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PDBsum entry 3fb0

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Hydrolase PDB id
3fb0
Jmol
Contents
Protein chain
316 a.a.
Ligands
DMS
Metals
_CA ×4
Waters ×273
HEADER    HYDROLASE                               18-NOV-08   3FB0
TITLE     METAL EXCHANGE IN THERMOLYSIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: THERMOLYSIN;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: UNP RESIDUES 233-548;
COMPND   5 SYNONYM: THERMOSTABLE NEUTRAL PROTEINASE;
COMPND   6 EC: 3.4.24.27
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS THERMOPROTEOLYTICUS;
SOURCE   3 ORGANISM_TAXID: 1427
KEYWDS    ZINC-FREE PROTEIN, CALCIUM, HYDROLASE, METAL-BINDING,
KEYWDS   2 METALLOPROTEASE, PROTEASE, SECRETED, ZINC, ZYMOGEN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    L.ENGLERT,A.HEINE,G.KLEBE
REVDAT   1   08-DEC-09 3FB0    0
JRNL        AUTH   L.ENGLERT,A.HEINE,G.KLEBE
JRNL        TITL   METAL EXCHANGE IN THERMOLYSIN
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : SHELXL-97
REMARK   3   AUTHORS     : G.M.SHELDRICK
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0
REMARK   3   CROSS-VALIDATION METHOD           : FREE R
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.182
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.182
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.246
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2199
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 43890
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.160
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.160
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.203
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 1658
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 33174
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 2454
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 8
REMARK   3   SOLVENT ATOMS      : 273
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 2701.00
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 6
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 10990
REMARK   3   NUMBER OF RESTRAINTS                     : 10298
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.008
REMARK   3   ANGLE DISTANCES                      (A) : 0.024
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.025
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.042
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.052
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.015
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.000
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.050
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: NULL
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY THE
REMARK   3  METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28(1995)53-56
REMARK   3  ANISOTROPIC REFINEMENT REDUCED FREE R (NO CUTOFF)
REMARK   4
REMARK   4 3FB0 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-08.
REMARK 100 THE RCSB ID CODE IS RCSB050367.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-07
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : BESSY
REMARK 200  BEAMLINE                       : 14.2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91841
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200                                   KMC-1
REMARK 200  OPTICS                         : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45208
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.590
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4
REMARK 200  DATA REDUNDANCY                : 4.600
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.04500
REMARK 200   FOR THE DATA SET  : 31.9800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.62
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.35400
REMARK 200   FOR SHELL         : 3.980
