Header list of 1x5j.pdb file
Complete list - r 2 2 Bytes
HEADER CELL ADHESION 15-MAY-05 1X5J
TITLE THE SOLUTION STRUCTURE OF THE FIFTH FIBRONECTIN TYPE III DOMAIN OF
TITLE 2 HUMAN NEOGENIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEOGENIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FN3 DOMAIN;
COMPND 5 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: NEO1;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041213-06;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS RGM BINDING, FIBRONECTIN TYPE III DOMAIN, STRUCTURAL GENOMICS,
KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 4 CELL ADHESION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.TOCHIO,A.SASAGAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X5J 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X5J 1 VERSN
REVDAT 1 15-NOV-05 1X5J 0
JRNL AUTH N.TOCHIO,A.SASAGAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL THE SOLUTION STRUCTURE OF THE FIFTH FIBRONECTIN TYPE III
JRNL TITL 2 DOMAIN OF HUMAN NEOGENIN
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 1X5J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024405.
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 : 1.3MM FN3 DOMAIN U-15N,13C; 20MM
REMARK 210 D-TRIS HCL; 100MM NACL; 1MM D-
REMARK 210 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 : 900 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9295, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE 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 SER A 6 -179.28 -60.33
REMARK 500 1 PRO A 12 -179.16 -69.77
REMARK 500 1 LEU A 34 153.52 -44.99
REMARK 500 1 PRO A 35 -175.10 -69.73
REMARK 500 1 LYS A 36 -70.32 -39.38
REMARK 500 1 SER A 43 64.49 -100.98
REMARK 500 1 TYR A 70 133.22 -173.14
REMARK 500 1 ASN A 78 53.95 36.41
REMARK 500 1 THR A 95 178.63 -59.92
REMARK 500 1 SER A 97 174.77 -50.50
REMARK 500 2 VAL A 15 107.27 -58.61
REMARK 500 2 ASP A 31 79.32 -115.04
REMARK 500 2 PRO A 35 -171.37 -69.77
REMARK 500 2 GLN A 38 66.90 -103.19
REMARK 500 2 THR A 41 75.99 -113.78
REMARK 500 2 LYS A 59 143.80 -34.52
REMARK 500 2 ALA A 65 117.32 -160.94
REMARK 500 2 LYS A 89 60.07 -110.14
REMARK 500 2 SER A 93 147.01 -172.28
REMARK 500 2 SER A 97 174.67 -59.69
REMARK 500 2 SER A 111 118.58 -36.15
REMARK 500 3 PRO A 8 -177.12 -69.71
REMARK 500 3 VAL A 15 102.13 -48.71
REMARK 500 3 ILE A 19 98.96 -62.51
REMARK 500 3 PRO A 35 -167.99 -69.78
REMARK 500 3 GLN A 38 52.94 -104.52
REMARK 500 3 ALA A 65 116.73 -161.77
REMARK 500 3 SER A 97 164.54 -44.09
REMARK 500 3 MET A 98 135.26 -38.91
REMARK 500 3 SER A 108 149.83 -37.48
REMARK 500 3 PRO A 110 89.45 -69.74
REMARK 500 4 SER A 6 159.59 -39.53
REMARK 500 4 PRO A 12 -179.82 -69.72
REMARK 500 4 ILE A 19 95.03 -69.83
REMARK 500 4 PRO A 35 -174.06 -69.76
REMARK 500 4 LYS A 36 -37.38 -36.12
REMARK 500 4 THR A 41 41.05 -81.14
REMARK 500 4 ASP A 42 28.85 37.72
REMARK 500 4 ASN A 78 52.75 36.77
REMARK 500 4 SER A 93 137.51 -174.71
