Header list of 1lb7.pdb file
Complete list - 23 20 Bytes
HEADER DE NOVO PROTEIN 02-APR-02 1LB7
TITLE IGF-F1-1, A PEPTIDE ANTAGONIST OF IGF-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IGF-1 ANTAGONIST F1-1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: DE NOVO SEQUENCE DERIVED FROM PHAGE DISPLAY LIBRARY
KEYWDS LOOP-HELIX, DISULFIDE, DE NOVO PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.DESHAYES,M.L.SCHAFFER,N.J.SKELTON,G.R.NAKAMURA,S.KADKHODAYAN,
AUTHOR 2 S.S.SIDHU
REVDAT 4 23-FEB-22 1LB7 1 REMARK
REVDAT 3 24-FEB-09 1LB7 1 VERSN
REVDAT 2 01-APR-03 1LB7 1 JRNL
REVDAT 1 19-JUN-02 1LB7 0
JRNL AUTH K.DESHAYES,M.L.SCHAFFER,N.J.SKELTON,G.R.NAKAMURA,
JRNL AUTH 2 S.KADKHODAYAN,S.S.SIDHU
JRNL TITL RAPID IDENTIFICATION OF SMALL BINDING MOTIFS WITH
JRNL TITL 2 HIGH-THROUGHPUT PHAGE DISPLAY: DISCOVERY OF PEPTIDIC
JRNL TITL 3 ANTAGONISTS OF IGF-1 FUNCTION.
JRNL REF CHEM.BIOL. V. 9 495 2002
JRNL REFN ISSN 1074-5521
JRNL PMID 11983338
JRNL DOI 10.1016/S1074-5521(02)00129-1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII V98.0, DISCOVER V98.0, TALOS FEB 2000
REMARK 3 AUTHORS : HAVEL (DGII), ACCELRYS (DISCOVER), DELAGLIO & BAX
REMARK 3 (TALOS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON 91 DISTANCE RESTRAINTS AND 26 DIHEDRAL
REMARK 3 ANGLE RESTRAINTS.
REMARK 3 NONE OF THE FINAL STRUCTURES HAVE VIOLATIONS > 0.07A OR 1.0
REMARK 3 DEGREES.
REMARK 3 THE MEAN RMSD TO THE MEAN COORDINATES FOR HEAVY ATOMS OF RESIDUES
REMARK 3 CYS3 TO TYR15 IS 0.31+/-0.06 A.
REMARK 4
REMARK 4 1LB7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-APR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015807.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.1
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : ATM
REMARK 210 SAMPLE CONTENTS : 5.0 MM IGF-F1-1 90%, H2O, 10%
REMARK 210 D2O, PH 5.1; 5.0 MM IGF-F1-F,
REMARK 210 100% D2O, PH* 5.1
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D-ROESY; COSY-35; 1H
REMARK 210 -13C-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY, MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK:
REMARK 210 THIS STRUCTURE WAS DETERMINED USING STANDARD 2D HOMONUCLEAR
REMARK 210 TECHNIQUES
REMARK 210 TO GENERATE DISTANCE (ROESY) AND DIHEDERAL ANGLE (DQF-COSY, COSY-
REMARK 210 35)RESTRAINTS.
REMARK 210 ADDITIONAL DIHEDRAL ANGLE RESTRAINTS WERE DERIVED FROM CHEMICAL
REMARK 210 SHIFT
REMARK 210 INFORMATION USING THE PROGRAM TALOS
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: 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 2 TYR A 15 40.75 -86.67
REMARK 500 5 GLU A 5 -71.67 -128.68
REMARK 500 6 GLU A 5 -51.67 -146.42
REMARK 500 6 TYR A 15 55.65 -93.82
REMARK 500 7 TYR A 15 49.56 -96.73
REMARK 500 8 ASN A 2 48.57 -80.72
REMARK 500 12 TYR A 15 49.25 -94.80
REMARK 500 13 PHE A 4 47.54 -89.38
REMARK 500 15 GLU A 5 -38.52 -150.18
REMARK 500 16 PHE A 4 50.17 -142.87
REMARK 500 16 TYR A 15 46.53 -85.83
REMARK 500 18 TYR A 15 68.39 -100.26
REMARK 500 19 PHE A 4 51.52 -144.25
REMARK 500
REMARK 500 REMARK: NULL
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 3 PHE A 4 0.07 SIDE CHAIN
REMARK 500 3 TYR A 15 0.07 SIDE CHAIN
REMARK 500 17 TYR A 15 0.08 SIDE CHAIN
REMARK 500 18 TYR A 15 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1LB7 A 1 16 PDB 1LB7 1LB7 1 16
SEQRES 1 A 16 ARG ASN CYS PHE GLU SER VAL ALA ALA LEU ARG ARG CYS
SEQRES 2 A 16 MET TYR GLY
HELIX 1 1 SER A 6 GLY A 16 1 11
SSBOND 1 CYS A 3 CYS A 13 1555 1555 2.04
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 - 23 20 Bytes