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PDBsum entry 1tlp

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Hydrolase/hydrolase inhibitor PDB id
1tlp
Jmol
Contents
Protein chain
316 a.a. *
Ligands
RDF
Metals
_ZN
_CA ×4
Waters ×163
* Residue conservation analysis
HEADER    HYDROLASE/HYDROLASE INHIBITOR           29-JUN-87   1TLP
TITLE     CRYSTALLOGRAPHIC STRUCTURAL ANALYSIS OF PHOSPHORAMIDATES AS INHIBITORS
TITLE    2 AND TRANSITION-STATE ANALOGS OF THERMOLYSIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: THERMOLYSIN;
COMPND   3 CHAIN: E;
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    METALLOPROTEINASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.E.TRONRUD,A.F.MONZINGO,B.W.MATTHEWS
REVDAT   5   13-JUL-11 1TLP    1       VERSN
REVDAT   4   25-AUG-09 1TLP    1       SOURCE
REVDAT   3   24-FEB-09 1TLP    1       VERSN
REVDAT   2   08-MAR-95 1TLP    1       COMPND
REVDAT   1   09-JAN-89 1TLP    0
JRNL        AUTH   D.E.TRONRUD,A.F.MONZINGO,B.W.MATTHEWS
JRNL        TITL   CRYSTALLOGRAPHIC STRUCTURAL ANALYSIS OF PHOSPHORAMIDATES AS
JRNL        TITL 2 INHIBITORS AND TRANSITION-STATE ANALOGS OF THERMOLYSIN.
JRNL        REF    EUR.J.BIOCHEM.                V. 157   261 1986
JRNL        REFN                   ISSN 0014-2956
JRNL        PMID   3709536
JRNL        DOI    10.1111/J.1432-1033.1986.TB09664.X
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   D.E.TRONRUD,H.M.HOLDEN,B.W.MATTHEWS
REMARK   1  TITL   STRUCTURES OF TWO THERMOLYSIN-INHIBITOR COMPLEXES THAT
REMARK   1  TITL 2 DIFFER BY A SINGLE HYDROGEN BOND
REMARK   1  REF    SCIENCE                       V. 235   571 1987
REMARK   1  REFN                   ISSN 0036-8075
REMARK   1 REFERENCE 2
REMARK   1  AUTH   D.G.HANGAUER,A.F.MONZINGO,B.W.MATTHEWS
REMARK   1  TITL   AN INTERACTIVE COMPUTER GRAPHICS STUDY OF
REMARK   1  TITL 2 THERMOLYSIN-CATALYZED PEPTIDE CLEAVAGE AND INHIBITION BY
REMARK   1  TITL 3 N-CARBOXYMETHYL DIPEPTIDES
REMARK   1  REF    BIOCHEMISTRY                  V.  23  5730 1984
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 3
REMARK   1  AUTH   A.F.MONZINGO,B.W.MATTHEWS
REMARK   1  TITL   BINDING OF N-CARBOXYMETHYL DIPEPETIDE INHIBITORS TO
REMARK   1  TITL 2 THERMOLYSIN DETERMINED BY X-RAY CRYSTALLOGRAPHY. A NOVEL
REMARK   1  TITL 3 CLASS OF TRANSITION-STATE ANALOGUES FOR ZINC PEPTIDASES
REMARK   1  REF    BIOCHEMISTRY                  V.  23  5724 1984
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 4
REMARK   1  AUTH   M.A.HOLMES,D.E.TRONRUD,B.W.MATTHEWS
REMARK   1  TITL   STRUCTURAL ANALYSIS OF THE INHIBITION OF THERMOLYSIN BY AN
REMARK   1  TITL 2 ACTIVE-SITE-DIRECTED IRREVERSIBLE INHIBITOR
REMARK   1  REF    BIOCHEMISTRY                  V.  22   236 1983
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 5
REMARK   1  AUTH   A.F.MONZINGO,B.W.MATTHEWS
REMARK   1  TITL   STRUCTURE OF A MERCAPTAN-THERMOLYSIN COMPLEX ILLUSTRATES
REMARK   1  TITL 2 MODE OF INHIBITION OF ZINC PROTEASES BY SUBSTRATE-ANALOGUE
REMARK   1  TITL 3 MERCAPTANS