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1TMN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM TRIS/HCL, 50%DMSO, 1,9MCSCL,
REMARK 280  PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 288K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+5/6
REMARK 290       6555   X-Y,X,Z+1/6
REMARK 290       7555   Y,X,-Z+1/3
REMARK 290       8555   X-Y,-Y,-Z
REMARK 290       9555   -X,-X+Y,-Z+2/3
REMARK 290      10555   -Y,-X,-Z+5/6
REMARK 290      11555   -X+Y,Y,-Z+1/2
REMARK 290      12555   X,X-Y,-Z+1/6
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.55267
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       87.10533
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       65.32900
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      108.88167
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       21.77633
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       43.55267
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       87.10533
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      108.88167
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       65.32900
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       21.77633
REMARK 290
REMARK 290 REMARK: NULL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     GLN A 128    CG   CD   OE1  NE2
REMARK 470     LYS A 182    CG   CD   CE   NZ
REMARK 470     GLN A 225    CG   CD   OE1  NE2
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  93   CB  -  CG  -  CD2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ASP A 261   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ARG A 269   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 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  25       88.76   -160.70
REMARK 500    THR A  26      -59.98     69.73
REMARK 500    SER A  92     -172.89     57.21
REMARK 500    SER A 107     -164.28     62.36
REMARK 500    ASN A 111       54.57    -92.40
REMARK 500    GLN A 128      -66.49   -103.12
REMARK 500    THR A 152      -98.62   -119.25
REMARK 500    ASN A 159     -142.97     53.32
REMARK 500    LYS A 182      -82.49    -90.51
REMARK 500    THR A 194       78.79     39.92
REMARK 500    TYR A 274      -34.72   -130.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A2002  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A  57   OD1
REMARK 620 2 ASP A  57   OD2  53.6
REMARK 620 3 ASP A  59   OD1 122.5  69.2
REMARK 620 4 GLN A  61   O    96.2  89.8  88.3
REMARK 620 5 HOH A5128   O   156.2 146.8  78.3  95.9
REMARK 620 6 HOH A5129   O    85.1  87.3  87.3 175.4  84.5
REMARK 620 7 HOH A5216   O    81.1 133.6 156.1  85.3  79.5  99.3
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A2000  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 138   OD2
REMARK 620 2 GLU A 177   OE1  73.6
REMARK 620 3 GLU A 177   OE2 123.4  49.7
REMARK 620 4 ASP A 185   OD1 160.8 125.6  75.8
REMARK 620 5 GLU A 187   O    85.7 144.7 140.5  77.7
REMARK 620 6 GLU A 190   OE1  85.0 126.9 126.0  82.0  77.9
REMARK 620 7 GLU A 190   OE2  96.5  83.1  78.4  86.4 128.4  51.3
REMARK 620 8 HOH A5126   O    96.9  78.1  74.4  88.7  76.2 153.8 152.8
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A2001  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 177   OE2
REMARK 620 2 ASN A 183   O    91.8
REMARK 620 3 ASP A 185   OD2  85.1  92.4
REMARK 620 4 GLU A 190   OE2  80.1 170.2  81.4
REMARK 620 5 HOH A5125   O    83.6  99.6 163.6  85.0
REMARK 620 6 HOH A5127   O   174.7  93.4  95.6  94.8  94.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A2003  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 193   O
REMARK 620 2 THR A 194   O    73.8
REMARK 620 3 THR A 194   OG1  76.1  70.9
REMARK 620 4 ILE A 197   O   155.9  82.6 101.5
REMARK 620 5 ASP A 200   OD1 122.4 137.6  75.8  79.0
REMARK 620 6 HOH A5215   O    91.5  84.7 154.7  80.9 128.8
