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PDBsum entry 3eim

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Hydrolase PDB id
3eim
Jmol
Contents
Protein chain
316 a.a.
Ligands
GOL
Metals
CU1
_CA ×4
Waters ×209
HEADER    HYDROLASE                               16-SEP-08   3EIM
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    PROTEIN COPPER COMPLEX, HYDROLASE, METAL-BINDING, METALLOPROTEASE,
KEYWDS   2 PROTEASE, SECRETED, ZYMOGEN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    L.ENGLERT,A.HEINE,G.KLEBE
REVDAT   3   13-JUL-11 3EIM    1       VERSN
REVDAT   2   24-NOV-09 3EIM    1       HET    HETNAM
REVDAT   1   06-OCT-09 3EIM    0
JRNL        AUTH   L.ENGLERT,A.HEINE,G.KLEBE
JRNL        TITL   METAL EXCHANGE IN THERMOLYSIN
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.88 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) : 1.88
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
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) : 0.188
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.186
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.252
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 1356
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 27030
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.173
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.171
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.231
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 1181
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 23284
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 2413
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 11
REMARK   3   SOLVENT ATOMS      : 209
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 2632.69
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 3
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 10671
REMARK   3   NUMBER OF RESTRAINTS                     : 10188
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.006
REMARK   3   ANGLE DISTANCES                      (A) : 0.021
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.024
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.032
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.038
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.009
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.000
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.051
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 & 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) BY ?
REMARK   4
REMARK   4 3EIM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-08.
REMARK 100 THE RCSB ID CODE IS RCSB049369.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 03-NOV-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               : EMBL/DESY, HAMBURG
REMARK 200  BEAMLINE                       : X12
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200  OPTICS                         : DOUBLE CRYSTAL SI[111]
REMARK 200                                   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   : 27294
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.880
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 7.300
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.10600
REMARK 200   FOR THE DATA SET  : 18.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.91
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.50
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.46100
REMARK 200   FOR SHELL         : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1TMN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM TRIS/HCL, 50%DMSO, 1,9MCSCL, PH
REMARK 280  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       42.88333
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       85.76667
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       64.32500
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      107.20833
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       21.44167
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       42.88333
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       85.76667
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      107.20833
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       64.32500
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       21.44167
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     LEU A 144    CG   CD1  CD2
REMARK 470     GLN A 158    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    ARG A  11   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 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       84.59   -162.04
REMARK 500    THR A  26      -55.24     74.55
REMARK 500    SER A  92     -167.10     58.08
REMARK 500    SER A 107     -163.39     62.06
REMARK 500    SER A 118        5.96   -150.57
REMARK 500    THR A 152     -100.78   -119.73
REMARK 500    ASN A 159     -140.63     53.46
REMARK 500    THR A 194       78.92     38.45
REMARK 500    ASP A 207       79.77   -156.14
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 A2003  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A  57   OD1
REMARK 620 2 ASP A  57   OD2  54.4
REMARK 620 3 ASP A  59   OD1 123.0  69.1
REMARK 620 4 GLN A  61   O    98.1  90.5  89.2
REMARK 620 5 HOH A2161   O   157.4 142.7  74.4  96.4
REMARK 620 6 HOH A2190   O    83.2  88.9  88.7 178.0  83.0
REMARK 620 7 HOH A2138   O    84.0 137.0 153.0  84.3  80.3  97.5
REMARK 620 N                    1     2     3     4     5     6
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 ASP A 138   OD2
REMARK 620 2 GLU A 177   OE1  78.2
REMARK 620 3 GLU A 177   OE2 127.0  49.0
REMARK 620 4 ASP A 185   OD1 158.1 123.6  74.9
REMARK 620 5 GLU A 187   O    79.8 144.6 145.8  80.0
REMARK 620 6 GLU A 190   OE1  84.6 129.1 122.6  82.3  75.4
REMARK 620 7 GLU A 190   OE2 103.9  84.7  71.4  82.2 127.7  53.6
REMARK 620 8 HOH A2036   O    92.4  77.0  81.1  91.0  76.6 151.9 152.4
REMARK 620 N                    1     2     3     4     5     6     7
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 GLU A 177   OE2
REMARK 620 2 ASN A 183   O    95.5
REMARK 620 3 ASP A 185   OD2  89.6  91.2
REMARK 620 4 GLU A 190   OE2  83.2 171.0  79.9
REMARK 620 5 HOH A2189   O    90.2  87.9 179.1 101.0
