Header list of 1u0i.pdb file
Complete list - r 2 2 Bytes
HEADER DE NOVO PROTEIN 13-JUL-04 1U0I TITLE IAAL-E3/K3 HETERODIMER COMPND MOL_ID: 1; COMPND 2 MOLECULE: IAAL-E3; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: IAAL-K3; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED USING T- SOURCE 4 BUTYLOXYCARBONYL SOLID-PHASE TECHNIQUE; SOURCE 5 MOL_ID: 2; SOURCE 6 SYNTHETIC: YES; SOURCE 7 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED USING T- SOURCE 8 BUTYLOXYCARBONYL SOLID-PHASE TECHNIQUE KEYWDS COILED-COIL, DE NOVO PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR D.A.LINDHOUT,J.R.LITOWSKI,P.MERCIER,R.S.HODGES,B.D.SYKES REVDAT 4 02-MAR-22 1U0I 1 REMARK REVDAT 3 24-FEB-09 1U0I 1 VERSN REVDAT 2 25-JAN-05 1U0I 1 JRNL REVDAT 1 19-OCT-04 1U0I 0 JRNL AUTH D.A.LINDHOUT,J.R.LITOWSKI,P.MERCIER,R.S.HODGES,B.D.SYKES JRNL TITL NMR SOLUTION STRUCTURE OF A HIGHLY STABLE DE NOVO JRNL TITL 2 HETERODIMERIC COILED-COIL JRNL REF BIOPOLYMERS V. 75 367 2004 JRNL REFN ISSN 0006-3525 JRNL PMID 15457434 JRNL DOI 10.1002/BIP.20150 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CYANA 1.0 REMARK 3 AUTHORS : GUNTERT REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: SOFTWARE USED WAS CYANA AND ITS REMARK 3 INTEGRATED AUTO-ASSIGNMENT MODULE CANDID. THE CHEMICAL SHIFT REMARK 3 IDENTIFICATION TOLERANCE AND TRANSPOSE ERRORS WERE SET TO 0.015 REMARK 3 PPM IN BOTH PROTON DIMENSIONS. STARTING WITH DISTANCE RESTRAINTS REMARK 3 DERIVED FROM MANUALLY ASSIGNED NOE CROSS-PEAKS IN NMRVIEW, A REMARK 3 TOTAL NUMBER OF 100 STRUCTURES WERE GENERATED PER CANDID ROUND REMARK 3 WITH 8000 STEPS IN THE CYANA ANNEALING PROTOCOL. FOR EACH CANDID REMARK 3 RUN, TALOS DERIVED ANGLE RESTRAINTS WERE INCORPORATED (WITH A REMARK 3 MINIMUM ERROR SET MANUALLY TO 20 DEGREES) . THE BEST 20 LOW REMARK 3 TARGET FUNCTION VALUE STRUCTURES OF CANDIDS FINAL ROUND WERE REMARK 3 KEPT AS AN ENSEMBLE REPRESENTATION OF THE FAMILY OF GENERATED REMARK 3 STRUCTURES. REMARK 4 REMARK 4 1U0I COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-04. REMARK 100 THE DEPOSITION ID IS D_1000023092. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 6.7 REMARK 210 IONIC STRENGTH : 0.15 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM IAAL-E3/K3 COILED-COIL, NA REMARK 210 -15N, PH 6.7, 100MM KCL, 50MM REMARK 210 KPO4,90%/10% H2O/D2O, 23.1% TFE- REMARK 210 D3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : UNITY REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CYANA 1.0 REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING, CHEMICAL-SHIFT AUTO - REMARK 210 ASSIGNMENT, DISTANCE GEOMETRY, REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH REMARK 210 EXPERIMENTAL NOESY SPECTRUM REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 3 ILE B 2 -55.89 -122.33 REMARK 500 15 ILE A 2 -62.35 -128.82 REMARK 500 REMARK 500 REMARK: NULL DBREF 1U0I A 1 21 PDB 1U0I 1U0I 1 21 DBREF 1U0I B 1 21 PDB 1U0I 1U0I 1 21 SEQRES 1 A 21 GLU ILE ALA ALA LEU GLU LYS GLU ILE ALA ALA LEU GLU SEQRES 2 A 21 LYS GLU ILE ALA ALA LEU GLU LYS SEQRES 1 B 21 LYS ILE ALA ALA LEU LYS GLU LYS ILE ALA ALA LEU LYS SEQRES 2 B 21 GLU LYS ILE ALA ALA LEU LYS GLU HELIX 1 1 GLU A 1 LYS A 21 1 21 HELIX 2 2 LYS B 1 GLU B 21 1 21 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