Header list of 1ata.pdb file
Complete list - 16 202 Bytes
HEADER PROTEINASE INHIBITOR(TRYPSIN) 20-MAY-94 1ATA
TITLE HIGH-RESOLUTION STRUCTURE OF ASCARIS TRYPSIN INHIBITOR IN SOLUTION:
TITLE 2 DIRECT EVIDENCE FOR A PH INDUCED CONFORMATIONAL TRANSITION IN THE
TITLE 3 REACTIVE SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASCARIS TRYPSIN INHIBITOR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASCARIS SUUM;
SOURCE 3 ORGANISM_COMMON: PIG ROUNDWORM;
SOURCE 4 ORGANISM_TAXID: 6253
KEYWDS PROTEINASE INHIBITOR(TRYPSIN)
EXPDTA SOLUTION NMR
AUTHOR G.M.CLORE,B.L.GRASBERGER,A.M.GRONENBORN
REVDAT 3 16-FEB-22 1ATA 1 REMARK
REVDAT 2 24-FEB-09 1ATA 1 VERSN
REVDAT 1 31-AUG-94 1ATA 0
JRNL AUTH B.L.GRASBERGER,G.M.CLORE,A.M.GRONENBORN
JRNL TITL HIGH-RESOLUTION STRUCTURE OF ASCARIS TRYPSIN INHIBITOR IN
JRNL TITL 2 SOLUTION: DIRECT EVIDENCE FOR A PH-INDUCED CONFORMATIONAL
JRNL TITL 3 TRANSITION IN THE REACTIVE SITE.
JRNL REF STRUCTURE V. 2 669 1994
JRNL REFN ISSN 0969-2126
JRNL PMID 7922043
JRNL DOI 10.1016/S0969-2126(00)00067-8
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.M.GRONENBORN,M.NILGES,R.J.PEANASKY,G.M.CLORE
REMARK 1 TITL SEQUENTIAL RESONANCE ASSIGNMENT AND SECONDARY STRUCTURE
REMARK 1 TITL 2 DETERMINATION OF THE ASCARIS TRYPSIN INHIBITOR, A MEMBER OF
REMARK 1 TITL 3 A NOVEL CLASS OF PROTEINASE INHIBITORS
REMARK 1 REF BIOCHEMISTRY V. 29 183 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE 3D STRUCTURE OF THE PH 4.75 FORM OF THE ASCARIS TRYPSIN
REMARK 3 INHIBITOR IN SOLUTION BY NMR IS BASED ON 1078 EXPERIMENTAL
REMARK 3 RESTRAINTS COMPRISING: 43 SHORT RANGE (1 < |I-J| <=5) AND
REMARK 3 218 LONG RANGE (|I-J|>5) INTERRESIDUE INTERPROTON
REMARK 3 DISTANCE RESTRAINTS, 320 INTRARESIDUE INTERPROTON DISTANCE
REMARK 3 RESTRAINTS, 48 DISTANCE RESTRAINTS FOR 4 HYDROGEN BONDS,
REMARK 3 AND 59 PHI, 49 PSI AND 41 CHI1 TORSION ANGLE RESTRAINTS. A
REMARK 3 COMPLETE LIST OF EXPERIMENTAL RESTRAINTS HAS BEEN
REMARK 3 DEPOSITED WITH THE BROOKHAVEN DATA BANK.
REMARK 3
REMARK 3 THE STRUCTURES ARE CALCULATED USING THE HYBRID METRIC
REMARK 3 MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING
REMARK 3 METHOD DESCRIBED BY: NILGES, M., CLORE, G.M. &
REMARK 3 GRONENBORN, A.M. (1988) FEBS LETT 29, 317-324 ALL
REMARK 3 STRUCTURAL STATISTICS ARE GIVEN IN REFERENCE 1.