REMARK   1  REF    BIOCHEMISTRY                  V.  21  3390 1982
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 6
REMARK   1  AUTH   M.A.HOLMES,B.W.MATTHEWS
REMARK   1  TITL   STRUCTURE OF THERMOLYSIN REFINED AT 1.6 ANGSTROMS RESOLUTION
REMARK   1  REF    J.MOL.BIOL.                   V. 160   623 1982
REMARK   1  REFN                   ISSN 0022-2836
REMARK   1 REFERENCE 7
REMARK   1  AUTH   M.A.HOLMES,B.W.MATTHEWS
REMARK   1  TITL   BINDING OF HYDROXAMIC ACID INHIBITORS TO CRYSTALLINE
REMARK   1  TITL 2 THERMOLYSIN SUGGESTS A PENTACOORDINATE ZINC INTERMEDIATE IN
REMARK   1  TITL 3 CATALYSIS
REMARK   1  REF    BIOCHEMISTRY                  V.  20  6912 1981
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 8
REMARK   1  AUTH   M.C.BOLOGNESI,B.W.MATTHEWS
REMARK   1  TITL   BINDING OF THE BIPRODUCT ANALOG L-BENZYLSUCCINIC ACID TO
REMARK   1  TITL 2 THERMOLYSIN DETERMINED BY X-RAY CRYSTALLOGRAPHY
REMARK   1  REF    J.BIOL.CHEM.                  V. 254   634 1979
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1 REFERENCE 9
REMARK   1  AUTH   W.R.KESTER,B.W.MATTHEWS
REMARK   1  TITL   COMPARISON OF THE STRUCTURES OF CARBOXYPEPTIDASE A AND
REMARK   1  TITL 2 THERMOLYSIN
REMARK   1  REF    J.BIOL.CHEM.                  V. 252  7704 1977
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1 REFERENCE 10
REMARK   1  AUTH   L.H.WEAVER,W.R.KESTER,B.W.MATTHEWS
REMARK   1  TITL   A CRYSTALLOGRAPHIC STUDY OF THE COMPLEX OF PHOSPHORAMIDON
REMARK   1  TITL 2 WITH THERMOLYSIN. A MODEL FOR THE PRESUMED CATALYTIC
REMARK   1  TITL 3 TRANSITION STATE AND FOR THE BINDING OF EXTENDED SUBSTRATES
REMARK   1  REF    J.MOL.BIOL.                   V. 114   119 1977
REMARK   1  REFN                   ISSN 0022-2836
REMARK   1 REFERENCE 11
REMARK   1  AUTH   W.R.KESTER,B.W.MATTHEWS
REMARK   1  TITL   CRYSTALLOGRAPHIC STUDY OF THE BINDING OF DIPEPTIDE
REMARK   1  TITL 2 INHIBITORS TO THERMOLYSIN. IMPLICATIONS FOR THE MECHANISM OF
REMARK   1  TITL 3 CATALYSIS
REMARK   1  REF    BIOCHEMISTRY                  V.  16  2506 1977
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 12
REMARK   1  AUTH   F.W.DAHLQUIST,J.W.LONG,W.L.BIGBEE
REMARK   1  TITL   ROLE OF CALCIUM IN THE THERMAL STABILITY OF THERMOLYSIN
REMARK   1  REF    BIOCHEMISTRY                  V.  15  1103 1976
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 13
REMARK   1  AUTH   P.L.LEVY,M.K.PANGBURN,Y.BURSTEIN,L.H.ERICSSON,H.NEURATH,
REMARK   1  AUTH 2 K.A.WALSH
REMARK   1  TITL   EVIDENCE OF HOMOLOGOUS RELATIONSHIP BETWEEN THERMOLYSIN AND
REMARK   1  TITL 2 NEUTRAL PROTEASE A OF BACILLUS SUBTILIS
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  72  4341 1975
REMARK   1  REFN                   ISSN 0027-8424
REMARK   1 REFERENCE 14
REMARK   1  AUTH   L.H.WEAVER,W.R.KESTER,L.F.TENEYCK,B.W.MATTHEWS
REMARK   1  TITL   THE STRUCTURE AND STABILITY OF THERMOLYSIN
REMARK   1  REF    EXPERIENTIA,SUPPL.            V.  26    31 1976
REMARK   1  REFN                   ISSN 0071-335X
REMARK   1 REFERENCE 15
