Header list of 1gd3.pdb file
Complete list - 10 20 Bytes
HEADER PROTEIN BINDING 08-SEP-00 1GD3
TITLE REFINED SOLUTION STRUCTURE OF HUMAN 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 1GD3 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1GD3 1 VERSN
REVDAT 2 03-JUN-03 1GD3 1 JRNL
REVDAT 1 08-SEP-01 1GD3 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
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GD3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-SEP-00.
REMARK 100 THE DEPOSITION ID IS D_1000005045.
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 CYSTATIN A U-15N,13C; 10MM
REMARK 210 ACETATE BUFFER NA; 95% H2O, 5%
REMARK 210 D2O; 1.4MM CYSTATIN A U-15N;
REMARK 210 10MM ACETATE BUFFER NA; 95% H2O,
REMARK 210 5% D2O; 1.4MM CYSTATIN A; 10MM
REMARK 210 ACETATE BUFFER NA; 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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 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: 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 20 H LYS A 24 1.45
REMARK 500 O GLU A 39 H ARG A 58 1.51
REMARK 500 H GLN A 46 O ASN A 52 1.54
REMARK 500 O VAL A 87 H LYS A 89 1.59
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 SER A 7 -156.64 -78.69
REMARK 500 GLU A 8 -137.21 -74.44
REMARK 500 ALA A 9 117.26 -166.58
REMARK 500 LYS A 37 81.67 63.56
REMARK 500 TYR A 43 -173.32 -177.43
REMARK 500 LYS A 44 -151.68 -161.21
REMARK 500 GLN A 46 -149.79 -107.95
REMARK 500 VAL A 47 109.54 -164.66
REMARK 500 VAL A 48 -130.51 -143.46
REMARK 500 ALA A 49 39.64 -84.43
REMARK 500 ALA A 59 62.47 -154.81
REMARK 500 ASN A 62 -34.12 -161.25
REMARK 500 HIS A 66 110.27 -160.83
REMARK 500 VAL A 69 76.88 -160.07
REMARK 500 SER A 72 -128.52 -58.28
REMARK 500 GLN A 76 -83.36 -138.21
REMARK 500 GLU A 78 -40.97 -23.80
REMARK 500 ASP A 79 168.98 -41.98
REMARK 500 VAL A 87 -126.95 -112.86
REMARK 500 ASP A 88 51.89 -67.42
REMARK 500 LYS A 89 -159.30 -64.68
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 0.28 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: 1GD4 RELATED DB: PDB
REMARK 900 1GD4 CONTAINS CYSTATIN A (P25S).
DBREF 1GD3 A 1 98 UNP P01040 CYTA_HUMAN 1 98
SEQADV 1GD3 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 PRO 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 THR A 31 1 19
SHEET 1 A 4 LYS A 10 PRO A 11 0
SHEET 2 A 4 ALA A 40 THR A 45 -1 N TYR A 43 O LYS A 10
SHEET 3 A 4 TYR A 53 ARG A 58 -1 O TYR A 54 N LYS A 44
SHEET 4 A 4 TYR A 64 LYS A 68 -1 N LEU A 65 O VAL A 57
SHEET 1 B 2 PHE A 70 LYS A 71 0
SHEET 2 B 2 LEU A 80 VAL A 81 -1 O VAL A 81 N PHE A 70
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