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PDBsum entry 1trl

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Hydrolase (metalloprotease) PDB id
1trl
Jmol
Contents
Protein chains
62 a.a. *
* Residue conservation analysis
HEADER    HYDROLASE (METALLOPROTEASE)             02-SEP-94   1TRL
TITLE     NMR SOLUTION STRUCTURE OF THE C-TERMINAL FRAGMENT 255-316
TITLE    2 OF THERMOLYSIN: A DIMER FORMED BY SUBUNITS HAVING THE
TITLE    3 NATIVE STRUCTURE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: THERMOLYSIN FRAGMENT 255 - 316;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 3.4.24.27;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS THERMOPROTEOLYTICUS;
SOURCE   3 ORGANISM_TAXID: 1427
KEYWDS    HYDROLASE (METALLOPROTEASE)
EXPDTA    SOLUTION NMR
NUMMDL    8
AUTHOR    M.RICO,M.A.JIMENEZ,C.GONZALEZ,V.DE FILIPPIS,A.FONTANA
REVDAT   2   24-FEB-09 1TRL    1       VERSN
REVDAT   1   07-FEB-95 1TRL    0
JRNL        AUTH   M.RICO,M.A.JIMENEZ,C.GONZALEZ,V.DE FILIPPIS,
JRNL        AUTH 2 A.FONTANA
JRNL        TITL   NMR SOLUTION STRUCTURE OF THE C-TERMINAL FRAGMENT
JRNL        TITL 2 255-316 OF THERMOLYSIN: A DIMER FORMED BY SUBUNITS
JRNL        TITL 3 HAVING THE NATIVE STRUCTURE.
JRNL        REF    BIOCHEMISTRY                  V.  33 14834 1994
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   7993910
JRNL        DOI    10.1021/BI00253A023
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   M.A.JIMENEZ,M.BRUIX,C.GONZALEZ,F.J.BLANCO,
REMARK   1  AUTH 2 J.L.NIETO,J.HERRANZ,M.RICO
REMARK   1  TITL   CD AND H-NMR STUDIES ON THE CONFORMATIONAL
REMARK   1  TITL 2 PROPERTIES OF PEPTIDE FRAGMENTS FROM THE
REMARK   1  TITL 3 C-TERMINAL DOMAIN OF THERMOLYSIN
REMARK   1  REF    EUR.J.BIOCHEM.                V. 211   569 1993
REMARK   1  REFN                   ISSN 0014-2956
REMARK   1 REFERENCE 2
REMARK   1  AUTH   D.DALZOPPO,C.VITA,A.FONTANA
REMARK   1  TITL   FOLDING OF THERMOLYSIN FRAGMENTS: IDENTIFICATION
REMARK   1  TITL 2 OF THE MINIMUM SIZE OF A CARBOXYL-TERMINAL
REMARK   1  TITL 3 FRAGMENT THAT CAN FOLD INTO A STABLE NATIVE-LIKE
REMARK   1  TITL 4 STRUCTURE
REMARK   1  REF    J.MOL.BIOL.                   V. 182   331 1985
REMARK   1  REFN                   ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION. NOT APPLICABLE.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : GROMOS
REMARK   3   AUTHORS     : VAN GUNSTEREN,BERENDSEN
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1TRL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
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    : 8
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 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  1 TYR A 274   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500  1 ARG A 285   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500  1 TYR A 296   CB  -  CG  -  CD2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500  1 ARG B 260   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500  2 ARG A 260   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500  2 TYR A 274   CB  -  CG  -  CD2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500  2 ARG A 285   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500  2 TYR A 296   CB  -  CG  -  CD2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500  2 TYR B 296   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500  3 TYR A 274   CB  -  CG  -  CD2 ANGL. DEV. =  -4.6 DEGREES
REMARK 500  3 TYR B 268   CB  -  CG  -  CD2 ANGL. DEV. =  -4.5 DEGREES
REMARK 500  3 TYR B 274   CB  -  CG  -  CD2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500  4 ARG A 260   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500  4 PHE A 267   CB  -  CG  -  CD1 ANGL. DEV. =  -4.2 DEGREES