REMARK   1  AUTH   B.W.MATTHEWS,L.H.WEAVER,W.R.KESTER
REMARK   1  TITL   THE CONFORMATION OF THERMOLYSIN
REMARK   1  REF    J.BIOL.CHEM.                  V. 249  8030 1974
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1 REFERENCE 16
REMARK   1  AUTH   B.W.MATTHEWS,L.H.WEAVER
REMARK   1  TITL   BINDING OF LANTHANIDE IONS TO THERMOLYSIN
REMARK   1  REF    BIOCHEMISTRY                  V.  13  1719 1974
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 17
REMARK   1  AUTH   P.M.COLMAN,J.N.JANSONIUS,B.W.MATTHEWS
REMARK   1  TITL   THE STRUCTURE OF THERMOLYSIN. AN ELECTRON DENSITY MAP AT 2.3
REMARK   1  TITL 2 ANGSTROMS RESOLUTION
REMARK   1  REF    J.MOL.BIOL.                   V.  70   701 1972
REMARK   1  REFN                   ISSN 0022-2836
REMARK   1 REFERENCE 18
REMARK   1  AUTH   K.TITANI,M.A.HERMODSON,L.H.ERICSSON,K.A.WALSH,H.NEURATH
REMARK   1  TITL   AMINO-ACID SEQUENCE OF THERMOLYSIN
REMARK   1  REF    NATURE NEW BIOL.              V. 238    35 1972
REMARK   1  REFN                   ISSN 0369-4887
REMARK   1 REFERENCE 19
REMARK   1  AUTH   B.W.MATTHEWS,J.N.JANSONIUS,P.M.COLMAN,B.P.SCHOENBORN,
REMARK   1  AUTH 2 D.DUPORQUE
REMARK   1  TITL   THREE DIMENSIONAL STRUCTURE OF THERMOLYSIN
REMARK   1  REF    NATURE NEW BIOL.              V. 238    37 1972
REMARK   1  REFN                   ISSN 0369-4887
REMARK   1 REFERENCE 20
REMARK   1  AUTH   B.W.MATTHEWS,P.M.COLMAN,J.N.JANSONIUS,K.TITANI,K.A.WALSH,
REMARK   1  AUTH 2 H.NEURATH
REMARK   1  TITL   STRUCTURE OF THERMOLYSIN
REMARK   1  REF    NATURE NEW BIOL.              V. 238    41 1972
REMARK   1  REFN                   ISSN 0369-4887
REMARK   1 REFERENCE 21
REMARK   1  AUTH   B.W.MATTHEWS
REMARK   1  TITL   THE GAMMA TURN. EVIDENCE FOR A NEW FOLDED CONFORMATION IN
REMARK   1  TITL 2 PROTEINS
REMARK   1  REF    MACROMOLECULES                V.   5   818 1972
REMARK   1  REFN                   ISSN 0024-9297
REMARK   1 REFERENCE 22
REMARK   1  AUTH   P.M.COLMAN,L.H.WEAVER,B.W.MATTHEWS
REMARK   1  TITL   RARE EARTHS AS ISOMORPHOUS CALCIUM REPLACEMENTS FOR PROTEIN
REMARK   1  TITL 2 CRYSTALLOGRAPHY
REMARK   1  REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V.  46  1999 1972
REMARK   1  REFN                   ISSN 0006-291X
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : TNT
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.30
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 13523
REMARK   3
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.174
REMARK   3   R VALUE            (WORKING SET) : NULL
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2432
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 42
REMARK   3   SOLVENT ATOMS            : 163
REMARK   3
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT
REMARK   3   BOND LENGTHS                 (A) : 0.022 ; NULL  ; NULL
REMARK   3   BOND ANGLES            (DEGREES) : 2.900 ; NULL  ; NULL
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL
REMARK   3
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  RESTRAINT LIBRARIES.
