Header list of 2fry.pdb file
Complete list - 9 20 Bytes
HEADER PROTEIN BINDING 20-JAN-06 2FRY
TITLE SOLUTION STRUCTURE OF THE THIRD SH3 DOMAIN OF HUMAN NCK2 ADAPTOR
TITLE 2 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOPLASMIC PROTEIN NCK2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3_3;
COMPND 5 SYNONYM: NCK ADAPTOR PROTEIN 2, SH2/SH3 ADAPTOR PROTEIN NCK-BETA,
COMPND 6 NCK-2;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET32-A
KEYWDS SH3, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR J.LIU
REVDAT 3 09-MAR-22 2FRY 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2FRY 1 VERSN
REVDAT 1 20-JUN-06 2FRY 0
JRNL AUTH J.LIU,M.LI,X.RAN,J.S.FAN,J.SONG
JRNL TITL STRUCTURAL INSIGHT INTO THE BINDING DIVERSITY BETWEEN THE
JRNL TITL 2 HUMAN NCK2 SH3 DOMAINS AND PROLINE-RICH PROTEINS
JRNL REF BIOCHEMISTRY V. 45 7171 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16752908
JRNL DOI 10.1021/BI060091Y
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 812 RESTRAINTS, 722 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 90
REMARK 3 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 2FRY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000036238.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 50MM PHOSPHATE BUFFER, 90% H2O,
REMARK 210 10% D2O, 0.01% NAN3, 10MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
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 2004
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 H VAL A 5 O MET A 27 1.55
REMARK 500
REMARK 500 REMARK: NULL
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 LEU A 8 -34.66 -131.71
REMARK 500 1 VAL A 14 -55.31 -132.54
REMARK 500 1 THR A 15 158.40 -46.17
REMARK 500 1 GLU A 25 -147.13 -94.91
REMARK 500 1 PRO A 37 177.14 -44.43
REMARK 500 2 PRO A 10 175.42 -46.10
REMARK 500 2 VAL A 14 -47.88 -132.47
REMARK 500 2 THR A 15 172.50 -55.38
REMARK 500 2 GLU A 17 32.77 -92.73
REMARK 500 2 GLU A 22 99.33 -69.40
REMARK 500 2 GLU A 38 -75.46 -114.55
REMARK 500 2 PRO A 53 87.36 -60.43
REMARK 500 3 PRO A 10 151.72 -44.11
REMARK 500 3 VAL A 14 89.58 -173.06
REMARK 500 3 GLU A 22 -156.03 -63.85
REMARK 500 3 ILE A 30 -77.11 -79.31
REMARK 500 3 GLU A 38 -77.09 -121.75
REMARK 500 3 LYS A 54 -11.48 -45.24
REMARK 500 4 LEU A 8 -35.81 -131.09
REMARK 500 4 GLU A 22 -157.39 -63.61
REMARK 500 4 PRO A 37 -75.40 -42.17
REMARK 500 4 GLU A 38 17.89 -175.41
REMARK 500 5 LEU A 8 -40.02 -131.76
REMARK 500 5 PRO A 10 -176.27 -54.59
REMARK 500 5 VAL A 14 -31.36 -144.86
REMARK 500 5 GLU A 17 32.68 -98.63
REMARK 500 5 GLU A 22 98.32 -64.94
REMARK 500 5 PRO A 37 79.36 -61.75
REMARK 500 5 GLU A 38 -83.71 -119.30
REMARK 500 5 PRO A 53 82.14 -60.79
REMARK 500 6 LEU A 8 -44.08 -131.31
REMARK 500 6 VAL A 14 -45.16 -135.88
REMARK 500 6 GLU A 18 -171.67 -54.54
REMARK 500 6 ILE A 30 -81.99 -81.23
REMARK 500 6 PRO A 33 62.36 -66.90
REMARK 500 6 GLU A 38 -98.69 -152.84
REMARK 500 7 LEU A 8 -41.24 -131.50
REMARK 500 7 PRO A 10 -166.12 -54.45
REMARK 500 7 VAL A 14 55.21 -145.15
REMARK 500 7 GLU A 18 -168.64 -124.85
REMARK 500 7 LEU A 19 148.94 -178.85
REMARK 500 7 ILE A 30 -78.37 -86.53
REMARK 500 7 GLU A 38 -88.07 -102.76
REMARK 500 7 PRO A 53 88.13 -60.55
REMARK 500 8 LEU A 8 -40.66 -131.51
REMARK 500 8 VAL A 14 -42.69 -173.34
REMARK 500 8 PRO A 33 92.70 -59.02
REMARK 500 8 GLU A 38 -94.36 -98.53
REMARK 500 9 PRO A 10 173.38 -46.68
REMARK 500 9 VAL A 14 -41.36 -167.57
REMARK 500
REMARK 500 THIS ENTRY HAS 59 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FRW RELATED DB: PDB
REMARK 900 THE SECOND SH3 DOMAIN OF THE SAME PROTEIN
DBREF 2FRY A 3 61 UNP O43639 NCK2_HUMAN 198 256
SEQADV 2FRY GLY A 1 UNP O43639 CLONING ARTIFACT
SEQADV 2FRY SER A 2 UNP O43639 CLONING ARTIFACT
SEQRES 1 A 61 GLY SER HIS VAL VAL GLN THR LEU TYR PRO PHE SER SER
SEQRES 2 A 61 VAL THR GLU GLU GLU LEU ASN PHE GLU LYS GLY GLU THR
SEQRES 3 A 61 MET GLU VAL ILE GLU LYS PRO GLU ASN ASP PRO GLU TRP
SEQRES 4 A 61 TRP LYS CYS LYS ASN ALA ARG GLY GLN VAL GLY LEU VAL
SEQRES 5 A 61 PRO LYS ASN TYR VAL VAL VAL LEU SER
HELIX 1 1 PRO A 53 ASN A 55 5 3
SHEET 1 A 3 THR A 26 MET A 27 0
SHEET 2 A 3 VAL A 5 THR A 7 -1 N VAL A 5 O MET A 27
SHEET 3 A 3 VAL A 57 VAL A 59 -1 O VAL A 58 N GLN A 6
SHEET 1 B 2 TRP A 40 LYS A 43 0
SHEET 2 B 2 VAL A 49 VAL A 52 -1 O VAL A 52 N TRP A 40
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 - 9 20 Bytes