Header list of 1dtv.pdb file
Complete list - 16 202 Bytes
HEADER HYDROLASE INHIBITOR 13-JAN-00 1DTV
TITLE NMR STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR (LCI)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYPEPTIDASE INHIBITOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LCI
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HIRUDO MEDICINALIS;
SOURCE 3 ORGANISM_COMMON: MEDICINAL LEECH;
SOURCE 4 ORGANISM_TAXID: 6421
KEYWDS LEECH CARBOXYPEPTIDASE INHIBITOR, LCI, HYDROLASE INHIBITOR
EXPDTA SOLUTION NMR
AUTHOR D.REVERTER,C.FERNANDEZ-CATALAN,W.BODE,T.A.HOLAK,F.X.AVILES
REVDAT 3 16-FEB-22 1DTV 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1DTV 1 VERSN
REVDAT 1 19-JUL-00 1DTV 0
JRNL AUTH D.REVERTER,C.FERNANDEZ-CATALAN,R.BAUMGARTNER,R.PFANDER,
JRNL AUTH 2 R.HUBER,W.BODE,J.VENDRELL,T.A.HOLAK,F.X.AVILES
JRNL TITL STRUCTURE OF A NOVEL LEECH CARBOXYPEPTIDASE INHIBITOR
JRNL TITL 2 DETERMINED FREE IN SOLUTION AND IN COMPLEX WITH HUMAN
JRNL TITL 3 CARBOXYPEPTIDASE A2.
JRNL REF NAT.STRUCT.BIOL. V. 7 322 2000
JRNL REFN ISSN 1072-8368
JRNL PMID 10742178
JRNL DOI 10.1038/74092
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DTV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-00.
REMARK 100 THE DEPOSITION ID IS D_1000010361.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 20MM TRIS
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM IN 20 MM PHOSPHATE BUFFER,
REMARK 210 PH 6.5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 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 : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 15
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 GLN A 13 OH TYR A 65 2.19
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 TYR A 65 CB - CG - CD2 ANGL. DEV. = -3.8 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 SER A 2 -160.47 -112.05
REMARK 500 GLU A 7 -169.67 -118.17
REMARK 500 PRO A 14 -9.05 -57.26
REMARK 500 ASP A 15 15.63 -143.94
REMARK 500 ALA A 25 -148.87 -145.70
REMARK 500 PRO A 38 -129.47 -69.12
REMARK 500 THR A 39 107.44 -162.35
REMARK 500 ALA A 40 -172.27 -67.82
REMARK 500 SER A 54 -90.60 -20.81
REMARK 500 TYR A 65 -110.36 -109.95
REMARK 500 VAL A 66 26.44 -76.24
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 23 0.18 SIDE CHAIN
REMARK 500 ARG A 44 0.16 SIDE CHAIN
REMARK 500 ARG A 59 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1DTV A 1 67 UNP P81511 MCPI_HIRME 15 81
SEQADV 1DTV GLY A 1 UNP P81511 SER 15 CONFLICT
SEQRES 1 A 67 GLY SER HIS THR PRO ASP GLU SER PHE LEU CYS TYR GLN
SEQRES 2 A 67 PRO ASP GLN VAL CYS CYS PHE ILE CYS ARG GLY ALA ALA
SEQRES 3 A 67 PRO LEU PRO SER GLU GLY GLU CYS ASN PRO HIS PRO THR
SEQRES 4 A 67 ALA PRO TRP CYS ARG GLU GLY ALA VAL GLU TRP VAL PRO
SEQRES 5 A 67 TYR SER THR GLY GLN CYS ARG THR THR CYS ILE PRO TYR
SEQRES 6 A 67 VAL GLU
HELIX 1 1 ALA A 40 ALA A 47 1 8
SHEET 1 A 5 GLU A 33 PRO A 36 0
SHEET 2 A 5 GLU A 7 GLN A 13 -1 N LEU A 10 O ASN A 35
SHEET 3 A 5 GLN A 16 CYS A 22 -1 O GLN A 16 N GLN A 13
SHEET 4 A 5 GLY A 56 ILE A 63 -1 N ARG A 59 O ILE A 21
SHEET 5 A 5 PRO A 52 TYR A 53 -1 N TYR A 53 O GLY A 56
SSBOND 1 CYS A 11 CYS A 34 1555 1555 2.02
SSBOND 2 CYS A 18 CYS A 62 1555 1555 2.03
SSBOND 3 CYS A 19 CYS A 43 1555 1555 2.01
SSBOND 4 CYS A 22 CYS A 58 1555 1555 2.01
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