REMARK   3   STEREOCHEMISTRY : NULL
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1TLP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 23.300
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 285
REMARK 285 THE ENTRY COORDINATES
REMARK 285 ARE NOT PRESENTED IN THE STANDARD CRYSTAL FRAME.
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 -0.499959 -0.866026  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500041  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.80201
REMARK 290   SMTRY1   3 -0.500041  0.866026  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.499959  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       87.60403
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       65.70302
REMARK 290   SMTRY1   5  0.499959  0.866026  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500041  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      109.50504
REMARK 290   SMTRY1   6  0.500041 -0.866026  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.499959  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       21.90101
REMARK 290   SMTRY1   7  0.499959  0.866026  0.000000        0.00000
REMARK 290   SMTRY2   7  0.866072 -0.499959  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       43.80201
REMARK 290   SMTRY1   8  0.500041 -0.866026  0.000000        0.00000
REMARK 290   SMTRY2   8 -0.865978 -0.500041  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       87.60403
REMARK 290   SMTRY1  10 -0.499959 -0.866026  0.000000        0.00000
REMARK 290   SMTRY2  10 -0.866072  0.499959  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      109.50504
REMARK 290   SMTRY1  11 -0.500041  0.866026  0.000000        0.00000
REMARK 290   SMTRY2  11  0.865978  0.500041  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       65.70302
REMARK 290   SMTRY1  12  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  12  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       21.90101
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: E
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 THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH E   434     O    HOH E   434     7555     1.03
REMARK 500   O    HOH E   387     O    HOH E   387    12565     1.86
REMARK 500
REMARK 500 REMARK: NULL
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    SER E   5   N   -  CA  -  CB  ANGL. DEV. =   9.1 DEGREES
REMARK 500    VAL E   9   CA  -  CB  -  CG2 ANGL. DEV. =   9.1 DEGREES
REMARK 500    THR E  26   N   -  CA  -  CB  ANGL. DEV. =  12.4 DEGREES
REMARK 500    TYR E  27   CB  -  CG  -  CD2 ANGL. DEV. =  -4.6 DEGREES
REMARK 500    TYR E  29   CB  -  CG  -  CD2 ANGL. DEV. =   4.6 DEGREES
REMARK 500    TYR E  29   CB  -  CG  -  CD1 ANGL. DEV. =  -7.4 DEGREES
REMARK 500    ARG E  35   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    TYR E  42   CB  -  CG  -  CD1 ANGL. DEV. =  -4.5 DEGREES
REMARK 500    TYR E  46   CB  -  CG  -  CD1 ANGL. DEV. =  -4.6 DEGREES
REMARK 500    TYR E  75   CB  -  CG  -  CD1 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    TYR E 106   CB  -  CG  -  CD2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    TYR E 151   CB  -  CG  -  CD2 ANGL. DEV. =  -5.7 DEGREES
