Header list of 1qfd.pdb file
Complete list - 29 20 Bytes
HEADER INHIBITOR 08-APR-99 1QFD
TITLE NMR SOLUTION STRUCTURE OF ALPHA-AMYLASE INHIBITOR (AAI)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (ALPHA-AMYLASE INHIBITOR);
COMPND 3 CHAIN: A;
COMPND 4 OTHER_DETAILS: SYNTHETIC
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AMARANTHUS HYPOCHONDRIACUS;
SOURCE 3 ORGANISM_COMMON: GRAIN AMARANTH;
SOURCE 4 ORGANISM_TAXID: 28502;
SOURCE 5 ORGAN: SEED;
SOURCE 6 OTHER_DETAILS: SYNTHETIC SEQUENCE
KEYWDS INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR S.LU,P.DENG,X.LIU,J.LUO,R.HAN,X.GU,S.LIANG,X.WANG,L.FENG,V.LOZANOV,
AUTHOR 2 A.PATTHY,S.PONGOR
REVDAT 4 29-NOV-17 1QFD 1 REMARK HELIX
REVDAT 3 24-FEB-09 1QFD 1 VERSN
REVDAT 2 01-APR-03 1QFD 1 JRNL
REVDAT 1 16-JUL-99 1QFD 0
JRNL AUTH S.LU,P.DENG,X.LIU,J.LUO,R.HAN,X.GU,S.LIANG,X.WANG,F.LI,
JRNL AUTH 2 V.LOZANOV,A.PATTHY,S.PONGOR
JRNL TITL SOLUTION STRUCTURE OF THE MAJOR ALPHA-AMYLASE INHIBITOR OF
JRNL TITL 2 THE CROP PLANT AMARANTH.
JRNL REF J.BIOL.CHEM. V. 274 20473 1999
JRNL REFN ISSN 0021-9258
JRNL PMID 10400675
JRNL DOI 10.1074/JBC.274.29.20473
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH V.LOZANOV,C.GUARNACCIA,A.PATTHY,S.FOTI,S.PONGOR
REMARK 1 TITL SYNTHESIS AND CYSTINE/CYSTEINE-CATALYZED OXIDATIVE FOLDING
REMARK 1 TITL 2 OF THE AMARANTH ALPHA-AMYLASE INHIBITOR
REMARK 1 REF J.PEPT.RES. V.50(1 65 1997
REMARK 1 REFN ISSN 1397-002X
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.CHAGOLLA-LOPEZ,A.BLANCO-LABRA,A.PATTHY,R.SANCHEZ,S.PONGOR
REMARK 1 TITL A NOVEL ALPHA-AMYLASE INHIBITOR FROM AMARANTH (AMARANTHUS
REMARK 1 TITL 2 HYPOCONDRIACUS)SEEDS
REMARK 1 REF J.BIOL.CHEM. V. 269 23675 1994
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QFD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000816.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 20 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SYBYL, X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION AND
REMARK 210 RESULT OF PROCHECK
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: 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 LYS A 4 153.20 -46.68
REMARK 500 4 CYS A 18 170.44 -59.16
REMARK 500 5 PRO A 20 0.25 -68.51
REMARK 500 6 TYR A 27 -61.39 -106.90
REMARK 500 7 PRO A 20 0.88 -67.74
REMARK 500 8 PRO A 20 0.82 -69.17
REMARK 500 8 SER A 25 -159.87 -119.38
REMARK 500 9 TYR A 27 -60.78 -93.91
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 7 0.30 SIDE CHAIN
REMARK 500 2 ARG A 7 0.32 SIDE CHAIN
REMARK 500 3 ARG A 7 0.32 SIDE CHAIN
REMARK 500 4 ARG A 7 0.29 SIDE CHAIN
REMARK 500 5 ARG A 7 0.30 SIDE CHAIN
REMARK 500 6 ARG A 7 0.32 SIDE CHAIN
REMARK 500 7 ARG A 7 0.29 SIDE CHAIN
REMARK 500 8 ARG A 7 0.31 SIDE CHAIN
REMARK 500 9 ARG A 7 0.32 SIDE CHAIN
REMARK 500 10 ARG A 7 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1QFD A 1 32 UNP P80403 IAAI_AMAHP 1 32
SEQRES 1 A 32 CYS ILE PRO LYS TRP ASN ARG CYS GLY PRO LYS MET ASP
SEQRES 2 A 32 GLY VAL PRO CYS CYS GLU PRO TYR THR CYS THR SER ASP
SEQRES 3 A 32 TYR TYR GLY ASN CYS SER
HELIX 1 1 PRO A 10 ASP A 13 1 4
SHEET 1 S1 1 ARG A 7 CYS A 8 0
SHEET 1 S2 1 THR A 22 THR A 24 0
SHEET 1 S3 1 GLY A 29 SER A 32 0
SSBOND 1 CYS A 1 CYS A 18 1555 1555 2.02
SSBOND 2 CYS A 8 CYS A 23 1555 1555 2.02
SSBOND 3 CYS A 17 CYS A 31 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 - 29 20 Bytes