Header list of 2dmo.pdb file
Complete list - r 9 2 Bytes
HEADER SIGNALING PROTEIN 22-APR-06 2DMO
TITLE REFINED SOLUTION STRUCTURE OF THE 1ST SH3 DOMAIN FROM HUMAN NEUTROPHIL
TITLE 2 CYTOSOL FACTOR 2 (NCF-2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUTROPHIL CYTOSOL FACTOR 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN;
COMPND 5 SYNONYM: NCF-2, NEUTROPHIL NADPH OXIDASE FACTOR 2, 67 KDA NEUTROPHIL
COMPND 6 OXIDASE FACTOR, P67-PHOX, NOXA2;
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: NCF2;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040921-05;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS SH3 DOMAIN, NEUTROPHIL CYTOSOL FACTOR, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, SIGNALING
KEYWDS 4 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.TOCHIO,E.CHIKAYAMA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2DMO 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DMO 1 VERSN
REVDAT 1 02-MAY-06 2DMO 0
SPRSDE 02-MAY-06 2DMO 1X3V
JRNL AUTH N.TOCHIO,E.CHIKAYAMA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE 1ST SH3 DOMAIN FROM HUMAN
JRNL TITL 2 NEUTROPHIL CYTOSOL FACTOR 2 (NCF-2)
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 2.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DMO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000025595.
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 SH3 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 : 700 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 0.955, CYANA 2.1
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 PRO A 18 81.83 -69.79
REMARK 500 1 GLN A 25 99.75 -67.76
REMARK 500 1 TYR A 58 45.53 -101.03
REMARK 500 1 VAL A 62 69.62 -114.25
REMARK 500 2 PRO A 18 79.54 -69.74
REMARK 500 2 LEU A 35 -63.14 -108.07
REMARK 500 2 ASN A 39 52.42 -108.16
REMARK 500 2 ASP A 40 26.36 -141.74
REMARK 500 2 TYR A 58 48.06 -99.62
REMARK 500 2 PRO A 65 -175.73 -69.78
REMARK 500 3 SER A 3 -64.75 -101.69
REMARK 500 3 SER A 6 74.68 -109.66
REMARK 500 3 PRO A 18 87.06 -69.74
REMARK 500 3 GLU A 23 176.86 -56.07
REMARK 500 3 ASP A 40 42.55 -93.40
REMARK 500 3 TYR A 58 32.68 -97.17
REMARK 500 3 PRO A 65 84.65 -69.77
REMARK 500 4 PRO A 18 90.39 -69.81
REMARK 500 4 ASP A 40 43.44 -92.82
REMARK 500 4 TYR A 58 45.89 -94.45
REMARK 500 5 LEU A 13 -74.08 -71.01
REMARK 500 5 PRO A 18 81.48 -69.72
REMARK 500 5 LEU A 35 -60.53 -103.79
REMARK 500 5 ASP A 40 45.36 -93.21
REMARK 500 5 TYR A 58 40.53 -97.06
REMARK 500 6 LEU A 13 34.22 -99.03
REMARK 500 6 PRO A 18 82.74 -69.85
REMARK 500 6 TYR A 58 33.06 -97.48
REMARK 500 7 SER A 2 -71.20 -72.85
REMARK 500 7 PRO A 18 80.72 -69.74
REMARK 500 7 PRO A 65 -172.13 -69.79
REMARK 500 8 PRO A 18 83.39 -69.76
REMARK 500 8 ASP A 40 42.14 -93.83
REMARK 500 8 TYR A 58 49.18 -98.07
REMARK 500 8 VAL A 62 -64.69 -95.75
REMARK 500 9 PRO A 18 83.27 -69.79
REMARK 500 9 GLU A 22 -70.68 -61.48
REMARK 500 9 TYR A 58 49.71 -103.47
REMARK 500 9 PRO A 65 -175.77 -69.72
REMARK 500 9 SER A 66 77.87 -115.43
REMARK 500 10 SER A 6 53.38 -119.35
REMARK 500 10 LEU A 13 -67.51 -122.51
REMARK 500 10 PRO A 18 78.73 -69.80
REMARK 500 10 TYR A 58 50.52 -100.49
REMARK 500 10 SER A 63 74.16 -110.21
REMARK 500 11 PRO A 18 79.00 -69.81
REMARK 500 11 GLN A 25 103.77 -54.21
REMARK 500 11 TYR A 58 30.21 -96.69
REMARK 500 12 SER A 3 -73.90 -114.20
REMARK 500 12 PRO A 18 88.96 -69.81
REMARK 500
REMARK 500 THIS ENTRY HAS 90 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002004901.1 RELATED DB: TARGETDB
DBREF 2DMO A 8 62 UNP P19878 NCF2_HUMAN 242 297
SEQADV 2DMO GLY A 1 UNP P19878 CLONING ARTIFACT
SEQADV 2DMO SER A 2 UNP P19878 CLONING ARTIFACT
SEQADV 2DMO SER A 3 UNP P19878 CLONING ARTIFACT
SEQADV 2DMO GLY A 4 UNP P19878 CLONING ARTIFACT
SEQADV 2DMO SER A 5 UNP P19878 CLONING ARTIFACT
SEQADV 2DMO SER A 6 UNP P19878 CLONING ARTIFACT
SEQADV 2DMO GLY A 7 UNP P19878 CLONING ARTIFACT
SEQADV 2DMO SER A 63 UNP P19878 CLONING ARTIFACT
SEQADV 2DMO GLY A 64 UNP P19878 CLONING ARTIFACT
SEQADV 2DMO PRO A 65 UNP P19878 CLONING ARTIFACT
SEQADV 2DMO SER A 66 UNP P19878 CLONING ARTIFACT
SEQADV 2DMO SER A 67 UNP P19878 CLONING ARTIFACT
SEQADV 2DMO GLY A 68 UNP P19878 CLONING ARTIFACT
SEQRES 1 A 68 GLY SER SER GLY SER SER GLY GLU ALA HIS ARG VAL LEU
SEQRES 2 A 68 PHE GLY PHE VAL PRO GLU THR LYS GLU GLU LEU GLN VAL
SEQRES 3 A 68 MET PRO GLY ASN ILE VAL PHE VAL LEU LYS LYS GLY ASN
SEQRES 4 A 68 ASP ASN TRP ALA THR VAL MET PHE ASN GLY GLN LYS GLY
SEQRES 5 A 68 LEU VAL PRO CYS ASN TYR LEU GLU PRO VAL SER GLY PRO
SEQRES 6 A 68 SER SER GLY
SHEET 1 A 3 ILE A 31 VAL A 34 0
SHEET 2 A 3 GLU A 8 VAL A 12 -1 N GLU A 8 O VAL A 34
SHEET 3 A 3 LEU A 59 PRO A 61 -1 O GLU A 60 N ARG A 11
SHEET 1 B 3 LYS A 36 LYS A 37 0
SHEET 2 B 3 ALA A 43 PHE A 47 -1 O THR A 44 N LYS A 36
SHEET 3 B 3 GLN A 50 VAL A 54 -1 O VAL A 54 N ALA A 43
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