REMARK 500    ARG E 220   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ARG E 220   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.2 DEGREES
REMARK 500    ARG E 260   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ARG E 260   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    TYR E 268   CB  -  CG  -  CD2 ANGL. DEV. =  -5.0 DEGREES
REMARK 500    TYR E 274   CB  -  CG  -  CD1 ANGL. DEV. =  -6.0 DEGREES
REMARK 500    VAL E 313   CA  -  CB  -  CG1 ANGL. DEV. =  10.6 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 E  25       87.59   -161.52
REMARK 500    THR E  26      -56.39     70.21
REMARK 500    PHE E  62       61.31   -112.02
REMARK 500    SER E  92     -176.32     62.74
REMARK 500    SER E 107     -162.40     56.67
REMARK 500    ASN E 111       52.64    -92.66
REMARK 500    SER E 118      -12.70   -141.34
REMARK 500    THR E 152     -102.03   -107.68
REMARK 500    ASN E 159     -147.37     59.20
REMARK 500    THR E 194       79.22     30.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    THR E  26        15.4      L          L   OUTSIDE RANGE
REMARK 500    ALA E  68        21.9      L          L   OUTSIDE RANGE
REMARK 500    VAL E  79        17.2      L          L   OUTSIDE RANGE
REMARK 500    TYR E  84        24.4      L          L   OUTSIDE RANGE
REMARK 500    SER E 118        23.6      L          L   OUTSIDE RANGE
REMARK 500    LEU E 133        21.6      L          L   OUTSIDE RANGE
REMARK 500    ASN E 159        23.9      L          L   OUTSIDE RANGE
REMARK 500    ARG E 260        12.7      L          L   OUTSIDE RANGE
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 E 318  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 138   OD1
REMARK 620 2 GLU E 177   OE1  74.3
REMARK 620 3 GLU E 177   OE2 120.0  45.9
REMARK 620 4 GLU E 187   O    82.0 139.9 146.2
REMARK 620 5 GLU E 190   OE1  82.9 127.1 125.0  80.0
REMARK 620 6 GLU E 190   OE2  97.7  84.6  74.8 131.0  51.7
REMARK 620 7 ASP E 185   OD2 162.7 122.5  77.2  81.6  88.8  88.8
REMARK 620 8 HOH E 335   O    94.7  77.2  79.5  73.0 152.9 154.3  85.8
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA E 319  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 177   OE2
REMARK 620 2 GLU E 190   OE2  89.7
REMARK 620 3 HOH E 342   O    91.7  96.6
REMARK 620 4 HOH E 424   O   176.9  89.8  85.3
REMARK 620 5 ASN E 183   O    85.7 166.7  95.9  95.4
REMARK 620 6 ASP E 185   OD1  88.4  79.6 176.2  94.6  87.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA E 320  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH E 447   O
REMARK 620 2 HOH E 431   O    88.7
REMARK 620 3 GLN E  61   O   176.5  92.5
REMARK 620 4 ASP E  59   OD1  85.4  74.2  91.7
REMARK 620 5 ASP E  57   OD2  90.0 144.7  87.1  70.6
REMARK 620 6 ASP E  57   OD1  84.0 163.5  95.6 119.8  50.3
REMARK 620 7 HOH E 388   O    99.3  84.0  84.1 157.6 130.8  82.6
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA E 321  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH E 343   O
REMARK 620 2 ASP E 200   OD1  76.5
REMARK 620 3 ILE E 197   O   114.5  88.6
