Header list of 3lri.pdb file
Complete list - v 3 2 Bytes
HEADER GROWTH FACTOR 13-APR-99 3LRI TITLE SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF LONG-[ARG(3)]INSULIN-LIKE TITLE 2 GROWTH FACTOR-I COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (INSULIN-LIKE GROWTH FACTOR I); COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: JM101; SOURCE 7 EXPRESSION_SYSTEM_COLLECTION: ATCC 33876; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID KEYWDS INSULIN-LIKE GROWTH FACTOR-1, GROWTH FACTOR, PROTEIN STRUCTURE, KEYWDS 2 DISTANCE GEOMETRY EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR L.G.LAAJOKI,G.L.FRANCIS,J.C.WALLACE,J.A.CARVER,M.A.KENIRY REVDAT 5 03-NOV-21 3LRI 1 SEQADV REVDAT 4 29-NOV-17 3LRI 1 REMARK HELIX REVDAT 3 24-FEB-09 3LRI 1 VERSN REVDAT 2 01-APR-03 3LRI 1 JRNL REVDAT 1 23-MAY-00 3LRI 0 JRNL AUTH L.G.LAAJOKI,G.L.FRANCIS,J.C.WALLACE,J.A.CARVER,M.A.KENIRY JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF JRNL TITL 2 LONG-[ARG(3)]INSULIN-LIKE GROWTH FACTOR-I JRNL REF J.BIOL.CHEM. V. 275 10009 2000 JRNL REFN ISSN 0021-9258 JRNL PMID 10744677 JRNL DOI 10.1074/JBC.275.14.10009 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5 REMARK 3 AUTHORS : GEUNTERT, P., WUTHRICH,K. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3LRI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-99. REMARK 100 THE DEPOSITION ID IS D_1000000840. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 3.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 15N-NOESY-HSQC; 3D 15N-TOCSY REMARK 210 -HSQC; 3D 15N-HSQC-NOESY-HSQC; REMARK 210 3D HNHA; 3D HNHB; 2D NOESY; 2D REMARK 210 TOCSY; 2D 15N-HSQC-TOCSY; 2D 15N- REMARK 210 HSQC-NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA 1.5 REMARK 210 METHOD USED : DISTANCE GEOMETRY AND MOLECULAR REMARK 210 DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING NMR ON 15N-LABELLED REMARK 210 LONG-[ARG3]-IGF-I. HOMONUCLEAR NMR EXPERIMENTS WERE PERFORMED ON REMARK 210 A SAMPLE WITH 100% D2O 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: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O GLY A 55 H GLU A 59 1.27 REMARK 500 O GLN A 28 H GLY A 32 1.46 REMARK 500 O GLU A 59 H ARG A 63 1.59 REMARK 500 O TYR A 73 N ALA A 75 1.75 REMARK 500 O GLN A 28 C GLY A 32 1.93 REMARK 500 O GLY A 55 N GLU A 59 2.09 REMARK 500 O GLN A 28 O GLY A 32 2.15 REMARK 500 O GLN A 28 N GLY A 32 2.18 REMARK 500 REMARK 500 REMARK: NULL 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 PHE A 2 100.84 50.04 REMARK 500 1 PRO A 3 -87.39 -75.01 REMARK 500 1 ALA A 4 -51.69 -24.25 REMARK 500 1 MET A 5 164.77 -41.28 REMARK 500 1 SER A 8 54.91 -162.09 REMARK 500 1 SER A 9 92.69 -161.69 REMARK 500 1 LEU A 10 -23.27 159.36 REMARK 500 1 PHE A 11 -20.95 -161.19 REMARK 500 1 ASN A 13 50.42 -101.47 REMARK 500 1 PRO A 15 -157.49 -75.01 REMARK 500 1 ARG A 16 -93.53 -100.66 REMARK 500 1 ASP A 33 -24.54 -38.41 REMARK 500 1 ARG A 34 -31.13 -32.41 REMARK 500 1 TYR A 37 -138.70 -102.72 REMARK 500 1 PHE A 38 -115.15 -146.38 REMARK 500 1 PRO A 41 49.05 -74.95 REMARK 500 1 THR A 42 -99.49 -38.26 REMARK 500 1 SER A 47 64.24 -170.15 REMARK 500 1 ARG A 49 114.10 -38.34 REMARK 500 1 ARG A 50 95.52 -33.84 REMARK 500 1 ALA A 51 -143.24 -160.22 REMARK 500 1 CYS A 52 -72.90 67.14 REMARK 500 1 GLN A 53 -28.37 -37.05 REMARK 500 1 THR A 54 33.87 -81.34 REMARK 500 1 ILE A 56 -6.73 -57.65 REMARK 500 1 SER A 64 97.53 -26.40 REMARK 500 1 ASP A 66 -137.75 -60.64 REMARK 500 1 CYS A 74 51.49 -4.36 REMARK 500 1 LEU A 77 151.27 -35.87 REMARK 500 1 ALA A 80 -44.48 -162.02 REMARK 500 1 LYS A 81 37.19 -179.36 REMARK 500 1 SER A 82 -70.82 -25.16 REMARK 500 2 PHE A 2 144.90 69.16 REMARK 500 2 PRO A 3 -79.83 -75.04 REMARK 500 2 ALA A 4 -68.99 -19.33 REMARK 500 2 SER A 8 55.14 -162.02 REMARK 500 2 LEU A 10 -2.13 90.90 REMARK 500 2 PHE A 11 -13.35 -170.85 REMARK 500 2 PRO A 15 -161.89 -75.01 REMARK 500 2 THR A 17 -76.90 -100.66 REMARK 500 2 LEU A 18 -121.42 -74.96 REMARK 500 2 LEU A 23 -44.60 -28.85 REMARK 500 2 ASP A 33 -27.98 -27.79 REMARK 500 2 PHE A 38 -86.42 -31.21 REMARK 500 2 ASN A 39 -149.33 -103.17 REMARK 500 2 THR A 42 170.17 -38.99 REMARK 500 2 ARG A 49 109.82 -35.84 REMARK 500 2 ARG A 50 110.46 -35.23 REMARK 500 2 THR A 54 33.81 -80.53 REMARK 500 2 ILE A 56 -6.12 -50.00 REMARK 500 REMARK 500 THIS ENTRY HAS 406 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: NTR REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: THE N TERMINUS OF IGF-I IS IMPORTANT FOR BINDING REMARK 800 TO IGF BINDING PROTEINS. RESIDUES 1-3 OF IGF-I ARE IMPLICATED AS REMARK 800 HAVING A ROLE ALTHOUGH GLU 3 IS MOST IMPORTANT. IN LONG-[ARG3]- REMARK 800 IGF-I THE RESPECTIVE RESIDUES ARE GLY 14, PRO 15 AND ARG 16. REMARK 800 REMARK 800 SITE_IDENTIFIER: AR REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: THESE THREE AROMATIC RESIDUES ARE INVOLVED IN REMARK 800 BINDING TO THE IGF RECEPTORS. THEY ARE CLOSE IN SPACE TO THE REMARK 800 HYDROPHOBIC CORE FORMED BY THE THREE HELICES. PHE 36 AND PHE 38 REMARK 800 POINT INTO THE HYDROPHOBIC CORE, WHILE THE AROMATIC RING OF TYR REMARK 800 37 POINTS AWAY FROM THE HYDROPHOBIC CORE. THE RESPECTIVE REMARK 800 RESIDUES IN IGF-I ARE PHE 23, TYR 24 AND PHE REMARK 999 REMARK 999 SEQUENCE REMARK 999 HAS A 13 AMINO ACID EXTENSION AT THE N-TERMINUS. THIS IS NUMBERED REMARK 999 FROM 1 SO THAT THE FIRST RESIDUE OF THE NATIVE IGF-I DOMAIN REMARK 999 RESIDUE NUMBER 14. DBREF 3LRI A 14 83 UNP P05019 IGF1B_HUMAN 33 102 SEQADV 3LRI ARG A 16 UNP P05019 GLU 35 ENGINEERED MUTATION SEQADV 3LRI CYS A 52 UNP P05019 PRO 71 ENGINEERED MUTATION SEQRES 1 A 83 MET PHE PRO ALA MET PRO LEU SER SER LEU PHE VAL ASN SEQRES 2 A 83 GLY PRO ARG THR LEU CYS GLY ALA GLU LEU VAL ASP ALA SEQRES 3 A 83 LEU GLN PHE VAL CYS GLY ASP ARG GLY PHE TYR PHE ASN SEQRES 4 A 83 LYS PRO THR GLY TYR GLY SER SER SER ARG ARG ALA CYS SEQRES 5 A 83 GLN THR GLY ILE VAL ASP GLU CYS CYS PHE ARG SER CYS SEQRES 6 A 83 ASP LEU ARG ARG LEU GLU MET TYR CYS ALA PRO LEU LYS SEQRES 7 A 83 PRO ALA LYS SER ALA HELIX 1 H1 ALA A 21 CYS A 31 1 11 HELIX 2 H2 ILE A 56 ARG A 63 1 8 HELIX 3 H3 LEU A 67 TYR A 73 1 7 SSBOND 1 CYS A 19 CYS A 61 1555 1555 2.11 SSBOND 2 CYS A 31 CYS A 74 1555 1555 2.13 SSBOND 3 CYS A 60 CYS A 65 1555 1555 1.81 SITE 1 NTR 3 ARG A 16 PRO A 15 GLY A 14 SITE 1 AR 3 PHE A 36 TYR A 37 PHE A 38 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 - v 3 2 Bytes