REMARK 500  4 TYR A 274   CB  -  CG  -  CD2 ANGL. DEV. =  -4.9 DEGREES
REMARK 500  4 GLN A 301   CG  -  CD  -  OE1 ANGL. DEV. =  20.7 DEGREES
REMARK 500  4 GLN A 301   CG  -  CD  -  NE2 ANGL. DEV. = -20.6 DEGREES
REMARK 500  4 ARG B 260   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.3 DEGREES
REMARK 500  4 ARG B 260   NE  -  CZ  -  NH2 ANGL. DEV. =   4.4 DEGREES
REMARK 500  4 TYR B 268   CB  -  CG  -  CD1 ANGL. DEV. =  -4.4 DEGREES
REMARK 500  4 ARG B 285   CD  -  NE  -  CZ  ANGL. DEV. =  10.2 DEGREES
REMARK 500  4 VAL B 303   CG1 -  CB  -  CG2 ANGL. DEV. = -10.0 DEGREES
REMARK 500  5 ARG B 269   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500  5 PHE B 281   CB  -  CG  -  CD2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500  6 TYR B 274   CB  -  CG  -  CD2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500  7 ARG A 285   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 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  1 ARG A 260      -33.29    -29.27
REMARK 500  1 ILE B 258      -81.11     33.98
REMARK 500  1 ARG B 260      -79.01     23.37
REMARK 500  1 THR B 278       54.97    -90.20
REMARK 500  1 THR B 299       21.10    -78.04
REMARK 500  1 ALA B 312       32.40    -94.79
REMARK 500  2 ARG A 260      -91.42   -137.09
REMARK 500  2 THR A 278       39.24    -94.28
REMARK 500  2 TYR A 296      -34.91   -161.94
REMARK 500  2 VAL B 256      108.44    -52.10
REMARK 500  2 ARG B 260      -37.30    -28.02
REMARK 500  2 VAL B 315       30.41    -83.77
REMARK 500  3 ARG A 260      -78.33     10.70
REMARK 500  3 SER A 298      -51.24     -9.10
REMARK 500  3 THR A 299       56.82    -66.81
REMARK 500  3 ARG B 260      -64.21   -105.71
REMARK 500  3 THR B 278       54.49    -99.56
REMARK 500  4 THR A 278       40.45   -100.00
REMARK 500  4 ILE B 258      -81.02     43.71
REMARK 500  4 ASP B 261      -54.93   -134.29
REMARK 500  4 LEU B 263      -36.58    -39.70
REMARK 500  4 THR B 278       35.25    -97.58
REMARK 500  4 THR B 299       47.93    -80.90
REMARK 500  5 ARG A 260      -82.33   -117.80
REMARK 500  5 ILE B 258     -134.75   -111.58
REMARK 500  5 THR B 278       38.04    -92.79
REMARK 500  5 THR B 299       40.14    -72.40
REMARK 500  6 ARG A 260      -76.37   -117.35
REMARK 500  6 THR A 278       79.57   -102.86
REMARK 500  6 THR A 299       22.40    -71.32
REMARK 500  6 ARG B 260      -64.00    -15.21
REMARK 500  6 LEU B 263      -36.95    -34.83
REMARK 500  6 THR B 278       36.99    -75.11
REMARK 500  6 LEU B 295      -70.33    -76.69
REMARK 500  6 THR B 299       49.25    -78.63
REMARK 500  6 VAL B 313       90.38    -66.97
REMARK 500  7 VAL A 256      101.50    -59.44
REMARK 500  7 ARG A 260      -59.07   -174.20
REMARK 500  7 SER A 279       95.17    -60.38
REMARK 500  7 GLN A 301        6.55    -68.95
REMARK 500  7 ILE B 258      -93.37     37.79
REMARK 500  7 GLN B 301       -6.78    -56.08
REMARK 500  8 THR A 299       40.21    -67.84
REMARK 500  8 ILE B 258      -75.17    -19.43
REMARK 500  8 THR B 278       58.06    -92.35
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 TYR A 268         0.07    SIDE_CHAIN
REMARK 500  1 TYR A 296         0.10    SIDE_CHAIN
REMARK 500  1 TYR B 268         0.07    SIDE_CHAIN
REMARK 500  1 TYR B 274         0.14    SIDE_CHAIN
REMARK 500  1 PHE B 281         0.10    SIDE_CHAIN
REMARK 500  2 TYR A 268         0.12    SIDE_CHAIN
REMARK 500  2 PHE A 281         0.10    SIDE_CHAIN
REMARK 500  2 TYR A 296         0.24    SIDE_CHAIN
REMARK 500  2 TYR B 268         0.10    SIDE_CHAIN