REMARK 620 4 TYR E 193   O    83.5 129.2 141.9
REMARK 620 5 THR E 194   OG1 131.3  76.5 104.6  83.2
REMARK 620 6 THR E 194   O   154.1 129.3  73.5  77.2  63.6
REMARK 620 7 HOH E 429   O    81.4 137.0  67.7  83.3 142.5  79.3
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN E 322  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 166   OE1
REMARK 620 2 HIS E 142   NE2 128.2
REMARK 620 3 HIS E 146   NE2  97.9 101.1
REMARK 620 4 GLU E 166   OE2  52.2  81.2 134.6
REMARK 620 5 RDF E 317   O1P  98.9 115.8 114.1 104.8
REMARK 620 N                    1     2     3     4
REMARK 630
REMARK 630 MOLECULE TYPE: NULL
REMARK 630 MOLECULE NAME: N-ALPHA-L-RHAMNOPYRANOSYLOXY(HYDROXYPHOSPHINYL)-L-
REMARK 630 LEUCYL-L-TRYPTOPHAN
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630   M RES C SSSEQI
REMARK 630     RDF E   317
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP:    RHA LEU TRP
REMARK 630 DETAILS: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE *ACTIVE-SITE* SHEET SUBSTRUCTURE OF THIS MOLECULE HAS
REMARK 700 ONE EDGE-STRAND COMPRISED OF TWO DISTINCT SEQUENCES OF THE
REMARK 700 POLYPEPTIDE CHAIN.  TO REPRESENT THIS FEATURE AN EXTRA
REMARK 700 SHEET IS DEFINED.  STRANDS 2,3,4,5 OF S1 ARE IDENTICAL TO
REMARK 700 STRANDS 2,3,4,5 OF S2.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RDF E 317
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 318
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 320
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 322
DBREF  1TLP E    1   316  UNP    P00800   THER_BACTH       1    316
SEQRES   1 E  316  ILE THR GLY THR SER THR VAL GLY VAL GLY ARG GLY VAL
SEQRES   2 E  316  LEU GLY ASP GLN LYS ASN ILE ASN THR THR TYR SER THR
SEQRES   3 E  316  TYR TYR TYR LEU GLN ASP ASN THR ARG GLY ASP GLY ILE
SEQRES   4 E  316  PHE THR TYR ASP ALA LYS TYR ARG THR THR LEU PRO GLY
SEQRES   5 E  316  SER LEU TRP ALA ASP ALA ASP ASN GLN PHE PHE ALA SER
SEQRES   6 E  316  TYR ASP ALA PRO ALA VAL ASP ALA HIS TYR TYR ALA GLY
SEQRES   7 E  316  VAL THR TYR ASP TYR TYR LYS ASN VAL HIS ASN ARG LEU
SEQRES   8 E  316  SER TYR ASP GLY ASN ASN ALA ALA ILE ARG SER SER VAL
SEQRES   9 E  316  HIS TYR SER GLN GLY TYR ASN ASN ALA PHE TRP ASN GLY
SEQRES  10 E  316  SER GLU MET VAL TYR GLY ASP GLY ASP GLY GLN THR PHE
SEQRES  11 E  316  ILE PRO LEU SER GLY GLY ILE ASP VAL VAL ALA HIS GLU
SEQRES  12 E  316  LEU THR HIS ALA VAL THR ASP TYR THR ALA GLY LEU ILE
SEQRES  13 E  316  TYR GLN ASN GLU SER GLY ALA ILE ASN GLU ALA ILE SER
SEQRES  14 E  316  ASP ILE PHE GLY THR LEU VAL GLU PHE TYR ALA ASN LYS
SEQRES  15 E  316  ASN PRO ASP TRP GLU ILE GLY GLU ASP VAL TYR THR PRO
SEQRES  16 E  316  GLY ILE SER GLY ASP SER LEU ARG SER MET SER ASP PRO
SEQRES  17 E  316  ALA LYS TYR GLY ASP PRO ASP HIS TYR SER LYS ARG TYR
SEQRES  18 E  316  THR GLY THR GLN ASP ASN GLY GLY VAL HIS ILE ASN SER
SEQRES  19 E  316  GLY ILE ILE ASN LYS ALA ALA TYR LEU ILE SER GLN GLY
SEQRES  20 E  316  GLY THR HIS TYR GLY VAL SER VAL VAL GLY ILE GLY ARG
SEQRES  21 E  316  ASP LYS LEU GLY LYS ILE PHE TYR ARG ALA LEU THR GLN
SEQRES  22 E  316  TYR LEU THR PRO THR SER ASN PHE SER GLN LEU ARG ALA
