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PDBsum entry 1kei

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Hydrolase PDB id
1kei
Jmol
Contents
Protein chain
316 a.a. *
Ligands
VAL-LYS
Metals
_CA ×4
_ZN
Waters ×185
* Residue conservation analysis
HEADER    HYDROLASE                               16-NOV-01   1KEI
TITLE     THERMOLYSIN (SUBSTRATE-FREE)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: THERMOLYSIN;
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.4.24.27
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS THERMOPROTEOLYTICUS;
SOURCE   3 ORGANISM_TAXID: 1427
KEYWDS    HYDROLASE, METALLOPROTEINASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.SENDA,T.SENDA,S.KIDOKORO
REVDAT   2   24-FEB-09 1KEI    1       VERSN
REVDAT   1   16-NOV-02 1KEI    0
JRNL        AUTH   M.SENDA,T.SENDA,S.KIDOKORO
JRNL        TITL   CRYSTAL STRUCTURE ANALYSES OF THERMOLYSIN IN
JRNL        TITL 2 COMPLEX WITH ITS INHIBITORS
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     : CNS 1.0
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.48
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2120087.230
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.5
REMARK   3   NUMBER OF REFLECTIONS             : 45042
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.172
REMARK   3   FREE R VALUE                     : 0.188
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2271
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.70
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 5.40
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6915
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2460
REMARK   3   BIN FREE R VALUE                    : 0.2590
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.40
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 392
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2478
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 22
REMARK   3   SOLVENT ATOMS            : 185
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 20.90
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.20
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.64000
REMARK   3    B22 (A**2) : -0.64000
REMARK   3    B33 (A**2) : 1.27000
REMARK   3    B12 (A**2) : -0.55000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.16
REMARK   3   ESD FROM SIGMAA              (A) : 0.10
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.18
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.14
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.004
REMARK   3   BOND ANGLES            (DEGREES) : 1.20
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.20
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.66
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.30
REMARK   3   BSOL        : 37.48
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : ION.PARAM
REMARK   3  PARAMETER FILE  3  : WATER.PARAM
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1KEI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-NOV-01.
REMARK 100 THE RCSB ID CODE IS RCSB014869.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-00
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : BL-18B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00
REMARK 200  MONOCHROMATOR                  : SI 111
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (TRUNCATE)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45120
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5
REMARK 200  DATA REDUNDANCY                : 5.900
REMARK 200  R MERGE                    (I) : 0.06100
REMARK 200  R SYM                      (I) : 0.05600
REMARK 200   FOR THE DATA SET  : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20
REMARK 200  R MERGE FOR SHELL          (I) : 0.37600
REMARK 200  R SYM FOR SHELL            (I) : 0.33900
REMARK 200   FOR SHELL         : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: DMSO, CALCIUM ACETATE, TRIS, PH
REMARK 280  7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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       43.71367
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       87.42733
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       65.57050
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      109.28417
