Header list of 2ait.pdb file
Complete list - 29 20 Bytes
HEADER ALPHA-AMYLASE INHIBITOR 24-MAY-89 2AIT
TITLE DETERMINATION OF THE COMPLETE THREE-DIMENSIONAL STRUCTURE OF THE
TITLE 2 ALPHA-AMYLASE INHIBITOR TENDAMISTAT IN AQUEOUS SOLUTION BY NUCLEAR
TITLE 3 MAGNETIC RESONANCE AND DISTANCE GEOMETRY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TENDAMISTAT;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES TENDAE;
SOURCE 3 ORGANISM_TAXID: 1932
KEYWDS ALPHA-AMYLASE INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 9
AUTHOR A.D.KLINE,W.BRAUN,P.GUNTERT,M.BILLETER,K.WUTHRICH
REVDAT 4 29-NOV-17 2AIT 1 REMARK HELIX
REVDAT 3 24-FEB-09 2AIT 1 VERSN
REVDAT 2 15-JUL-91 2AIT 1 AUTHOR JRNL REMARK
REVDAT 1 15-APR-90 2AIT 0
JRNL AUTH A.D.KLINE,W.BRAUN,K.WUTHRICH
JRNL TITL DETERMINATION OF THE COMPLETE THREE-DIMENSIONAL STRUCTURE OF
JRNL TITL 2 THE ALPHA-AMYLASE INHIBITOR TENDAMISTAT IN AQUEOUS SOLUTION
JRNL TITL 3 BY NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY.
JRNL REF J.MOL.BIOL. V. 204 675 1988
JRNL REFN ISSN 0022-2836
JRNL PMID 3265733
JRNL DOI 10.1016/0022-2836(88)90364-6
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.D.KLINE,K.WUTHRICH
REMARK 1 TITL COMPLETE SEQUENCE-SPECIFIC 1H NUCLEAR MAGNETIC RESONANCE
REMARK 1 TITL 2 ASSIGNMENTS FOR THE ALPHA-AMYLASE POLYPEPTIDE INHIBITOR
REMARK 1 TITL 3 TENDAMISTAT FROM STREPTOMYCES TENDAE
REMARK 1 REF J.MOL.BIOL. V. 192 869 1986
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.D.KLINE,W.BRAUN,K.WUTHRICH
REMARK 1 TITL STUDIES BY 1H NUCLEAR MAGNETIC RESONANCE AND DISTANCE
REMARK 1 TITL 2 GEOMETRY OF THE SOLUTION CONFORMATION OF THE ALPHA-AMYLASE
REMARK 1 TITL 3 INHIBITOR TENDAMISTAT
REMARK 1 REF J.MOL.BIOL. V. 189 377 1986
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH A.D.KLINE,K.WUTHRICH
REMARK 1 TITL SECONDARY STRUCTURE OF THE ALPHA-AMYLASE POLYPEPTIDE
REMARK 1 TITL 2 INHIBITOR TENDAMISTAT FROM STREPTOMYCES TENDAE DETERMINED IN
REMARK 1 TITL 3 SOLUTION BY 1H NUCLEAR MAGNETIC RESONANCE
REMARK 1 REF J.MOL.BIOL. V. 183 503 1985
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISMAN
REMARK 3 AUTHORS : BRAUN,GO
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2AIT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177756.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 9
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 H ALA A 8 O LEU A 70 1.51
REMARK 500 H TYR A 15 O GLN A 22 1.51
REMARK 500 OH TYR A 37 H ASP A 58 1.57
REMARK 500 O VAL A 36 H ARG A 68 1.57
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 THR A 2 -96.21 44.22
REMARK 500 1 SER A 5 -93.21 -54.79
REMARK 500 1 GLU A 6 142.69 88.23
REMARK 500 1 TYR A 15 70.14 -115.67
REMARK 500 1 SER A 17 -152.92 -106.68
REMARK 500 1 ASP A 40 31.00 81.52
REMARK 500 1 LEU A 44 154.62 61.98
REMARK 500 1 TYR A 60 36.04 -94.20
REMARK 500 1 SER A 63 -98.57 -59.30
REMARK 500 1 HIS A 64 33.11 -91.59
REMARK 500 1 TYR A 69 166.94 177.21
REMARK 500 2 THR A 2 -34.47 171.51
REMARK 500 2 SER A 5 -156.33 -177.20
REMARK 500 2 GLU A 6 141.97 -170.50
REMARK 500 2 TYR A 15 59.22 -96.19
REMARK 500 2 SER A 17 -149.36 -107.88
REMARK 500 2 ALA A 28 32.68 39.88
REMARK 500 2 TYR A 60 40.99 -92.60
