Header list of 2cui.pdb file
Complete list - r 9 2 Bytes
HEADER CELL ADHESION 26-MAY-05 2CUI
TITLE SOLUTION STRUCTURE OF THE 31ST FIBRONECTIN TYPE III DOMAIN OF THE
TITLE 2 HUMAN TENASCIN X
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TENASCIN-X;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THE 29TH FIBRONECTIN TYPE III DOMAIN;
COMPND 5 SYNONYM: TN-X, HEXABRACHION-LIKE PROTEIN;
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: TNXB;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050131-02;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS FIBRONECTIN TYPE III DOMAIN, TENASCIN X PRECURSOR, EXTRACELLULAR
KEYWDS 2 MATIRX, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 3 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, CELL ADHESION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.OHNISHI,T.KIGAWA,N.TOCHIO,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CUI 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CUI 1 VERSN
REVDAT 1 26-NOV-05 2CUI 0
JRNL AUTH S.OHNISHI,T.KIGAWA,N.TOCHIO,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE 31ST FIBRONECTIN TYPE III DOMAIN
JRNL TITL 2 OF THE HUMAN TENASCIN X
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CUI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000024633.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.23MM PROTEIN U-15N, 13C; 20MM
REMARK 210 D-TRISHCL; 100MM NACL; 1MM D-DTT;
REMARK 210 0.02% NAN3; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 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 : TORSION 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 VAL A 20 103.91 -46.30
REMARK 500 1 HIS A 70 67.44 -119.18
REMARK 500 1 LEU A 90 107.53 -58.88
REMARK 500 2 ARG A 9 53.54 39.71
REMARK 500 2 VAL A 20 103.31 -45.72
REMARK 500 2 HIS A 70 67.57 -118.55
REMARK 500 3 ASP A 19 32.42 71.90
REMARK 500 3 VAL A 20 103.08 -45.57
REMARK 500 3 HIS A 70 67.48 -117.27
REMARK 500 3 LEU A 90 108.60 -56.76
REMARK 500 3 SER A 111 173.40 -52.16
REMARK 500 4 VAL A 20 104.33 -45.83
REMARK 500 4 PRO A 55 0.87 -69.72
REMARK 500 4 HIS A 70 67.60 -117.71
REMARK 500 5 SER A 2 -51.45 -121.50
REMARK 500 5 VAL A 20 103.09 -48.94
REMARK 500 5 LEU A 25 -179.86 -174.44
REMARK 500 5 PRO A 55 2.20 -69.80
REMARK 500 5 HIS A 70 67.29 -117.80
REMARK 500 6 VAL A 20 103.16 -45.94
REMARK 500 6 ALA A 35 -66.68 -90.25
REMARK 500 6 LEU A 59 98.40 -61.99
REMARK 500 6 HIS A 70 67.71 -117.20
REMARK 500 6 THR A 105 170.88 -58.95
REMARK 500 6 PRO A 109 2.04 -69.72
REMARK 500 7 VAL A 20 104.19 -45.92
REMARK 500 7 PRO A 55 2.53 -69.69
REMARK 500 7 HIS A 70 67.35 -117.53
REMARK 500 8 VAL A 20 103.20 -50.44
REMARK 500 8 LEU A 25 -179.22 -174.90
REMARK 500 8 HIS A 70 67.42 -116.10
REMARK 500 9 SER A 8 153.69 -37.17
REMARK 500 9 VAL A 20 102.88 -47.72
REMARK 500 9 LEU A 25 -179.89 -175.45
REMARK 500 9 PRO A 55 0.21 -69.71
REMARK 500 9 SER A 110 91.81 -69.45
REMARK 500 10 SER A 5 -56.32 -120.97
REMARK 500 10 VAL A 20 105.29 -48.26
REMARK 500 10 LEU A 25 -179.17 -172.51
REMARK 500 10 PRO A 55 3.19 -69.83
REMARK 500 10 HIS A 70 67.51 -117.25
REMARK 500 11 VAL A 20 103.03 -51.24
REMARK 500 11 HIS A 70 67.69 -116.91
REMARK 500 12 VAL A 20 102.89 -51.85
REMARK 500 12 HIS A 70 67.34 -116.36
REMARK 500 13 VAL A 20 103.88 -46.10
REMARK 500 13 PRO A 55 3.43 -69.78
REMARK 500 13 HIS A 70 67.72 -117.45
REMARK 500 14 SER A 6 41.85 -87.67
REMARK 500 14 VAL A 20 104.05 -50.07
REMARK 500
REMARK 500 THIS ENTRY HAS 76 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSO002001012.3 RELATED DB: TARGETDB
DBREF 2CUI A 8 106 UNP P22105 TENX_HUMAN 3699 3797
SEQADV 2CUI GLY A 1 UNP P22105 CLONING ARTIFACT
SEQADV 2CUI SER A 2 UNP P22105 CLONING ARTIFACT
SEQADV 2CUI SER A 3 UNP P22105 CLONING ARTIFACT
SEQADV 2CUI GLY A 4 UNP P22105 CLONING ARTIFACT
SEQADV 2CUI SER A 5 UNP P22105 CLONING ARTIFACT
SEQADV 2CUI SER A 6 UNP P22105 CLONING ARTIFACT
SEQADV 2CUI GLY A 7 UNP P22105 CLONING ARTIFACT
SEQADV 2CUI SER A 107 UNP P22105 CLONING ARTIFACT
SEQADV 2CUI GLY A 108 UNP P22105 CLONING ARTIFACT
SEQADV 2CUI PRO A 109 UNP P22105 CLONING ARTIFACT
SEQADV 2CUI SER A 110 UNP P22105 CLONING ARTIFACT
SEQADV 2CUI SER A 111 UNP P22105 CLONING ARTIFACT
SEQADV 2CUI GLY A 112 UNP P22105 CLONING ARTIFACT
SEQRES 1 A 112 GLY SER SER GLY SER SER GLY SER ARG PRO ARG LEU SER
SEQRES 2 A 112 GLN LEU SER VAL THR ASP VAL THR THR SER SER LEU ARG
SEQRES 3 A 112 LEU ASN TRP GLU ALA PRO PRO GLY ALA PHE ASP SER PHE
SEQRES 4 A 112 LEU LEU ARG PHE GLY VAL PRO SER PRO SER THR LEU GLU
SEQRES 5 A 112 PRO HIS PRO ARG PRO LEU LEU GLN ARG GLU LEU MET VAL
SEQRES 6 A 112 PRO GLY THR ARG HIS SER ALA VAL LEU ARG ASP LEU ARG
SEQRES 7 A 112 SER GLY THR LEU TYR SER LEU THR LEU TYR GLY LEU ARG
SEQRES 8 A 112 GLY PRO HIS LYS ALA ASP SER ILE GLN GLY THR ALA ARG
SEQRES 9 A 112 THR LEU SER GLY PRO SER SER GLY
SHEET 1 A 3 SER A 16 THR A 21 0
SHEET 2 A 3 SER A 24 ASN A 28 -1 O ARG A 26 N THR A 18
SHEET 3 A 3 SER A 71 LEU A 74 -1 O ALA A 72 N LEU A 27
SHEET 1 B 4 ARG A 61 PRO A 66 0
SHEET 2 B 4 SER A 38 GLY A 44 -1 N PHE A 39 O VAL A 65
SHEET 3 B 4 LEU A 82 LEU A 90 -1 O THR A 86 N ARG A 42
SHEET 4 B 4 LYS A 95 ARG A 104 -1 O ALA A 103 N TYR A 83
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