SEQRES  23 E  316  ALA ALA VAL GLN SER ALA THR ASP LEU TYR GLY SER THR
SEQRES  24 E  316  SER GLN GLU VAL ALA SER VAL LYS GLN ALA PHE ASP ALA
SEQRES  25 E  316  VAL GLY VAL LYS
HET    RDF  E 317      37
HET     CA  E 318       1
HET     CA  E 319       1
HET     CA  E 320       1
HET     CA  E 321       1
HET     ZN  E 322       1
HETNAM     RDF N-ALPHA-L-RHAMNOPYRANOSYLOXY(HYDROXYPHOSPHINYL)-L-
HETNAM   2 RDF  LEUCYL-L-TRYPTOPHAN
HETNAM      CA CALCIUM ION
HETNAM      ZN ZINC ION
HETSYN     RDF PHOSPHORAMIDON
FORMUL   2  RDF    C23 H34 N3 O10 P
FORMUL   3   CA    4(CA 2+)
FORMUL   7   ZN    ZN 2+
FORMUL   8  HOH   *163(H2 O)
HELIX    1  H1 SER E   65  VAL E   87  165,66 3/10 OR ALPHA-II CONFN      23
HELIX    2  H2 LEU E  133  GLY E  135  5                                   3
HELIX    3  H3 ILE E  137  ASP E  150  1151 IN ALPHA-II CONFORMATION      14
HELIX    4  H4 GLU E  160  ALA E  180  1180 IN 3/10 CONFORMATION          21
HELIX    5  H5 GLU E  190  VAL E  192  1192 IN 3/10 OR ALPHA-II CONFN      3
HELIX    6  H6 PRO E  208  TYR E  211  5                                   4
HELIX    7  H7 TYR E  217  LYS E  219  5                                   3
HELIX    8  H8 ASP E  226  GLY E  229  6LEFT-HAND ALPHA HELIX              4
HELIX    9  H9 ASN E  233  GLN E  246  1233,234 IN 3/10 CONFORMATION      14
HELIX   10 H10 ARG E  260  TYR E  274  1262 IN ALPHA-II CONFORMATION      15
HELIX   11 H11 PHE E  281  TYR E  296  1                                  16
HELIX   12 H12 GLN E  301  VAL E  313  1313 IN 3/10 CONFORMATION          13
SHEET    1  S1 5 GLN E  31  ASP E  32  0
SHEET    2  S1 5 ILE E  39  ASP E  43 -1  N  ILE E  39   O  ASP E  32
SHEET    3  S1 5 ILE E 100  TYR E 106  1  N  SER E 102   O  PHE E  40
SHEET    4  S1 5 GLU E 119  TYR E 122  1  N  TYR E 122   O  SER E 103
SHEET    5  S1 5 ASN E 112  TRP E 115 -1  N  PHE E 114   O  VAL E 121
SHEET    1  S2 5 GLY E  52  LEU E  54  0
SHEET    2  S2 5 ILE E  39  ASP E  43 -1  N  ASP E  43   O  SER E  53
SHEET    3  S2 5 ILE E 100  TYR E 106  1  N  SER E 102   O  PHE E  40
SHEET    4  S2 5 GLU E 119  TYR E 122  1  N  TYR E 122   O  SER E 103
SHEET    5  S2 5 ASN E 112  TRP E 115 -1  N  PHE E 114   O  VAL E 121
SHEET    1  S3 5 TRP E  55  ASP E  57  0
SHEET    2  S3 5 TYR E  27  TYR E  29 -1  O  TYR E  28   N  ASP E  57
SHEET    3  S3 5 ASP E  16  SER E  25 -1  O  THR E  23   N  TYR E  29
SHEET    4  S3 5 THR E   2  ARG E  11 -1  O  THR E   6   N  THR E  22
SHEET    5  S3 5 GLN E  61  PHE E  62  1  O  VAL E   9   N  PHE E  62
LINK        CA    CA E 318                 OD1 ASP E 138     1555   1555  2.44
LINK        CA    CA E 318                 OE1 GLU E 177     1555   1555  2.73
LINK        CA    CA E 318                 OE2 GLU E 177     1555   1555  2.87
LINK        CA    CA E 318                 O   GLU E 187     1555   1555  2.34
LINK        CA    CA E 318                 OE1 GLU E 190     1555   1555  2.50
LINK        CA    CA E 318                 OE2 GLU E 190     1555   1555  2.58
LINK        CA    CA E 318                 OD2 ASP E 185     1555   1555  2.45
LINK        CA    CA E 318                 O   HOH E 335     1555   1555  2.67
