Header list of 2frw.pdb file
Complete list - 9 20 Bytes
HEADER PROTEIN BINDING 20-JAN-06 2FRW TITLE SOLUTION STRUCTURE OF THE SECOND SH3 DOMAIN OF HUMAN ADAPTOR PROTEIN TITLE 2 NCK2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYTOPLASMIC PROTEIN NCK2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SH3_2; 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 2FRW 1 REMARK REVDAT 2 24-FEB-09 2FRW 1 VERSN REVDAT 1 20-JUN-06 2FRW 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 : A.T.BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 974 RESTRAINTS, 880 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 87 REMARK 3 DIHEDRAL ANGLE RESTRAINTS,7 DISTANCE RESTRAINTS FROM HYDROGEN REMARK 3 BONDS REMARK 4 REMARK 4 2FRW 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_1000036236. 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, PH 6.8, REMARK 210 90% H2O, 10% D2O, 0.01% NAN3, REMARK 210 DDT 10MM 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 : NULL 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 O ARG A 13 H GLU A 16 1.60 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 LYS A 6 -68.80 -108.95 REMARK 500 1 ALA A 11 114.13 179.67 REMARK 500 1 GLU A 14 106.79 -54.10 REMARK 500 1 ASP A 15 9.82 95.64 REMARK 500 1 MET A 28 101.33 -167.87 REMARK 500 1 ASN A 41 86.59 -59.86 REMARK 500 1 SER A 49 -16.61 -45.02 REMARK 500 1 TYR A 51 64.11 -158.62 REMARK 500 2 ALA A 11 110.42 161.68 REMARK 500 2 ASP A 15 -43.98 134.60 REMARK 500 2 MET A 28 100.94 -167.89 REMARK 500 2 ASN A 41 86.36 -59.75 REMARK 500 2 SER A 49 -6.80 -56.47 REMARK 500 2 TYR A 51 64.29 -156.81 REMARK 500 3 ALA A 11 -169.98 -119.73 REMARK 500 3 ARG A 13 -154.74 -82.80 REMARK 500 3 GLU A 14 105.51 -50.46 REMARK 500 3 ASP A 15 -54.14 154.76 REMARK 500 3 MET A 28 -176.14 -64.35 REMARK 500 3 ASN A 41 86.46 -59.35 REMARK 500 4 LYS A 6 -96.53 -92.23 REMARK 500 4 ALA A 11 96.86 -171.59 REMARK 500 4 GLU A 14 107.32 -53.50 REMARK 500 4 ASP A 15 15.76 85.16 REMARK 500 4 VAL A 27 101.82 -54.13 REMARK 500 4 MET A 28 -175.42 -49.03 REMARK 500 4 LYS A 30 96.98 -66.21 REMARK 500 4 ASN A 41 86.30 -59.56 REMARK 500 4 PRO A 48 33.99 -94.64 REMARK 500 4 SER A 49 -28.46 -34.45 REMARK 500 4 TYR A 51 64.89 -160.58 REMARK 500 5 LYS A 6 -72.20 -83.30 REMARK 500 5 ARG A 13 -154.53 -82.69 REMARK 500 5 GLU A 14 105.67 -50.29 REMARK 500 5 ASP A 15 -55.57 152.45 REMARK 500 5 MET A 28 -176.33 -54.12 REMARK 500 5 LYS A 30 96.47 -69.64 REMARK 500 5 ASN A 41 86.36 -59.51 REMARK 500 5 PRO A 48 88.45 -50.60 REMARK 500 6 LYS A 6 -75.91 -106.00 REMARK 500 6 ALA A 11 88.39 162.14 REMARK 500 6 GLU A 14 106.01 -54.16 REMARK 500 6 ASP A 15 -31.84 124.69 REMARK 500 6 MET A 28 -175.82 -60.55 REMARK 500 6 ASN A 41 86.15 -62.94 REMARK 500 6 PRO A 48 37.04 -94.49 REMARK 500 6 SER A 49 -9.60 -53.55 REMARK 500 6 TYR A 51 64.64 -157.81 REMARK 500 7 ALA A 11 104.81 -178.57 REMARK 500 7 GLU A 14 108.10 -53.62 REMARK 500 REMARK 500 THIS ENTRY HAS 84 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2FRY RELATED DB: PDB REMARK 900 THE THIRD SH3 DOMAIN OF THE SAME PROTEIN DBREF 2FRW A 1 57 UNP O43639 NCK2_HUMAN 114 170 SEQRES 1 A 57 ILE PRO ALA PHE VAL LYS PHE ALA TYR VAL ALA GLU ARG SEQRES 2 A 57 GLU ASP GLU LEU SER LEU VAL LYS GLY SER ARG VAL THR SEQRES 3 A 57 VAL MET GLU LYS CYS SER ASP GLY TRP TRP ARG GLY SER SEQRES 4 A 57 TYR ASN GLY GLN ILE GLY TRP PHE PRO SER ASN TYR VAL SEQRES 5 A 57 LEU GLU GLU VAL ASP HELIX 1 1 PRO A 48 ASN A 50 5 3 SHEET 1 A 3 ARG A 24 VAL A 25 0 SHEET 2 A 3 ALA A 3 VAL A 5 -1 N ALA A 3 O VAL A 25 SHEET 3 A 3 VAL A 52 LEU A 53 -1 O LEU A 53 N PHE A 4 SHEET 1 B 2 ARG A 37 TYR A 40 0 SHEET 2 B 2 GLN A 43 TRP A 46 -1 O GLN A 43 N TYR 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