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       21.85683
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       43.71367
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       87.42733
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      109.28417
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       65.57050
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       21.85683
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 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       84.44   -163.10
REMARK 500    THR A  26      -59.52     76.56
REMARK 500    PHE A  62       69.02   -117.82
REMARK 500    SER A  92     -175.09     62.74
REMARK 500    SER A 107     -161.13     58.97
REMARK 500    ASN A 111       54.24    -91.41
REMARK 500    PRO A 132      117.09    -39.57
REMARK 500    THR A 152      -99.10   -118.25
REMARK 500    ASN A 159     -140.94     49.13
REMARK 500    THR A 194       77.38     37.70
REMARK 500    ASP A 207       79.08   -150.98
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 A 404  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 197   O
REMARK 620 2 THR A 194   OG1 102.6
REMARK 620 3 HOH A1009   O   116.6 124.9
REMARK 620 4 THR A 194   O    79.4  69.7 150.4
REMARK 620 5 HOH A1051   O    82.1 144.7  80.7  77.1
REMARK 620 6 ASP A 200   OD1  81.1  75.3  74.4 134.7 139.4
REMARK 620 7 TYR A 193   O   154.0  75.3  83.5  75.5  85.5 122.1
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 405  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 142   NE2
REMARK 620 2 HIS A 146   NE2 103.7
REMARK 620 3 GLU A 166   OE2 124.3  96.9
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 401  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 138   OD2
REMARK 620 2 GLU A 187   O    86.0
REMARK 620 3 GLU A 190   OE1  84.2  77.8
REMARK 620 4 GLU A 190   OE2  97.5 128.5  51.8
REMARK 620 5 HOH A1005   O   100.6  74.9 151.8 151.6
REMARK 620 6 GLU A 177   OE1  77.6 146.2 128.7  83.3  79.3
REMARK 620 7 GLU A 177   OE2 125.8 142.8 119.8  71.5  80.1  48.9
REMARK 620 8 ASP A 185   OD1 162.4  79.5  83.1  84.1  85.3 119.9  71.5
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 402  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 190   OE2
REMARK 620 2 GLU A 177   OE2  84.0
REMARK 620 3 ASN A 183   O   172.9  91.6
REMARK 620 4 ASP A 185   OD2  83.4  90.5  91.0
REMARK 620 5 HOH A1030   O    89.6  88.2  95.9 173.0
REMARK 620 6 HOH A1019   O    93.6 171.7  91.5  97.1  83.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 403  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1014   O
REMARK 620 2 HOH A1016   O    99.8
REMARK 620 3 ASP A  59   OD1 155.7  86.8
REMARK 620 4 ASP A  57   OD1  81.7  84.6 122.4
REMARK 620 5 GLN A  61   O    83.1 174.8  88.8 100.1
REMARK 620 6 HOH A1021   O    80.2  82.5  77.5 155.6  93.8
REMARK 620 7 ASP A  57   OD2 131.7  92.2  70.8  52.8  89.0 148.0
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 401
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 402
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 403
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 404
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 405
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VAL A 1001
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LYS A 1002
DBREF  1KEI A    1   316  UNP    P00800   THER_BACTH       1    316
SEQADV 1KEI ASN A   37  UNP  P00800    ASP    37 SEE REMARK 999
SEQADV 1KEI GLN A  119  UNP  P00800    GLU   119 SEE REMARK 999
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  A 401       1
HET     CA  A 402       1
HET     CA  A 403       1
HET     CA  A 404       1
HET     ZN  A 405       1
HET    VAL  A1001       7
HET    LYS  A1002      10
HETNAM      CA CALCIUM ION
HETNAM      ZN ZINC ION
HETNAM     VAL VALINE
HETNAM     LYS LYSINE
FORMUL   2   CA    4(CA 2+)
FORMUL   6   ZN    ZN 2+
FORMUL   7  VAL    C5 H11 N O2
FORMUL   8  LYS    C6 H15 N2 O2 1+
FORMUL   9  HOH   *185(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  ALA A  180  1                                  23
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 THR A  224  VAL A  230  1                                   7