REMARK 500 4 THR A 95 174.47 -52.24
REMARK 500 4 PRO A 110 91.49 -69.72
REMARK 500 5 ILE A 19 93.25 -68.60
REMARK 500 5 ASP A 31 77.37 -113.67
REMARK 500 5 ASN A 32 -39.11 -39.33
REMARK 500 5 PRO A 35 -165.02 -69.77
REMARK 500 5 GLN A 38 64.63 -100.70
REMARK 500 5 ILE A 40 81.69 -69.02
REMARK 500 5 THR A 41 46.68 -93.44
REMARK 500 5 PRO A 55 -175.27 -69.71
REMARK 500
REMARK 500 THIS ENTRY HAS 204 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSO002001179.5 RELATED DB: TARGETDB
DBREF 1X5J A 8 107 UNP Q92859 NEO1_HUMAN 853 952
SEQADV 1X5J GLY A 1 UNP Q92859 CLONING ARTIFACT
SEQADV 1X5J SER A 2 UNP Q92859 CLONING ARTIFACT
SEQADV 1X5J SER A 3 UNP Q92859 CLONING ARTIFACT
SEQADV 1X5J GLY A 4 UNP Q92859 CLONING ARTIFACT
SEQADV 1X5J SER A 5 UNP Q92859 CLONING ARTIFACT
SEQADV 1X5J SER A 6 UNP Q92859 CLONING ARTIFACT
SEQADV 1X5J GLY A 7 UNP Q92859 CLONING ARTIFACT
SEQADV 1X5J SER A 108 UNP Q92859 CLONING ARTIFACT
SEQADV 1X5J GLY A 109 UNP Q92859 CLONING ARTIFACT
SEQADV 1X5J PRO A 110 UNP Q92859 CLONING ARTIFACT
SEQADV 1X5J SER A 111 UNP Q92859 CLONING ARTIFACT
SEQADV 1X5J SER A 112 UNP Q92859 CLONING ARTIFACT
SEQADV 1X5J GLY A 113 UNP Q92859 CLONING ARTIFACT
SEQRES 1 A 113 GLY SER SER GLY SER SER GLY PRO MET MET PRO PRO VAL
SEQRES 2 A 113 GLY VAL GLN ALA SER ILE LEU SER HIS ASP THR ILE ARG
SEQRES 3 A 113 ILE THR TRP ALA ASP ASN SER LEU PRO LYS HIS GLN LYS
SEQRES 4 A 113 ILE THR ASP SER ARG TYR TYR THR VAL ARG TRP LYS THR
SEQRES 5 A 113 ASN ILE PRO ALA ASN THR LYS TYR LYS ASN ALA ASN ALA
SEQRES 6 A 113 THR THR LEU SER TYR LEU VAL THR GLY LEU LYS PRO ASN
SEQRES 7 A 113 THR LEU TYR GLU PHE SER VAL MET VAL THR LYS GLY ARG
SEQRES 8 A 113 ARG SER SER THR TRP SER MET THR ALA HIS GLY THR THR
SEQRES 9 A 113 PHE GLU LEU SER GLY PRO SER SER GLY
SHEET 1 A 3 VAL A 13 SER A 21 0
SHEET 2 A 3 THR A 24 ALA A 30 -1 O ARG A 26 N SER A 18
SHEET 3 A 3 SER A 69 THR A 73 -1 O TYR A 70 N ILE A 27
SHEET 1 B 3 LYS A 61 ASN A 62 0
SHEET 2 B 3 TYR A 45 TRP A 50 -1 N TRP A 50 O LYS A 61
SHEET 3 B 3 SER A 84 THR A 88 -1 O SER A 84 N ARG A 49
SHEET 1 C 2 LEU A 80 TYR A 81 0
SHEET 2 C 2 GLY A 102 THR A 103 -1 O GLY A 102 N TYR A 81
CISPEP 1 ILE A 54 PRO A 55 1 -0.14
CISPEP 2 ILE A 54 PRO A 55 2 -0.12
CISPEP 3 ILE A 54 PRO A 55 3 -0.11
CISPEP 4 ILE A 54 PRO A 55 4 -0.18
CISPEP 5 ILE A 54 PRO A 55 5 -0.14
CISPEP 6 ILE A 54 PRO A 55 6 -0.15
CISPEP 7 ILE A 54 PRO A 55 7 -0.07
CISPEP 8 ILE A 54 PRO A 55 8 -0.14
CISPEP 9 ILE A 54 PRO A 55 9 0.01
CISPEP 10 ILE A 54 PRO A 55 10 -0.05
CISPEP 11 ILE A 54 PRO A 55 11 -0.06
CISPEP 12 ILE A 54 PRO A 55 12 -0.14
CISPEP 13 ILE A 54 PRO A 55 13 -0.11
CISPEP 14 ILE A 54 PRO A 55 14 -0.18
CISPEP 15 ILE A 54 PRO A 55 15 -0.07
CISPEP 16 ILE A 54 PRO A 55 16 -0.06
CISPEP 17 ILE A 54 PRO A 55 17 -0.10
CISPEP 18 ILE A 54 PRO A 55 18 -0.14
CISPEP 19 ILE A 54 PRO A 55 19 -0.09
CISPEP 20 ILE A 54 PRO A 55 20 -0.09
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 2 2 Bytes