Header list of 1pmx.pdb file
Complete list - b 23 2 Bytes
HEADER HORMONE/GROWTH FACTOR 11-JUN-03 1PMX TITLE INSULIN-LIKE GROWTH FACTOR-I BOUND TO A PHAGE-DERIVED PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: INSULIN-LIKE GROWTH FACTOR IB; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: IGF-IB, SOMATOMEDIN C; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: IGF-1 ANTAGONIST F1-1; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: 43E7; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBKIGF2B; SOURCE 10 MOL_ID: 2; SOURCE 11 SYNTHETIC: YES; SOURCE 12 OTHER_DETAILS: SEQUENCE DERIVED FROM PHAGE DISPLAY LIBRARY AND SOURCE 13 PREPARED BY CHEMICAL SYNTHESIS KEYWDS IGF-I, PEPTIDE BINDING, HIGH AFFINITY LIGAND, HORMONE-GROWTH FACTOR KEYWDS 2 COMPLEX EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR N.J.SKELTON REVDAT 3 23-FEB-22 1PMX 1 REMARK REVDAT 2 24-FEB-09 1PMX 1 VERSN REVDAT 1 21-OCT-03 1PMX 0 JRNL AUTH M.L.SCHAFFER,K.DESHAYES,G.NAKAMURA,S.SIDHU,N.J.SKELTON JRNL TITL COMPLEX WITH A PHAGE DISPLAY-DERIVED PEPTIDE PROVIDES JRNL TITL 2 INSIGHT INTO THE FUNCTION OF INSULIN-LIKE GROWTH FACTOR I JRNL REF BIOCHEMISTRY V. 42 9324 2003 JRNL REFN ISSN 0006-2960 JRNL PMID 12899619 JRNL DOI 10.1021/BI034386C REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH K.DESHAYES,M.L.SCHAFFER,N.J.SKELTON,G.R.NAKAMURA, REMARK 1 AUTH 2 S.KADKHODAYAN,S.S.SIDHU REMARK 1 TITL RAPID IDENTIFICATION OF SMALL BINDING MOTIFS WITH REMARK 1 TITL 2 HIGH-THROUGHPUT PHAGE DISPLAY. DISCOVERY OF PEPTIDIC REMARK 1 TITL 3 ANTAGONISTS OF IGF-1 FUNCTION REMARK 1 REF CHEM.BIOL. V. 9 495 2002 REMARK 1 REFN ISSN 1074-5521 REMARK 1 DOI 10.1016/S1074-5521(02)00129-1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 2000.1 REMARK 3 AUTHORS : ACCELRYS REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE COMPLEX WAS DETERMINED USING A REMARK 3 TOTAL OF 905 NOE DISTANCE RESTRAINTS (146 INTRA RESIDUE, 203 REMARK 3 SEQUENTIAL, 232 MEDIUM RANGE, 237 LONG-RANGE AND 87 REMARK 3 INTERMOLECULAR), 24 HYDROGEN BOND RESTRAINTS, 139 DIHEDRAL ANGLE REMARK 3 RESTRAINTS (72 PHI, 44 PSI AND 23 CHI-1). THE BEST 20 CONFORMERS REMARK 3 (OF 100) HAD NO DISTANCE VIOLATIONS GREATER THAN 0.11A AND NO REMARK 3 DIHEDRAL ANGLE VIOLATIONS GREATER THAN 1.5 DEGREES. RMSD FROM REMARK 3 EXPERIMENTAL DISTANCE RESTRAINTS WAS 0.0049+/-0.0008. THE MEAN REMARK 3 BACKBONE RMSD FROM THE MEAN STRUCTURE WAS 0.35 +/- 0.06 A FOR N, REMARK 3 CA AND C ATOMS OF RESIDUES 3-26, 42-63 OF IGF-I AND RESIDUES 3- REMARK 3 15 OF THE PEPTIDE. 82% (17%) OF RESIDUES WERE IN THE MOST REMARK 3 FAVOURED (ALLOWED) REGION OF PHI/PSI SPACE; NO RESIDUES WERE REMARK 3 CONSISTENTLY IN THE DISALLOWED REGION. REMARK 4 REMARK 4 1PMX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUN-03. REMARK 100 THE DEPOSITION ID IS D_1000019435. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 313 REMARK 210 PH : 5.1 REMARK 210 IONIC STRENGTH : 25 MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1.4 MM IGF-I (15N), 2.0 MM REMARK 210 PEPTIDE, 25 MM SODIUM ACETATE; REMARK 210 1.4 MM IGF-I (13C,15N), 2.0 MM REMARK 210 PEPTIDE, 25 MM SODIUM ACETATE; REMARK 210 1.4 MM IGF-I (13C,15N), 2.0 MM REMARK 210 PEPTIDE, 25 MM SODIUM ACETATE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA; D REMARK 210 -HNHB; 3D 15N-SEPARATED LOW REMARK 210 MIXING TIME TOCSY; 2D-15N- REMARK 210 FILTERED NOESY; 3D_13C-SEPARATED_ REMARK 210 NOESY; 3D-13_FILTERED; 13C- REMARK 210 EDITED NOESY; 2D-13C-FILTERED REMARK 210 NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.1, FELIX 98 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST VIOLATION OF EXPERIMENTAL REMARK 210 RESTRAINTS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE RESONANCE ASSIGNMENTS WERE DETERMINED USING TRIPLE REMARK 210 -RESONANCE NMR SPECTROSCOPY. 