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  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 5 ALA A 113  TRP A 115  0
SHEET    2   B 5 MET A 120  TYR A 122 -1  O  VAL A 121   N  PHE A 114
SHEET    3   B 5 ILE A 100  VAL A 104  1  N  SER A 103   O  TYR A 122
SHEET    4   B 5 ILE A  39  ASP A  43  1  N  TYR A  42   O  SER A 102
SHEET    5   B 5 GLN A  31  ASP A  32 -1  N  ASP A  32   O  ILE A  39
SHEET    1   C 5 ALA A 113  TRP A 115  0
SHEET    2   C 5 MET A 120  TYR A 122 -1  O  VAL A 121   N  PHE A 114
SHEET    3   C 5 ILE A 100  VAL A 104  1  N  SER A 103   O  TYR A 122
SHEET    4   C 5 ILE A  39  ASP A  43  1  N  TYR A  42   O  SER A 102
SHEET    5   C 5 SER A  53  LEU A  54 -1  O  SER A  53   N  ASP A  43
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        CA    CA A 404                 O   ILE A 197     1555   1555  2.15
LINK        ZN    ZN A 405                 NE2 HIS A 142     1555   1555  2.05
LINK        ZN    ZN A 405                 NE2 HIS A 146     1555   1555  2.00
LINK        ZN    ZN A 405                 OE2 GLU A 166     1555   1555  1.85
LINK         C   VAL A1001                 N   LYS A1002     1555   1555  1.33
LINK        CA    CA A 401                 OD2 ASP A 138     1555   1555  2.37
LINK        CA    CA A 401                 O   GLU A 187     1555   1555  2.33
LINK        CA    CA A 401                 OE1 GLU A 190     1555   1555  2.48
LINK        CA    CA A 401                 OE2 GLU A 190     1555   1555  2.54
LINK        CA    CA A 401                 O   HOH A1005     1555   1555  2.45
LINK        CA    CA A 401                 OE1 GLU A 177     1555   1555  2.47
LINK        CA    CA A 401                 OE2 GLU A 177     1555   1555  2.80
LINK        CA    CA A 401                 OD1 ASP A 185     1555   1555  2.48
LINK        CA    CA A 402                 OE2 GLU A 190     1555   1555  2.29
LINK        CA    CA A 402                 OE2 GLU A 177     1555   1555  2.38
LINK        CA    CA A 402                 O   ASN A 183     1555   1555  2.33
LINK        CA    CA A 402                 OD2 ASP A 185     1555   1555  2.34
LINK        CA    CA A 402                 O   HOH A1030     1555   1555  2.39
LINK        CA    CA A 402                 O   HOH A1019     1555   1555  2.37
LINK        CA    CA A 403                 O   HOH A1014     1555   1555  2.44
LINK        CA    CA A 403                 O   HOH A1016     1555   1555  2.32
LINK        CA    CA A 403                 OD1 ASP A  59     1555   1555  2.38
LINK        CA    CA A 403                 OD1 ASP A  57     1555   1555  2.38
LINK        CA    CA A 403                 O   GLN A  61     1555   1555  2.28
LINK        CA    CA A 403                 O   HOH A1021     1555   1555  2.50
LINK        CA    CA A 403                 OD2 ASP A  57     1555   1555  2.53
LINK        CA    CA A 404                 OG1 THR A 194     1555   1555  2.34
LINK        CA    CA A 404                 O   HOH A1009     1555   1555  2.39
LINK        CA    CA A 404                 O   THR A 194     1555   1555  2.33
LINK        CA    CA A 404                 O   HOH A1051     1555   1555  2.47
LINK        CA    CA A 404                 OD1 ASP A 200     1555   1555  2.36
LINK        CA    CA A 404                 O   TYR A 193     1555   1555  2.32
CISPEP   1 LEU A   50    PRO A   51          0         0.21
SITE     1 AC1  6 ASP A 138  GLU A 177  ASP A 185  GLU A 187
SITE     2 AC1  6 GLU A 190  HOH A1005
SITE     1 AC2  6 GLU A 177  ASN A 183  ASP A 185  GLU A 190
SITE     2 AC2  6 HOH A1019  HOH A1030
SITE     1 AC3  6 ASP A  57  ASP A  59  GLN A  61  HOH A1014
SITE     2 AC3  6 HOH A1016  HOH A1021
SITE     1 AC4  6 TYR A 193  THR A 194  ILE A 197  ASP A 200
SITE     2 AC4  6 HOH A1009  HOH A1051
SITE     1 AC5  3 HIS A 142  HIS A 146  GLU A 166
SITE     1 AC6  7 ASN A 112  ALA A 113  GLU A 143  ARG A 203
SITE     2 AC6  7 HIS A 231  LYS A1002  HOH A1185
SITE     1 AC7  6 ASN A 112  PHE A 130  LEU A 202  HIS A 231
SITE     2 AC7  6 VAL A1001  HOH A1164
CRYST1   93.541   93.541  131.141  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      0.010691  0.006172  0.000000        0.00000
SCALE2      0.000000  0.012344  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007625        0.00000
      
PROCHECK
Go to PROCHECK summary
 References