Header list of 1gd4.pdb file
Complete list - 10 20 Bytes
HEADER PROTEIN BINDING 08-SEP-00 1GD4 TITLE SOLUTION STRUCTURE OF P25S CYSTATIN A COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYSTATIN A; 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_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS CYSTATIN A, THIOL PROTEASE INHIBITOR, PROTEIN BINDING EXPDTA SOLUTION NMR AUTHOR N.SHIMBA,E.KARIYA,S.TATE,H.KAJI,M.KAINOSHO REVDAT 4 10-NOV-21 1GD4 1 REMARK SEQADV REVDAT 3 24-FEB-09 1GD4 1 VERSN REVDAT 2 03-JUN-03 1GD4 1 JRNL REVDAT 1 08-SEP-01 1GD4 0 JRNL AUTH N.SHIMBA,E.KARIYA,S.TATE,H.KAJI,M.KAINOSHO JRNL TITL STRUCTURAL COMPARISON BETWEEN WILD-TYPE AND P25S HUMAN JRNL TITL 2 CYSTATIN A BY NMR SPECTROSCOPY. DOES THIS MUTATION AFFECT JRNL TITL 3 THE A-HELIX CONFORMATION ? JRNL REF J.STRUCT.FUNCT.GENOM. V. 1 26 2000 JRNL REFN ISSN 1345-711X JRNL PMID 12836678 JRNL DOI 10.1023/A:1011380315619 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.85, X-PLOR 3.85 REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1GD4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-SEP-00. REMARK 100 THE DEPOSITION ID IS D_1000005046. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 4.0 REMARK 210 IONIC STRENGTH : 0 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.4MM P25S CYSTATIN A U-15N,13C; REMARK 210 10MM ACETATE BUFFER ; 95% H2O, 5% REMARK 210 D2O; 1.4MM P25S CYSTATIN A U- REMARK 210 15N; 10MM ACETATE BUFFER ; 90% REMARK 210 H2O 10% D2O; 1.4MM P25S CYSTATIN REMARK 210 A; 10MM ACETATE BUFFER ; 98% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: NULL 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 VAL A 23 H LEU A 27 1.51 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 PRO A 3 -166.00 -73.43 REMARK 500 GLU A 8 -139.87 -134.93 REMARK 500 ALA A 9 66.86 166.28 REMARK 500 THR A 13 -149.04 -125.09 REMARK 500 GLU A 33 -143.81 -78.21 REMARK 500 THR A 34 -47.36 -170.65 REMARK 500 TYR A 35 -171.26 45.04 REMARK 500 VAL A 48 -123.35 -141.75 REMARK 500 ASP A 61 21.52 -152.69 REMARK 500 ASN A 62 33.27 -172.43 REMARK 500 SER A 72 -119.52 -104.74 REMARK 500 LEU A 73 -49.98 145.88 REMARK 500 GLN A 76 -43.53 -28.51 REMARK 500 ASN A 77 -45.61 -29.23 REMARK 500 GLU A 78 -73.99 -69.62 REMARK 500 ASP A 79 134.50 54.73 REMARK 500 LEU A 80 48.46 30.18 REMARK 500 LEU A 82 91.30 -60.76 REMARK 500 TYR A 85 177.80 169.55 REMARK 500 ASP A 88 69.04 39.98 REMARK 500 ASN A 90 27.93 -144.95 REMARK 500 LYS A 91 -34.38 -147.05 REMARK 500 ASP A 93 51.09 -106.15 REMARK 500 LEU A 95 -116.89 51.11 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 ARG A 58 0.20 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1CYU RELATED DB: PDB REMARK 900 1CYU CONTAINS CYSTATIN A (M65L) AND 15 STRUCTURES. REMARK 900 RELATED ID: 1CYV RELATED DB: PDB REMARK 900 1CYV CONTAINS CYSTATIN A (M65L) AND MINIMIZED AVERAGE STRUCTURE. REMARK 900 RELATED ID: 1GD3 RELATED DB: PDB REMARK 900 1GD3 CONTAINS CYSTATIN A (M65L). DBREF 1GD4 A 1 98 UNP P01040 CYTA_HUMAN 1 98 SEQADV 1GD4 SER A 25 UNP P01040 PRO 25 ENGINEERED MUTATION SEQADV 1GD4 LEU A 65 UNP P01040 MET 65 ENGINEERED MUTATION SEQRES 1 A 98 MET ILE PRO GLY GLY LEU SER GLU ALA LYS PRO ALA THR SEQRES 2 A 98 PRO GLU ILE GLN GLU ILE VAL ASP LYS VAL LYS SER GLN SEQRES 3 A 98 LEU GLU GLU LYS THR ASN GLU THR TYR GLY LYS LEU GLU SEQRES 4 A 98 ALA VAL GLN TYR LYS THR GLN VAL VAL ALA GLY THR ASN SEQRES 5 A 98 TYR TYR ILE LYS VAL ARG ALA GLY ASP ASN LYS TYR LEU SEQRES 6 A 98 HIS LEU LYS VAL PHE LYS SER LEU PRO GLY GLN ASN GLU SEQRES 7 A 98 ASP LEU VAL LEU THR GLY TYR GLN VAL ASP LYS ASN LYS SEQRES 8 A 98 ASP ASP GLU LEU THR GLY PHE HELIX 1 1 THR A 13 GLU A 29 1 17 SHEET 1 A 3 TYR A 64 LYS A 71 0 SHEET 2 A 3 THR A 51 ARG A 58 -1 O THR A 51 N LYS A 71 SHEET 3 A 3 GLU A 39 TYR A 43 -1 O GLU A 39 N ARG A 58 SHEET 1 B 3 TYR A 64 LYS A 71 0 SHEET 2 B 3 THR A 51 ARG A 58 -1 O THR A 51 N LYS A 71 SHEET 3 B 3 GLN A 46 VAL A 47 -1 N GLN A 46 O ASN A 52 CRYST1 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
Complete list - 10 20 Bytes