REMARK 500 2 SER A 63 -97.55 -59.18
REMARK 500 2 ALA A 67 108.79 -45.20
REMARK 500 3 THR A 2 -96.80 29.96
REMARK 500 3 VAL A 4 83.44 68.07
REMARK 500 3 SER A 5 -77.65 -79.33
REMARK 500 3 GLU A 6 95.59 175.18
REMARK 500 3 CYS A 27 -155.64 -88.20
REMARK 500 3 CYS A 45 101.46 -42.80
REMARK 500 3 ILE A 61 51.48 -93.36
REMARK 500 3 SER A 63 -138.32 -60.40
REMARK 500 3 HIS A 64 37.48 -79.44
REMARK 500 3 ALA A 67 113.18 -39.66
REMARK 500 3 TYR A 69 -166.12 179.53
REMARK 500 3 CYS A 73 -102.06 -79.57
REMARK 500 4 THR A 2 75.17 40.48
REMARK 500 4 SER A 5 -149.59 -124.01
REMARK 500 4 TYR A 15 58.06 -93.23
REMARK 500 4 LYS A 34 110.48 -160.67
REMARK 500 4 ASP A 39 34.00 -93.73
REMARK 500 4 CYS A 45 103.54 -51.53
REMARK 500 4 TYR A 69 -177.50 -174.85
REMARK 500 4 CYS A 73 -117.47 -78.76
REMARK 500 5 THR A 2 63.10 -151.13
REMARK 500 5 THR A 3 53.37 -94.27
REMARK 500 5 SER A 5 -97.03 -156.95
REMARK 500 5 GLU A 6 138.99 79.13
REMARK 500 5 SER A 17 -144.22 -87.77
REMARK 500 5 LYS A 34 89.46 -160.64
REMARK 500 5 ASP A 40 -1.25 78.52
REMARK 500 5 ASP A 58 126.32 -170.24
REMARK 500 5 TYR A 69 161.74 178.92
REMARK 500 6 THR A 2 -167.63 43.52
REMARK 500
REMARK 500 THIS ENTRY HAS 87 RAMACHANDRAN OUTLIERS.
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 19 0.29 SIDE CHAIN
REMARK 500 1 ARG A 72 0.29 SIDE CHAIN
REMARK 500 2 ARG A 19 0.09 SIDE CHAIN
REMARK 500 2 ARG A 68 0.11 SIDE CHAIN
REMARK 500 2 ARG A 72 0.30 SIDE CHAIN
REMARK 500 3 ARG A 19 0.30 SIDE CHAIN
REMARK 500 3 ARG A 68 0.26 SIDE CHAIN
REMARK 500 3 ARG A 72 0.23 SIDE CHAIN
REMARK 500 4 ARG A 19 0.24 SIDE CHAIN
REMARK 500 4 ARG A 68 0.19 SIDE CHAIN
REMARK 500 4 ARG A 72 0.28 SIDE CHAIN
REMARK 500 5 ARG A 19 0.13 SIDE CHAIN
REMARK 500 5 ARG A 68 0.24 SIDE CHAIN
REMARK 500 6 ARG A 19 0.16 SIDE CHAIN
REMARK 500 6 ARG A 68 0.11 SIDE CHAIN
REMARK 500 6 ARG A 72 0.09 SIDE CHAIN
REMARK 500 7 ARG A 19 0.30 SIDE CHAIN
REMARK 500 7 ARG A 68 0.29 SIDE CHAIN
REMARK 500 7 ARG A 72 0.20 SIDE CHAIN
REMARK 500 8 ARG A 19 0.11 SIDE CHAIN
REMARK 500 8 ARG A 68 0.23 SIDE CHAIN
REMARK 500 8 ARG A 72 0.18 SIDE CHAIN
REMARK 500 9 ARG A 19 0.08 SIDE CHAIN
REMARK 500 9 ARG A 68 0.13 SIDE CHAIN
REMARK 500 9 ARG A 72 0.21 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2AIT A 1 74 UNP P01092 IAA_STRTE 31 104
SEQADV 2AIT GLU A 29 UNP P01092 GLN 59 CONFLICT
SEQRES 1 A 74 ASP THR THR VAL SER GLU PRO ALA PRO SER CYS VAL THR
SEQRES 2 A 74 LEU TYR GLN SER TRP ARG TYR SER GLN ALA ASP ASN GLY
SEQRES 3 A 74 CYS ALA GLU THR VAL THR VAL LYS VAL VAL TYR GLU ASP
SEQRES 4 A 74 ASP THR GLU GLY LEU CYS TYR ALA VAL ALA PRO GLY GLN
SEQRES 5 A 74 ILE THR THR VAL GLY ASP GLY TYR ILE GLY SER HIS GLY
SEQRES 6 A 74 HIS ALA ARG TYR LEU ALA ARG CYS LEU
SHEET 1 S1 3 VAL A 12 SER A 17 0
SHEET 2 S1 3 TYR A 20 ASN A 25 -1 N SER A 17 O TYR A 20
SHEET 3 S1 3 GLN A 52 ASP A 58 -1 N ASN A 25 O GLN A 52
SHEET 1 S2 3 ALA A 67 CYS A 73 0
SHEET 2 S2 3 THR A 30 TYR A 37 -1 H VAL A 36 O TYR A 69
SHEET 3 S2 3 THR A 41 ALA A 49 -1 H VAL A 48 O VAL A 31
SSBOND 1 CYS A 11 CYS A 27 1555 1555 2.16
SSBOND 2 CYS A 45 CYS A 73 1555 1555 2.10
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 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