REMARK 620 6 HOH A2169   O   177.5  87.0  89.8  94.3  90.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A2004  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 193   O
REMARK 620 2 THR A 194   O    76.4
REMARK 620 3 THR A 194   OG1  77.6  68.1
REMARK 620 4 ILE A 197   O   155.8  80.6 101.0
REMARK 620 5 ASP A 200   OD1 123.7 132.9  75.3  78.2
REMARK 620 6 HOH A2164   O    83.7 154.8 122.7 115.8  71.5
REMARK 620 7 HOH A2166   O    85.8  82.7 149.0  83.6 135.1  80.4
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             CU1 A2000  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 142   NE2
REMARK 620 2 HIS A 146   NE2 100.8
REMARK 620 3 GLU A 166   OE2 118.2  96.5
REMARK 620 4 HOH A2102   O   102.0 154.3  83.0
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2007
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8TLN   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH VAL-LYS
REMARK 900 RELATED ID: 1TMN   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH N-CARBOXYMETHYLDIPEPTIDE
REMARK 900 INHIBITOR
DBREF  3EIM A    1   316  UNP    P00800   THER_BACTH     233    548
SEQADV 3EIM ASP A   37  UNP  P00800    ASN   269 VARIANT
SEQADV 3EIM GLU A  119  UNP  P00800    GLN   351 VARIANT
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 ASP 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 GLU 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    CU1  A2000       1
HET     CA  A2001       1
HET     CA  A2002       1
HET     CA  A2003       1
HET     CA  A2004       1
HET    GOL  A2007       6
HETNAM     CU1 COPPER (I) ION
HETNAM      CA CALCIUM ION
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2  CU1    CU 1+
FORMUL   3   CA    4(CA 2+)
FORMUL   7  GOL    C3 H8 O3
FORMUL   8  HOH   *209(H2 O)
HELIX    1   1 ASP A   67  ASN A   89  1                                  23
HELIX    2   2 PRO A  132  GLY A  135  5                                   4
HELIX    3   3 GLY A  136  THR A  152  1                                  17
HELIX    4   4 GLN A  158  ASN A  181  1                                  24
HELIX    5   5 ASP A  207  GLY A  212  5                                   6
HELIX    6   6 HIS A  216  ARG A  220  5                                   5
HELIX    7   7 GLN A  225  VAL A  230  1                                   6
HELIX    8   8 ASN A  233  GLY A  247  1                                  15
HELIX    9   9 GLY A  259  TYR A  274  1                                  16
HELIX   10  10 ASN A  280  GLY A  297  1                                  18
HELIX   11  11 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  GLY A   8   O  ILE A  20
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  MET A 120   N  ARG A 101
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 A2003     1555   1555  2.32
LINK         OD2 ASP A  57                CA    CA A2003     1555   1555  2.51
LINK         OD1 ASP A  59                CA    CA A2003     1555   1555  2.40
LINK         O   GLN A  61                CA    CA A2003     1555   1555  2.23
LINK         OD2 ASP A 138                CA    CA A2001     1555   1555  2.48
LINK         OE1 GLU A 177                CA    CA A2001     1555   1555  2.50
LINK         OE2 GLU A 177                CA    CA A2002     1555   1555  2.29
LINK         OE2 GLU A 177                CA    CA A2001     1555   1555  2.79
LINK         O   ASN A 183                CA    CA A2002     1555   1555  2.26
LINK         OD1 ASP A 185                CA    CA A2001     1555   1555  2.38
LINK         OD2 ASP A 185                CA    CA A2002     1555   1555  2.32
LINK         O   GLU A 187                CA    CA A2001     1555   1555  2.29
LINK         OE1 GLU A 190                CA    CA A2001     1555   1555  2.46
LINK         OE2 GLU A 190                CA    CA A2002     1555   1555  2.31
LINK         OE2 GLU A 190                CA    CA A2001     1555   1555  2.41
LINK         O   TYR A 193                CA    CA A2004     1555   1555  2.30
LINK         O   THR A 194                CA    CA A2004     1555   1555  2.33
LINK         OG1 THR A 194                CA    CA A2004     1555   1555  2.37
LINK         O   ILE A 197                CA    CA A2004     1555   1555  2.24
LINK         OD1 ASP A 200                CA    CA A2004     1555   1555  2.48
LINK        CA    CA A2001                 O   HOH A2036     1555   1555  2.44
LINK        CA    CA A2002                 O   HOH A2189     1555   1555  2.34
LINK        CA    CA A2002                 O   HOH A2169     1555   1555  2.25
LINK        CA    CA A2003                 O   HOH A2161     1555   1555  2.42
LINK        CA    CA A2003                 O   HOH A2190     1555   1555  2.35
LINK        CA    CA A2003                 O   HOH A2138     1555   1555  2.47
LINK        CA    CA A2004                 O   HOH A2164     1555   1555  2.44
LINK        CA    CA A2004                 O   HOH A2166     1555   1555  2.25
LINK         NE2 HIS A 142                CU   CU1 A2000     1555   1555  2.02
LINK         NE2 HIS A 146                CU   CU1 A2000     1555   1555  2.06
LINK         OE2 GLU A 166                CU   CU1 A2000     1555   1555  1.98
LINK        CU   CU1 A2000                 O   HOH A2102     1555   1555  2.25
CISPEP   1 LEU A   50    PRO A   51          0         3.27
SITE     1 AC1  5 HIS A 142  HIS A 146  GLU A 166  HOH A2102
SITE     2 AC1  5 HOH A2192
SITE     1 AC2  6 ASP A 138  GLU A 177  ASP A 185  GLU A 187
SITE     2 AC2  6 GLU A 190  HOH A2036
SITE     1 AC3  6 GLU A 177  ASN A 183  ASP A 185  GLU A 190
SITE     2 AC3  6 HOH A2169  HOH A2189
SITE     1 AC4  6 ASP A  57  ASP A  59  GLN A  61  HOH A2138
SITE     2 AC4  6 HOH A2161  HOH A2190
SITE     1 AC5  6 TYR A 193  THR A 194  ILE A 197  ASP A 200
SITE     2 AC5  6 HOH A2164  HOH A2166
SITE     1 AC6 11 THR A 152  GLY A 248  VAL A 255  GLN A 273
SITE     2 AC6 11 TYR A 274  LEU A 275  HOH A2068  HOH A2094
SITE     3 AC6 11 HOH A2108  HOH A2162  HOH A2193
CRYST1   92.710   92.710  128.650  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      0.010786  0.006227  0.000000        0.00000
SCALE2      0.000000  0.012455  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007773        0.00000
      
PROCHECK
Go to PROCHECK summary
 References