REMARK 3
REMARK 3 THIS ENTRY PRESENTS THE RESTRAINED MINIMIZED AVERAGE
REMARK 3 STRUCTURE (SA)R. THIS IS OBTAINED BY FIRST AVERAGING THE
REMARK 3 COORDINATES OF THE INDIVIDUAL 32 DYNAMICAL SIMULATED
REMARK 3 ANNEALING SA STRUCTURES BEST FITTED TO RESIDUES 5 - 60, AND
REMARK 3 SUBJECTING THE RESULTING COORDINATES TO RESTRAINED
REMARK 3 MINIMIZATION. COLUMNS 61 - 66 IN THIS SET OF COORDINATES
REMARK 3 (THE B VALUE FIELD IN X-RAY STRUCTURES) GIVES THE AVERAGE
REMARK 3 RMS DIFFERENCE BETWEEN THE INDIVIDUAL SA STRUCTURES AND THE
REMARK 3 MEAN STRUCTURE. THE QUANTITIES IN THIS FIELD OF THE
REMARK 3 INDIVIDUAL STRUCTURES HAVE NO MEANING. THE INDIVIDUAL
REMARK 3 STRUCTURES ARE PRESENTED IN PROTEIN DATA BANK ENTRY 1ATD.
REMARK 4
REMARK 4 1ATA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171230.
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 : 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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 12 CG TRP A 12 CD2 -0.121
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TRP A 12 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 TRP A 12 NE1 - CE2 - CZ2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 TRP A 12 NE1 - CE2 - CD2 ANGL. DEV. = -6.8 DEGREES
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 GLU A 3 100.33 -43.86
REMARK 500 THR A 6 -64.76 -90.39
REMARK 500 PRO A 8 -175.18 -60.38
REMARK 500 ASN A 9 -80.10 57.08
REMARK 500 GLU A 10 99.78 -47.78
REMARK 500 GLU A 19 -155.51 -154.09
REMARK 500 CYS A 29 116.74 -161.43
REMARK 500 ARG A 31 -168.50 -64.87
REMARK 500 GLU A 32 -77.04 -122.22
REMARK 500 CYS A 33 119.04 -168.18
REMARK 500 GLU A 39 -172.76 -171.81
REMARK 500 SER A 43 -6.32 -57.40
REMARK 500 LYS A 56 162.61 -48.03
REMARK 500 PRO A 61 -162.74 -55.64
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 31 0.22 SIDE CHAIN
REMARK 500 ARG A 37 0.25 SIDE CHAIN
REMARK 500 ARG A 48 0.30 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ATD RELATED DB: PDB
DBREF 1ATA A 1 62 UNP P19398 ITR1_ASCSU 1 62
SEQRES 1 A 62 GLU ALA GLU LYS CYS THR LYS PRO ASN GLU GLN TRP THR
SEQRES 2 A 62 LYS CYS GLY GLY CYS GLU GLY THR CYS ALA GLN LYS ILE
SEQRES 3 A 62 VAL PRO CYS THR ARG GLU CYS LYS PRO PRO ARG CYS GLU
SEQRES 4 A 62 CYS ILE ALA SER ALA GLY PHE VAL ARG ASP ALA GLN GLY
SEQRES 5 A 62 ASN CYS ILE LYS PHE GLU ASP CYS PRO LYS
SHEET 1 A 2 GLN A 11 THR A 13 0
SHEET 2 A 2 ARG A 37 GLU A 39 -1 N ARG A 37 O THR A 13
SHEET 1 B 2 PHE A 46 ASP A 49 0
SHEET 2 B 2 ASN A 53 LYS A 56 -1 O ASN A 53 N ASP A 49
SSBOND 1 CYS A 5 CYS A 38 1555 1555 2.02
SSBOND 2 CYS A 15 CYS A 33 1555 1555 2.02
SSBOND 3 CYS A 18 CYS A 29 1555 1555 2.02
SSBOND 4 CYS A 22 CYS A 60 1555 1555 2.02
SSBOND 5 CYS A 40 CYS A 54 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
Complete list - 16 202 Bytes