Header list of 1d5q.pdb file
Complete list - 16 202 Bytes
HEADER BINDING PROTEIN 11-OCT-99 1D5Q TITLE SOLUTION STRUCTURE OF A MINI-PROTEIN REPRODUCING THE CORE OF THE CD4 TITLE 2 SURFACE INTERACTING WITH THE HIV-1 ENVELOPE GLYCOPROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHIMERIC MINI-PROTEIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: SYNTHETIC MINIPROTEIN (SOLID PHASE METHOD USING FMOC- SOURCE 4 PROTECTED AMINO ACIDS) KEYWDS ALPHA-BETA STRUCTURE, CHARYBDOTOXIN-LIKE MOTIF, BINDING PROTEIN EXPDTA SOLUTION NMR AUTHOR C.VITA,E.DRAKOPOULOU,J.VIZZANOVA,S.ROCHETTE,L.MARTIN,A.MENEZ, AUTHOR 2 C.ROUMESTAND,Y.S.YANG,L.YLISASTIGUI,A.BENJOUAD,J.C.GLUCKMAN REVDAT 4 16-FEB-22 1D5Q 1 REMARK REVDAT 3 24-FEB-09 1D5Q 1 VERSN REVDAT 2 01-APR-03 1D5Q 1 JRNL REVDAT 1 11-OCT-00 1D5Q 0 JRNL AUTH C.VITA,E.DRAKOPOULOU,J.VIZZAVONA,S.ROCHETTE,L.MARTIN, JRNL AUTH 2 A.MENEZ,C.ROUMESTAND,Y.S.YANG,L.YLISASTIGUI,A.BENJOUAD, JRNL AUTH 3 J.C.GLUCKMAN JRNL TITL RATIONAL ENGINEERING OF A MINIPROTEIN THAT REPRODUCES THE JRNL TITL 2 CORE OF THE CD4 SITE INTERACTING WITH HIV-1 ENVELOPE JRNL TITL 3 GLYCOPROTEIN. JRNL REF PROC.NATL.ACAD.SCI.USA V. 96 13091 1999 JRNL REFN ISSN 0027-8424 JRNL PMID 10557278 JRNL DOI 10.1073/PNAS.96.23.13091 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : GIFA 4.22, X-PLOR 3.1 REMARK 3 AUTHORS : PONS, J.L.,MALLIAVIN, T., DELSUC, M.A. (GIFA), REMARK 3 BRUNGER, A.T. (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON A TOTAL OF REMARK 3 239 DISTANCE RESTRAINTS, 46 ANGULAR RESTRAINTS, AND 9 ADDITIONAL REMARK 3 RESTRAINTS FOR THE DISULFIDE BRIDGES REMARK 4 REMARK 4 1D5Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-99. REMARK 100 THE DEPOSITION ID IS D_1000009816. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 3.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : H2O AND D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : GIFA 4.22, X-PLOR 3.1 REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR REMARK 210 DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 40 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: ADDITIONAL EXPERIMENTS (2D NOESY, 2D DQF-COSY) RECORDED AT REMARK 210 35 C 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: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 5 0.32 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1CDH RELATED DB: PDB REMARK 900 RELATED ID: 1SCY RELATED DB: PDB DBREF 1D5Q A 1 27 PDB 1D5Q 1D5Q 1 27 SEQRES 1 A 27 CYS ASN LEU ALA ARG CYS GLN LEU SER CYS LYS SER LEU SEQRES 2 A 27 GLY LEU LYS GLY GLY CYS GLN GLY SER PHE CYS THR CYS SEQRES 3 A 27 GLY HELIX 1 1 ASN A 2 GLY A 14 1 13 SHEET 1 A 2 GLY A 17 GLN A 20 0 SHEET 2 A 2 PHE A 23 CYS A 26 -1 O PHE A 23 N GLN A 20 SSBOND 1 CYS A 1 CYS A 19 1555 1555 2.02 SSBOND 2 CYS A 6 CYS A 24 1555 1555 2.02 SSBOND 3 CYS A 10 CYS A 26 1555 1555 2.02 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
Complete list - 16 202 Bytes