Header list of 1bhu.pdb file
Complete list - 16 20 Bytes
HEADER METALLOPROTEINASE INHIBITOR 10-JUN-98 1BHU
TITLE THE 3D STRUCTURE OF THE STREPTOMYCES METALLOPROTEINASE INHIBITOR,
TITLE 2 SMPI, ISOLATED FROM STREPTOMYCES NIGRESCENS TK-23, NMR, MINIMIZED
TITLE 3 AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METALLOPROTEINASE INHIBITOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SMPI;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES NIGRESCENS;
SOURCE 3 ORGANISM_TAXID: 1920;
SOURCE 4 STRAIN: TK-23;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS METALLOPROTEINASE INHIBITOR
EXPDTA SOLUTION NMR
AUTHOR S.TATE,A.OHNO,S.S.SEERAM,K.HIRAGA,K.ODA,M.KAINOSHO
REVDAT 4 16-FEB-22 1BHU 1 REMARK
REVDAT 3 24-FEB-09 1BHU 1 VERSN
REVDAT 2 16-FEB-99 1BHU 1 SOURCE COMPND REMARK TITLE
REVDAT 2 2 1 JRNL EXPDTA KEYWDS SHEET
REVDAT 1 06-JAN-99 1BHU 0
JRNL AUTH A.OHNO,S.TATE,S.S.SEERAM,K.HIRAGA,M.B.SWINDELLS,K.ODA,
JRNL AUTH 2 M.KAINOSHO
JRNL TITL NMR STRUCTURE OF THE STREPTOMYCES METALLOPROTEINASE
JRNL TITL 2 INHIBITOR, SMPI, ISOLATED FROM STREPTOMYCES NIGRESCENS
JRNL TITL 3 TK-23: ANOTHER EXAMPLE OF AN ANCESTRAL BETA GAMMA-CRYSTALLIN
JRNL TITL 4 PRECURSOR STRUCTURE.
JRNL REF J.MOL.BIOL. V. 282 421 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9735297
JRNL DOI 10.1006/JMBI.1998.2022
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.TATE,A.OHNO,S.S.SEERAM,K.HIRAGA,K.ODA,M.KAINOSHO
REMARK 1 TITL ELUCIDATION OF THE MODE OF INTERACTION OF THERMOLYSIN WITH A
REMARK 1 TITL 2 PROTEINACEOUS METALLOPROTEINASE INHIBITOR, SMPI, BASED ON A
REMARK 1 TITL 3 MODEL COMPLEX STRUCTURE AND A STRUCTURAL DYNAMICS ANALYSIS
REMARK 1 REF J.MOL.BIOL. V. 282 435 1998
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1BHU 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_1000171775.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 3.3
REMARK 210 IONIC STRENGTH : NO SALT
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : WATER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HETERONUCLEAR MULTI-DIMENSIONAL
REMARK 210 EXPERIMENT
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.8
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETEMINED ON THE BASIS OF THE HETERO
REMARK 210 -NUCLEAR MUTLIDIMENSIONAL NMR TECHNIQUES USING 13C, 15N ENRICHED
REMARK 210 PROTEINS.
