Header list of 1g26.pdb file
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HEADER CYTOKINE 17-OCT-00 1G26 TITLE THE SOLUTION STRUCTURE OF A WELL-FOLDED PEPTIDE BASED ON THE 31- TITLE 2 RESIDUE AMINO-TERMINAL SUBDOMAIN OF HUMAN GRANULIN A COMPND MOL_ID: 1; COMPND 2 MOLECULE: GRANULIN A; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL DOMAIN (RESIDUES 1-31); COMPND 5 SYNONYM: HGA; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED USING STANDARD SOURCE 4 FMOC CHEMISTRY AND OXIDIZED BY AIR IN SOLUTION, CYS17 AND CYS27 WERE SOURCE 5 BLOCKED WITH S-ACETAMIDOMETHYL GROUPS (ACM) KEYWDS GRANULIN/EPITHELIN PROTEIN REPEATS, BETA-HAIRPIN STACK, CYTOKINE EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR D.TOLKATCHEV,A.NG,W.VRANKEN,F.NI REVDAT 3 03-NOV-21 1G26 1 REMARK SEQADV REVDAT 2 24-FEB-09 1G26 1 VERSN REVDAT 1 01-NOV-00 1G26 0 JRNL AUTH D.TOLKATCHEV,A.NG,W.VRANKEN,F.NI JRNL TITL DESIGN AND SOLUTION STRUCTURE OF A WELL-FOLDED STACK OF TWO JRNL TITL 2 BETA-HAIRPINS BASED ON THE AMINO-TERMINAL FRAGMENT OF HUMAN JRNL TITL 3 GRANULIN A. JRNL REF BIOCHEMISTRY V. 39 2878 2000 JRNL REFN ISSN 0006-2960 JRNL PMID 10715107 JRNL DOI 10.1021/BI992130U REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 241 RESTRAINTS, 174 ARE UNAMBIGUOUS NOE-DERIVED DISTANCE REMARK 3 CONSTRAINTS, 47 AMBIGUOUS NOE-DERIVED DISTANCE CONSTRAINTS, 8 REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 10 DISTANCE RESTRAINTS FROM HYDROGEN REMARK 3 BONDS, 2 DISTANCE RESTRAINTS FROM DISULFIDE BONDS. REMARK 4 REMARK 4 1G26 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-00. REMARK 100 THE DEPOSITION ID IS D_1000012140. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 288; 298 REMARK 210 PH : 5.0; 5.0 REMARK 210 IONIC STRENGTH : NULL; NULL REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5 MM HGA 1-31 (D1V, K3H, S9I, REMARK 210 Q20P); 20 MM SODIUM ACETATE-D3, REMARK 210 10% D2O, 90% H2O; 0.5 MM HGA 1- REMARK 210 31 (D1V, K3H, S9I, Q20P); 20 MM REMARK 210 SODIUM ACETATE-D3, 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.1 REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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: 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 PRO A 11 H TYR A 14 1.56 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 HIS A 3 89.77 -51.59 REMARK 500 1 ASP A 5 -170.79 177.90 REMARK 500 2 VAL A 8 119.62 -167.19 REMARK 500 2 ASP A 12 -77.57 54.12 REMARK 500 3 HIS A 3 106.67 -46.05 REMARK 500 3 ASP A 5 -139.71 -156.87 REMARK 500 3 PRO A 11 41.06 -81.15 REMARK 500 3 ASP A 12 -57.97 66.34 REMARK 500 3 