REMARK 500  3 TYR A 268         0.11    SIDE_CHAIN
REMARK 500  3 PHE A 281         0.11    SIDE_CHAIN
REMARK 500  3 TYR A 296         0.09    SIDE_CHAIN
REMARK 500  3 PHE A 310         0.08    SIDE_CHAIN
REMARK 500  3 TYR B 274         0.17    SIDE_CHAIN
REMARK 500  3 PHE B 281         0.10    SIDE_CHAIN
REMARK 500  3 TYR B 296         0.08    SIDE_CHAIN
REMARK 500  4 PHE A 267         0.10    SIDE_CHAIN
REMARK 500  4 TYR A 274         0.09    SIDE_CHAIN
REMARK 500  4 TYR B 268         0.12    SIDE_CHAIN
REMARK 500  4 TYR B 274         0.09    SIDE_CHAIN
REMARK 500  4 PHE B 281         0.10    SIDE_CHAIN
REMARK 500  4 TYR B 296         0.08    SIDE_CHAIN
REMARK 500  5 TYR A 268         0.10    SIDE_CHAIN
REMARK 500  5 TYR A 274         0.08    SIDE_CHAIN
REMARK 500  5 TYR A 296         0.08    SIDE_CHAIN
REMARK 500  5 TYR B 296         0.07    SIDE_CHAIN
REMARK 500  5 PHE B 310         0.08    SIDE_CHAIN
REMARK 500  6 TYR A 268         0.11    SIDE_CHAIN
REMARK 500  6 PHE A 281         0.10    SIDE_CHAIN
REMARK 500  6 TYR A 296         0.08    SIDE_CHAIN
REMARK 500  6 TYR B 296         0.13    SIDE_CHAIN
REMARK 500  7 TYR B 268         0.08    SIDE_CHAIN
REMARK 500  7 TYR B 274         0.10    SIDE_CHAIN
REMARK 500  7 TYR B 296         0.06    SIDE_CHAIN
REMARK 500  8 GLN A 308         0.07    SIDE_CHAIN
REMARK 500  8 PHE A 310         0.08    SIDE_CHAIN
REMARK 500  8 TYR B 274         0.08    SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500  1 ASP B 261        -10.27
REMARK 500  3 SER A 279         11.40
REMARK 500  3 GLY B 259        -14.84
REMARK 500  4 ILE A 258        -10.80
REMARK 500  4 VAL A 306        -11.47
REMARK 500  4 PRO B 277        -11.45
REMARK 500  4 ALA B 312        -10.01
REMARK 500  5 ILE A 258        -11.14
REMARK 500  5 ALA A 286        -10.47
REMARK 500  5 VAL B 313         11.39
REMARK 500  6 ILE A 258        -12.05
REMARK 500  6 GLY B 259        -10.65
REMARK 500  7 ILE A 258        -10.93
REMARK 500  7 GLY B 259        -10.58
REMARK 500  8 GLY A 259        -10.85
REMARK 500  8 THR A 278         11.66
REMARK 500  8 ALA A 309        -10.79
REMARK 500  8 VAL A 313         11.50
REMARK 500
REMARK 500 REMARK: NULL
DBREF  1TRL A  255   316  UNP    P00800   THER_BACTH     255    316
DBREF  1TRL B  255   316  UNP    P00800   THER_BACTH     255    316
SEQRES   1 A   62  VAL VAL GLY ILE GLY ARG ASP LYS LEU GLY LYS ILE PHE
SEQRES   2 A   62  TYR ARG ALA LEU THR GLN TYR LEU THR PRO THR SER ASN
SEQRES   3 A   62  PHE SER GLN LEU ARG ALA ALA ALA VAL GLN SER ALA THR
SEQRES   4 A   62  ASP LEU TYR GLY SER THR SER GLN GLU VAL ALA SER VAL
SEQRES   5 A   62  LYS GLN ALA PHE ASP ALA VAL GLY VAL LYS
SEQRES   1 B   62  VAL VAL GLY ILE GLY ARG ASP LYS LEU GLY LYS ILE PHE
SEQRES   2 B   62  TYR ARG ALA LEU THR GLN TYR LEU THR PRO THR SER ASN
SEQRES   3 B   62  PHE SER GLN LEU ARG ALA ALA ALA VAL GLN SER ALA THR
SEQRES   4 B   62  ASP LEU TYR GLY SER THR SER GLN GLU VAL ALA SER VAL
SEQRES   5 B   62  LYS GLN ALA PHE ASP ALA VAL GLY VAL LYS
HELIX    1   1 LYS A  262  LEU A  275  1                                  14
HELIX    2   2 ASN A  280  GLY A  297  1                                  18
HELIX    3   3 SER A  300  GLY A  314  1                                  15
HELIX    4   4 GLY B  259  LYS B  262  5                                   4
HELIX    5   5 LEU B  263  GLN B  273  1                                  11
HELIX    6   6 ASN B  280  GLY B  297  1                                  18
HELIX    7   7 SER B  300  ALA B  312  1                                  13
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
      
PROCHECK
Go to PROCHECK summary
 References