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 OG1 THR A 11 HG1 THR A 22 1.41
REMARK 500 O ALA A 73 HG1 THR A 74 1.45
REMARK 500 H ASN A 48 O LEU A 87 1.48
REMARK 500 O THR A 11 H THR A 22 1.49
REMARK 500 O MET A 29 H GLY A 33 1.49
REMARK 500 HG SER A 45 O SER A 89 1.51
REMARK 500 O PHE A 46 H SER A 89 1.59
REMARK 500 O TYR A 56 H VAL A 75 1.60
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 PRO A 5 -111.08 -81.28
REMARK 500 ALA A 6 139.10 -176.64
REMARK 500 SER A 13 66.97 -112.52
REMARK 500 THR A 15 104.98 39.70
REMARK 500 SER A 18 -155.01 -98.65
REMARK 500 ALA A 26 68.92 35.10
REMARK 500 SER A 27 -52.93 -164.00
REMARK 500 ASP A 35 48.40 32.77
REMARK 500 VAL A 37 -158.28 -162.55
REMARK 500 PRO A 40 -166.37 -71.97
REMARK 500 ALA A 41 -42.10 -148.59
REMARK 500 SER A 42 102.81 -54.56
REMARK 500 ARG A 44 59.22 -177.99
REMARK 500 SER A 45 -145.57 -116.08
REMARK 500 PHE A 46 173.84 171.47
REMARK 500 THR A 50 -168.40 174.14
REMARK 500 HIS A 51 30.07 -99.35
REMARK 500 PHE A 52 62.58 -16.94
REMARK 500 THR A 53 82.73 -18.65
REMARK 500 ARG A 60 39.33 -147.73
REMARK 500 ARG A 66 32.45 -165.75
REMARK 500 PHE A 67 -44.90 113.28
REMARK 500 PRO A 68 58.03 -67.46
REMARK 500 GLN A 71 25.30 34.30
REMARK 500 TYR A 72 -161.33 -169.24
REMARK 500 ALA A 73 21.85 -141.29
REMARK 500 THR A 74 114.55 61.92
REMARK 500 ALA A 79 -77.91 -50.82
REMARK 500 GLN A 83 -66.49 169.62
REMARK 500 ARG A 85 41.48 -77.71
REMARK 500 SER A 86 81.41 -164.57
REMARK 500 PRO A 90 -157.75 -100.33
REMARK 500 ALA A 92 100.28 77.92
REMARK 500 THR A 93 19.89 51.08
REMARK 500 LEU A 100 50.08 -119.88
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 21 0.30 SIDE CHAIN
REMARK 500 ARG A 44 0.30 SIDE CHAIN
REMARK 500 ARG A 55 0.31 SIDE CHAIN
REMARK 500 ARG A 60 0.32 SIDE CHAIN
REMARK 500 ARG A 66 0.32 SIDE CHAIN
REMARK 500 ARG A 85 0.30 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BHU A 1 102 UNP P01077 IMEP_STRNI 30 131
SEQRES 1 A 102 ALA PRO SER CYS PRO ALA GLY SER LEU CYS THR TYR SER
SEQRES 2 A 102 GLY THR GLY LEU SER GLY ALA ARG THR VAL ILE PRO ALA
SEQRES 3 A 102 SER ASP MET GLU LYS ALA GLY THR ASP GLY VAL LYS LEU
SEQRES 4 A 102 PRO ALA SER ALA ARG SER PHE ALA ASN GLY THR HIS PHE
SEQRES 5 A 102 THR LEU ARG TYR GLY PRO ALA ARG LYS VAL THR CYS VAL
SEQRES 6 A 102 ARG PHE PRO CYS TYR GLN TYR ALA THR VAL GLY LYS VAL
SEQRES 7 A 102 ALA PRO GLY ALA GLN LEU ARG SER LEU PRO SER PRO GLY
SEQRES 8 A 102 ALA THR VAL THR VAL GLY GLN ASP LEU GLY ASP
HELIX 1 H1 ALA A 26 ALA A 32 1 7
SHEET 1 S1 4 ALA A 20 ILE A 24 0
SHEET 2 S1 4 LEU A 9 SER A 13 -1 O THR A 11 N THR A 22
SHEET 3 S1 4 SER A 45 GLY A 49 -1 O SER A 45 N TYR A 12
SHEET 4 S1 4 SER A 86 SER A 89 -1 N LEU A 87 O ASN A 48
SHEET 1 S2 4 THR A 34 LEU A 39 0
SHEET 2 S2 4 VAL A 94 ASP A 99 -1 N VAL A 96 O VAL A 37
SHEET 3 S2 4 THR A 53 GLY A 57 -1 N THR A 53 O ASP A 99
SHEET 4 S2 4 LYS A 77 ALA A 79 -1 O VAL A 78 N LEU A 54
SHEET 1 S3 2 ALA A 59 ARG A 60 0
SHEET 2 S3 2 GLN A 71 TYR A 72 -1 O GLN A 71 N ARG A 60
SSBOND 1 CYS A 4 CYS A 10 1555 1555 2.48
SSBOND 2 CYS A 64 CYS A 69 1555 1555 2.53
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 20 Bytes