
SEQADV 2CUB GLY A 84 UNP P16333 CLONING ARTIFACT
SEQADV 2CUB PRO A 85 UNP P16333 CLONING ARTIFACT
SEQADV 2CUB SER A 86 UNP P16333 CLONING ARTIFACT
SEQADV 2CUB SER A 87 UNP P16333 CLONING ARTIFACT
SEQADV 2CUB GLY A 88 UNP P16333 CLONING ARTIFACT
SEQRES 1 A 88 GLY SER SER GLY SER SER GLY ASP PRO GLY GLU ARG LEU
SEQRES 2 A 88 TYR ASP LEU ASN MET PRO ALA TYR VAL LYS PHE ASN TYR
SEQRES 3 A 88 MET ALA GLU ARG GLU ASP GLU LEU SER LEU ILE LYS GLY
SEQRES 4 A 88 THR LYS VAL ILE VAL MET GLU LYS CYS SER ASP GLY TRP
SEQRES 5 A 88 TRP ARG GLY SER TYR ASN GLY GLN VAL GLY TRP PHE PRO
SEQRES 6 A 88 SER ASN TYR VAL THR GLU GLU GLY ASP SER PRO LEU GLY
SEQRES 7 A 88 ASP HIS VAL GLY SER GLY PRO SER SER GLY
HELIX 1 1 SER A 66 TYR A 68 5 3
SHEET 1 A 5 GLN A 60 PRO A 65 0
SHEET 2 A 5 TRP A 52 TYR A 57 -1
SHEET 3 A 5 THR A 40 LYS A 47 -1
SHEET 4 A 5 LEU A 13 VAL A 22 -1
SHEET 5 A 5 VAL A 69 GLU A 71 -1
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