LINK        CA    CA E 319                 OE2 GLU E 177     1555   1555  2.35
LINK        CA    CA E 319                 OE2 GLU E 190     1555   1555  2.35
LINK        CA    CA E 319                 O   HOH E 342     1555   1555  2.22
LINK        CA    CA E 319                 O   HOH E 424     1555   1555  2.29
LINK        CA    CA E 319                 O   ASN E 183     1555   1555  2.51
LINK        CA    CA E 319                 OD1 ASP E 185     1555   1555  2.45
LINK        CA    CA E 320                 O   HOH E 447     1555   1555  2.33
LINK        CA    CA E 320                 O   HOH E 431     1555   1555  2.44
LINK        CA    CA E 320                 O   GLN E  61     1555   1555  2.24
LINK        CA    CA E 320                 OD1 ASP E  59     1555   1555  2.32
LINK        CA    CA E 320                 OD2 ASP E  57     1555   1555  2.80
LINK        CA    CA E 320                 OD1 ASP E  57     1555   1555  2.34
LINK        CA    CA E 320                 O   HOH E 388     1555   1555  2.39
LINK        CA    CA E 321                 O   HOH E 343     1555   1555  2.60
LINK        CA    CA E 321                 OD1 ASP E 200     1555   1555  2.24
LINK        CA    CA E 321                 O   ILE E 197     1555   1555  2.29
LINK        CA    CA E 321                 O   TYR E 193     1555   1555  2.54
LINK        CA    CA E 321                 OG1 THR E 194     1555   1555  2.40
LINK        CA    CA E 321                 O   THR E 194     1555   1555  2.47
LINK        CA    CA E 321                 O   HOH E 429     1555   1555  2.36
LINK        ZN    ZN E 322                 OE1 GLU E 166     1555   1555  1.95
LINK        ZN    ZN E 322                 NE2 HIS E 142     1555   1555  2.22
LINK        ZN    ZN E 322                 NE2 HIS E 146     1555   1555  2.19
LINK        ZN    ZN E 322                 OE2 GLU E 166     1555   1555  2.68
LINK         O1P RDF E 317                ZN    ZN E 322     1555   1555  1.75
CISPEP   1 LEU E   50    PRO E   51          0        -0.95
SITE     1 AC1 14 ASN E 111  ASN E 112  ALA E 113  PHE E 114
SITE     2 AC1 14 PHE E 130  HIS E 142  GLU E 143  HIS E 146
SITE     3 AC1 14 TYR E 157  GLU E 166  ARG E 203  HIS E 231
SITE     4 AC1 14  ZN E 322  HOH E 485
SITE     1 AC2  6 ASP E 138  GLU E 177  ASP E 185  GLU E 187
SITE     2 AC2  6 GLU E 190  HOH E 335
SITE     1 AC3  6 GLU E 177  ASN E 183  ASP E 185  GLU E 190
SITE     2 AC3  6 HOH E 342  HOH E 424
SITE     1 AC4  6 ASP E  57  ASP E  59  GLN E  61  HOH E 388
SITE     2 AC4  6 HOH E 431  HOH E 447
SITE     1 AC5  6 TYR E 193  THR E 194  ILE E 197  ASP E 200
SITE     2 AC5  6 HOH E 343  HOH E 429
SITE     1 AC6  5 HIS E 142  HIS E 146  TYR E 157  GLU E 166
SITE     2 AC6  5 RDF E 317
CRYST1   94.100   94.100  131.400  90.00  90.00 120.00 P 61 2 2     12
ORIGX1      0.866025 -0.500000  0.000000        0.00000
ORIGX2      0.500000  0.866025  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.012271  0.000000  0.000000        0.00000
SCALE2      0.006135  0.010627  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007610        0.00000
      
PROCHECK
Go to PROCHECK summary
 References