Header list of 1imw.pdb file
Complete list - 25 20 Bytes
HEADER ANTAGONIST 11-MAY-01 1IMW
TITLE PEPTIDE ANTAGONIST OF IGFBP-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IGFBP-1 ANTAGONIST;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. IT IS A NOVEL
SOURCE 4 SEQUENCE DERIVED FROM PHAGE-DISPLAY SELECTION.
KEYWDS LOOP-TURN-HELIX, DE NOVO PROTEIN, ANTAGONIST
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.B.LOWMAN,Y.M.CHEN,N.J.SKELTON,D.L.MORTENSEN,E.E.TOMLINSON,
AUTHOR 2 M.D.SADICK,I.C.ROBINSON,R.G.CLARK
REVDAT 3 13-JUL-11 1IMW 1 VERSN
REVDAT 2 24-FEB-09 1IMW 1 VERSN
REVDAT 1 30-MAY-01 1IMW 0
JRNL AUTH N.J.SKELTON,Y.M.CHEN,N.DUBREE,C.QUAN,D.Y.JACKSON,A.COCHRAN,
JRNL AUTH 2 K.ZOBEL,K.DESHAYES,M.BACA,M.T.PISABARRO,H.B.LOWMAN
JRNL TITL STRUCTURE-FUNCTION ANALYSIS OF A PHAGE DISPLAY-DERIVED
JRNL TITL 2 PEPTIDE THAT BINDS TO INSULIN-LIKE GROWTH FACTOR BINDING
JRNL TITL 3 PROTEIN 1.
JRNL REF BIOCHEMISTRY V. 40 8487 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11456486
JRNL DOI 10.1021/BI980426E
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII 970, DISCOVER 970
REMARK 3 AUTHORS : HAVEL (DGII), MSI/BIOSYM (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES WERE DETEMINED ON THE
REMARK 3 BASIS OF 149 NOE DISTANCE RESTRAINTS AND 15 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS. THE RESULTING ENSEMBLE HAD NO RESTRAINT VIOLATIONS
REMARK 3 GREATER THAN 0.07 ANGSTROMS OR 1.4 DEG. THE MEAN RESTRAINT
REMARK 3 VIOLATION ENERGY WAS 0.17+/- 0.06 KCAL/MOL.
REMARK 4
REMARK 4 1IMW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAY-01.
REMARK 100 THE RCSB ID CODE IS RCSB013416.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 303
REMARK 210 PH : 5.3; 5.3
REMARK 210 IONIC STRENGTH : 0; 0
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 6.7 MM PEPTIDE; 6.7 MM PEPTIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-ROESY; DQF-COSY; COSY-35
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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 3 PHE A 14 46.22 -89.43
REMARK 500 6 LEU A 6 37.55 -99.59
REMARK 500 6 PHE A 14 -78.48 -89.47
REMARK 500 7 PRO A 5 44.34 -80.08
REMARK 500 7 LEU A 6 -24.77 -140.05
REMARK 500 7 TYR A 13 -60.18 -95.60
REMARK 500 7 PHE A 14 41.03 -89.67
REMARK 500 8 PHE A 14 48.34 -89.49
REMARK 500 9 ALA A 3 98.37 -67.30
REMARK 500 12 ARG A 2 82.83 -169.03
REMARK 500 13 PHE A 14 47.25 -89.73
REMARK 500 14 PHE A 14 37.49 -89.71
REMARK 500 15 ALA A 3 79.85 -69.27
REMARK 500 18 LEU A 6 31.83 -99.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IN2 RELATED DB: PDB
REMARK 900 PEPTIDE ANTAGONIST OF IGFBP1, (I,I+7) COVALENTLY RESTRAINED
REMARK 900 ANALOG
REMARK 900 RELATED ID: 1IN3 RELATED DB: PDB
REMARK 900 PEPTIDE ANTAGONIST OF IGFBP1, (I,I+8) COVALENTLY RESTRAINED
REMARK 900 ANALOG
REMARK 900 RELATED ID: 1GJE RELATED DB: PDB
REMARK 900 PEPTIDE ANTAGONIST OF IGFBP-1, MINIMIZED AVERAGE STRUCTURE
REMARK 900 RELATED ID: 1GJF RELATED DB: PDB
REMARK 900 PEPTIDE ANTAGONIST OF IGFBP1, (I,I+7) COVALENTLY RESTRAINED
REMARK 900 ANALOG, MINIMIZED AVERAGE STRUCTURE
REMARK 900 RELATED ID: 1GJG RELATED DB: PDB
REMARK 900 PEPTIDE ANTAGONIST OF IGFBP1, (I,I+8) COVALENTLY RESTRAINED
REMARK 900 ANALOG, MINIMIZED AVERAGE STRUCTURE
DBREF 1IMW A 1 16 PDB 1IMW 1IMW 1 16
SEQRES 1 A 16 CYS ARG ALA GLY PRO LEU GLN TRP LEU CYS GLU LYS TYR
SEQRES 2 A 16 PHE GLY NH2
HET NH2 A 16 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 LEU A 6 TYR A 13 1 8
SSBOND 1 CYS A 1 CYS A 10 1555 1555 2.05
LINK C GLY A 15 N NH2 A 16 1555 1555 1.33
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 - 25 20 Bytes