REMARK 620 7 HOH A5217   O    84.0 150.3 123.1 115.8  71.3  76.3
REMARK 620 N                    1     2     3     4     5     6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2000
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2001
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2002
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2003
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 4000
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EIM   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH COPPER(I) IN ITS ACTIVE SITE
REMARK 900 RELATED ID: 8TLN   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH VAL-LYS
DBREF  3FB0 A    1   316  UNP    P00800   THER_BACTH     233    548
SEQRES   1 A  316  ILE THR GLY THR SER THR VAL GLY VAL GLY ARG GLY VAL
SEQRES   2 A  316  LEU GLY ASP GLN LYS ASN ILE ASN THR THR TYR SER THR
SEQRES   3 A  316  TYR TYR TYR LEU GLN ASP ASN THR ARG GLY ASN GLY ILE
SEQRES   4 A  316  PHE THR TYR ASP ALA LYS TYR ARG THR THR LEU PRO GLY
SEQRES   5 A  316  SER LEU TRP ALA ASP ALA ASP ASN GLN PHE PHE ALA SER
SEQRES   6 A  316  TYR ASP ALA PRO ALA VAL ASP ALA HIS TYR TYR ALA GLY
SEQRES   7 A  316  VAL THR TYR ASP TYR TYR LYS ASN VAL HIS ASN ARG LEU
SEQRES   8 A  316  SER TYR ASP GLY ASN ASN ALA ALA ILE ARG SER SER VAL
SEQRES   9 A  316  HIS TYR SER GLN GLY TYR ASN ASN ALA PHE TRP ASN GLY
SEQRES  10 A  316  SER GLN MET VAL TYR GLY ASP GLY ASP GLY GLN THR PHE
SEQRES  11 A  316  ILE PRO LEU SER GLY GLY ILE ASP VAL VAL ALA HIS GLU
SEQRES  12 A  316  LEU THR HIS ALA VAL THR ASP TYR THR ALA GLY LEU ILE
SEQRES  13 A  316  TYR GLN ASN GLU SER GLY ALA ILE ASN GLU ALA ILE SER
SEQRES  14 A  316  ASP ILE PHE GLY THR LEU VAL GLU PHE TYR ALA ASN LYS
SEQRES  15 A  316  ASN PRO ASP TRP GLU ILE GLY GLU ASP VAL TYR THR PRO
SEQRES  16 A  316  GLY ILE SER GLY ASP SER LEU ARG SER MET SER ASP PRO
SEQRES  17 A  316  ALA LYS TYR GLY ASP PRO ASP HIS TYR SER LYS ARG TYR
SEQRES  18 A  316  THR GLY THR GLN ASP ASN GLY GLY VAL HIS ILE ASN SER
SEQRES  19 A  316  GLY ILE ILE ASN LYS ALA ALA TYR LEU ILE SER GLN GLY
SEQRES  20 A  316  GLY THR HIS TYR GLY VAL SER VAL VAL GLY ILE GLY ARG
SEQRES  21 A  316  ASP LYS LEU GLY LYS ILE PHE TYR ARG ALA LEU THR GLN
SEQRES  22 A  316  TYR LEU THR PRO THR SER ASN PHE SER GLN LEU ARG ALA
SEQRES  23 A  316  ALA ALA VAL GLN SER ALA THR ASP LEU TYR GLY SER THR
SEQRES  24 A  316  SER GLN GLU VAL ALA SER VAL LYS GLN ALA PHE ASP ALA
SEQRES  25 A  316  VAL GLY VAL LYS
HET     CA  A2000       1
HET     CA  A2001       1
HET     CA  A2002       1
HET     CA  A2003       1
HET    DMS  A4000       4
HETNAM      CA CALCIUM ION
HETNAM     DMS DIMETHYL SULFOXIDE
FORMUL   2   CA    4(CA 2+)
FORMUL   6  DMS    C2 H6 O S
FORMUL   7  HOH   *273(H2 O)
HELIX    1   1 ALA A   64  TYR A   66  5                                   3
HELIX    2   2 ASP A   67  ASN A   89  1                                  23
HELIX    3   3 PRO A  132  GLY A  135  5                                   4
HELIX    4   4 GLY A  136  THR A  152  1                                  17
HELIX    5   5 GLN A  158  ASN A  181  1                                  24
HELIX    6   6 ASP A  207  GLY A  212  5                                   6
HELIX    7   7 HIS A  216  ARG A  220  5                                   5
HELIX    8   8 THR A  224  VAL A  230  1                                   7
HELIX    9   9 ASN A  233  GLY A  247  1                                  15
HELIX   10  10 GLY A  259  TYR A  274  1                                  16
HELIX   11  11 ASN A  280  GLY A  297  1                                  18
HELIX   12  12 SER A  300  VAL A  313  1                                  14
SHEET    1   A 5 ALA A  56  ASP A  57  0
SHEET    2   A 5 TYR A  28  TYR A  29 -1  N  TYR A  28   O  ASP A  57
SHEET    3   A 5 GLN A  17  TYR A  24 -1  N  THR A  23   O  TYR A  29
SHEET    4   A 5 THR A   4  ARG A  11 -1  N  THR A   4   O  TYR A  24
