Header list of 1in2.pdb file
Complete list - 25 20 Bytes
HEADER ANTAGONIST 11-MAY-01 1IN2
TITLE PEPTIDE ANTAGONIST OF IGFBP1, (I,I+7) COVALENTLY RESTRAINED ANALOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IGFBP-1 ANTAGONIST;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: (I,I+7) LOCKED HELIX VARIANT OF BP1-01
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. IT WAS
SOURCE 4 DESIGNED FROM SEQUENCE SELECTED FROM A PHAGE DISPLAY LIBRARY.
KEYWDS COVALENTLY CONSTRAINED HELIX, ANTAGONIST
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.J.SKELTON,Y.M.CHEN,N.DUBREE,C.QUAN,D.Y.JACKSON,A.G.COCHRAN,K.ZOBEL,
AUTHOR 2 K.DESHAYES,M.BACA,M.T.PISABARRO,H.B.LOWMAN
REVDAT 3 13-JUL-11 1IN2 1 VERSN
REVDAT 2 24-FEB-09 1IN2 1 VERSN
REVDAT 1 30-MAY-01 1IN2 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/BI0103866
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.B.LOWMAN,Y.M.CHEN,N.J.SKELTON,D.L.MORTENSEN,E.E.TOMLINSON,
REMARK 1 AUTH 2 M.D.SADICK,I.C.ROBINSON,R.G.CLARK
REMARK 1 TITL MOLECULAR MIMICS OF INSULIN-LIKE GROWTH FACTOR 1 (IGF-1) FOR
REMARK 1 TITL 2 INHIBITING IGF-1: IGF-BINDING PROTEIN INTERACTIONS
REMARK 1 REF BIOCHEMISTRY V. 37 8870 1998
REMARK 1 REFN ISSN 0006-2960
REMARK 1 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 (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS DETEMINED ON THE
REMARK 3 BASIS OF 138 NOE DISTANCE RESTRAINTS AND 11 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 0.04 +/- 0.03 KCAL/MOL.
REMARK 4
REMARK 4 1IN2 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 RCSB013420.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 303
REMARK 210 PH : 5.0; 5.0
REMARK 210 IONIC STRENGTH : 0; 0
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 5 MM PEPTIDE; 5 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 : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 970
REMARK 210 METHOD USED : RESTRAINED MOLECULAR 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: 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 1 LEU A 6 -47.62 -156.76
REMARK 500 2 LEU A 6 -46.69 -160.07
REMARK 500 3 PRO A 5 73.82 -65.88
REMARK 500 3 LEU A 6 -41.55 -160.15
REMARK 500 4 LEU A 6 -41.02 -160.38
REMARK 500 5 PRO A 5 47.97 -80.18
REMARK 500 5 LEU A 6 -45.07 -160.55
REMARK 500 6 LEU A 6 -31.16 -151.37
REMARK 500 7 LEU A 6 -39.60 -156.77
REMARK 500 8 LEU A 6 -39.73 -160.22
REMARK 500 9 PRO A 5 74.45 -66.27
REMARK 500 9 LEU A 6 -38.85 -139.21
REMARK 500 10 LEU A 6 -38.46 -160.33
REMARK 500 11 LEU A 6 -48.35 -159.84
REMARK 500 13 LEU A 6 -41.70 -160.23
REMARK 500 14 LEU A 6 -45.21 -160.58
REMARK 500 15 PRO A 5 74.47 -64.28
REMARK 500 15 LEU A 6 -40.71 -160.11
REMARK 500 16 LEU A 6 -42.40 -160.56
REMARK 500 19 PRO A 5 45.03 -86.81
REMARK 500 19 LEU A 6 -50.41 -160.46
REMARK 500 20 LEU A 6 -41.38 -148.25
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 7 TYR A 13 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LNK A 17
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IMW RELATED DB: PDB
REMARK 900 PEPTIDE ANTAGONIST OF IGFBP1
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 1IN2 A 1 16 PDB 1IN2 1IN2 1 16
SEQRES 1 A 16 ACE ARG ALA GLY PRO LEU GLN TRP LEU ALA GLU LYS TYR
SEQRES 2 A 16 GLN GLY NH2
HET ACE A 1 6
HET NH2 A 16 3
HET LNK A 17 15
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
HETNAM LNK PENTANE
FORMUL 1 ACE C2 H4 O
FORMUL 1 NH2 H2 N
FORMUL 2 LNK C5 H12
HELIX 1 1 LEU A 6 GLN A 14 1 9
LINK NE2 GLN A 7 C1 LNK A 17 1555 1555 1.46
LINK NE2 GLN A 14 C5 LNK A 17 1555 1555 1.46
LINK C ACE A 1 N ARG A 2 1555 1555 1.34
LINK C GLY A 15 N NH2 A 16 1555 1555 1.34
SITE 1 AC1 2 GLN A 7 GLN A 14
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