PHE A 29 59.84 -147.63 REMARK 500 3 THR A 30 69.92 -116.18 REMARK 500 4 ASP A 5 -166.45 -168.88 REMARK 500 4 SER A 21 31.66 -99.14 REMARK 500 5 HIS A 3 82.32 -59.07 REMARK 500 5 GLU A 7 -33.16 -136.61 REMARK 500 5 PRO A 11 38.01 -80.33 REMARK 500 5 ASP A 12 -56.33 66.32 REMARK 500 5 PHE A 29 -45.42 -147.66 REMARK 500 6 ASP A 5 -80.08 -169.54 REMARK 500 6 MET A 6 -53.79 -146.15 REMARK 500 6 PRO A 11 43.14 -78.59 REMARK 500 6 ASP A 12 -58.95 65.05 REMARK 500 7 HIS A 3 93.50 56.07 REMARK 500 7 ASP A 5 -153.61 -163.40 REMARK 500 7 PRO A 11 38.84 -80.25 REMARK 500 7 ASP A 12 138.19 66.69 REMARK 500 7 PHE A 29 20.56 -153.60 REMARK 500 8 ASP A 5 -147.27 -145.46 REMARK 500 8 ASP A 12 -19.16 -48.86 REMARK 500 8 PRO A 20 41.58 -80.01 REMARK 500 8 SER A 21 30.05 -168.33 REMARK 500 8 THR A 30 37.65 -143.26 REMARK 500 9 ASP A 5 -134.10 -160.18 REMARK 500 9 GLU A 7 -60.92 -121.83 REMARK 500 9 PRO A 11 42.77 -78.98 REMARK 500 9 ASP A 12 137.91 63.04 REMARK 500 9 PHE A 29 53.74 -158.53 REMARK 500 10 VAL A 2 56.07 -104.40 REMARK 500 10 ASP A 5 -60.61 -146.54 REMARK 500 10 MET A 6 -36.03 -176.51 REMARK 500 10 PRO A 11 32.98 -82.09 REMARK 500 10 ASP A 12 -56.31 66.59 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 1 ARG A 18 0.28 SIDE CHAIN REMARK 500 2 ARG A 18 0.20 SIDE CHAIN REMARK 500 3 ARG A 18 0.18 SIDE CHAIN REMARK 500 4 ARG A 18 0.32 SIDE CHAIN REMARK 500 5 ARG A 18 0.28 SIDE CHAIN REMARK 500 6 ARG A 18 0.26 SIDE CHAIN REMARK 500 7 ARG A 18 0.18 SIDE CHAIN REMARK 500 8 ARG A 18 0.23 SIDE CHAIN REMARK 500 9 ARG A 18 0.26 SIDE CHAIN REMARK 500 10 ARG A 18 0.28 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1QGM RELATED DB: PDB REMARK 900 1QGM BELONGS TO A FAMILY OF GRANULIN-LIKE REPEATS REMARK 900 RELATED ID: 1FWO RELATED DB: PDB REMARK 900 1FWO BELONGS TO A FAMILY OF GRANULIN-LIKE REPEATS DBREF 1G26 A 1 31 UNP P28799 GRN_HUMAN 281 311 SEQADV 1G26 VAL A 1 UNP P28799 ASP 281 ENGINEERED MUTATION SEQADV 1G26 HIS A 3 UNP P28799 LYS 283 ENGINEERED MUTATION SEQADV 1G26 ILE A 9 UNP P28799 SER 289 ENGINEERED MUTATION SEQADV 1G26 PRO A 20 UNP P28799 GLN 300 ENGINEERED MUTATION SEQRES 1 A 31 VAL VAL HIS CYS ASP MET GLU VAL ILE CYS PRO ASP GLY SEQRES 2 A 31 TYR THR CYS CYS ARG LEU PRO SER GLY ALA TRP GLY CYS SEQRES 3 A 31 CYS PRO PHE THR GLN SHEET 1 A 2 VAL A 2 ASP A 5 0 SHEET 2 A 2 VAL A 8 CYS A 10 -1 O VAL A 8 N ASP A 5 SHEET 1 B 2 TYR A 14 ARG A 18 0 SHEET 2 B 2 TRP A 24 PRO A 28 -1 N GLY A 25 O CYS A 17 SSBOND 1 CYS A 4 CYS A 16 1555 1555 2.02 SSBOND 2 CYS A 10 CYS A 26 1555 1555 2.02 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 - 3 20 Bytes