SHEET    5   A 5 GLN A  61  PHE A  62  1  O  PHE A  62   N  VAL A   9
SHEET    1   B 3 GLN A  31  ASP A  32  0
SHEET    2   B 3 ILE A  39  ASP A  43 -1  O  ILE A  39   N  ASP A  32
SHEET    3   B 3 SER A  53  LEU A  54 -1  O  SER A  53   N  ASP A  43
SHEET    1   C 5 GLN A  31  ASP A  32  0
SHEET    2   C 5 ILE A  39  ASP A  43 -1  O  ILE A  39   N  ASP A  32
SHEET    3   C 5 ILE A 100  VAL A 104  1  O  SER A 102   N  TYR A  42
SHEET    4   C 5 MET A 120  TYR A 122  1  O  TYR A 122   N  SER A 103
SHEET    5   C 5 ALA A 113  TRP A 115 -1  N  PHE A 114   O  VAL A 121
SHEET    1   D 2 GLU A 187  ILE A 188  0
SHEET    2   D 2 ARG A 203  SER A 204 -1  O  ARG A 203   N  ILE A 188
SHEET    1   E 2 GLY A 248  HIS A 250  0
SHEET    2   E 2 VAL A 253  VAL A 255 -1  O  VAL A 255   N  GLY A 248
LINK         OD1 ASP A  57                CA    CA A2002     1555   1555  2.32
LINK         OD2 ASP A  57                CA    CA A2002     1555   1555  2.51
LINK         OD1 ASP A  59                CA    CA A2002     1555   1555  2.48
LINK         O   GLN A  61                CA    CA A2002     1555   1555  2.25
LINK         OD2 ASP A 138                CA    CA A2000     1555   1555  2.34
LINK         OE1 GLU A 177                CA    CA A2000     1555   1555  2.52
LINK         OE2 GLU A 177                CA    CA A2001     1555   1555  2.65
LINK         OE2 GLU A 177                CA    CA A2000     1555   1555  2.70
LINK         O   ASN A 183                CA    CA A2001     1555   1555  2.30
LINK         OD1 ASP A 185                CA    CA A2000     1555   1555  2.46
LINK         OD2 ASP A 185                CA    CA A2001     1555   1555  2.36
LINK         O   GLU A 187                CA    CA A2000     1555   1555  2.34
LINK         OE1 GLU A 190                CA    CA A2000     1555   1555  2.51
LINK         OE2 GLU A 190                CA    CA A2001     1555   1555  2.41
LINK         OE2 GLU A 190                CA    CA A2000     1555   1555  2.45
LINK         O   TYR A 193                CA    CA A2003     1555   1555  2.36
LINK         O   THR A 194                CA    CA A2003     1555   1555  2.39
LINK         OG1 THR A 194                CA    CA A2003     1555   1555  2.48
LINK         O   ILE A 197                CA    CA A2003     1555   1555  2.31
LINK         OD1 ASP A 200                CA    CA A2003     1555   1555  2.36
LINK        CA    CA A2000                 O   HOH A5126     1555   1555  2.53
LINK        CA    CA A2001                 O   HOH A5125     1555   1555  2.43
LINK        CA    CA A2001                 O   HOH A5127     1555   1555  2.21
LINK        CA    CA A2002                 O   HOH A5128     1555   1555  2.47
LINK        CA    CA A2002                 O   HOH A5129     1555   1555  2.35
LINK        CA    CA A2002                 O   HOH A5216     1555   1555  2.33
LINK        CA    CA A2003                 O   HOH A5215     1555   1555  2.45
LINK        CA    CA A2003                 O   HOH A5217     1555   1555  2.36
CISPEP   1 LEU A   50    PRO A   51          0         4.69
SITE     1 AC1  6 ASP A 138  GLU A 177  ASP A 185  GLU A 187
SITE     2 AC1  6 GLU A 190  HOH A5126
SITE     1 AC2  6 GLU A 177  ASN A 183  ASP A 185  GLU A 190
SITE     2 AC2  6 HOH A5125  HOH A5127
SITE     1 AC3  6 ASP A  57  ASP A  59  GLN A  61  HOH A5128
SITE     2 AC3  6 HOH A5129  HOH A5216
SITE     1 AC4  6 TYR A 193  THR A 194  ILE A 197  ASP A 200
SITE     2 AC4  6 HOH A5215  HOH A5217
SITE     1 AC5  5 TYR A  66  HIS A 216  SER A 218  TYR A 251
SITE     2 AC5  5 HOH A5137
CRYST1   92.961   92.961  130.658  90.00  90.00 120.00 P 61 2 2     12
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      0.010757  0.006211  0.000000        0.00000
SCALE2      0.000000  0.012421  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007654        0.00000
      
PROCHECK
Go to PROCHECK summary
 References