Header list of 1qgb.pdb file
Complete list - v 3 2 Bytes
HEADER CELL ADHESION 21-APR-99 1QGB TITLE SOLUTION STRUCTURE OF THE N-TERMINAL F1 MODULE PAIR FROM HUMAN TITLE 2 FIBRONECTIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (FIBRONECTIN); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL F1 MODULE PAIR; 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 EXPRESSION_SYSTEM: PICHIA PASTORIS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: GS115 KEYWDS FIBRONECTIN TYPE 1 MODULE PAIR, CELL ADHESION EXPDTA SOLUTION NMR NUMMDL 24 AUTHOR J.R.POTTS,J.R.BRIGHT,D.BOLTON,A.R.PICKFORD,I.D.CAMPBELL REVDAT 3 03-NOV-21 1QGB 1 REMARK REVDAT 2 24-FEB-09 1QGB 1 VERSN REVDAT 1 08-DEC-99 1QGB 0 JRNL AUTH J.R.POTTS,J.R.BRIGHT,D.BOLTON,A.R.PICKFORD,I.D.CAMPBELL JRNL TITL SOLUTION STRUCTURE OF THE N-TERMINAL F1 MODULE PAIR FROM JRNL TITL 2 HUMAN FIBRONECTIN. JRNL REF BIOCHEMISTRY V. 38 8304 1999 JRNL REFN ISSN 0006-2960 JRNL PMID 10387076 JRNL DOI 10.1021/BI990202B REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION ABOVE. REMARK 4 REMARK 4 1QGB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-99. REMARK 100 THE DEPOSITION ID IS D_1000000929. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 4.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : 2.2 MM [U-15N] 1F1-2F1, 90% REMARK 210 H2O/10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; TOCSY; NOESY; 3D-NOESY REMARK 210 -HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : OXFORD REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.851 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOW ENERGY AND AGREEMENT WITH REMARK 210 EXPERIMENTAL RESTRAINTS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING NMR SPECTROSCOPY ON REMARK 210 UNIFORMLY 15N-LABELLED 1F1-2F1 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 ASP A 23 H LYS A 26 1.58 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 18 131.26 -171.89 REMARK 500 1 PRO A 19 -165.48 -74.19 REMARK 500 1 ILE A 30 151.62 -36.47 REMARK 500 1 LEU A 39 -48.42 82.89 REMARK 500 1 ALA A 42 141.96 -36.53 REMARK 500 1 LEU A 43 99.38 -169.92 REMARK 500 1 LYS A 59 103.05 -36.55 REMARK 500 1 GLU A 61 57.39 -157.45 REMARK 500 1 ALA A 62 105.67 50.85 REMARK 500 1 GLU A 64 63.05 159.37 REMARK 500 1 THR A 65 154.54 170.66 REMARK 500 1 CYS A 66 -154.55 -126.07 REMARK 500 1 PHE A 67 -40.31 -158.30 REMARK 500 1 ASP A 68 70.07 71.01 REMARK 500 1 TYR A 81 110.70 -160.65 REMARK 500 1 ASP A 86 -159.16 80.65 REMARK 500 1 CYS A 94 69.65 -63.08 REMARK 500 1 ILE A 95 46.89 -89.64 REMARK 500 1 ALA A 97 -89.05 61.38 REMARK 500 1 ARG A 99 -67.68 -174.87 REMARK 500 1 ARG A 101 42.28 -109.25 REMARK 500 1 ILE A 102 95.90 -52.55 REMARK 500 2 LYS A 18 89.76 55.21 REMARK 500 2 PRO A 19 -163.87 -56.24 REMARK 500 2 ASN A 24 -75.67 -34.96 REMARK 500 2 ALA A 42 147.57 -35.04 REMARK 500 2 SER A 51 -0.56 85.78 REMARK 500 2 LYS A 59 136.70 -39.55 REMARK 500 2 PRO A 60 -169.10 -49.23 REMARK 500 2 GLU A 64 57.03 -95.85 REMARK 500 2 PHE A 67 97.94 -163.83 REMARK 500 2 LYS A 69 -30.25 -39.41 REMARK 500 2 ASP A 91 95.07 -66.88 REMARK 500 2 CYS A 94 51.01 -96.80 REMARK 500 2 ALA A 97 94.84 83.70 REMARK 500 2 ARG A 99 34.59 -166.67 REMARK 500 2 ARG A 101 56.77 -106.90 REMARK 500 2 ALA A 107 -178.57 46.51 REMARK 500 2 ASN A 108 40.78 -97.58 REMARK 500 3 LYS A 18 145.76 58.32 REMARK 500 3 ILE A 30 140.38 -35.00 REMARK 500 3 ARG A 36 -163.91 -115.63 REMARK 500 3 THR A 37 32.37 -167.08 REMARK 500 3 ALA A 42 135.10 -31.01 REMARK 500 3 PHE A 54 172.97 -59.70 REMARK 500 3 GLU A 57 -94.06 -141.28 REMARK 500 3 SER A 58 131.33 178.86 REMARK 500 3 ALA A 62 -165.02 -161.50 REMARK 500 3 GLU A 64 -172.65 72.77 REMARK 500 3 THR A 65 -167.03 48.83 REMARK 500 REMARK 500 THIS ENTRY HAS 441 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1QGB A 17 109 UNP P02751 FINC_HUMAN 48 140 SEQRES 1 A 93 SER LYS PRO GLY CYS TYR ASP ASN GLY LYS HIS TYR GLN SEQRES 2 A 93 ILE ASN GLN GLN TRP GLU ARG THR TYR LEU GLY ASN ALA SEQRES 3 A 93 LEU VAL CYS THR CYS TYR GLY GLY SER ARG GLY PHE ASN SEQRES 4 A 93 CYS GLU SER LYS PRO GLU ALA GLU GLU THR CYS PHE ASP SEQRES 5 A 93 LYS TYR THR GLY ASN THR TYR ARG VAL GLY ASP THR TYR SEQRES 6 A 93 GLU ARG PRO LYS ASP SER MET ILE TRP ASP CYS THR CYS SEQRES 7 A 93 ILE GLY ALA GLY ARG GLY ARG ILE SER CYS THR ILE ALA SEQRES 8 A 93 ASN ARG SHEET 1 A 2 CYS A 21 ASP A 23 0 SHEET 2 A 2 LYS A 26 TYR A 28 -1 N LYS A 26 O ASP A 23 SHEET 1 B 2 GLN A 33 THR A 37 0 SHEET 2 B 2 ALA A 42 THR A 46 -1 O LEU A 43 N ARG A 36 SHEET 1 C 2 TRP A 90 THR A 93 0 SHEET 2 C 2 SER A 103 ILE A 106 -1 O SER A 103 N THR A 93 SSBOND 1 CYS A 21 CYS A 47 1555 1555 2.03 SSBOND 2 CYS A 45 CYS A 56 1555 1555 2.03 SSBOND 3 CYS A 66 CYS A 94 1555 1555 2.03 SSBOND 4 CYS A 92 CYS A 104 1555 1555 2.03 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 - v 3 2 Bytes