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 1 THR A 29 -47.15 -151.29 REMARK 500 1 SER A 33 -48.76 -150.06 REMARK 500 1 CYS A 52 -163.05 -105.49 REMARK 500 1 LEU A 64 170.95 -58.34 REMARK 500 1 PRO A 66 -169.18 -69.85 REMARK 500 2 PRO A 2 -168.80 -72.90 REMARK 500 2 THR A 29 -46.65 -172.58 REMARK 500 2 SER A 34 -56.39 -157.80 REMARK 500 2 THR A 41 127.77 -177.56 REMARK 500 2 LEU A 64 -179.73 -58.16 REMARK 500 2 ALA A 67 -68.00 -156.45 REMARK 500 2 PHE B 104 36.37 -97.92 REMARK 500 3 PHE A 25 -75.00 -59.23 REMARK 500 3 SER A 34 -65.24 -94.41 REMARK 500 3 ARG A 36 -68.92 -105.32 REMARK 500 3 ARG A 37 34.73 -162.92 REMARK 500 3 PRO A 39 -168.64 -73.33 REMARK 500 3 PHE B 104 46.57 -94.63 REMARK 500 4 THR A 29 32.22 -164.42 REMARK 500 4 SER A 35 -65.54 -148.80 REMARK 500 4 ALA A 38 -64.17 -168.94 REMARK 500 4 PHE B 104 32.84 -96.52 REMARK 500 5 PRO A 2 -168.71 -71.84 REMARK 500 5 SER A 34 -63.37 -147.55 REMARK 500 5 SER A 35 -74.83 -159.45 REMARK 500 5 LEU A 64 176.33 -59.22 REMARK 500 5 PRO A 66 83.21 -61.47 REMARK 500 5 ALA A 67 -176.21 -175.58 REMARK 500 6 ALA A 67 -51.89 -152.45 REMARK 500 6 LYS A 68 -48.16 -139.25 REMARK 500 6 SER A 69 32.73 -158.72 REMARK 500 6 PHE B 104 37.89 -96.04 REMARK 500 7 SER A 34 -65.45 -163.48 REMARK 500 7 PRO A 39 -168.17 -65.74 REMARK 500 7 ALA A 67 -70.99 -93.86 REMARK 500 8 SER A 35 33.40 -153.50 REMARK 500 8 PRO A 39 -168.83 -75.01 REMARK 500 8 PHE B 104 32.86 -98.60 REMARK 500 9 SER A 34 35.96 -99.21 REMARK 500 9 ALA A 38 94.88 -174.75 REMARK 500 9 PRO A 66 -167.80 -65.21 REMARK 500 9 PHE B 104 32.82 -97.27 REMARK 500 10 THR A 29 -58.08 -126.41 REMARK 500 10 SER A 35 -64.06 -91.35 REMARK 500 10 CYS A 52 -169.20 -111.77 REMARK 500 11 PRO A 2 43.53 -90.25 REMARK 500 11 THR A 29 -50.37 -179.20 REMARK 500 11 TYR A 31 -52.64 -148.57 REMARK 500 11 SER A 34 -70.67 -155.18 REMARK 500 11 SER A 35 34.69 -170.17 REMARK 500 REMARK 500 THIS ENTRY HAS 104 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1LB7 RELATED DB: PDB REMARK 900 STRUCTURE OF FREE PEPTIDE IGF-F1-1 DBREF 1PMX A 1 70 UNP P05019 IGF1B_HUMAN 49 118 DBREF 1PMX B 101 116 PDB 1PMX 1PMX 101 116 SEQRES 1 A 70 GLY PRO GLU THR LEU CYS GLY ALA GLU LEU VAL ASP ALA SEQRES 2 A 70 LEU GLN PHE VAL CYS GLY ASP ARG GLY PHE TYR PHE ASN SEQRES 3 A 70 LYS PRO THR GLY TYR GLY SER SER SER ARG ARG ALA PRO SEQRES 4 A 70 GLN THR GLY ILE VAL ASP GLU CYS CYS PHE ARG SER CYS SEQRES 5 A 70 ASP LEU ARG ARG LEU GLU MET TYR CYS ALA PRO LEU LYS SEQRES 6 A 70 PRO ALA LYS SER ALA SEQRES 1 B 16 ARG ASN CYS PHE GLU SER VAL ALA ALA LEU ARG ARG CYS SEQRES 2 B 16 MET TYR GLY HELIX 1 1 GLY A 7 CYS A 18 1 12 HELIX 2 2 GLY A 19 GLY A 22 5 4 HELIX 3 3 ILE A 43 CYS A 48 1 6 HELIX 4 4 ARG A 55 CYS A 61 1 7 HELIX 5 5 SER B 106 TYR B 115 1 10 SSBOND 1 CYS A 6 CYS A 48 1555 1555 2.03 SSBOND 2 CYS A 18 CYS A 61 1555 1555 2.03 SSBOND 3 CYS A 47 CYS A 52 1555 1555 2.03 SSBOND 4 CYS B 103 CYS B 113 1555 1555 2.03 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 - b 23 2 Bytes